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APP

gene
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Also known as alpha-sAPP

Summary

APP (amyloid beta precursor protein, HGNC:620) is a protein-coding gene on chromosome 21q21.3, encoding Amyloid-beta precursor protein (P05067). Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis.

This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. In addition, two of the peptides are antimicrobial peptides, having been shown to have bacteriocidal and antifungal activities. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.

Source: NCBI Gene 351 — RefSeq curated summary.

At a glance

  • Gene–disease (curated): cerebral amyloid angiopathy, APP-related (Definitive, ClinGen) — +8 more curated relationships
  • GWAS associations: 7
  • Clinical variants (ClinVar): 652 total — 23 pathogenic, 9 likely-pathogenic (top 5% of genes corpus-wide)
  • GTEx eGene: eQTL in 24 tissues, sQTL in 18 (q < 0.05)
  • Phenotypes (HPO): 55
  • Drug target: yes — 13 curated mechanism-of-action drugs; 40 molecules with ChEMBL bioactivity (top 1% of genes corpus-wide)
  • Approved drugs (ChEMBL mechanism of action): 3 — Aducanumab, Donanemab, Lecanemab
  • Dosage sensitivity (ClinGen): haploinsufficiency no evidence, triplosensitivity little evidence
  • Constraint (gnomAD): pLI 1.00 (loss-of-function intolerant), LOEUF 0.41 (moderately constrained)
  • Transcription factor: yes — 31 downstream targets (CollecTRI)
  • MANE Select transcript: NM_000484
  • Interaction hub: 6,488 STRING partners (top 1% of genes corpus-wide)

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:620
Approved symbolAPP
Nameamyloid beta precursor protein
Location21q21.3
Locus typegene with protein product
StatusApproved
Aliasesalpha-sAPP
Ensembl geneENSG00000142192
Ensembl biotypeprotein_coding
OMIM104760
Entrez351

Gene structure

Transcript identifiers

Ensembl transcripts: 63 — 50 protein_coding, 8 protein_coding_CDS_not_defined, 3 nonsense_mediated_decay, 2 retained_intron

MANE Select: ENST00000346798

Transcript support level (Ensembl TSL; 1 = fully mRNA-supported): TSL 1: 8, TSL 2: 6, TSL 3: 2, TSL 5: 1

ENST00000346798, ENST00000348990, ENST00000354192, ENST00000357903, ENST00000358918, ENST00000359726, ENST00000415997, ENST00000439274, ENST00000440126, ENST00000448850, ENST00000462267, ENST00000463070, ENST00000464867, ENST00000466453, ENST00000474136, ENST00000491395, ENST00000548570, ENST00000707132, ENST00000707133, ENST00000707134, ENST00000872524, ENST00000872525, ENST00000872526, ENST00000872527, ENST00000872528, ENST00000872529, ENST00000872530, ENST00000872531, ENST00000872532, ENST00000872533, ENST00000872534, ENST00000872535, ENST00000872536, ENST00000872537, ENST00000872538, ENST00000932837, ENST00000932838, ENST00000965079, ENST00000965080, ENST00000965081, ENST00001003894, ENST00001003895, ENST00001003897, ENST00001046380, ENST00001046382, ENST00001086896, ENST00001086897, ENST00001086898, ENST00001107673, ENST00001107674, ENST00001107675, ENST00001107676, ENST00001107677, ENST00001107678, ENST00001107679, ENST00001107680, ENST00001107681, ENST00001114381, ENST00001114382, ENST00001114383, ENST00001114384, ENST00001114385, ENST00001131782

RefSeq mRNA: 11 — MANE Select: NM_000484 NM_000484, NM_001136016, NM_001136129, NM_001136130, NM_001136131, NM_001204301, NM_001204302, NM_001204303, NM_001385253, NM_201413, NM_201414

CCDS: CCDS13576, CCDS13577, CCDS33523, CCDS46638, CCDS46639, CCDS56211, CCDS56212, CCDS56213

Canonical transcript exons

ENST00000346798 — 18 exons

ExonStartEnd
ENSE000013093222599736025997416
ENSE000036917232600001526000182
ENSE000038454662617056426170770
ENSE000039982792595562725955755
ENSE000039982822605323626053348
ENSE000039982852605100026051193
ENSE000039982862589172225891868
ENSE000039982872591174125911962
ENSE000039982882595459025954689
ENSE000039982902597507025975228
ENSE000039982912611197926112146
ENSE000039982922590502425905077
ENSE000039982932597595425976028
ENSE000039982942598234425982477
ENSE000039982962589757325897673
ENSE000039982972588055025881771
ENSE000039982982602184026022042
ENSE000039982992608994326090072

Expression profiles

Bgee: expression breadth ubiquitous, 295 present calls, max score 99.79.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 311.6966 / max 5368.2517, expressed in 1755 samples.

Highest expression (Bgee): prefrontal cortex, renal medulla, Brodmann (1909) area 9, medial globus pallidus, stromal cell of endometrium.

Genetic regulation across tissues (GTEx eQTL / sQTL)

APP is an eGene in GTEx v10 — its expression is genetically regulated (eQTL) in 24 tissues and its splicing (sQTL) in 18 (q < 0.05). Strongest associations first; slope = normalized effect of the lead variant’s alternative allele.

showing 20 of 42 significant tissue × QTL associations:

TissueQTLq-valueSlopeLead variant
Esophagus Musculariseqtl1.4e-17+0.2421:26154029:C:A
Cells Cultured fibroblastssqtl7.3e-15+0.3321:25999019:A:C
Whole Bloodeqtl4.9e-13+0.1921:26162498:G:A
Nerve Tibialsqtl3.4e-12+0.4021:25996907:G:A
Adipose Visceral Omentumsqtl5.4e-08+0.4121:25996907:G:A
Esophagus Gastroesophageal Junctionsqtl8.2e-08+0.5221:25990433:T:C
Esophagus Muscularissqtl9.7e-08+0.3521:25991674:A:G
Skin Not Sun Exposed Suprapubicsqtl1.2e-07+0.4021:25996383:G:A
Artery Tibialsqtl1.4e-07+0.3121:25996383:G:A
Artery Aortasqtl1.9e-07+0.4321:25999019:A:C
Adipose Subcutaneoussqtl3.4e-07+0.3221:25996907:G:A
Skin Sun Exposed Lower legsqtl4.1e-06+0.3621:25995506:C:G
Esophagus Gastroesophageal Junctioneqtl1.7e-05+0.2321:26153541:G:C
Lungsqtl1.8e-05+0.3921:25999019:A:C
Testiseqtl2.6e-05-0.1921:26116134:A:G
Adipose Subcutaneouseqtl4.9e-05-0.1921:25933408:T:G
Thyroidsqtl1.1e-04+0.2621:25984667:A:T
Heart Left Ventriclesqtl1.3e-04+0.4821:25997094:T:C
Brain Putamen basal gangliaeqtl1.5e-04+0.1421:25983644:A:G
Heart Atrial Appendagesqtl2.8e-04+0.4521:25996383:G:A

FANTOM5 promoters

showing 10 of 17 alternative TSS:

Promoter IDTPM avgSamples expressed
189996294.25221754
1899524.33321257
1899903.22051229
1899862.0240841
1899801.6386649
1899871.5998821
1899601.1338583
1899710.9956564
1899940.7367398
1899950.6492380

Top tissues by expression

showing 100 of 295 tissues by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
prefrontal cortexUBERON:000045199.79gold quality
renal medullaUBERON:000036299.69gold quality
Brodmann (1909) area 9UBERON:001354099.69gold quality
medial globus pallidusUBERON:000247799.66gold quality
stromal cell of endometriumCL:000225599.65gold quality
tendon of biceps brachiiUBERON:000818899.64gold quality
cortical plateUBERON:000534399.61gold quality
globus pallidusUBERON:000187599.58gold quality
primary visual cortexUBERON:000243699.58gold quality
islet of LangerhansUBERON:000000699.56gold quality
C1 segment of cervical spinal cordUBERON:000646999.56gold quality
choroid plexus epitheliumUBERON:000391199.55gold quality
metanephros cortexUBERON:001053399.55gold quality
occipital lobeUBERON:000202199.53gold quality
dorsolateral prefrontal cortexUBERON:000983499.51gold quality
nucleus accumbensUBERON:000188299.47gold quality
colonic epitheliumUBERON:000039799.46gold quality
Brodmann (1909) area 23UBERON:001355499.46gold quality
frontal cortexUBERON:000187099.45gold quality
putamenUBERON:000187499.45gold quality
gall bladderUBERON:000211099.45gold quality
ventral tegmental areaUBERON:000269199.45gold quality
caudate nucleusUBERON:000187399.44gold quality
spinal cordUBERON:000224099.44gold quality
hypothalamusUBERON:000189899.43gold quality
endothelial cellCL:000011599.42gold quality
neocortexUBERON:000195099.41gold quality
corpus callosumUBERON:000233699.41gold quality
inferior vagus X ganglionUBERON:000536399.41gold quality
left lobe of thyroid glandUBERON:000112099.40gold quality
amygdalaUBERON:000187699.40gold quality
thyroid glandUBERON:000204699.38gold quality
right lobe of thyroid glandUBERON:000111999.37gold quality
left adrenal glandUBERON:000123499.35gold quality
telencephalonUBERON:000189399.35gold quality
descending thoracic aortaUBERON:000234599.35gold quality
cerebral cortexUBERON:000095699.34gold quality
trigeminal ganglionUBERON:000167599.34gold quality
mucosa of paranasal sinusUBERON:000503099.34gold quality
left adrenal gland cortexUBERON:003582599.34gold quality
midbrainUBERON:000189199.33gold quality
substantia nigraUBERON:000203899.33gold quality
adrenal glandUBERON:000236999.33gold quality
adrenal cortexUBERON:000123599.32gold quality
right frontal lobeUBERON:000281099.32gold quality
Ammon’s hornUBERON:000195499.31gold quality
dorsal plus ventral thalamusUBERON:000189799.30gold quality
right lungUBERON:000216799.30gold quality
superior vestibular nucleusUBERON:000722799.30gold quality
right adrenal gland cortexUBERON:003582799.30gold quality
subthalamic nucleusUBERON:000190699.29gold quality
lateral nuclear group of thalamusUBERON:000273699.29gold quality
forebrainUBERON:000189099.28gold quality
substantia nigra pars compactaUBERON:000196599.28gold quality
ponsUBERON:000098899.27gold quality
right adrenal glandUBERON:000123399.27gold quality
cingulate cortexUBERON:000302799.27gold quality
medulla oblongataUBERON:000189699.26gold quality
central nervous systemUBERON:000101799.25gold quality
rectumUBERON:000105299.25gold quality
substantia nigra pars reticulataUBERON:000196699.25gold quality
lateral globus pallidusUBERON:000247699.25gold quality
anterior cingulate cortexUBERON:000983599.25gold quality
brainUBERON:000095599.24gold quality
thoracic aortaUBERON:000151599.21gold quality
dorsal motor nucleus of vagus nerveUBERON:000287099.21gold quality
ganglionic eminenceUBERON:000402399.21gold quality
ascending aortaUBERON:000149699.20gold quality
Brodmann (1909) area 10UBERON:001354199.20gold quality
dorsal root ganglionUBERON:000004499.19gold quality
adrenal tissueUBERON:001830399.19gold quality
smooth muscle tissueUBERON:000113599.16gold quality
epithelium of mammary glandUBERON:000324499.16gold quality
temporal lobeUBERON:000187199.14gold quality
mammary ductUBERON:000176599.13gold quality
ventricular zoneUBERON:000305399.13gold quality
type B pancreatic cellCL:000016999.12gold quality
pigmented layer of retinaUBERON:000178299.12gold quality
lower esophagus muscularis layerUBERON:003583399.10gold quality
tendonUBERON:000004399.09gold quality
cerebellar cortexUBERON:000212999.09gold quality
cerebellar hemisphereUBERON:000224599.09gold quality
lower esophagusUBERON:001347399.08gold quality
adult mammalian kidneyUBERON:000008299.07gold quality
aortaUBERON:000094799.06gold quality
transverse colonUBERON:000115799.05gold quality
kidneyUBERON:000211399.05gold quality
upper lobe of left lungUBERON:000895299.03gold quality
metanephrosUBERON:000008199.01gold quality
cortex of kidneyUBERON:000122599.01gold quality
superior frontal gyrusUBERON:000266199.00gold quality
sural nerveUBERON:001548899.00gold quality
esophagogastric junction muscularis propriaUBERON:003584199.00gold quality
upper lobe of lungUBERON:000894898.99gold quality
epithelial cell of pancreasCL:000008398.96gold quality
popliteal arteryUBERON:000225098.94gold quality
calcaneal tendonUBERON:000370198.94gold quality
olfactory segment of nasal mucosaUBERON:000538698.94gold quality
tibial arteryUBERON:000761098.94gold quality
right ovaryUBERON:000211898.93gold quality

Single-cell (SCXA)

Detected in 38 experiment(s), a significant marker in 34.

ExperimentMarker?Max mean expression
E-CURD-88yes2964.07
E-CURD-112yes1694.18
E-HCAD-56yes1361.47
E-MTAB-9435yes781.93
E-GEOD-150728yes658.52
E-GEOD-149689yes619.29
E-MTAB-6819yes321.97
E-MTAB-8142yes121.08
E-MTAB-6701yes119.49
E-HCAD-4yes71.80
E-MTAB-10287yes70.18
E-MTAB-10553yes64.61
E-HCAD-1yes46.89
E-GEOD-135922yes43.26
E-HCAD-6yes34.40

HPA expression

RNA tissue specificity: Low tissue specificity

showing 60 of 76 HPA tissues / cells by nTPM:

Tissue / cellAxisnTPMProtein (IHC)
Caudate putamentissue1066.9
Frontal cortextissue972.7
Postcentral gyrustissue850.9
Midbraintissue756.2
Cerebral cortextissue753.0medium
Somatosensory cortextissue753.0
Nucleus accumbenstissue742.4
Thalamustissue726.1
Ponstissue701.5
Superior colliculitissue694.8
Choroid plexustissue691.5
Occipital cortextissue669.7
Motor cortextissue662.5
Prefrontal cortextissue661.1
Locus coeruleustissue615.9
Hippocampustissue608.6medium
Retrosplenial and cingulate cortextissue593.4
Substantia nigratissue572.4
Spinal cordtissue571.6
Hippocampal formationtissue565.4
Entorhinal cortextissue565.4
Putamentissue559.6
Medulla oblongatatissue556.0
Retrosplenial cortextissue542.8
Corpus callosumtissue529.3
Ventral forebraintissue515.7
Temporal cortextissue512.3
Basal gangliatissue495.4medium
Insular cortextissue482.0
Septumtissue474.0
Kidneytissue464.8not detected
Thyroid glandtissue434.2not detected
Hypothalamustissue428.5
Adrenal glandtissue422.0not detected
Placentatissue417.2low
Ovarytissue401.1not detected
Periaqueductal graytissue396.6
Breasttissue392.7low
Amygdalatissue375.4
Heart muscletissue356.3not detected
Smooth muscletissue353.7not detected
Olfactory bulbtissue353.0
Colontissue322.5low
Gallbladdertissue321.7low
Seminal vesicletissue315.9low
Pancreastissue305.2low
Cerebellumtissue303.3high
Rectumtissue296.0low
Fallopian tubetissue289.3not detected
Urinary bladdertissue275.5not detected
Parathyroid glandtissue259.7not detected
Lungtissue255.6not detected
Endometrium 1tissue254.0not detected
Livertissue251.5not detected
Cervixtissue239.9not detected
Prostatetissue232.5low
Adipose tissuetissue220.7not detected
Epididymistissue214.2low
Duodenumtissue204.9low
Stomach 1tissue197.5not detected

Brain sub-regions (HPA Brain Atlas): detected in 190; highest nTPM — Occipital cortex (white matter) (921.2), Corpus callosum, splenium (white matter) (884.6), Parieto-temporal junction (white matter) (880.1), Median raphe nucleus (879.4), Corpus callosum, genu (white matter) (855.7).

