GLRX2

gene
On this page

Also known as GRX2bA101E13.1

Summary

GLRX2 (glutaredoxin 2, HGNC:16065) is a protein-coding gene on chromosome 1q31.2, encoding Glutaredoxin-2, mitochondrial (Q9NS18). Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress.

The protein encoded by this gene is a member of the glutaredoxin family of proteins, which maintain cellular thiol homeostasis. These proteins are thiol-disulfide oxidoreductases that use a glutathione-binding site and one or two active cysteines in their active site. This gene undergoes alternative splicing to produce multiple isoforms, one of which is ubiquitously expressed and localizes to mitochondria, where it functions in mitochondrial redox homeostasis and is important for the protection against and recovery from oxidative stress. Other isoforms, which have more restrictive expression patterns, show cytosolic and nuclear localization, and are thought to function in cellular differentiation and transformation, possibly with a role in tumor progression.

Source: NCBI Gene 51022 — RefSeq curated summary.

At a glance

  • Clinical variants (ClinVar): 25 total
  • MANE Select transcript: NM_197962

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:16065
Approved symbolGLRX2
Nameglutaredoxin 2
Location1q31.2
Locus typegene with protein product
StatusApproved
AliasesGRX2, bA101E13.1
Ensembl geneENSG00000023572
Ensembl biotypeprotein_coding
OMIM606820
Entrez51022

Gene structure

Transcript identifiers

Ensembl transcripts: 4 — 2 protein_coding, 1 protein_coding_CDS_not_defined, 1 nonsense_mediated_decay

ENST00000367439, ENST00000367440, ENST00000472197, ENST00000608166

RefSeq mRNA: 3 — MANE Select: NM_197962 NM_001243399, NM_016066, NM_197962

CCDS: CCDS1380, CCDS1381

Canonical transcript exons

ENST00000367439 — 4 exons

ExonStartEnd
ENSE00001444503193105264193105414
ENSE00003574589193101141193101204
ENSE00003691498193097584193097760
ENSE00003901270193096470193096759

Expression profiles

Bgee: expression breadth ubiquitous, 287 present calls, max score 98.25.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 31.4971 / max 253.1374, expressed in 1821 samples.

FANTOM5 promoters (3 alternative TSS)

Promoter IDTPM avgSamples expressed
1645231.44951821
164540.04405
164530.00362

Top tissues by expression

288 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
spermCL:000001998.25gold quality
male germ cellCL:000001596.37gold quality
left testisUBERON:000453394.56gold quality
right testisUBERON:000453494.42gold quality
oocyteCL:000002393.80gold quality
adult organismUBERON:000702393.67gold quality
endothelial cellCL:000011593.41gold quality
testisUBERON:000047392.95gold quality
ponsUBERON:000098892.83gold quality
heart right ventricleUBERON:000208092.61gold quality
heart left ventricleUBERON:000208492.57gold quality
cardiac ventricleUBERON:000208292.52gold quality
Brodmann (1909) area 23UBERON:001355492.38gold quality
secondary oocyteCL:000065592.17gold quality
adrenal tissueUBERON:001830391.84gold quality
mucosa of transverse colonUBERON:000499191.66gold quality
gastrocnemiusUBERON:000138891.54gold quality
middle temporal gyrusUBERON:000277191.16gold quality
primary visual cortexUBERON:000243691.09gold quality
muscle of legUBERON:000138391.06gold quality
skeletal muscle tissue of rectus abdominisUBERON:000451190.80gold quality
muscle organUBERON:000163090.69gold quality
heartUBERON:000094890.64gold quality
Brodmann (1909) area 9UBERON:001354090.33gold quality
cartilage tissueUBERON:000241890.31gold quality
biceps brachiiUBERON:000150790.29gold quality
mucosa of sigmoid colonUBERON:000499390.24gold quality
right adrenal glandUBERON:000123390.04gold quality
anterior cingulate cortexUBERON:000983589.94gold quality
skeletal muscle tissueUBERON:000113489.93gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-ANND-3yes5.87
E-MTAB-4850no234.44

