ADH5 Antibody, Biotin conjugated

1. Data (including data from studies using knockout and transgenic mice) suggest that obesity and diabetes are accompanied by decreases in GSNOR activity in hepatocytes engendering nitrosative stress; obesity promotes S-nitrosylation of lysosomal proteins in liver, thereby impairing lysosomal enzyme activities and compromising autophagy. PMID: 29074597
2. GSNOR represents the prototype enzyme to disclose how denitrosylation plays a crucial role in tuning NO-bioactivity and how much it deeply impacts on cell homeostasis and human pathophysiology. (Review) PMID: 28533171
3. It was concluded that in HepG2 cells, ADH5 is a source of formate for de novo purine biosynthesis, especially during folate deficiency when folate-dependent formate production is limited. PMID: 28228507
4. GSNOR expression has different effect on neuronal viability in dependence on the stimulus applied, and plays opposite roles in SH-SY5Y models of Parkinson's disease and amyotrophic lateral sclerosis PMID: 26491229
5. ADH5 counteracts neuronal differentiation of neural stem cells and this effect can be reversed by pharmacological inhibition of ADH5. PMID: 24895131
6. study compared individuals occupationally exposed to formaldehyde and controls to effects of XRCC3 Thr241Met, ADH5 Val309Ile and Asp353Glu polymorphisms; ADH5 polymorphisms did not show significant association with genotoxicity biomarkers PMID: 23355119
7. N6022 binds in the GSNO binding pocket like a competitive inhibitor, although in kinetic assays it behaves with a mixed uncompetitive mode of inhibition (MOI) toward GSNO and a mixed competitive MOI toward formaldehyde adduct S-hydroxymethylglutathione. PMID: 22335564
8. biological significance of SNPs rs11568816, rs17028487 and rs13832 PMID: 21920416
9. Data suggest that GSNOR deficiency, through dysregulated S-nitrosylation, may promote hepatocellular carcinoma, possibly by inactivating a DNA repair system. PMID: 20371487
10. Significant associations were found however, for reactions to alcohol with a SNP in ADH5 (rs6827292, p = .001) and a SNP just upstream of ADH5 (rs6819724, p = .0007) that is in strong LD with rs6827292. PMID: 20158305
11. POZ domain of FBI1 represses transcription of ADH5. PMID: 12004059
12. The structural determination of apo, binary alcohol, and inhibitory ternary FDH complexes provides new insight into the enzyme's metal-assisted catalysis and substrate-binding properties. PMID: 12196016
13. Formation of a FDH-S-(hydroxymethyl)glutathione-NADH ternary complex causes movement of glutathione-dependent formaldehyde dehydrogenase catalytic domain toward the coenzyme-binding domain, and a change in active-site zinc coordination. PMID: 12484756
14. No evidence that alcohol dehydrogenase 3genotype modifies risk related to alcohol and lung cancer. PMID: 14608084
15. data suggest that genetic variation in S-nitrosoglutathione reductase (GSNOR) might play a role in asthma susceptibility PMID: 17543375
16. A statistically significant increase of class III alcohol dehydrogenase isoenzymes was found in the sera of pancreatic cancer patients. PMID: 18095160
17. GSNOR inhibitors to be novel tools for regulating nitric oxide bioactivity and assessing the role of SNOs in vivo. PMID: 19596685

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HGNC: 253

OMIM: 103710

KEGG: hsa:128

STRING: 9606.ENSP00000296412

UniGene: Hs.78989