Regulation

Is transcription factor: yes

Downstream targets (CollecTRI)

showing 30 of 31 targets:

TargetRegulation
ABCB1Repression
ABCC1Unknown
AGERActivation
ARG1Activation
AXIN2Repression
BECN1Repression
CCL2Repression
CCL5Activation
CCND1Activation
CLURepression
DKK1Activation
EGR1Activation
FCGR2BActivation
FOSActivation
FZD5Unknown
IL10Activation
IL1BActivation
KLF10Activation
LEF1Repression
LRP1Repression
MMEUnknown
NAB2Activation
NEDD4Activation
PFKFB3Activation
PTENActivation
ROCK1Activation
SLC40A1Repression
SLC8A2Unknown
SLC8A3Unknown
TNFRepression

Upstream regulators (CollecTRI, top): AHR, AP1, AR, BSX, CEBPG, CNOT4, CTCF, CTNNB1, EGR1, ESR1, ESR2, ETS2, FOS, FOXI1, FOXO3, HDAC9, HIF1A, JUN, KAT7, LEF1, MBD2, MYC, NCOR2, NFATC2, NFIL3, NFKB, NR1I2, NR1I3, PPARA, PPARG, PURA, RARA, RXRA, SMAD2, SMAD3, SMAD4, SP1, SP3, STAT1, STAT3

miRNA regulators (miRDB)

Targeting APP by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific).

showing 30 of 137 miRNAs:

miRNAMax scoreAvg scoremiRNA target_count
HSA-LET-7A-3P100.0074.033932
HSA-LET-7B-3P100.0074.083913
HSA-LET-7F-1-3P100.0074.023928
HSA-MIR-98-3P100.0074.083907
HSA-MIR-5692A100.0074.406850
HSA-MIR-3646100.0073.565283
HSA-MIR-188-3P100.0068.761240
HSA-MIR-3613-3P100.0076.367965
HSA-MIR-4692100.0067.322066
HSA-MIR-366299.9973.825684
HSA-MIR-453199.9969.703181
HSA-MIR-548C-3P99.9974.017587
HSA-MIR-477599.9875.006394
HSA-MIR-314899.9775.066478
HSA-MIR-3688-3P99.9772.022834
HSA-MIR-302E99.9670.742669
HSA-MIR-9-3P99.9670.882068
HSA-MIR-4666A-3P99.9671.713434
HSA-MIR-551B-5P99.9671.283493
HSA-LET-7C-3P99.9573.422862
HSA-MIR-101-3P99.9475.032230
HSA-MIR-144-3P99.9473.982698
HSA-MIR-6835-3P99.9370.492904
HSA-MIR-381-3P99.9371.872854
HSA-MIR-30099.9271.762856
HSA-MIR-497-5P99.9271.832674
HSA-MIR-10523-5P99.9169.222038
HSA-MIR-106A-5P99.9073.942683
HSA-MIR-368699.9070.532432
HSA-MIR-627-3P99.9071.423316

Functional genomics

gnomAD constraint: pLI 1, LOEUF 0.41, missense Z 2.26 — population loss-of-function intolerance (pLI ≥ 0.9 = LoF-intolerant; lower LOEUF = more constrained). gnomAD

Regional missense constraint (gnomAD RMC): no regional variation along ENST00000346798 — one region, missense o/e 0.84. ClinGen dosage: haploinsufficiency 0 (no evidence), triplosensitivity 1 (little evidence). ClinGen Gene Dosage Map

Literature-anchored findings (GeneRIF, showing 40)

  • Kunitz protease inhibitor (KPI) domain forms of APP regulate extracellular cleavage of secreted APP by inhibiting the activity of a secreted APP-degrading protease (PMID:10561592)
  • Alzheimer’s Amyloid-beta peptide contains catalase binding site and inhibits anti-oxidant activity (PMID:10567208)
  • Mutations in APP may predispose to very-late-onset Alzheimer disease. (PMID:11500807)
  • helix-containing intermediates in amyloid beta-protein fibrillogenesis (PMID:11580253)
  • Serine phosphorylation site within the Alzheimer’s Amyloid-beta sequence (PMID:11726805)
  • Here the technique of small angle neutron scattering has been used to determine the structure of these Abeta micelles (PMID:11756677)
  • Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). (PMID:11809755)
  • Estrogen lowers Alzheimer beta-amyloid generation by stimulating trans-Golgi network vesicle biogenesis (PMID:11823458)
  • a biomarker for Alzheimer disease (PMID:11831556)
  • Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. (PMID:11877420)
  • mitochondrial dysfunction in Down’s syndrome may lead to intracellular deposition of Abeta42, reduced levels of AbetaPPs, and a chronic state of increased neuronal vulnerability. (PMID:11879646)
  • early signaling mechanisms involved in Abeta toxicity using the SH-SY5Y neuroblastoma cell line (amyloid beta protein) (PMID:11882652)
  • Apolipoprotein E4 potentiates amyloid beta peptide-induced lysosomal leakage and apoptosis in neuronal cells (PMID:11912196)
  • Oxidation of methionine 35 attenuates formation of amyloid beta -peptide 1-40 oligomers (PMID:11912198)
  • Accelerated plaque accumulation, associative learning deficits, and up-regulation of alpha 7 nicotinic receptor protein in transgenic mice co-expressing mutant human presenilin 1 and amyloid precursor proteins (PMID:11912199)
  • binds to G(M1)ganglioside and promotes the soluble amyloid beta protein polymerization (PMID:11915325)
  • forms a seed of amyloid beta protein aggregation via binding to G(M1)ganglioside (PMID:11915326)
  • natural oligomers of human Abeta are secreted and cerebral microinjection of cell medium containing these oligomers and abundant Abeta monomers but no amyloid fibrils markedly inhibited hippocampal long-term potentiation in rats (amyloid beta protein). (PMID:11932745)
  • Activation of Cyclin-Dependent-Kinase-1 by Alzheimer’s Amyloid-beta peptide (PMID:11958860)
  • Munc18a acts through direct and indirect interactions with X11 proteins and powerfully regulates APP metabolism and Abeta secretion. (PMID:12016213)
  • A second locus for very-late-onset Alzheimer disease: a genome scan reveals linkage to 20p and epistasis between 20p and the amyloid precursor protein region. (PMID:12016588)
  • results show that the constrained decapeptide dimers rapidly form an intramolecular, antiparallel beta-sheet and polymerize into amyloid fibrils at low concentrations (PMID:12023906)
  • gamma secretase cleavage of APP may contribute to Alzheimer’s disease-related neurodegeneration [GAMMA SECRETASE] (PMID:12032152)
  • Rac1 generates reactive oxygen species through beta-amyloid signaling (PMID:12038964)
  • mutation of leucine 166 in presenilin-1 affects generation independent of effect on Abea 42 production (PMID:12048239)
  • Mechanism of membrane depolarization caused by the Alzheimer Abeta1-42 peptide (PMID:12054502)
  • Eliminating membrane depolarization caused by the Alzheimer peptide Abeta(1-42, aggr.). (PMID:12054503)
  • REVIEW: the folding pathways of an Alzheimer’s amyloid Abeta-Peptide explored by long time dynamic simulations. (PMID:12069633)
  • Mutations that reduce aggregation of the Alzheimer’s Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. (PMID:12079364)
  • [alpha]-Secretase ADAM10 as well as [alpha]APPs is reduced in platelets and CSF of Alzheimer disease patients. (PMID:12080182)
  • Profile of cholesterol-related sterols in aged amyloid precursor protein transgenic mouse brain (PMID:12091492)
  • Transcriptional activation and increase in expression of Alzheimer’s beta-amyloid precursor protein gene is mediated by TGF-beta in normal human astrocytes (PMID:12099697)
  • Transforming growth factor-beta-induced transcription of the Alzheimer beta-amyloid precursor protein gene involves interaction between the CTCF-complex and Smads (PMID:12099698)
  • description of APP binding site for fibrillar Abeta and identification by alanine scanning mutagenesis (PMID:12107175)
  • mutations in PSEN1 increase Abeta42 production (PMID:12119298)
  • mutant proteins form annular protofibrils (similar to pore-forming bacterial toxins), suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases, as Alzheimers and Parkinsons (PMID:12124613)
  • Human APP expressed in rat cortical cell neurons in culture is processed to produce amyloid beta and soluible APP. Expression of APP triggers neuronal cell death. (PMID:12128077)
  • laminin affects polymerization, depolymerization and neurotoxicity of this protein. (PMID:12128080)
  • Several months after intracerebral injections of this protein into betaAPP transgenic mice, cerebral beta-amyloidosis was induced. (PMID:12128081)
  • Annexin 5 and apolipoprotein E-2 protect PC12 rat cells against the cytotoxicity of this protein. (PMID:12128082)

Cross-species orthologs

6 orthologs

OrganismSymbolGene ID
danio_rerioappbENSDARG00000055543
danio_rerioappaENSDARG00000104279
mus_musculusAppENSMUSG00000022892
rattus_norvegicusAppENSRNOG00000006997
drosophila_melanogasterApplFBGN0000108
caenorhabditis_elegansWBGENE00000149

Paralogs (2): APLP2 (ENSG00000084234), APLP1 (ENSG00000105290)

Mouse-model phenotypes

Observed phenotypes of the mouse ortholog (MGI:88059) from MGI (Alliance of Genome Resources) — knockout/mutant phenotypes, ranked by annotation count. 88 distinct phenotype terms.

Mouse phenotype (MP)Records
amyloid beta deposits6
decreased body weight5
decreased grip strength5
abnormal astrocyte morphology4
abnormal locomotor activation4
astrocytosis4
abnormal spatial learning3
abnormal learning/memory/conditioning3
premature death3
decreased brain weight3
increased thigmotaxis3
decreased locomotor activity2
decreased exploration in new environment2
gliosis2
absent corpus callosum2
abnormal neuron morphology2
microgliosis2
abnormal circadian behavior2
increased locomotor activity2
abnormal microglial cell morphology1
increased circulating calcium level1
increased neutrophil cell number1
increased monocyte cell number1
myoclonus1
amyloidosis1

+63 more (showing top 25).

Additional cross-species homologs

Sequence homologs in species beyond Ensembl Compara’s model organisms, by Diamond local protein alignment (% sequence identity; best hit per species). Lower-identity rows are more distant homologs. The matched accessions’ gene symbols aren’t in biobtree yet, so each row shows the UniProt accession.

OrganismUniProtIdentityMethod
Radianthus crispaC0HJU7100.0%Diamond
Heteractis magnificaC0HK72100.0%Diamond
Cyriopagopus hainanusD2Y2G1100.0%Diamond
Cyriopagopus schmidtiP0DJ84100.0%Diamond
Macaca mulattaP29216100.0%Diamond
Macaca fascicularisP53601100.0%Diamond
Sus scrofaP79307100.0%Diamond
Bos taurusQ28053100.0%Diamond
Canis lupus familiarisQ28280100.0%Diamond
Oryctolagus cuniculusQ28748100.0%Diamond
Ovis ariesQ28757100.0%Diamond
Ursus maritimusQ29149100.0%Diamond
Pan troglodytesQ5IS80100.0%Diamond
Cavia porcellusQ60495100.0%Diamond
Saimiri sciureusQ95241100.0%Diamond
Felis catusP8690697.5%Diamond
Stichodactyla helianthusP3171392.7%Diamond
Mesocricetus auratusQ6055986.8%Diamond
Meriones unguiculatusQ6257786.8%Diamond
Equus caballusP0436586.6%Diamond
Dichotomyctere fluviatilisO7368383.9%Diamond
Takifugu rubripesO9327980.4%Diamond
Vespa bicolorC0LNR266.2%Diamond
Pimpla hypochondriacaQ8T0W466.2%Diamond
Gallus gallusP1598965.3%Diamond
Pinctada margaritiferaH2A0N958.8%Diamond
Amblyomma hebraeumQ5VJG257.8%Diamond
Rhipicephalus microplusP8360956.6%Diamond
Austrelaps labialisB2BS8454.7%Diamond
Ixodes scapularisQ964Q053.8%Diamond

Genomic neighbors (locus context)

Genes flanking this one on the chromosome (NCBI/Entrez gene neighborhood). Positional context only — some neighbors share regulatory elements (bidirectional promoters, antisense/overlapping transcripts), but chromosomal adjacency is not itself a functional relationship (see Interactions for that).

SymbolTypeEntrez
GABPAprotein-coding2551
ATP5PFprotein-coding522
APP-DTncRNA118568803
CYYR1-AS1ncRNA100996571
CYYR1protein-coding116159

Protein

Protein identifiers

Amyloid-beta precursor protein — P05067 (reviewed: P05067)

Alternative names: ABPP, APPI, Alzheimer disease amyloid A4 protein homolog, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta (A4) precursor protein, Amyloid-beta A4 protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II

All UniProt accessions (6): A0A0A0MRG2, A0A140VJC8, E9PG40, P05067, H7C0V9, H7C2L2

UniProt curated annotations — full annotation on UniProt →

Function. Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Amyloid-beta peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Amyloid-beta peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in lipid rafts. More effective reductant than amyloid-beta protein 40. May activate mononuclear phagocytes in the brain and elicit inflammatory responses. Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain. The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.

Subunit / interactions. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and, NUMB and DAB1. Binding to DAB1 inhibits its serine phosphorylation. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in hippocampal neurons. Interacts with CPEB1 and AGER. Interacts with ANKS1B. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Homodimerizes; dimerization is enhanced in the presence of Cu(2+) ions and is promoted by heparin binding. Interacts with PLD3. Interacts with VDAC1. Interacts with NSG1; could regulate APP processing. Interacts with SYT7. Interacts (via transmembrane region) with PSEN1; the interaction is direct. Interacts with LRRK2. Interacts (via cytoplasmic domain) with KIF5B. Interacts (via C-terminus) with APBB2/FE65L1 (via C-terminus). Interacts (via intracellular domain) with APBB3. Amyloid-beta associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Interacts with S100A9. Interacts with FPR2. Interacts with GSAP. Interacts with SORL1 (via N-terminal ectodomain); this interaction retains APP in the trans-Golgi network and reduces processing into soluble APP-alpha and amyloid-beta peptides. Interacts with SORL1. Interacts with SORL1. Interacts with SORL1.