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

8 targeting GLRX2, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-4778-3P99.9370.401818
HSA-MIR-3617-5P99.7569.411968
HSA-MIR-64199.7569.351975
HSA-MIR-4666B99.6468.691282
HSA-MIR-6853-3P99.3670.791558
HSA-MIR-371A-5P99.0866.511914
HSA-MIR-1255B-2-3P97.8067.04880
HSA-MIR-5196-3P97.5765.98979

Literature-anchored findings (GeneRIF, showing 22)

  • results suggest an important role for glutaredoxin 2 in protection and recovery from oxidative stress (PMID:14676218)
  • Grx1 and Grx2 were present in placenta extracts and in cell lysates prepared from tumor cell lines; however, the levels of Grx1 were at least 20 times higher than those of Grx2; Grx2 was not detected in plasma from healthy blood donors (PMID:15184054)
  • Lung cells can synthesize Grx2 mRNA and protein. (PMID:15297967)
  • characterization of Grx2 as an iron-sulfur center-containing member of the thioredoxin fold protein family (PMID:15917333)
  • Grx2 has a novel function as a peroxidase, accepting electrons both from GSH and TR. This unique property may play a role in protecting the mitochondria from oxidative damage. (PMID:17065220)
  • The iron-sulfur cluster is complexed by the two N-terminal active site thiols of two Grx2 monomers and two molecules of glutathione that are bound noncovalently to the proteins and in equilibrium with glutathione in solution. (PMID:17115894)
  • Eficence of an iron-sulfur cluster in which binding of the cluster inactivates the protein by sequestering active site residues and where loss of the cluster through changes in subcellular redox status creates a catalytically active protein. (PMID:17121859)
  • Human Grx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins. (PMID:17546662)
  • Grx2 is constitutively expressed in both neuron and glia in mouse and human brain including the neurons in human substantia nigra. (PMID:17961515)
  • Grx1 and Grx2 exhibit key catalytic similarities, including selectivity for protein-SSG substrates and a nucleophilic, double-displacement, monothiol mechanism exhibiting a strong commitment to catalysis. (PMID:18816065)
  • cluster signal of Grx2 is stable at positive potentials up to 0.5 V but that cluster destruction occurs readily when oxidative pulses in excess of this value are applied (PMID:19292455)
  • Studies indicate that the mechanism of Grx2 protection against H(2)O(2)-induced apoptosis is likely associated with its ability to preserve complex I. (PMID:20547138)
  • Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3. (PMID:20929858)
  • Exchange of [2Fe-2S] centers between glutaredoxin 2 and the cluster scaffold protein ISU, supports a direct link for glutaredoxin 2 and glutathione involvement in ISU promoted Fe-S cluster biosynthesis. (PMID:21437321)
  • These results suggest that Grx2a plays proliferative and anti-apoptotic roles under serum deprivation. (PMID:21735102)
  • Grx2 thiol redox regulation is essential for vertebrate embryonic development (PMID:22139372)
  • The Grx2 system could help to keep Trx2/1 reduced during an oxidative stress, thereby contributing to the anti-apoptotic signaling. (PMID:24295294)
  • Grx2 and Trx1 contribute significantly to neuronal integrity and could be clinically relevant in neuronal damage following perinatal asphyxia and other neuronal disorders. (PMID:25735211)
  • Study shows that Grx2 detoxifies *NO in mature oligodendrocytes and oligodendroglial precursor cellsvia the formation of dinitrosyl-iron-complexes, inhibiting the formation of harmful peroxynitrite and reducing subsequent oligodendroglial damage. Findings link inorganic biochemistry to neuroinflammation and identify glutaredoxin 2 as a protective factor against neuroinflammation-mediated myelin damage. (PMID:28618115)
  • GRX2 is important in the control of cardiac mitochondrial structure and function, and protects against human cardiac pathologies. (PMID:29101900)
  • By sensing the overall cellular redox conditions, mitochondrial Grx2 dimers become active monomers upon oxidative stress induced by sodium selenite with the consequent release of the iron-sulfur cluster, leading to activation of the intrinsic apoptotic pathway. (PMID:31168542)
  • Glutaredoxin 2 Protein (Grx2) as an Independent Prognostic Factor Associated with the Survival of Colon Adenocarcinoma Patients. (PMID:38256132)