Subcellular location. Cell membrane. Membrane. Perikaryon. Cell projection. Growth cone. Clathrin-coated pit. Early endosome. Cytoplasmic vesicle Endoplasmic reticulum. Golgi apparatus. Early endosome Early endosome Secreted Cell surface Cell surface Nucleus. Cytoplasm.

Tissue specificity. Expressed in the brain and in cerebrospinal fluid (at protein level). Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.

Post-translational modifications. Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid-beta proteins, amyloid-beta protein 40 and amyloid-beta protein 42, major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as substrate (in vitro). Amyloid-beta protein 40 and Amyloid-beta protein 42 are cleaved by ACE. Many other minor amyloid-beta peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid (CSF) including the amyloid-beta X-15 peptides, produced from the cleavage by alpha-secretase and all terminating at Gln-686. Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either CASP6, CASP8 or CASP9 results in the production of the neurotoxic C31 peptide and the increased production of amyloid-beta peptides. N-glycosylated. N- and O-glycosylated. O-glycosylation on Ser and Thr residues with core 1 or possibly core 8 glycans. Partial tyrosine glycosylation (Tyr-681) is found on some minor, short amyloid-beta peptides (amyloid-beta 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but not found on amyloid-beta protein 38, amyloid-beta protein 40 nor on amyloid-beta protein 42. Modification on a tyrosine is unusual and is more prevelant in AD patients. Glycans had Neu5AcHex(Neu5Ac)HexNAc-O-Tyr, Neu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr and O-AcNeu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr structures, where O-Ac is O-acetylation of Neu5Ac. Neu5AcNeu5Ac is most likely Neu5Ac 2,8Neu5Ac linked. O-glycosylations in the vicinity of the cleavage sites may influence the proteolytic processing. Appicans are L-APP isoforms with O-linked chondroitin sulfate. Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. In dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes the production and the nuclear translocation of the APP intracellular domain (AICD) which induces DA neuron apoptosis. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin. Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of amyloid-beta-containing peptides. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Amyloid-beta peptides are degraded by IDE. Sulfated on tyrosine residues.

Disease relevance. Alzheimer disease 1 (AD1) [MIM:104300] A form of Alzheimer disease, a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituents of these plaques are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that are produced by the proteolysis of the transmembrane APP protein. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products, such as C31, are also implicated in neuronal death. It can be associated with cerebral amyloid angiopathy. Alzheimer disease can be associated with cerebral amyloid angiopathy. The disease is caused by variants affecting the gene represented in this entry. Cerebral amyloid angiopathy, APP-related (CAA-APP) [MIM:605714] A hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. Some affected individuals manifest progressive aphasic dementia, leukoencephalopathy, and occipital calcifications. The disease is caused by variants affecting the gene represented in this entry.

Domain organisation. The transmembrane helix undergoes a conformation change and unravels partially when bound to PSEN1, facilitating cleavage by PSEN1. The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. The GFLD subdomain binds Cu(2+) ions; this promotes homodimerization. The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The YENPXY site is also involved in clathrin-mediated endocytosis. The C-terminal region can bind zinc ions; this favors dimerization and formation of higher oligomers. The OX-2 motif shows some similarity to a region in the N-terminus of CD200/MOX2.

Induction. Increased levels during neuronal differentiation.

Miscellaneous. Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between amyloid-beta molecules resulting in amyloid-beta-metal aggregates. The affinity for copper is much higher than for other transient metals and is increased under acidic conditions. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding. A major isoform. The L-isoforms are referred to as appicans. A major isoform. The L-isoforms are referred to as appicans. The L-isoforms are referred to as appicans. A major isoform.

Similarity. Belongs to the APP family.

Isoforms (11)

UniProt IDNamesCanonical?
P05067-1APP770, PreA4 770yes
P05067-2APP305
P05067-3L-APP677
P05067-4APP695, PreA4 695
P05067-5L-APP696
P05067-6APP714
P05067-7L-APP733
P05067-8APP751, PreA4 751
P05067-9L-APP752
P05067-10APP639
P05067-1111

RefSeq proteins (11): NP_000475, NP_001129488, NP_001129601, NP_001129602, NP_001129603, NP_001191230, NP_001191231, NP_001191232, NP_001372182, NP_958816, NP_958817 (=MANE)

Domains & families (InterPro)

IDNameType
IPR002223Kunitz_BPTIDomain
IPR008154Amyloid_glyco_extraDomain
IPR008155Amyloid_glycoFamily
IPR011178Amyloid_glyco_Cu-bdDomain
IPR011993PH-like_dom_sfHomologous_superfamily
IPR013803Amyloid_glyco_AbetaDomain
IPR015849Amyloid_glyco_heparin-bdDomain
IPR019543APP_amyloid_CDomain
IPR019744APP_CUBD_CSConserved_site
IPR019745Amyloid_glyco_intracell_CSConserved_site
IPR020901Prtase_inh_Kunz-CSConserved_site
IPR024329Amyloid_glyco_E2_domainDomain
IPR036176E2_sfHomologous_superfamily
IPR036454Amyloid_glyco_heparin-bd_sfHomologous_superfamily
IPR036669Amyloid_Cu-bd_sfHomologous_superfamily
IPR036880Kunitz_BPTI_sfHomologous_superfamily
IPR037071Amyloid_glyco_Abeta_sfHomologous_superfamily

Pfam: PF00014, PF02177, PF03494, PF10515, PF12924, PF12925

UniProt features (232 total): mutagenesis site 41, strand 29, sequence variant 21, helix 18, binding site 15, site 15, chain 13, splice variant 13, modified residue 11, glycosylation site 10, region of interest 9, disulfide bond 9, turn 7, sequence conflict 5, domain 3, short sequence motif 3, compositionally biased region 3, peptide 2, topological domain 2, signal peptide 1, transmembrane region 1, cross-link 1

Structure

Experimental structures (PDB)

showing 30 of 263 structures by resolution:

PDBTitleMethodResolution (Å)
2FMAStructure of the Alzheimer’s Amyloid Precursor Protein (APP) Copper Binding Domain in …X-RAY DIFFRACTION0.85
6NB9Amyloid-Beta (20-34) with L-isoaspartate 23ELECTRON CRYSTALLOGRAPHY1.05
6OIZAmyloid-Beta (20-34) wild typeELECTRON CRYSTALLOGRAPHY1.1
8T82Racemic mixture of amyloid beta segment 35-MVGGVV-40 forms heterochiral rippled …X-RAY DIFFRACTION1.1
5ONQAlzheimer’s Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd-substituted ThermolysinX-RAY DIFFRACTION1.17
3JQLCrystal Structure of the Complex Formed Between Phospholipase A2 and a Hexapeptide …X-RAY DIFFRACTION1.2
3PZZStructure of an amyloid forming peptide GAIIGL (29-34) from amyloid betaX-RAY DIFFRACTION1.29
4PQDThe longer crystal structure of the grow factor like domain from Beta amypoid precusor …X-RAY DIFFRACTION1.33
5ONPAlzheimer’s Amyloid-Beta Peptide Fragment 1-40 in Complex with Cd-substituted ThermolysinX-RAY DIFFRACTION1.34
5ONRAlzheimer’s Amyloid-Beta Peptide Fragment 1-40 in Complex with ThermolysinX-RAY DIFFRACTION1.39
4PWQHIGH-RESOLUTION CRYSTAL STRUCTURE OF THE E1-DOMAIN of THE AMYLOID PRECURSOR PROTEINX-RAY DIFFRACTION1.4
7OW1Crystal Structure of TAP01 in complex with amyloid beta peptideX-RAY DIFFRACTION1.4
6O4JAmyloid Beta KLVFFAENVGS 16-26 D23N Iowa mutationELECTRON CRYSTALLOGRAPHY1.4
5VOSVGSNKGAIIGL from Amyloid Beta determined by MicroEDELECTRON CRYSTALLOGRAPHY1.42
3Q2XStructure of an amyloid forming peptide NKGAII (residues 27-32) from amyloid betaX-RAY DIFFRACTION1.45
5TXDStructure of amyloid-beta derived peptide - NKGAIFX-RAY DIFFRACTION1.45
5MYXStructure of Pyroglutamate-Abeta-specific Fab c#24 in complex with human Abeta-pE3-18X-RAY DIFFRACTION1.49
1AAPX-RAY CRYSTAL STRUCTURE OF THE PROTEASE INHIBITOR DOMAIN OF ALZHEIMER’S AMYLOID …X-RAY DIFFRACTION1.5
3IFLX-ray structure of amyloid beta peptide:antibody (Abeta1-7:12A11) complexX-RAY DIFFRACTION1.5
3IFNX-ray structure of amyloid beta peptide:antibody (Abeta1-40:12A11) complexX-RAY DIFFRACTION1.5
4MVKCrystal structure of an engineered lipocalin (Anticalin US7) in complex with the …X-RAY DIFFRACTION1.5
8T89Racemic mixture of amyloid beta segment 16-KLVFFA-21 forms heterochiral rippled beta-sheetX-RAY DIFFRACTION1.5
5AMBCrystal structure of the Angiotensin-1 converting enzyme N-domain in complex with …X-RAY DIFFRACTION1.55
3BKJCrystal structure of Fab wo2 bound to the n terminal domain of amyloid beta peptide (1-16)X-RAY DIFFRACTION1.59
5MYOStructure of Pyroglutamate-Abeta-specific Fab c#6 in complex with human Abeta-pE3-12-PEGbX-RAY DIFFRACTION1.59
3BAECrystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)X-RAY DIFFRACTION1.59
2FK1Structure of the Alzheimer’s Amyloid Precursor Protein (APP) Copper Binding Domain in …X-RAY DIFFRACTION1.6
3L81Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain, in …X-RAY DIFFRACTION1.6
2FJZStructure of the Alzheimer’s Amyloid Precursor Protein (APP) copper binding domain …X-RAY DIFFRACTION1.61
2FK2Structure of the Alzheimer’s Amyloid Precursor Protein (APP) Copper Binding Domain in …X-RAY DIFFRACTION1.65

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-P05067-F168.110.30

Antibody-complex structures (SAbDab)

33 antibodies co-crystallized with this protein: 2IPU, 2R0W, 3BAE, 3BKJ, 3IFL, 3IFN, 3IFO, 3IFP, 3MOQ, 3U0T, 4HIX, 4M1C, 4OJF, 4ONF, 4ONG, 4XXD, 5CSZ, 5MY4, 5MYO, 5MYX, 5VZY, 5W3P, 6CO3, 7E6P, 7OW1 (+8 more)

Human Protein Atlas

Protein class: Transporters, Transporter channels and pores, Predicted membrane proteins, Predicted secreted proteins, Predicted intracellular proteins, Plasma proteins, Disease related genes, FDA approved drug targets, Small molecule drugs, Human disease related genes

Protein evidence: Evidence at protein level

Subcellular location (HPA, imaging): golgi apparatus; vesicles

Antibody reliability (HPA): IH enhanced · IF supported

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (15)

PositionRole
170required for cu(2+) reduction
197–198cleavage; by caspases
219–220cleavage; by caspases
301–302reactive bond
671–672cleavage; by beta-secretase
672–673cleavage; by caspase-6; when associated with variant 670-n-l-671
678–679cleavage; by ace
687–688cleavage; by alpha-secretase
690–691cleavage; by theta-secretase
704implicated in free radical propagation
706susceptible to oxidation
711–712cleavage; by gamma-secretase; site 1
713–714cleavage; by gamma-secretase; site 2
720–721cleavage; by gamma-secretase; site 3
739–740cleavage; by caspase-6, caspase-8 or caspase-9

Ligand- & substrate-binding residues (15)

PositionRole
96–110heparin
147Cu(2+)
151Cu(2+)
168Cu(2+)
183Zn(2+)
186Zn(2+)
187Zn(2+)
677Cu(2+)
677Zn(2+)
681Cu(2+)
681Zn(2+)
684Cu(2+)
684Zn(2+)
685Cu(2+)
685Zn(2+)

Post-translational modifications (12)

TypePositions
Phosphoserine198, 206, 441, 730
Sulfotyrosine217, 262, 336
Phosphotyrosine497, 757
Phosphothreonine729, 743
Glycyl lysine isopeptide (lys-gly) (interchain with g-cter in ubiquitin)763

Disulfide bonds (9)

TypePositions
Disulfide bond38–62, 73–117, 98–105, 133–187, 144–174, 158–186, 291–341, 300–324, 316–337

Glycosylation sites (10)

TypePositions
N-linked (glcnac…) asparagine542, 571
O-linked (galnac…) threonine633, 651, 652, 663
O-linked (xyl…) (chondroitin sulfate) serine656
O-linked (hexnac…) threonine659
O-linked (galnac…) serine667
O-linked (hexnac…) tyrosine681

Mutagenesis-validated functional residues (41)

PositionPhenotype
99–102reduced heparin-binding.
108loss of the copper binding site in the gfld subdomain; when associated with a-110.
110loss of the copper binding site in the gfld subdomain; when associated with a-108.
137binds copper. forms dimer.
141binds copper. forms dimer.
144binds copper. no dimer formation. no copper reducing activity.
147–14950% decrease in copper reducing activity.
147loss of a copper binding site; when associated with a-151.
147some decrease in copper reducing activity.
147binds copper. forms dimer.
147greatly reduced copper-mediated low-density lipoprotein oxidation.
151loss of a copper binding site; when associated with a-147.
151greatly reduced copper-mediated low-density lipoprotein oxidation.
151binds copper. forms dimer.
198greatly reduced casein kinase phosphorylation.
206reduced casein kinase phosphorylation.
499reduced affinity for heparin; when associated with a-503.
503reduced affinity for heparin; when associated with a-499.
656abolishes chondroitin sulfate binding in l-app733 isoform.
67660-70% zinc-induced amyloid-beta protein 28 aggregation.
68160-70% zinc-induced amyloid-beta protein 28 aggregation.
684only 23% zinc-induced amyloid-beta protein 28 aggregation.
695causes formation of an artifactual disulfide bond with psen1.
704reduced protein oxidation. no hippocampal neuron toxicity.
706reduced lipid peroxidation inhibition.

Function

Pathways and Gene Ontology

Reactome pathways

18 curated (TAS) of 69; 12 disease pathways. Curated-first; evidence = TAS (manually curated) vs IEA (electronic inference).

showing 60 of 69 pathways:

IDPathwayEvidence
R-HSA-9936900Aggregated β-amyloid induces FXII autocatalysis ⚕curated
R-HSA-9936686Aggregated β-amyloid interacts with fibrinogen ⚕curated
R-HSA-8862803Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer’s disease models ⚕curated
R-HSA-9660826Purinergic signaling in leishmaniasis infection ⚕curated
R-HSA-977225Amyloid fiber formationcurated
R-HSA-3000178ECM proteoglycanscurated
R-HSA-444473Formyl peptide receptors bind formyl peptides and many other ligandscurated
R-HSA-418594G alpha (i) signalling eventscurated
R-HSA-416476G alpha (q) signalling eventscurated
R-HSA-432720Lysosome Vesicle Biogenesiscurated
R-HSA-9837999Mitochondrial protein degradationcurated
R-HSA-114608Platelet degranulationcurated
R-HSA-8957275Post-translational protein phosphorylationcurated
R-HSA-381426Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)curated
R-HSA-9769739Regulation of clotting cascadecurated
R-HSA-445989TAK1-dependent IKK and NF-kappa-B activationcurated
R-HSA-933542TRAF6 mediated NF-kB activationcurated
R-HSA-844456The NLRP3 inflammasomecurated
R-HSA-9664424Cell recruitment (pro-inflammatory response) ⚕—
R-HSA-9734009Defective Intrinsic Pathway for Apoptosis ⚕—
R-HSA-1643685Disease ⚕—
R-HSA-9645723Diseases of programmed cell death ⚕—
R-HSA-5663205Infectious disease ⚕—
R-HSA-9658195Leishmania infection ⚕—
R-HSA-8863678Neurodegenerative Diseases ⚕—
R-HSA-9824443Parasitic Infection Pathways ⚕—
R-HSA-879415Advanced glycosylation endproduct receptor signalingelectronic
R-HSA-373076Class A/1 (Rhodopsin-like receptors)—
R-HSA-1280215Cytokine Signaling in Immune system—
R-HSA-168928DDX58/IFIH1-mediated induction of interferon-alpha/beta—
R-HSA-1474244Extracellular matrix organization—
R-HSA-388396GPCR downstream signalling—
R-HSA-500792GPCR ligand binding—
R-HSA-109582Hemostasis—
R-HSA-168256Immune System—
R-HSA-622312Inflammasomes—
R-HSA-168249Innate Immune System—
R-HSA-9609523Insertion of tail-anchored proteins into the endoplasmic reticulum membraneelectronic
R-HSA-446652Interleukin-1 family signaling—
R-HSA-9020702Interleukin-1 signaling—
R-HSA-199991Membrane Trafficking—
R-HSA-392499Metabolism of proteins—
R-HSA-975871MyD88 cascade initiated on plasma membrane—
R-HSA-975155MyD88 dependent cascade initiated on endosome—
R-HSA-166166MyD88-independent TLR4 cascade—
R-HSA-166058MyD88:MAL(TIRAP) cascade initiated on plasma membrane—
R-HSA-168643Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signaling pathways—
R-HSA-375276Peptide ligand-binding receptors—
R-HSA-76002Platelet activation, signaling and aggregation—
R-HSA-597592Post-translational protein modification—
R-HSA-9609507Protein localization—
R-HSA-76005Response to elevated platelet cytosolic Ca2+—
R-HSA-162582Signal Transduction—
R-HSA-372790Signaling by GPCR—
R-HSA-449147Signaling by Interleukins—
R-HSA-975138TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation—
R-HSA-937061TRIF (TICAM1)-mediated TLR4 signaling—
R-HSA-168142Toll Like Receptor 10 (TLR10) Cascade—
R-HSA-181438Toll Like Receptor 2 (TLR2) Cascade—
R-HSA-168164Toll Like Receptor 3 (TLR3) Cascade—

MSigDB gene sets: 1131 (showing top): GOBP_MYELOID_CELL_DIFFERENTIATION, VALK_AML_WITH_FLT3_ITD, REACTOME_DDX58_IFIH1_MEDIATED_INDUCTION_OF_INTERFERON_ALPHA_BETA, GOBP_CELLULAR_RESPONSE_TO_LIPOPROTEIN_PARTICLE_STIMULUS, GOBP_DENDRITE_DEVELOPMENT, GOBP_G_PROTEIN_COUPLED_RECEPTOR_INTERNALIZATION, GOBP_MEMORY, GOBP_REGULATION_OF_CELL_ACTIVATION, RNGTGGGC_UNKNOWN, VERHAAK_AML_WITH_NPM1_MUTATED_DN, FXR_IR1_Q6, RRAGTTGT_UNKNOWN, GOBP_RESPONSE_TO_NITROGEN_COMPOUND, GOBP_RESPONSE_TO_ETHANOL, GOBP_NEURON_RECOGNITION

GO Biological Process (76): microglial cell activation (GO:0001774), astrocyte activation involved in immune response (GO:0002265), regulation of translation (GO:0006417), calcium ion transport (GO:0006816), intracellular copper ion homeostasis (GO:0006878), endocytosis (GO:0006897), cell adhesion (GO:0007155), Notch signaling pathway (GO:0007219), axonogenesis (GO:0007409), central nervous system development (GO:0007417), learning or memory (GO:0007611), learning (GO:0007612), mating behavior (GO:0007617), locomotory behavior (GO:0007626), axo-dendritic transport (GO:0008088), negative regulation of cell population proliferation (GO:0008285), adult locomotory behavior (GO:0008344), visual learning (GO:0008542), response to lead ion (GO:0010288), regulation of gene expression (GO:0010468), positive regulation of gene expression (GO:0010628), negative regulation of gene expression (GO:0010629), microglia development (GO:0014005), axon midline choice point recognition (GO:0016199), neuron remodeling (GO:0016322), dendrite development (GO:0016358), regulation of Wnt signaling pathway (GO:0030111), extracellular matrix organization (GO:0030198), neuron projection development (GO:0031175), positive regulation of synaptic transmission, cholinergic (GO:0032224), positive regulation of chemokine production (GO:0032722), positive regulation of interleukin-1 beta production (GO:0032731), positive regulation of interleukin-6 production (GO:0032755), positive regulation of tumor necrosis factor production (GO:0032760), ionotropic glutamate receptor signaling pathway (GO:0035235), swimming behavior (GO:0036269), regulation of multicellular organism growth (GO:0040014), regulation of neuron apoptotic process (GO:0043523), response to ethanol (GO:0045471), positive regulation of glycolytic process (GO:0045821), positive regulation of mitotic cell cycle (GO:0045931), positive regulation of transcription by RNA polymerase II (GO:0045944), positive regulation of JNK cascade (GO:0046330), astrocyte activation (GO:0048143), regulation of long-term neuronal synaptic plasticity (GO:0048169), collateral sprouting in absence of injury (GO:0048669), positive regulation of inflammatory response (GO:0050729), regulation of synapse structure or activity (GO:0050803), synapse organization (GO:0050808), positive regulation of calcium-mediated signaling (GO:0050850), cognition (GO:0050890), positive regulation of protein metabolic process (GO:0051247), positive regulation of ERK1 and ERK2 cascade (GO:0070374), response to interleukin-1 (GO:0070555), cellular response to copper ion (GO:0071280), cellular response to manganese ion (GO:0071287), cellular response to cAMP (GO:0071320), cellular response to norepinephrine stimulus (GO:0071874), modulation of excitatory postsynaptic potential (GO:0098815), NMDA selective glutamate receptor signaling pathway (GO:0098989)

+16 more (showing top 60).

GO Molecular Function (17): DNA binding (GO:0003677), serine-type endopeptidase inhibitor activity (GO:0004867), signaling receptor binding (GO:0005102), heparin binding (GO:0008201), peptidase activator activity (GO:0016504), enzyme binding (GO:0019899), signaling receptor activator activity (GO:0030546), identical protein binding (GO:0042802), transition metal ion binding (GO:0046914), receptor ligand activity (GO:0048018), PTB domain binding (GO:0051425), growth factor receptor binding (GO:0070851), protein serine/threonine kinase binding (GO:0120283), protein binding (GO:0005515), peptidase inhibitor activity (GO:0030414), metal ion binding (GO:0046872), molecular function activator activity (GO:0140677)

GO Cellular Component (43): extracellular region (GO:0005576), nuclear envelope lumen (GO:0005641), cytoplasm (GO:0005737), mitochondrial inner membrane (GO:0005743), endosome (GO:0005768), early endosome (GO:0005769), endoplasmic reticulum (GO:0005783), endoplasmic reticulum lumen (GO:0005788), Golgi apparatus (GO:0005794), Golgi lumen (GO:0005796), Golgi-associated vesicle (GO:0005798), cytosol (GO:0005829), plasma membrane (GO:0005886), clathrin-coated pit (GO:0005905), cell surface (GO:0009986), membrane (GO:0016020), axon (GO:0030424), dendrite (GO:0030425), platelet alpha granule lumen (GO:0031093), early endosome membrane (GO:0031901), endosome lumen (GO:0031904), trans-Golgi network membrane (GO:0032588), synaptic cleft (GO:0043083), dendritic spine (GO:0043197), dendritic shaft (GO:0043198), perikaryon (GO:0043204), signaling receptor complex (GO:0043235), main axon (GO:0044304), membrane raft (GO:0045121), synapse (GO:0045202), perinuclear region of cytoplasm (GO:0048471), recycling endosome (GO:0055037), extracellular exosome (GO:0070062), astrocyte projection (GO:0097449), neuronal dense core vesicle (GO:0098992), amyloid-beta complex (GO:0106003), growth cone lamellipodium (GO:1990761), growth cone filopodium (GO:1990812), nucleus (GO:0005634), growth cone (GO:0030426), platelet alpha granule (GO:0031091), cytoplasmic vesicle (GO:0031410), neuron projection (GO:0043005)

Reactome top-level categories

22 top-level categories:

CategoryPathways
Metabolism of proteins3
GPCR downstream signalling2
Response to elevated platelet cytosolic Ca2+1
Extracellular matrix organization1
trans-Golgi Network Vesicle Budding1
Peptide ligand-binding receptors1
MyD88:MAL(TIRAP) cascade initiated on plasma membrane1
Toll Like Receptor 3 (TLR3) Cascade1
Interleukin-1 signaling1
TRIF (TICAM1)-mediated TLR4 signaling1
TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation1
MyD88 cascade initiated on plasma membrane1
Inflammasomes1
Innate Immune System1
Neurodegenerative Diseases1
Post-translational protein modification1
DDX58/IFIH1-mediated induction of interferon-alpha/beta1
Protein localization1
Cell recruitment (pro-inflammatory response)1
Coagulation pathway1
Defects of Coagulation cascade1
Defects of contact activation system and kallikrein-kinin system1

GO top-level categories

showing 60 of 82 GO namespaces:

CategoryTerms
cellular anatomical structure5
endomembrane system4
neuron projection3
protein binding3
cytoplasm3
behavior2
peptidase activity2
peptidase regulator activity2
signaling receptor binding2
cytoplasmic vesicle2
intracellular membrane-bounded organelle2
intracellular organelle lumen2
membrane2
leukocyte activation involved in inflammatory response1
macrophage activation1
glial cell activation1
cell activation involved in immune response1
immune response1
astrocyte activation1
translation1
post-transcriptional regulation of gene expression1
regulation of protein metabolic process1
metal ion transport1
intracellular monoatomic cation homeostasis1
copper ion homeostasis1
vesicle budding from membrane1
membrane invagination1
import into cell1
cellular process1
cell surface receptor signaling pathway1
cell morphogenesis involved in neuron differentiation1
neuron projection morphogenesis1
axon development1
nervous system development1
system development1
animal gross anatomical part developmental process1
cognition1
learning or memory1
reproductive behavior1
transport along microtubule1
cell population proliferation1
regulation of cell population proliferation1
negative regulation of cellular process1
locomotory behavior1
adult behavior1
visual behavior1
associative learning1
response to metal ion1
gene expression1
regulation of macromolecule biosynthetic process1
nucleic acid binding1
serine-type endopeptidase activity1
endopeptidase inhibitor activity1
glycosaminoglycan binding1
sulfur compound binding1
enzyme activator activity1
signaling receptor regulator activity1
signaling receptor activity1
molecular function activator activity1
metal ion binding1

Experimentally-supported GO annotations

GO terms backed by direct experimental evidence (ECO experimental codes) — 60 of 137 annotations. The rest are phylogenetic / computational / electronic (IEA).

60 experimentally-supported GO terms:

GO termNSEvidence
amyloid fibril formationBPmutant phenotype
astrocyte activationBPgenetic interaction
astrocyte activation involved in immune responseBPgenetic interaction
cellular response to amyloid-betaBPdirect assay
learningBPmutant phenotype
learning or memoryBPmutant phenotype
microglia developmentBPgenetic interaction
microglial cell activationBPgenetic interaction
modulation of excitatory postsynaptic potentialBPgenetic interaction
negative regulation of cell population proliferationBPdirect assay
negative regulation of gene expressionBPgenetic interaction
negative regulation of long-term synaptic potentiationBPgenetic interaction
neuron projection maintenanceBPgenetic interaction
positive regulation of ERK1 and ERK2 cascadeBPgenetic interaction
positive regulation of JNK cascadeBPgenetic interaction
positive regulation of T cell migrationBPmutant phenotype
positive regulation of amyloid fibril formationBPmutant phenotype
positive regulation of calcium-mediated signalingBPgenetic interaction
positive regulation of chemokine productionBPgenetic interaction
positive regulation of gene expressionBPmutant phenotype
positive regulation of glycolytic processBPgenetic interaction
positive regulation of inflammatory responseBPmutant phenotype
positive regulation of interleukin-1 beta productionBPgenetic interaction
positive regulation of interleukin-6 productionBPgenetic interaction
positive regulation of long-term synaptic potentiationBPgenetic interaction
positive regulation of non-canonical NF-kappaB signal transductionBPmutant phenotype
positive regulation of protein metabolic processBPmutant phenotype
positive regulation of synaptic transmission, cholinergicBPdirect assay
positive regulation of transcription by RNA polymerase IIBPgenetic interaction
positive regulation of tumor necrosis factor productionBPgenetic interaction
regulation of gene expressionBPmutant phenotype
regulation of long-term neuronal synaptic plasticityBPgenetic interaction
regulation of presynapse assemblyBPdirect assay
regulation of spontaneous synaptic transmissionBPgenetic interaction
synapse organizationBPgenetic interaction
Golgi apparatusCCdirect assay
amyloid-beta complexCCdirect assay
cell surfaceCCdirect assay
cytoplasmCCdirect assay
dendriteCCdirect assay
dendritic shaftCCdirect assay
dendritic spineCCdirect assay
early endosomeCCdirect assay
early endosome membraneCCdirect assay
endoplasmic reticulumCCdirect assay
endosomeCCdirect assay
extracellular exosomeCChigh-throughput assay
membrane raftCCdirect assay
nuclear envelope lumenCCdirect assay
perinuclear region of cytoplasmCCdirect assay
plasma membraneCCdirect assay
signaling receptor complexCCdirect assay
synapseCCdirect assay
PTB domain bindingMFphysical interaction
enzyme bindingMFphysical interaction
identical protein bindingMFphysical interaction
protein serine/threonine kinase bindingMFphysical interaction
receptor ligand activityMFdirect assay
serine-type endopeptidase inhibitor activityMFdirect assay
signaling receptor bindingMFphysical interaction