Cross-species orthologs

5 orthologs

OrganismSymbolGene ID
danio_rerioglrx2ENSDARG00000100944
rattus_norvegicusGlrx2ENSRNOG00000003385
drosophila_melanogasterGrx1tFBGN0034658
drosophila_melanogasterGrx1FBGN0036820
caenorhabditis_elegansWBGENE00017340

Paralogs (2): GRXCR2 (ENSG00000204928), GRXCR1 (ENSG00000215203)

Protein

Protein identifiers

Glutaredoxin-2, mitochondrialQ9NS18 (reviewed: Q9NS18)

All UniProt accessions (1): Q9NS18

UniProt curated annotations — full annotation on UniProt →

Function. Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.

Subunit / interactions. Monomer; active form. Homodimer; inactive form. The homodimer is probably linked by 1 2Fe-2S cluster.

Subcellular location. Mitochondrion Nucleus.

Tissue specificity. Widely expressed. Expressed in brain, heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine, placenta and lung. Not expressed in peripheral blood leukocytes.

Activity regulation. The 2Fe-2S present in the homodimer leads to inactivation of the enzyme. The 2Fe-2S may serve as a redox sensor: the presence of one-electron oxidants or reductants leading to the loss of the 2Fe-2S cluster, subsequent monomerization and activation of the enzyme. Unlike other glutaredoxins, it is not inhibited by oxidation of structural Cys residues.

Miscellaneous. The absence of GLRX2 dramatically sensitizes cells to cell death induced by doxorubicin/adriamycin and phenylarsine oxide.

Similarity. Belongs to the glutaredoxin family.

Isoforms (2)

UniProt IDNamesCanonical?
Q9NS18-11, Grx2ayes
Q9NS18-22, Grx2b

RefSeq proteins (3): NP_001230328, NP_057150, NP_932066* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR002109GlutaredoxinDomain
IPR011899Glutaredoxin_euk/virDomain
IPR014025Glutaredoxin_subgrDomain
IPR036249Thioredoxin-like_sfHomologous_superfamily

Pfam: PF00462

UniProt features (30 total): helix 7, strand 5, binding site 5, mutagenesis site 4, sequence variant 2, modified residue 2, transit peptide 1, chain 1, disulfide bond 1, splice variant 1, domain 1

Structure

Experimental structures (PDB)

3 structures.

PDBMethodResolution (Å)
2HT9X-RAY DIFFRACTION1.9
2FLSX-RAY DIFFRACTION2.05
2CQ9SOLUTION NMR

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9NS18-F183.480.65

Functional residue map

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

Ligand- & substrate-binding residues (5): 68 (in inactive form); 74; 109; 121; 153 (in inactive form)

Post-translational modifications (2): 20, 77

Disulfide bonds (1): 77–80

Mutagenesis-validated functional residues (4):

PositionPhenotype
68abolishes absorption at 320 nm and 420 nm suggesting the loss of 2fe-2s-binding.
78specifically increases the specific activity but decreases affinity for glutathionylated substrates.
80strongly impairs enzymatic activity.
153abolishes absorption at 320 nm and 420 nm suggesting the loss of 2fe-2s-binding.