Protein interactions and networks

STRING

showing 15 of 6,488 interactions by confidence (×1000):

Protein AProtein BPartner UniProtScore
APPPSEN1P49768982
APPBACE1P56817975
APPAPOEP02649956
APPPSEN2P49810949
APPMAPTP10636947
APPSNCAP37840919
APPNCSTNQ92542899
APPAPBB1O00213898
APPPSENENQ9NZ42887
APPAPH1AQ96BI3882
APPADAM10O14672869
APPPRNPP04156866
APPIDEP14735862
APPMMEL1Q495T6861
APPMMEP08473830

IntAct

Human interaction partners of APP in IntAct, one row per partner (best MIscore; records = supporting IntAct interaction records, in a sample of 1,094 of 1,656 records).

showing 30 of 338 partners by confidence:

PartnerInteraction typeMIscoreRecords
APBB1physical association0.91011
BACE1protein cleavage0.8708
APBB3physical association0.8504
APBB2association0.8305
MAPK8IP1physical association0.7804
PRNPphysical association0.7706
ITM2Bphysical association0.7705
HSD17B10physical association0.7509
MAPTphosphorylation reaction0.7509
APOA1physical association0.7508
CALRassociation0.7405
APBA3physical association0.7403
APBA1physical association0.7303
TGFB2proximity0.7006
PDIA3physical association0.7005
UCHL1physical association0.7004
SORL1physical association0.6905
APBA2direct interaction0.6902
SHC3physical association0.6805
PSEN2physical association0.6804
JUNphysical association0.6803
ACTBphysical association0.6706
HSPA8physical association0.6706
STXBP1physical association0.6706
CRYABassociation0.6705
HSP90AA1physical association0.6703
HSPA5physical association0.6703
PGAM1physical association0.6703
PPIAphysical association0.6703
TUBBphysical association0.6703

BioGRID (2,974 interactions; top human partners by supporting records in a sample of 600 records): CLU (FRET; 6 records), LRPPRC (Co-fractionation; 5 records), APBA1 (Affinity Capture-Western; 4 records), APBA2 (Affinity Capture-Western; 4 records), APBB1 (Affinity Capture-Western; 4 records), FBLN1 (Affinity Capture-Western; 4 records), GRIN1 (Affinity Capture-Western; 4 records), GSAP (Affinity Capture-Western; 4 records), NGFR (Affinity Capture-Western; 4 records), TMEM30A (Affinity Capture-MS; 4 records), APBA3 (Affinity Capture-MS; 3 records), APBB2 (Affinity Capture-MS; 3 records), FLRT3 (Two-hybrid; 3 records), GRIN2A (Affinity Capture-Western; 3 records), GRIN2B (Affinity Capture-Western; 3 records)

SIGNOR signaling

showing 32 of 56 signaling interactions:

AEffectBMechanism
MAPK8up-regulatesAPPphosphorylation
APPup-regulatesGSK3A
Avagacestatdown-regulatesAPP“chemical inhibition”
DAPTdown-regulatesAPP“chemical inhibition”
471905-41-6down-regulatesAPP“chemical inhibition”
PAFAH1B2up-regulatesAPP
MAPK10up-regulatesAPPphosphorylation
(2S)-2-hydroxy-3-methyl-N-[(2S)-1-[[(5S)-3-methyl-4-oxo-2,5-dihydro-1H-3-benzazepin-5-yl]amino]-1-oxopropan-2-yl]butanamidedown-regulatesAPP“chemical inhibition”
gamma-secretase“up-regulates activity”APPcleavage
APP“up-regulates activity”NAE1binding
APPup-regulatesAmyloid_fibril_formation
CTCF“up-regulates quantity by expression”APP“transcriptional regulation”
PITRM1“down-regulates activity”APPcleavage
CDK5RAP2“up-regulates quantity by stabilization”APPphosphorylation
PLD3“up-regulates quantity”APPbinding
BACE1“up-regulates activity”APPcleavage
BACE2“up-regulates activity”APPcleavage
ABCA7“down-regulates quantity”APPrelocalization
FYN“up-regulates quantity”APPphosphorylation
SYVN1“down-regulates quantity by destabilization”APPubiquitination
PRKN“down-regulates quantity”APPubiquitination
PLK2“up-regulates activity”APPphosphorylation
DAPK1“up-regulates quantity”APPphosphorylation
ROCK2“up-regulates quantity”APPphosphorylation
CDK2“down-regulates quantity by destabilization”APPphosphorylation
CDK4“down-regulates quantity by destabilization”APPphosphorylation
CDK5unknownAPPphosphorylation
GSK3BunknownAPPphosphorylation
CTSD“down-regulates quantity by destabilization”APPcleavage
CTSD“up-regulates activity”APPcleavage
CASP6“up-regulates activity”APPcleavage
ADAM17“up-regulates activity”APPcleavage

Protein complexes (CORUM) (22)

Experimentally-characterized complexes this protein is a subunit of (★ = the complex contains a known drug target).

22 complexes by size:

ComplexSubunitsMembers
★ APP(AICD)-FE65-TIP60-MED12-MED4 complex (incomplete Mediator complex)5MED4, APBB1, APP, KAT5, MED12
★ APP(AICD)-MED12-MED23-MED4 complex (incomplete Mediator complex)4APP, MED12, MED23, MED4
★ APP-Abeta42-VDAC1 complex3APP, VDAC1
★ APBB1-APP-KAT5 complex3APBB1, APP, KAT5
★ APP-TIMM23-TOMM40 supercomplex, mitochondrial3APP, TIMM23, TOMM40
★ Abeta(monomer)-APOE complex2APOE, APP
★ Abeta(dimer)-APOE complex2APOE, APP
★ Abeta(trimer)-APOE complex2APP, APOE
★ APP-TOMM40 complex, mitochondrial2APP, TOMM40
★ APP-TIMM23 complex, mitochondrial2APP, TIMM23
★ APP-TNFRSF21 complex2APP, TNFRSF21
★ APP-PSEN1 complex2APP, PSEN1
★ APP-PSEN2 complex2APP, PSEN2
★ APP(AICD)-FOXO3 complex2APP, FOXO3
★ APP(AICD)-FOXO1 complex2FOXO1, APP
★ APP(AICD)-FOXO4 complex2APP, FOXO4
★ Abeta-BCHE complex2APP, BCHE
★ Abeta-ACHE complex2ACHE, APP
★ APBB1-APP(AICD) complex2APBB1, APP
★ APBB2-APP complex2APBB2, APP
★ APP(CTF-C99)-NCSTN complex2APP, NCSTN
★ APP(CTF-C83)-NCSTN complex2NCSTN, APP

Ligand–receptor pairs (CellPhoneDB) (6)

Curated ligand–receptor partners (cell-cell communication), distinct from the protein–protein interactions above.

6 ligand–receptor pairs:

PartnerThis gene’s roleSignaling class
TREM2;TYROBPligandSignaling by Amyloid-beta precursor protein
SORL1ligandSignaling by Amyloid-beta precursor protein
CD74ligandSignaling by Amyloid-beta precursor protein
TNFRSF21ligandSignaling by Amyloid-beta precursor protein
PLXNA4ligandSignaling by Amyloid-beta precursor protein
FPR2ligandSignaling by Amyloid-beta precursor protein

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 338 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

PathwayPartnersFoldFDR
NRIF signals cell death from the nucleus922.5×8e-09
Role of LAT2/NTAL/LAB on calcium mobilization714.7×1e-05
DARPP-32 events813.3×5e-06
CD209 (DC-SIGN) signaling712.7×3e-05
Signalling to ERKs612.6×1e-04
Rap1 signalling512.5×5e-04
Advanced glycosylation endproduct receptor signaling512.5×5e-04
Signalling to RAS511.7×6e-04

GO biological processes:

GO termPartnersFoldFDR
astrocyte activation618.0×6e-05
cellular response to amyloid-beta1416.6×7e-11
amyloid fibril formation916.4×4e-07
positive regulation of superoxide anion generation616.1×1e-04
membrane protein ectodomain proteolysis815.7×4e-06
protein refolding815.1×5e-06
response to amyloid-beta515.0×7e-04
response to lead ion514.2×9e-04

Disease & clinical

Genetic variants

Variant evidence for APP: 652 ClinVar records (32 pathogenic / likely pathogenic); 7 GWAS associations. Per-variant detail is on Sugi Variant.

ClinVar

652 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic23
Likely pathogenic9
Uncertain significance281
Likely benign194
Benign69

Top pathogenic / likely-pathogenic (15)

Showing the 15 best-reviewed of 32 pathogenic / likely-pathogenic ClinVar records, ranked by ClinVar review status (expert panel → multiple submitters → single submitter), then by number of submitting labs.

Variant IDHGVSClassificationReviewSubmitters
18088NM_000484.4(APP):c.2149G>A (p.Val717Ile)Pathogeniccriteria provided, multiple submitters, no conflicts12
18093NM_000484.4(APP):c.2010_2011inv (p.Lys670_Met671delinsAsnLeu)Pathogeniccriteria provided, multiple submitters, no conflicts6
18101NM_000484.4(APP):c.2080G>A (p.Asp694Asn)Pathogeniccriteria provided, multiple submitters, no conflicts5
18089NM_000484.4(APP):c.2149G>T (p.Val717Phe)Pathogeniccriteria provided, multiple submitters, no conflicts4
18102NM_000484.4(APP):c.2140A>G (p.Thr714Ala)Pathogeniccriteria provided, multiple submitters, no conflicts4
18087NM_000484.4(APP):c.2077G>C (p.Glu693Gln)Pathogeniccriteria provided, multiple submitters, no conflicts3
1457308NM_000484.4(APP):c.2145_2146delinsTG (p.Ile716Val)Pathogeniccriteria provided, multiple submitters, no conflicts2
2498894NM_000484.4(APP):c.2146A>T (p.Ile716Phe)Pathogeniccriteria provided, multiple submitters, no conflicts2
18094NM_000484.4(APP):c.2137G>A (p.Ala713Thr)Likely pathogeniccriteria provided, multiple submitters, no conflicts9
18090NM_000484.4(APP):c.2150T>G (p.Val717Gly)Pathogeniccriteria provided, single submitter3
18096NM_000484.4(APP):c.2146A>G (p.Ile716Val)Pathogeniccriteria provided, single submitter3
18099NM_000484.4(APP):c.2077G>A (p.Glu693Lys)Pathogeniccriteria provided, single submitter3
18100NM_000484.4(APP):c.2141C>T (p.Thr714Ile)Pathogeniccriteria provided, single submitter3
18105NM_000484.4(APP):c.2149G>C (p.Val717Leu)Pathogeniccriteria provided, single submitter3
98240NM_000484.4(APP):c.2147T>C (p.Ile716Thr)Pathogeniccriteria provided, single submitter2

Per-variant reference — Sugi Variant

Explore APP’s pathogenic and likely-pathogenic variants individually — each with its ClinVar classification and conditions, applied ACMG criteria (ClinGen expert panel, where curated), the calibrated in-silico predictors (AlphaMissense, REVEL, SaProt, conservation), gnomAD frequency, and the predictor-disagreement QC signal — on Sugi Variant.

SpliceAI

Top 10 splice-impact sites by Δscore (adjacent positions with the same effect merged into one range; 40 predictions of 2,081):

Position(s)EffectΔscoreSites
21:25881772–25881773acceptor_loss1.00004
21:25891720–25891721donor_loss1.00005
21:25891869–25891870acceptor_gain1.00002
21:25891869–25891870acceptor_loss1.00004
21:25897571–25897572donor_loss1.00004
21:25911739–25911740donor_loss1.00005
21:25954588–25954589donor_loss1.00005
21:25954690–25954691acceptor_loss1.00004
21:25955625–25955626donor_loss1.00005
21:25955757acceptor_loss1.00002

AlphaMissense

2,171 missense substitutions predicted likely pathogenic (of 5,117 scored), across 476 residues. Top 20 hotspot residues, ranked by the number of likely-pathogenic substitutions (of those reachable by a single-nucleotide change), then by mean score:

ResidueLikely-pathogenic substitutionsMean am_pathogenicityMax am_pathogenicity
M75290.9801.000
M40690.9510.997
M17090.9100.996
M41090.9070.990
H45780.9991.000
H51480.9991.000
H50780.9980.999
N75980.9981.000
N32980.9971.000
H38880.9970.999
H51180.9971.000
D50480.9950.999
F33180.9931.000
H53380.9920.997
F39180.9871.000
F13580.9811.000
F76580.9810.998
F31980.9790.998
D51980.9770.999
S12480.9720.999

HPA cancer prognostics

RNA cancer specificity: Low cancer specificity

Human Protein Atlas survival analysis — favorable = higher expression predicts better survival.

2 prognostic cancer types:

CancerPrognosticp-value
Kidney Renal Clear Cell Carcinoma (TCGA)favorable8.44e-09
Kidney Renal Clear Cell Carcinoma (validation)favorable1.85e-05

Disease associations

OMIM: gene MIM:104760 | disease phenotypes: MIM:104300, MIM:605714

GenCC curated gene-disease

9 curated gene-disease records:

DiseaseClassificationInheritanceRecords
Alzheimer disease type 1StrongAutosomal dominant2
cerebral amyloid angiopathy, APP-relatedStrongAutosomal dominant2
ABeta amyloidosis, dutch typeSupportiveAutosomal dominant
early-onset autosomal dominant Alzheimer diseaseSupportiveAutosomal dominant
ABetaL34V amyloidosisSupportiveAutosomal dominant
ABeta amyloidosis, Iowa typeSupportiveAutosomal dominant
ABeta amyloidosis, Italian typeSupportiveAutosomal dominant
ABetaA21G amyloidosisSupportiveAutosomal dominant
ABeta amyloidosis, Arctic typeSupportiveAutosomal dominant

ClinGen Gene-Disease Validity

Expert-panel classifications — Definitive > Strong > Moderate > Limited > Disputed > Refuted.

1 validity classifications:

DiseaseClassificationInheritance
cerebral amyloid angiopathy, APP-relatedDefinitiveAD

Genomics England panels (PanelApp)

Clinical diagnostic gene panels including this gene (5 panels, 5 green/diagnostic-grade). Confidence: green = diagnostic, amber = moderate.

5 panels:

PanelRating
Adult-onset neurological disordersgreen
Early onset dementia (encompassing fronto-temporal dementia and prion disease)green
Familial cerebral small vessel diseasegreen
Leukodystrophy, adult onsetgreen
Neurodegenerative disorders, adult onsetgreen

Mondo (10): Alzheimer disease type 1 (MONDO:0007088), Alzheimer disease (MONDO:0004975), cerebral amyloid angiopathy, APP-related (MONDO:0011583), ABeta amyloidosis, dutch type (MONDO:0015033), ABetaA21G amyloidosis (MONDO:0017948), ABeta amyloidosis, Arctic type (MONDO:0017949), ABeta amyloidosis, Italian type (MONDO:0017947), ABeta amyloidosis, Iowa type (MONDO:0017946), early-onset autosomal dominant Alzheimer disease (MONDO:0015140), ABetaL34V amyloidosis (MONDO:0017945)

Orphanet (9): Early-onset autosomal dominant Alzheimer disease (Orphanet:1020), ABeta amyloidosis, Dutch type (Orphanet:100006), ABetaL34V amyloidosis (Orphanet:324703), ABeta amyloidosis, Iowa type (Orphanet:324708), ABeta amyloidosis, Italian type (Orphanet:324713), ABetaA21G amyloidosis (Orphanet:324718), ABeta amyloidosis, Arctic type (Orphanet:324723), Hereditary cerebral amyloid angiopathy (Orphanet:85458), NON RARE IN EUROPE: Alzheimer disease (Orphanet:238616)

HPO phenotypes

55 phenotypes (HPO-id order):

HPOTerm
HP:0000006Autosomal dominant inheritance
HP:0000504Abnormality of vision
HP:0000657Oculomotor apraxia
HP:0000708Atypical behavior
HP:0000713Agitation
HP:0000726Dementia
HP:0000734Disinhibition
HP:0000738Hallucinations
HP:0001249Intellectual disability
HP:0001250Seizure
HP:0001251Ataxia
HP:0001259Coma
HP:0001263Global developmental delay
HP:0001268Mental deterioration
HP:0001276Hypertonia
HP:0001288Gait disturbance
HP:0001289Confusion
HP:0001297Stroke
HP:0001300Parkinsonism
HP:0001336Myoclonus
HP:0001342Cerebral hemorrhage
HP:0002015Dysphagia
HP:0002076Migraine
HP:0002120Cerebral cortical atrophy
HP:0002138Subarachnoid hemorrhage
HP:0002185Neurofibrillary tangles
HP:0002186Apraxia
HP:0002315Headache
HP:0002354Memory impairment
HP:0002373Febrile seizure (within the age range of 3 months to 6 years)
HP:0002381Aphasia
HP:0002423Long-tract sign
HP:0002463Language impairment
HP:0002511Alzheimer disease
HP:0002514Cerebral calcification
HP:0002637Cerebral ischemia
HP:0003401Paresthesia
HP:0003474Somatic sensory dysfunction
HP:0003581Adult onset
HP:0003584Late onset
HP:0003596Middle age onset
HP:0003791Deposits immunoreactive to beta-amyloid protein
HP:0004938Tortuous cerebral arteries
HP:0004968Recurrent cerebral hemorrhage
HP:0010525Finger agnosia
HP:0010526Dysgraphia
HP:0011446Abnormality of mental function
HP:0011695Cerebellar hemorrhage
HP:0011970Cerebral amyloid angiopathy
HP:0012433Abnormal social behavior
HP:0012759Neurodevelopmental abnormality
HP:0030219Semantic dementia
HP:0100613Death in early adulthood
HP:0100659Abnormal cerebral vascular morphology
HP:0410054Decreased circulating GABA concentration

GWAS associations

7 associations:

StudyTraitp-value
GCST012182_4Alzheimer’s disease1e-11
GCST006279_3Cerebrospinal fluid α-synuclein levels2e-7
GCST90011770_79Glaucoma (primary open-angle)3e-7
GCST009306_7Spatial processing2e-6
GCST003082_7Longitudinal change in brain amyloid plaque burden3e-6
GCST90011768_22Glaucoma (primary open-angle)7e-6
GCST011743_86HDL cholesterol levels in HIV infection8e-6

EFO canonical traits (from GWAS)

4 canonical traits:

EFO IDTrait name
EFO:0007646amyloid plaque accumulation rate
EFO:0009323alpha synuclein measurement
EFO:0008354cognitive function measurement
EFO:0004612high density lipoprotein cholesterol measurement

MeSH disease descriptors

2 disease descriptors:

DescriptorNameTree numbers
D000544Alzheimer DiseaseC10.228.140.380.100; C10.574.945.249; F03.615.400.100
C536594Alzheimer disease type 1 *(supp.)*

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL2487 (SINGLE PROTEIN)

Drugs by curated mechanism of action (ChEMBL)

Drugs whose curated ChEMBL mechanism of action targets the APP protein itself — single-protein targets only (drugs acting on a protein family or complex that merely includes it are excluded). Includes antibodies and oligonucleotides that bioactivity screening does not capture.

13 curated-mechanism drugs:

DrugModalityMax phase
ADUCANUMABAntibody4
DONANEMABAntibody4
LECANEMABAntibody4
BAPINEUZUMABAntibody3
CRENEZUMABAntibody3
GANTENERUMABAntibody3
SOLANEZUMABAntibody3
TRAMIPROSATESmall molecule3
VALILTRAMIPROSATESmall molecule3
AMILOMOTIDEProtein2
GSK933776Unknown2
PONEZUMABAntibody2
VANUTIDE CRIDIFICARProtein2

Molecules with ChEMBL bioactivity

Phase ≥1, by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 1,397,231 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

40 molecules by phase:

MoleculeNamePhasePatents
CHEMBL682AMODIAQUINE47,237
CHEMBL723CARVEDILOL430,479
CHEMBL76CHLOROQUINE459,347
CHEMBL497CLIOQUINOL413,056
CHEMBL502DONEPEZIL443,884
CHEMBL566752FLORBETABEN F184793
CHEMBL1908919FLORBETAPIR4720
CHEMBL1774461FLORBETAPIR F 184415
CHEMBL579205FLUTEMETAMOL4334
CHEMBL2042122FLUTEMETAMOL F 184287
CHEMBL64894GENTIAN VIOLET4112,306
CHEMBL405110METHYLENE BLUE ANHYDROUS4114,909
CHEMBL191083METHYLENE BLUE CATION47,859
CHEMBL573NIACIN4355,192
CHEMBL986RETINOL4278,566
CHEMBL95TACRINE435,550
CHEMBL38TRETINOIN4195,980
CHEMBL149082TRAMIPROSATE38,405
CHEMBL145CAFFEIC ACID336,727
CHEMBL140CURCUMIN395,185
CHEMBL858EDETIC ACID3
CHEMBL297453EPIGALOCATECHIN GALLATE3
CHEMBL2048308FLUTAFURANOL3
CHEMBL3989948LANABECESTAT3
CHEMBL50QUERCETIN3
CHEMBL165RESVERATROL3
CHEMBL583912(-)-EPICATECHIN2
CHEMBL2364601AFTOBETIN2
CHEMBL3348861AMPELOPSIN2
CHEMBL284616CHLOROGENIC ACID2
CHEMBL6246ELLAGIC ACID2
CHEMBL31574FISETIN2
CHEMBL279014LUCANTHONE2
CHEMBL151LUTEOLIN2
CHEMBL289556OMAPATRILAT2
CHEMBL1368322PARAROSANILINE2
CHEMBL207456PITTSBURGH COMPOUND B2
CHEMBL93124PITTSBURGH COMPOUND B UNLABELLED2
CHEMBL468154SCYLLITOL2
CHEMBL150KAEMPFEROL1

PharmGKB: 1 entry (CPIC guideline: no)

Binding affinities (BindingDB)

1828 measured of 1947 human assays (2068 total across all organisms); most potent 50 below. Values come from heterogeneous assays and are not directly comparable.

LigandMeasureValuePatent
1-[4-(3-fluoropropoxy)-3-methoxyphenyl]-5-hydroxy-7-(4-hydroxy-3-methoxyphenyl)-1,4,6-heptatrien-3-oneKI0.07 nM
US10231967, Example 122IC500.1 nMUS-10231967: Compounds and their use as BACE inhibitors
(trans,trans)-1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzeneKI0.11 nM
5-[2-bromo-4-(3-carboxy-4-hydroxyphenethyl)phenethyl]-2-hydroxybenzoic acidKI0.13 nM
US8865911, 114IC500.14 nMUS-10231967: Compounds and their use as BACE inhibitors
5-(Biphenyl-4-ylazo)-bis (2-hydroxy-benzoic acid)(Chrysamine G)KI0.14 nM
US10231967, Example 94-Isomer-1IC500.17 nMUS-10231967: Compounds and their use as BACE inhibitors
5-[2-{4-[2-(3-carboxy-4-methoxyphenyl)-(E)-1-ethenyl]-2-iodophenyl}-(E)-1-ethenyl]-2-methoxybenzoic acidKI0.17 nM
5-[2-bromo-4-(3-carboxy-4-hydroxyphenethyl)phenethyl]-2-hydroxybenzoic acidKI0.19 nM
CHEMBL1774642KI0.2 nM
CHEMBL607562KD0.21 nM
N-{3-[(6-chloro-1,2,3,4-tetrahydroacridin-9-yl)amino]propyl}-5-(1,2-dithiolan-3-yl)pentanamideIC500.25 nM
US10231967, Example 125IC500.26 nMUS-10231967: Compounds and their use as BACE inhibitors
US8865911, 92 Isomer 2IC500.27 nMUS-10231967: Compounds and their use as BACE inhibitors
5-[2-bromo-4-(3-carboxy-4-hydroxyphenethyl)phenethyl]-2-hydroxybenzoic acidKI0.27 nM
1-((2R,6S)-1-(4-chlorophenylsulfonyl)-6-(3,5-difluorophenyl)piperidin-2-yl)cyclopropyl 4-(piperidin-1-yl)piperidine-1-carboxylateIC500.3 nM
CHEMBL1774643KI0.3 nM
US8865911, 20tIC500.36 nMUS-10231967: Compounds and their use as BACE inhibitors
2,7-bis(6-(ethyl(2-methoxybenzyl)amino)hexyl)benzo[lmn][3,8]phenanthroline-1,3,6,8(2H,7H)-tetraoneIC500.37 nM
US10231967, Example 68-Isomer-1IC500.38 nMUS-10231967: Compounds and their use as BACE inhibitors
(R,E)-2-(3-((2-fluoroethoxy)methyl)-4-(pyrimidin-2-yl)piperazin-1-yl)-5-(2-(6-(4-methyl-1H-imidazol-1-yl)pyridin-3-yl)vinyl)pyrimidineKI0.42 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
(R)-2-(2-((2-fluoroethoxy)methyl)-4-(5-((6-(1-methyl-1H-pyrazol-4-yl)pyridin-3-yl)ethynyl)pyrimidin-2-yl)piperazin-1-yl)-1,3,5-triazineKI0.449 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
N,N-dimethyl-4-[2-(6-thiophen-2-yl-1H-pyrrolo[2,3-b]pyridin-2-yl)ethynyl]anilineKD0.49 nMUS-10906900: Compounds for using in imaging and particularly for the diagnosis of neurodegenerative diseases
(R,E)-5-(2-(6-(1H-imidazol-1-yl)pyridin-3-yl)vinyl)-2-(3-((2-fluoroethoxy)methyl)-4-(pyrimidin-2-yl)piperazin-1-yl)pyrimidineKI0.5 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
(R,E)-5-(2-(6-(1H-imidazol-1-yl)pyridin-3-yl)vinyl)-2-(2-(methoxymethyl)-4-(pyridin-2-yl)piperazin-1-yl)pyrimidineKI0.5 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
(R,E)-(1-(5-(2-(6-(1H-imidazol-1-yl)pyridin-3-yl)vinyl)pyrimidin-2-yl)-4-(pyrimidin-4-yl)piperazin-2-yl)methanolKI0.5 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
(R,E)-5-(2-(6-(1H-imidazol-1-yl)pyridin-3-yl)vinyl)-2-(2-((2-fluoroethoxy)methyl)-4-(pyridin-4-yl)piperazin-1-yl)pyrimidineKI0.5 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
1-((2-((R)-4-(5-((E)-2-(6-(1H-imidazol-1-yl)pyridin-3-yl)vinyl)pyrimidin-2-yl)-2-(methoxymethyl)piperazin-1-yl)pyrimidin-5-yl)oxy)-3-fluoropropan-2-olKI0.52 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
N,N-dimethyl-4-[2-(1H-pyrrolo[2,3-b]pyridin-2-yl)ethynyl]anilineKD0.53 nMUS-10906900: Compounds for using in imaging and particularly for the diagnosis of neurodegenerative diseases
US8865911, 94 Isomer 2IC500.56 nMUS-10231967: Compounds and their use as BACE inhibitors
CHEMBL3314344KD0.56 nM
US8865911, 20eIC500.57 nMUS-10231967: Compounds and their use as BACE inhibitors
(R)-2-(2-((2-fluoroethoxy)methyl)-4-(5-((2-(1-methyl-1H-pyrazol-4-yl)pyrimidin-5-yl)ethynyl)pyrimidin-2-yl)piperazin-1-yl)-1,3,5-triazineKI0.57 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
US8865911, 100IC500.59 nMUS-10231967: Compounds and their use as BACE inhibitors
US8865911, 20uIC500.6 nMUS-9000182: 2H-imidazol-4-amine compounds and their use as BACE inhibitors
US8865911, 91IC500.62 nMUS-10231967: Compounds and their use as BACE inhibitors
(R,E)-5-(2-(6-(1-(2-fluoroethyl)-1H-pyrazol-4-yl)pyridin-3-yl)vinyl)-2-(3-(methoxymethyl)-4-(pyrimidin-2-yl)piperazin-1-yl)pyrimidineKI0.62 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
US9000182, 9, isomer 1IC500.7 nMUS-9000182: 2H-imidazol-4-amine compounds and their use as BACE inhibitors
US9000182, 11, isomer 1IC500.7 nMUS-9000182: 2H-imidazol-4-amine compounds and their use as BACE inhibitors
(2S,4S)-6-(3-chlorophenyl)-5’-methyl-2-[(3R)-oxan-3-yl]spiro[2,3-dihydrochromene-4,2’-imidazole]-4’-amineIC500.7 nMUS-10231967: Compounds and their use as BACE inhibitors
(R,E)-5-(2-(6-(1H-imidazol-1-yl)pyridin-3-yl)vinyl)-2-(3-(methoxymethyl)-4-(pyridin-2-yl)piperazin-1-yl)pyrimidineKI0.7 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
5-hydroxy-2-(4-methylaminophenyl)benzofuranKI0.7 nM
US10231967, Example 20aaIC500.72 nMUS-10231967: Compounds and their use as BACE inhibitors
N,N-dimethyl-4-[2-(6-thiophen-3-yl-1H-pyrrolo[2,3-b]pyridin-2-yl)ethynyl]anilineKD0.73 nMUS-10906900: Compounds for using in imaging and particularly for the diagnosis of neurodegenerative diseases
US10231967, Example 72IC500.76 nMUS-10231967: Compounds and their use as BACE inhibitors
US8865911, 20bIC500.78 nMUS-10231967: Compounds and their use as BACE inhibitors
(R,E)-5-(5-(2-(2-(3-((2-fluoroethoxy)methyl)-4-(pyrimidin-4-yl)piperazin-1-yl)pyrimidin-5-yl)vinyl)pyridin-2-yl)oxazoleKI0.78 nMWO-2024186584: ALPHA-SYNUCLEIN BINDERS AND METHODS OF USE
4-[2-(6-fluoro-1H-pyrrolo[2,3-b]pyridin-2-yl)ethynyl]-N,N-dimethylanilineKD0.79 nMUS-10906900: Compounds for using in imaging and particularly for the diagnosis of neurodegenerative diseases
US8865911, 85IC500.8 nMUS-10231967: Compounds and their use as BACE inhibitors
US9000183, 6 Isomer 1IC500.8 nMUS-9000183: Cyclohexane-1,2′-indene-1′,2″-imidazol compounds and their use as BACE inhibitors