Function

Pathways and Gene Ontology

Reactome pathways

0 pathways

MSigDB gene sets: 129 (showing top): RODRIGUES_THYROID_CARCINOMA_POORLY_DIFFERENTIATED_UP, WEI_MYCN_TARGETS_WITH_E_BOX, JAZAG_TGFB1_SIGNALING_DN, ONKEN_UVEAL_MELANOMA_UP, GOBP_CELL_REDOX_HOMEOSTASIS, GOBP_AMIDE_METABOLIC_PROCESS, JAZAG_TGFB1_SIGNALING_VIA_SMAD4_UP, GOBP_RESPONSE_TO_ABIOTIC_STIMULUS, GOBP_GLUTATHIONE_METABOLIC_PROCESS, BASAKI_YBX1_TARGETS_UP, CUI_TCF21_TARGETS_2_DN, GOBP_MODIFIED_AMINO_ACID_METABOLIC_PROCESS, GOBP_RESPONSE_TO_REDOX_STATE, NAKAMURA_TUMOR_ZONE_PERIPHERAL_VS_CENTRAL_UP, GOBP_HOMEOSTATIC_PROCESS

GO Biological Process (9): regulation of DNA-templated transcription (GO:0006355), glutathione metabolic process (GO:0006749), apoptotic process (GO:0006915), response to temperature stimulus (GO:0009266), regulation of signal transduction (GO:0009966), cell differentiation (GO:0030154), DNA protection (GO:0042262), cell redox homeostasis (GO:0045454), response to redox state (GO:0051775)

GO Molecular Function (9): protein disulfide isomerase activity (GO:0003756), arsenate reductase (glutaredoxin) activity (GO:0008794), electron transfer activity (GO:0009055), protein-disulfide reductase activity (GO:0015035), glutathione disulfide oxidoreductase activity (GO:0015038), metal ion binding (GO:0046872), 2 iron, 2 sulfur cluster binding (GO:0051537), protein binding (GO:0005515), iron-sulfur cluster binding (GO:0051536)

GO Cellular Component (3): nucleus (GO:0005634), nucleoplasm (GO:0005654), mitochondrion (GO:0005739)

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
catalytic activity, acting on a protein2
disulfide oxidoreductase activity2
intracellular membrane-bounded organelle2
DNA-templated transcription1
regulation of gene expression1
regulation of RNA biosynthetic process1
modified amino acid metabolic process1
sulfur compound metabolic process1
programmed cell death1
apoptotic signaling pathway1
execution phase of apoptosis1
response to abiotic stimulus1
signal transduction1
regulation of cell communication1
regulation of signaling1
regulation of response to stimulus1
cellular developmental process1
DNA metabolic process1
cellular response to stress1
cellular homeostasis1
response to stimulus1
intramolecular oxidoreductase activity, transposing S-S bonds1
oxidoreductase activity, acting on phosphorus or arsenic in donors, disulfide as acceptor1
molecular_function1
cation binding1
iron-sulfur cluster binding1
binding1
metal cluster binding1
nuclear lumen1
cellular anatomical structure1
cytoplasm1

Protein interactions and networks

STRING

2157 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
GLRX2GLRX3O76003844
GLRX2TXNP10599769
GLRX2GLRX5Q86SX6766
GLRX2TXN2Q99757743
GLRX2TXNRD2Q9NNW7688
GLRX2GSRP00390649
GLRX2PRDX3P30048642
GLRX2PRDX5P30044604
GLRX2GPX4P36969547
GLRX2ISCUQ9H1K1537
GLRX2SOD1P00441528
GLRX2PRDX4Q13162526
GLRX2GPX2P18283519
GLRX2GPX3P22352517
GLRX2F5H3C5F5H3C5511

IntAct

8 interactions, top by confidence:

ABTypeScore
DCXRGLRX2psi-mi:“MI:0915”(physical association)0.560
GLRX2ELF5psi-mi:“MI:0915”(physical association)0.560
SFXN1HAX1psi-mi:“MI:2364”(proximity)0.270
GLRX2DCXRpsi-mi:“MI:0915”(physical association)0.000
GLRX2ELF5psi-mi:“MI:0915”(physical association)0.000

BioGRID (15): GLRX2 (Co-fractionation), GLRX2 (Co-fractionation), MDH2 (Co-fractionation), PITPNB (Co-fractionation), GLRX2 (Biochemical Activity), GLRX2 (Biochemical Activity), GLRX2 (Proximity Label-MS), ELF5 (Two-hybrid), DCXR (Two-hybrid), GLRX2 (Affinity Capture-MS), GLRX2 (Co-fractionation), GLRX2 (Co-fractionation), GLRX2 (Co-fractionation), GLRX2 (Co-fractionation), GLRX2 (Affinity Capture-Luminescence)

ESM2 similar proteins: A2ZVG7, A8J353, B4H303, B4NE93, B5DKJ8, F4KF14, O22993, O23403, O48529, O49078, O49196, O49292, O64903, O81027, O81263, P13272, P24493, P27626, P54150, P54151, P60315, Q00497, Q10BX9, Q38853, Q42805, Q42836, Q5NTH3, Q5NTH4, Q5RC53, Q5VRL3, Q6H6R9, Q7X7H9, Q8GY88, Q8SY96, Q8VXV7, Q8W4D6, Q944S1, Q94JS0, Q94LA4, Q9AT00

Diamond homologs: A0A7H0DN48, O36032, P0DOQ9, P0DOR0, P10575, P12309, P12864, P35754, P38068, P68690, P68691, P68692, P79764, Q32L67, Q5RC53, Q6AXW1, Q6RZN3, Q76ZV3, Q775X4, Q77TL9, Q80E01, Q8JLF5, Q8QMY9, Q8V2V1, Q923X4, Q9ESH6, Q9FVX1, Q9JVU9, Q9JY15, Q9NS18, Q9QUH0, Q9UTI2, B7ZFT1, O05957, O23417, O23419, O23420, O23421, O81187, O82255

SIGNOR signaling

0 interactions.

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance19
Likely benign1
Benign0

Top pathogenic / likely-pathogenic (0)

SpliceAI

607 predictions. Top by Δscore:

VariantEffectΔscore
1:193096760:CTGTT:Cacceptor_loss1.0000
1:193096761:T:Aacceptor_loss1.0000
1:193097580:TCA:Tdonor_loss1.0000
1:193097581:CA:Cdonor_loss1.0000
1:193097582:A:ACdonor_gain1.0000
1:193097582:ACAGT:Adonor_loss1.0000
1:193097583:C:CGdonor_gain1.0000
1:193097583:CA:Cdonor_gain1.0000
1:193097583:CAG:Cdonor_gain1.0000
1:193097583:CAGT:Cdonor_gain1.0000
1:193097583:CAGTT:Cdonor_gain1.0000
1:193097756:GTTTC:Gacceptor_gain1.0000
1:193097757:TTTC:Tacceptor_gain1.0000
1:193097759:TC:Tacceptor_gain1.0000
1:193097759:TCC:Tacceptor_loss1.0000
1:193097760:CC:Cacceptor_gain1.0000
1:193097760:CCT:Cacceptor_loss1.0000
1:193097761:C:CCacceptor_gain1.0000
1:193097761:CTGAA:Cacceptor_loss1.0000
1:193097762:T:Aacceptor_loss1.0000
1:193101131:CATCA:Cdonor_gain1.0000
1:193101135:A:ACdonor_gain1.0000
1:193101136:C:CCdonor_gain1.0000
1:193101136:CTCA:Cdonor_gain1.0000
1:193101137:TCA:Tdonor_loss1.0000
1:193101138:CAC:Cdonor_loss1.0000
1:193101139:A:ACdonor_gain1.0000
1:193101139:A:Tdonor_loss1.0000
1:193101140:C:CTdonor_gain1.0000
1:193101140:CT:Cdonor_gain1.0000