ChEMBL bioactivities

1956 potent at pChembl≥5 of 2424 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
10.15Ki0.07nMCHEMBL384465
10.00IC500.1nMCHEMBL2152914
9.96Ki0.11nMCHEMBL74704
9.89Ki0.13nMCHEMBL76112
9.85Ki0.14nMCHRYSAMINE G
9.85IC500.14nMLANABECESTAT
9.80Ki0.16nMCHRYSAMINE G
9.77Ki0.17nMCHEMBL292910
9.77IC500.17nMCHEMBL6008112
9.72Ki0.19nMCHEMBL305634
9.70Ki0.2nMCHEMBL1774642
9.68Ki0.208nMCURCUMIN
9.68Kd0.21nMCHEMBL607562
9.59IC500.26nMCHEMBL2152915
9.57IC500.27nMCHEMBL4111546
9.57Ki0.27nMCHEMBL74348
9.55IC500.28nMCHEMBL2152914
9.52IC500.3nMCHEMBL240055
9.52IC500.3nMCHEMBL2152914
9.52Ki0.3nMCHEMBL1774643
9.44IC500.36nMCHEMBL2152917
9.42IC500.38nMCHEMBL5918838
9.40Ki0.4nMCHRYSAMINE G
9.30IC500.5nMCHEMBL2152915
9.25Kd0.56nMCHEMBL3314344
9.25IC500.56nMCHEMBL2152917
9.25IC500.56nMCHEMBL3936953
9.24IC500.57nMCHEMBL3965844
9.23IC500.59nMCHEMBL3974225
9.22IC500.6nMCHEMBL3959097
9.21IC500.62nMCHEMBL3907727
9.20IC500.63nMCHEMBL2152915
9.20IC500.63nMCHEMBL3959097
9.19IC500.65nMMRK-560
9.17IC500.67nMCHEMBL3965844
9.15Ki0.7nMFLUTEMETAMOL F 18
9.15Ki0.7nMCHEMBL204829
9.15IC500.7nMCHEMBL3898248
9.15IC500.7nMCHEMBL4110988
9.15IC500.7nMCHEMBL5773881
9.15IC500.7nMCHEMBL6008112
9.14IC500.72nMCHEMBL2152915
9.14IC500.72nMCHEMBL2152918
9.14IC500.72nMCHEMBL3974225
9.13Ki0.74nMFLUTEMETAMOL F 18
9.13Ki0.74nMFLUTEMETAMOL
9.12IC500.76nMCHEMBL2152920
9.11IC500.78nMCHEMBL3901045
9.10Ki0.8nMCHEMBL292910
9.10Ki0.8nMCHEMBL55401

PubChem BioAssay actives

768 with measured affinity, of 6100 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
5-[(E)-2-[3-bromo-4-[(E)-2-(3-carboxy-4-hydroxyphenyl)ethenyl]phenyl]ethenyl]-2-hydroxybenzoic acid38551: Inhibitory activity against binding of [125I]IMSB to amyloid beta in brainki0.0001uM
5-[(Z)-2-[3-bromo-4-[(Z)-2-(3-carboxy-4-hydroxyphenyl)ethenyl]phenyl]ethenyl]-2-hydroxybenzoic acid38551: Inhibitory activity against binding of [125I]IMSB to amyloid beta in brainki0.0001uM
5-[[4-[4-[(3-carboxy-4-hydroxyphenyl)diazenyl]phenyl]phenyl]diazenyl]-2-hydroxybenzoic acid38550: Inhibition constant for aggregates of amyloid beta compared to [125I]IMSBki0.0001uM
(1E,4Z,6E)-7-[4-(3-fluoropropoxy)-3-methoxyphenyl]-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one272869: Displacement of [125I]IMSB from beta amyloid protein 40ki0.0001uM
5-[(E)-2-[4-[(E)-2-(3-carboxy-4-methoxyphenyl)ethenyl]-3-iodophenyl]ethenyl]-2-methoxybenzoic acid38550: Inhibition constant for aggregates of amyloid beta compared to [125I]IMSBki0.0002uM
5-[(E)-2-[3-bromo-4-[(Z)-2-(3-carboxy-4-hydroxyphenyl)ethenyl]phenyl]ethenyl]-2-hydroxybenzoic acid38551: Inhibitory activity against binding of [125I]IMSB to amyloid beta in brainki0.0002uM
[1-[(2R,6S)-1-(4-chlorophenyl)sulfonyl-6-(3,5-difluorophenyl)piperidin-2-yl]cyclopropyl] 4-piperidin-1-ylpiperidine-1-carboxylate301167: Inhibition of gamma-secretase assessed as reduction of membrane A-beta-40 levelic500.0003uM
5-[(Z)-2-[3-bromo-4-[(E)-2-(3-carboxy-4-hydroxyphenyl)ethenyl]phenyl]ethenyl]-2-hydroxybenzoic acid38551: Inhibitory activity against binding of [125I]IMSB to amyloid beta in brainki0.0003uM
1-(125I)iodo-4-[(4-methoxyphenoxy)methyl]benzene1179998: Binding affinity to amyloid beta42 (unknown origin) after 3 hrs by gamma countingkd0.0006uM
2-[3-fluoro-4-(methylamino)phenyl]-1,3-benzothiazol-6-ol445593: Binding affinity to Beta amyloid aggregates in Alzheimer’s disease patient brain by competitive binding assayki0.0007uM
2-[4-(methylamino)phenyl]-1-benzofuran-5-ol264125: Displacement of [125I]IMPY from beta amyloid in human corpse AD brainki0.0007uM
Flutemetamol F-18668927: Displacement of [18F]-amyvid from amyloid-beta aggregates in alzheimer’s disease patient brain homogenates after 1 hrki0.0007uM
4-(6-bromo-1,3-benzothiazol-2-yl)-N,N-dimethylaniline38549: Inhibition constant for amyloid beta compared to [125I]TZDMki0.0008uM
2-[4-((111C)methylamino)phenyl]-1,3-benzothiazol-6-ol673978: Binding affinity to human amyloid beta plaqueki0.0008uM
2-[4-(methylamino)phenyl]-1,3-benzothiazol-6-ol445593: Binding affinity to Beta amyloid aggregates in Alzheimer’s disease patient brain by competitive binding assayki0.0009uM
4-(6-iodo-1,3-benzothiazol-2-yl)-N,N-dimethylaniline38549: Inhibition constant for amyloid beta compared to [125I]TZDMki0.0009uM
N-[3-[(6R)-4-amino-2-cyano-6-methyl-7H-pyrazolo[1,5-a]pyrazin-6-yl]-4-fluorophenyl]-5-cyanopyridine-2-carboxamide1819117: Inhibition of human amyloid beta (1 to 42) in human SKNBE2 cells expressing wild-type amyloid precursor protein hAPP695 incubated for 18 hrs by sandwich ELISAic500.0010uM
N-[3-[(6R)-4-amino-2-cyano-6-methyl-7H-pyrazolo[1,5-a]pyrazin-6-yl]-4-fluorophenyl]-5-(difluoromethoxy)pyridine-2-carboxamide1819117: Inhibition of human amyloid beta (1 to 42) in human SKNBE2 cells expressing wild-type amyloid precursor protein hAPP695 incubated for 18 hrs by sandwich ELISAic500.0010uM
(E,2Z,5Z)-2-[(2E,4E)-5-[4-(dimethylamino)phenyl]penta-2,4-dienylidene]-5-[(E)-3-[4-(dimethylamino)phenyl]prop-2-enylidene]hex-3-enedinitrile2213906: Binding affinity to amyloid beta plaques 1 to 42 (unknown origin) assessed as dissociation constantkd0.0010uM
4-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]phenol254419: Inhibition constant for I-125-IMPY binding to amyloid plaques in Alzheimers disease brain homogenateski0.0011uM
4-[(E)-2-[4-(methylamino)phenyl]ethenyl]phenol254419: Inhibition constant for I-125-IMPY binding to amyloid plaques in Alzheimers disease brain homogenateski0.0012uM
4-[2-[4-[2-(2-fluoroethoxy)ethoxy]phenyl]ethynyl]-N-methylaniline286796: Displacement of [125I]IMPY from human beta amyloid plaque in brain homogenateski0.0012uM
N-[3-[(6R)-4-amino-2-cyano-6-methyl-7H-pyrazolo[1,5-a]pyrazin-6-yl]-4-fluorophenyl]-5-(fluoromethoxy)pyrazine-2-carboxamide1819117: Inhibition of human amyloid beta (1 to 42) in human SKNBE2 cells expressing wild-type amyloid precursor protein hAPP695 incubated for 18 hrs by sandwich ELISAic500.0012uM
4-(6-iodoimidazo[1,2-a]pyridin-2-yl)-N,N-dimethylaniline445593: Binding affinity to Beta amyloid aggregates in Alzheimer’s disease patient brain by competitive binding assayki0.0013uM
4-(5-methoxy-1-benzofuran-2-yl)-N-methylaniline264125: Displacement of [125I]IMPY from beta amyloid in human corpse AD brainki0.0013uM
N-[3-[(6R)-4-amino-2-cyano-6-methyl-7H-pyrazolo[1,5-a]pyrazin-6-yl]-4-fluorophenyl]-5-methoxypyrazine-2-carboxamide1819117: Inhibition of human amyloid beta (1 to 42) in human SKNBE2 cells expressing wild-type amyloid precursor protein hAPP695 incubated for 18 hrs by sandwich ELISAic500.0013uM
4-[2-[4-(methylamino)phenyl]ethynyl]phenol286796: Displacement of [125I]IMPY from human beta amyloid plaque in brain homogenateski0.0015uM
5-[2-[4-[2-[2-(2-fluoroethoxy)ethoxy]ethoxy]phenyl]ethynyl]-1H-indole365222: Displacement of [125I]IMPY from beta-amyloid plaques in AD patient brainki0.0015uM
6-bromo-2-[4-(4-methylpiperazin-1-yl)phenyl]-1,3-benzothiazole38549: Inhibition constant for amyloid beta compared to [125I]TZDMki0.0016uM
5-[(E)-2-[5-(2-fluoroethoxy)-1,3-benzoselenazol-2-yl]ethenyl]-N,N-dimethylpyrimidin-2-amine1884928: Binding affinity to amyloid beta (1 to 42) (unknown origin) aggregateskd0.0016uM
4-(6-bromo-1,3-benzothiazol-2-yl)-N-methylaniline38663: Binding affinity for Amyloid beta 1-40 aggregates in competition with [N-methyl-3H] BTA-1.ki0.0017uM
2-[6-(methylamino)-3-pyridinyl]-1,3-benzothiazol-6-ol445593: Binding affinity to Beta amyloid aggregates in Alzheimer’s disease patient brain by competitive binding assayki0.0017uM
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline38663: Binding affinity for Amyloid beta 1-40 aggregates in competition with [N-methyl-3H] BTA-1.ki0.0019uM
4-[2-[4-[2-[2-(2-fluoroethoxy)ethoxy]ethoxy]phenyl]ethynyl]-N-methylaniline286796: Displacement of [125I]IMPY from human beta amyloid plaque in brain homogenateski0.0019uM
4-[(E)-2-(4-iodophenyl)ethenyl]-N,N-dimethylaniline445593: Binding affinity to Beta amyloid aggregates in Alzheimer’s disease patient brain by competitive binding assayki0.0020uM
2-[(2E,4E)-5-(1-benzylindol-5-yl)penta-2,4-dienylidene]propanedinitrile2037033: Competitive binding affinity to amyloid beta (1 to 42) (unknown origin) assessed as inhibition constant incubated for 0.5 hrs by ThT-based fluorescence microplate reader analysiski0.0020uM
florbetaben f-18668927: Displacement of [18F]-amyvid from amyloid-beta aggregates in alzheimer’s disease patient brain homogenates after 1 hrki0.0022uM
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole347533: Displacement of [125I]IMPY from beta-amyloid plaques in Alzheimer’s disease patient brain homogenateki0.0022uM
4-(5-methoxy-1-benzofuran-2-yl)aniline264125: Displacement of [125I]IMPY from beta amyloid in human corpse AD brainki0.0023uM
[1-[(2R,6S)-1-(4-chlorophenyl)sulfonyl-6-(3,5-difluorophenyl)piperidin-2-yl]cyclopropyl] 4-(2-hydroxyethyl)piperazine-1-carboxylate301167: Inhibition of gamma-secretase assessed as reduction of membrane A-beta-40 levelic500.0024uM
N-[3-[(6R)-4-amino-2-cyano-6-methyl-7H-pyrazolo[1,5-a]pyrazin-6-yl]-4-fluorophenyl]-5-(difluoromethyl)pyrazine-2-carboxamide1819117: Inhibition of human amyloid beta (1 to 42) in human SKNBE2 cells expressing wild-type amyloid precursor protein hAPP695 incubated for 18 hrs by sandwich ELISAic500.0025uM
N-[3-[(6R)-4-amino-2-cyano-6-methyl-7H-pyrazolo[1,5-a]pyrazin-6-yl]-4-fluorophenyl]-5-fluoropyridine-2-carboxamide1819117: Inhibition of human amyloid beta (1 to 42) in human SKNBE2 cells expressing wild-type amyloid precursor protein hAPP695 incubated for 18 hrs by sandwich ELISAic500.0026uM
2-[4-(dimethylamino)phenyl]-1-benzofuran-5-ol264125: Displacement of [125I]IMPY from beta amyloid in human corpse AD brainki0.0028uM
4-[2-(4-methoxyphenyl)ethynyl]phenol286796: Displacement of [125I]IMPY from human beta amyloid plaque in brain homogenateski0.0029uM
4-[2-[4-[2-[2-(2-fluoroethoxy)ethoxy]ethoxy]phenyl]ethynyl]-N,N-dimethylaniline286796: Displacement of [125I]IMPY from human beta amyloid plaque in brain homogenateski0.0029uM
Florbetapir F-18445593: Binding affinity to Beta amyloid aggregates in Alzheimer’s disease patient brain by competitive binding assayki0.0029uM
4-(1-benzothiophen-2-yl)phenol1500336: Inhibition of [125I]2-(3’-Iodo-4’-N-methylaminophenyl) benzothiazole binding to amyloid beta (1 to 40) (unknown origin) after 3 hrs by NaI well counting methodki0.0030uM
[1-(4-phenoxyphenyl)triazol-4-yl]methyl 4-hydroxy-3-methoxybenzoate2121957: Inhibition of amyloid beta (1 to 42) (unknown origin) aggregation incubated for 48 hrs by ThioflavinT staining based fluorescence assayic500.0030uM
2-[2-[4-[2-[4-(methylamino)phenyl]ethynyl]phenoxy]ethoxy]ethanol286796: Displacement of [125I]IMPY from human beta amyloid plaque in brain homogenateski0.0031uM
[4-[(2Z)-2-[9-[(E)-2-[4-(dimethylamino)phenyl]ethenyl]-2,3-dioxo-1,4,6,10-tetraoxa-5-boranuidaspiro[4.5]dec-8-en-7-ylidene]ethylidene]cyclohexa-2,5-dien-1-ylidene]-dimethylazanium1884916: Binding affinity to human amyloid beta (1 to 42) monomer measured by fluorescence assaykd0.0032uM