AlphaMissense

1068 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
1:193096743:A:TV126D0.993
1:193096745:A:CF125L0.993
1:193096745:A:TF125L0.993
1:193096747:A:GF125L0.993
1:193096749:A:TI124K0.993
1:193096758:A:TV121D0.992
1:193096683:A:GL146S0.991
1:193097727:A:GS73P0.990
1:193096749:A:CI124R0.988
1:193097704:A:CC80W0.988
1:193097728:G:CF72L0.987
1:193097728:G:TF72L0.987
1:193097730:A:GF72L0.987
1:193096755:G:TP122Q0.985
1:193097729:A:GF72S0.985
1:193096746:A:GF125S0.984
1:193097723:T:AK74I0.984
1:193096725:C:TG132E0.983
1:193097738:A:TV69E0.982
1:193096746:A:CF125C0.980
1:193096755:G:CP122R0.980
1:193097648:A:GL99P0.980
1:193097684:A:GF87S0.979
1:193097715:A:GC77R0.979
1:193096756:G:AP122S0.978
1:193097609:A:GL112P0.978
1:193097609:A:TL112H0.977
1:193097705:C:TC80Y0.977
1:193097732:A:TI71N0.977
1:193096701:A:GL140P0.976

dbSNP variants (sampled 300 via entrez): RS1000203072 (1:193107624 C>A,G,T), RS1000217073 (1:193101683 G>A), RS1000660422 (1:193096335 T>C), RS1000776735 (1:193103496 T>A,C), RS1000956560 (1:193103152 C>A,T), RS1001312213 (1:193107576 A>G), RS1001518021 (1:193102992 T>C,G), RS1001649998 (1:193096001 T>A,G), RS1002248546 (1:193101483 A>G), RS1002259628 (1:193106756 A>C,G), RS1002336274 (1:193098235 T>A,C), RS1002452439 (1:193097998 A>C), RS1002581982 (1:193104420 A>G), RS1002589853 (1:193105519 C>A,T), RS1002621029 (1:193099232 T>C)

Disease associations

OMIM: gene MIM:606820 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

0 associations (top):

Drugs & pharmacology

Drug and pharmacology data

Is drug target: no

PharmGKB: 1 entry (VIP=true, CPIC=false)

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
Valproic Acidaffects cotreatment, increases expression, affects expression7
trichostatin Aaffects cotreatment, increases expression3
methylmercuric chlorideincreases expression2
mercuric bromideincreases expression, affects cotreatment2
Panobinostataffects cotreatment, increases expression2
Benzo(a)pyreneincreases expression, increases methylation2
Cisplatindecreases expression, affects response to substance2
Phenylmercuric Acetateaffects cotreatment, increases expression2
Tobacco Smoke Pollutionaffects expression, increases expression2
aristolochic acid Iincreases expression1
bisphenol Aincreases expression1
potassium perchloratedecreases expression1
mono-(2-ethylhexyl)phthalateincreases expression1
sodium arseniteincreases expression1
potassium chromate(VI)affects cotreatment, decreases expression1
cupric chlorideincreases expression1
dibenzo(a,l)pyrenedecreases expression1
epigallocatechin gallateaffects cotreatment, decreases expression1
di-n-butylphosphoric acidaffects expression1
K 7174increases expression1
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamideaffects cotreatment, increases expression1
abrineincreases expression1
dorsomorphinaffects cotreatment, increases expression1
2-(1H-indazol-4-yl)-6-(4-methanesulfonylpiperazin-1-ylmethyl)-4-morpholin-4-ylthieno(3,2-d)pyrimidinedecreases expression, increases response to substance1
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)-2-furanyl)methylene)-4,5-dihydro-3-methyl-5-oxo-1H-pyrazol-1-yl)benzoic aciddecreases expression1
Resveratrolincreases expression1
Sunitinibdecreases expression1
Aerosolsdecreases expression1
Air Pollutantsdecreases expression, increases abundance1
Cannabidiolincreases expression1

Cellosaurus cell lines

1 cell lines: 1 cancer cell line

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

CellosaurusNameCategorySex
CVCL_B1SYAbcam HeLa GLRX2 KOCancer cell lineFemale

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.

No linked Atlas pages yet — the cross-entity mesh grows as the corpus expands.