CTD chemical–gene interactions

303 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
Copperdecreases reaction, increases chemical synthesis, increases abundance, affects binding, decreases expression (+13 more)26
Zincdecreases reaction, increases secretion, affects folding, increases reduction, increases reaction (+2 more)10
sulindac sulfidedecreases activity, affects cleavage, affects reaction, increases reaction, affects localization9
Hydrogen Peroxidedecreases reaction, decreases secretion, increases chemical synthesis, affects binding, affects expression (+4 more)8
Leadaffects splicing, affects binding, affects cotreatment, affects expression, increases secretion (+4 more)8
Resveratroldecreases reaction, affects cotreatment, affects reaction, affects folding, affects binding (+6 more)6
sodium arseniteaffects localization, affects cotreatment, increases expression, affects secretion, increases cleavage4
Curcumindecreases reaction, increases expression, affects binding, affects reaction4
Ibuprofenincreases secretion, decreases expression, affects cleavage, affects cotreatment, decreases reaction (+1 more)4
Tretinoinincreases metabolic processing, affects cotreatment, increases expression, increases reaction, decreases reaction (+2 more)4
Trientineincreases activity, decreases expression, increases metabolic processing, affects binding, affects cotreatment (+3 more)4
Particulate Matterincreases expression, decreases reaction, affects cotreatment, increases uptake, decreases expression (+4 more)4
lead acetateincreases reaction, increases expression, decreases reaction, affects cotreatment, decreases expression (+2 more)3
24-hydroxycholesteroldecreases secretion, increases metabolic processing, affects metabolic processing, increases activity, decreases metabolic processing3
27-hydroxycholesteroldecreases metabolic processing, decreases secretion, increases expression3
2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-onedecreases expression, decreases reaction, affects localization, increases expression, increases phosphorylation (+3 more)3
2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-oneaffects binding, decreases reaction, increases degradation, increases expression, decreases phosphorylation3
Acetylcysteinedecreases reaction, increases abundance, increases expression, affects localization, increases activity (+1 more)3
Acroleinincreases oxidation, increases reaction, increases abundance, affects binding, affects cotreatment (+1 more)3
Air Pollutantsincreases expression, increases reaction, decreases reaction, affects cotreatment, increases oxidation (+1 more)3
Aluminumincreases expression, affects binding3
Arsenicaffects methylation, decreases expression, increases abundance, affects cotreatment, affects expression3
Benzo(a)pyreneincreases expression, decreases methylation3
Cannabidiolaffects cotreatment, decreases expression, increases expression, decreases reaction, decreases response to substance3
DDTincreases cleavage, increases expression, decreases degradation, increases secretion, decreases reaction3
Estradiolincreases activity, increases cleavage, increases expression, increases secretion, decreases expression (+1 more)3
Indomethacinincreases metabolic processing, increases secretion, affects cleavage, decreases reaction, increases expression (+1 more)3
Paraquatincreases reaction, increases expression, increases response to substance, affects binding, decreases reaction3
Penicillamineaffects binding, affects cotreatment, decreases reaction, increases chemical synthesis, increases oxidation (+2 more)3
Quercetindecreases phosphorylation, decreases reaction, increases abundance, increases activity, increases cleavage (+2 more)3

ChEMBL screening assays

1744 unique, capped per target: 1699 binding, 44 functional, 1 admet

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1002439BindingDisplacement of [125I]IMPY from beta-amyloid plaques in brain homogenate of patient with Alzheimer’s disease by gamma counting11C-labelled PIB analogues as potential tracer agents for in vivo imaging of amyloid beta in Alzheimer’s disease. — *Eur J Med Chem*
CHEMBL1613905FunctionalPUBCHEM_BIOASSAY: Assay for Inhibitors of the fibrillation of the Beta-Amyloid Protein Fragment, A-beta 1-42. (Class of assay: confirmatory) [Related pubchem assays: 1460, 1468 ]PubChem BioAssay data set
CHEMBL4826780ADMETInhibition of amyloid beta(25 to 35) (unknown origin) binding to human SH-SY5Y cell plasma membrane at 10 uM measured after 20 mins by UV-vis microplate reader assaySynthesis, biological evaluation and molecular modeling of benzofuran piperidine derivatives as Aβ antiaggregant. — *Eur J Med Chem*

Cellosaurus cell lines

87 cell lines: 54 induced pluripotent stem cell, 18 cancer cell line, 11 transformed cell line, 3 spontaneously immortalized cell line, 1 embryonic stem cell

First 10 cell lines (id-ordered, not curated):

CellosaurusNameCategorySex
CVCL_0523SH-SY5Y-SPA4CTCancer cell lineFemale
CVCL_2707REM 885Transformed cell lineMale
CVCL_A3ZLZZUi024-AInduced pluripotent stem cellFemale
CVCL_A5CZHEK293 APPsweTransformed cell lineFemale
CVCL_A8YXF15553Induced pluripotent stem cell
CVCL_A8YYF16574Induced pluripotent stem cellSex unspecified
CVCL_A8YZUOMELBi002-AInduced pluripotent stem cellSex unspecified
CVCL_A9QAUEFi003-AInduced pluripotent stem cellMale
CVCL_B2RVAbcam HEK293T APP KOTransformed cell lineFemale
CVCL_B5GRXWHNi001-AInduced pluripotent stem cellFemale

Clinical trials (associated diseases)

Via MONDO — disease-level, not drug-specific.

showing 60 of 322 trials:

NCTPhaseStatusTitle
NCT04520308Phase 4UNKNOWNAn Open-label, Single-arm Longitudinal Study With Dupilumab for Patients With Atopic Dermatitis
NCT00009191Phase 4COMPLETEDThe Depression in Alzheimer’s Disease Study (DIADS)
NCT00009217Phase 4COMPLETEDTreatment of Behavioral Symptoms in Alzheimer’s Disease
NCT00018278Phase 4COMPLETEDElectrophysiologic Measures of Treatment Response in Alzheimer Disease
NCT00035204Phase 4COMPLETEDA Study of the Effects on Sleep, Attention, and Gastrointestinal Tolerance of Galantamine and Donepezil in Patients With Alzheimer’s Disease
NCT00042172Phase 4COMPLETEDTreatment for Early Memory Loss
NCT00046358Phase 4COMPLETEDThe Effect of Short-Term Statins and NSAIDs on Levels of Beta-Amyloid, a Protein Associated With Alzheimer’s Disease
NCT00104442Phase 4COMPLETEDStudy of the Effects of Current Drug Treatments on Levels of Certain Brain Chemicals in Alzheimer’s Disease
NCT00120874Phase 4COMPLETEDMemantine and Comprehensive, Individualized Management of Alzheimer’s Disease and Caregiver Training
NCT00142324Phase 4UNKNOWNCALM-AD
NCT00165724Phase 4COMPLETEDAlzheimer’s Disease Long-term Follow-up Study (ALF Study)
NCT00165750Phase 4TERMINATEDCorrelation Between Regional Brain Volume and Response to Donepezil Treatment in AD Patients
NCT00202124Phase 4COMPLETEDDouble Blind Study of Trp01 in Patients With Alzheimer’s Disease
NCT00208819Phase 4COMPLETEDA Comparison of Two Standard Therapies in the Management of Dementia With Agitation
NCT00216515Phase 4COMPLETEDThe Efficacy of Galantamine on the Attention and the Frontal Function of the Patients With Dementia of Alzheimer Type
NCT00230568Phase 4COMPLETEDEARTH 413: A Study of Aricept in Hispanic Patients With Mild to Moderate Alzheimer’s Disease (AD)
NCT00234637Phase 4COMPLETEDRivastigmine Monotherapy and Combination Therapy With Memantine in Patients With Moderately Severe Alzheimer’s Disease Who Failed to Benefit From Previous Cholinesterase Inhibitor Treatment
NCT00245206Phase 4COMPLETEDSide Effects of Newer Antipsychotics in Older Adults
NCT00254033Phase 4COMPLETEDApathy Associated With Alzheimer’s Disease
NCT00260624Phase 4COMPLETEDEscitalopram Treatment of Patients With Agitated Dementia
NCT00303277Phase 4COMPLETEDDo HMG CoA Reductase Inhibitors Affect Abeta Levels?
NCT00305903Phase 4COMPLETEDSafety and Tolerability of Rivastigmine With Add-on Memantine in Patients With Probable Alzheimer’s Disease
NCT00306124Phase 4UNKNOWNDopaminergic Enhancement of Learning and Memory in Healthy Adults and Patients With Dementia/Mild Cognitive Impairment
NCT00334906Phase 4COMPLETEDStudy of Memantine in Assessment of Selected Measures of Volumetric Magnetic Resonance Imaging (MRI) and Cognition in Moderate AD (Alzheimer’s Disease)
NCT00369603Phase 4TERMINATEDFunctional Brain Imaging of Medication Treatment Response in Mild Alzheimer’s Disease Patients
NCT00375557Phase 4WITHDRAWNSafety and Efficacy of Divalproex and Quetiapine in Elderly Alzheimer’s Dementia Patients
NCT00381381Phase 4COMPLETEDThe Clinical Response of Choline Acetyltransferase and Apolipoprotein Epsilon Gene Polymorphisms to Donepezil in Alzheimer’s Disease
NCT00385684Phase 4COMPLETEDLow-Dose Opiate Therapy for Discomfort in Dementia (L-DOT)
NCT00401167Phase 4COMPLETEDMemantine for Agitation and Aggression in Severe Alzheimer’s Disease
NCT00403520Phase 4COMPLETEDHippocampus Study: Comparative Effect of Donepezil 10mg/d and Placebo on Clinical and Radiological Markers
NCT00417482Phase 4COMPLETEDAntipsychotic Discontinuation in Alzheimer’s Disease
NCT00443014Phase 4COMPLETEDThe Dementia Study in Northern Norway
NCT00469456Phase 4COMPLETEDEffect of Memantine on Functional Communication in Patients With Alzheimer’s Disease
NCT00476008Phase 4COMPLETEDDelaying the Progression of Driving Impairment in Individuals With Mild Alzheimer’s Disease
NCT00477659Phase 4COMPLETEDNeural Correlates In Mild Alzheimer’s Disease
NCT00480870Phase 4COMPLETEDThe Effect of Anticholinesterase Drugs on Sleep in Alzheimer’s Disease Patients
NCT00495820Phase 4COMPLETEDMethylphenidate for Apathy in Alzheimer’s Dementia: A Controlled Study
NCT00523666Phase 4UNKNOWNDiffusion Tensor Weighted MRI in Alzheimer’s Disease Modifying Treatment Effects of Galantamine (Reminyl®)
NCT00549601Phase 4COMPLETEDConvenience, Tolerability, and Safety of Change in the Administration of Rivastigmine From Capsules to a Transdermal Patch in Patients With Mild to Moderate Alzheimer’s Disease
NCT00551161Phase 4COMPLETEDMagnetic Resonance Spectroscopy Study of Memantine in Alzheimer’s Disease
NCT00561392Phase 4COMPLETEDClinical Effectiveness of 10 cm^2 Rivastigmine Patch in Patients With Alzheimer’s Disease
NCT00622713Phase 4COMPLETEDA 24 Week, Multicenter, Open, Evaluation of the Clinical Effectiveness of the Once-daily 10 cm^2 Rivastigmine Patch Formulation in Patients With Probable Alzheimer’s Disease (EXTRA)
NCT00626210Phase 4TERMINATEDModafinil Treatment for Sleep/Wake Disturbances in Older Adults
NCT00626613Phase 4UNKNOWNThe Relationship Between Risperdal Treatment and Quality of Life in Patients With Alzheimer’s Disease and Behavioural and Psychological Symptoms of Dementia (BPSD)
NCT00649220Phase 4TERMINATEDMemantine and Antipsychotics Use
NCT00706186Phase 4TERMINATEDSafety and Feasibility of Sodium Oxybate in Mild Alzheimer’s Disease Patients
NCT00711204Phase 4WITHDRAWNEvaluating The Impact Of Donepezil Hydrochloride (Aricept) On Behavioral And Psychological Symptoms In Patients With Severe Alzheimer’s Disease
NCT00731224Phase 4COMPLETEDCompliance and Tolerability of Rivastigmine Transdermal Patch 10 cm² in Patients With Probable Alzheimer’s Disease.
NCT00792662Phase 4WITHDRAWNImproving Function, Quality of Life, Glycemia in Diabetics With Dementia
NCT00800709Phase 4COMPLETEDMemantine and Changes of Biological Markers and Brain PET Imaging in Alzheimer’s Disease
NCT00862940Phase 4COMPLETEDA Clinical Study Evaluating the Effects of Memantine on Brain Atrophy in Patients With Alzheimer’s Disease
NCT00933608Phase 4COMPLETEDEffects of Memantine on Magnetic Resonance (MR) Spectroscopy in Subjects at Risk for Alzheimer’s Disease
NCT00948766Phase 4COMPLETEDEffects of Rivastigmine Patch on Activities of Daily Living and Cognition in Patients With Severe Dementia of the Alzheimer’s Type (ACTION) (Study Protocol CENA713DUS44, NCT00948766) and a 24 Week Open-label Extension to Study CENA713DUS44
NCT00950430Phase 4ENROLLING_BY_INVITATIONImaging of Brain Amyloid Plaques in the Aging Population
NCT00980785Phase 4COMPLETEDStudying the Effects of Antihypertensives on Individuals at Risk for Alzheimer’s
NCT01025466Phase 4COMPLETEDExelon Patch and Combination With Memantine Comparative Trial
NCT01047579Phase 4COMPLETEDA 12 Week, Multicenter, Open Label Evaluation of Caregiver Preference, Safety and Tolerability of Exelon® Patch (Rivastigmine Transdermal) in Patients With Alzheimer’s Disease
NCT01054976Phase 4COMPLETEDThe Efficacy of Galantamine Treatment on Attention in Patients With Alzheimer’s Disease
NCT01119638Phase 4COMPLETEDEscitalopram Treatment for BPSD in Alzheimer’s Disease in Comparison to Risperidone
NCT01122329Phase 4COMPLETEDA Positron Emission Tomography (PET) Study Evaluating Brain Metabolism of a Medical Food in Alzheimer’s Disease

Predicted chemistry — Sugi Predict

The predicted patent-compound landscape for APP across ~30M SureChEMBL compounds — explore on Sugi Predict.