UGDH Antibody

1. Data indicate that the A136M substitution in UDP-glucose dehydrogenase (hUGDH) stabilizes the hexamer. PMID: 27966912
2. study has identified several new proteins like RHOC, DLG5, UGDH, TMOD3 in addition to known chemoresistance associated proteins in non-small cell lung carcinoma. PMID: 26898345
3. UGDH protein level in osteoarthritis cartilage was much lower than in control cartilage. PMID: 25465897
4. UGDH displays hysteresis because of a slow isomerization from an inactive state (E*) to an active state (E). We show that the structure of E* constrains UGDH in a conformation that favors feedback inhibition at physiological pH. PMID: 25478983
5. Kinetic analysis of wild-type UGDH and hexamer T325A showed that upon increasing enzyme concentration, which favors the hexameric species, activity was decreased and exhibited cooperativity. Cooperative kinetics was not observed in obligate dimer T325D. PMID: 24145036
6. Mammalian UGDH displays hysteresis (observed as a lag in progress curves), indicating that the enzyme undergoes a slow transition from an inactive to an active state. Human UGDH is sensitive to product inhibition during the lag. PMID: 23363239
7. both missense mutations significantly reducing the ability of UGDH to provide precursors for cardiac cushion formation, which is essential to subsequent valve formation. PMID: 22815472
8. Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates. PMID: 22123821
9. An alternate crystal structure of human UGDH (hUGDH) in complex with UDP-glucose at 2.8 A resolution, is reported. PMID: 21984906
10. A structurally detailed model of UDP-alpha-D-glucose 6-dehydrogenase (UGDH) demonstrates hinge-bending motion that represents allosteric feedback inhibition and substrate-product exchange during the catalytic cycle. PMID: 21961565
11. high UGDH levels may underlie susceptibility of the orbit to localized overproduction of hyaluronan in Graves disease. PMID: 21576248
12. Structure and mechanism of human UDP-glucose 6-dehydrogenase. PMID: 21502315
13. An atypical allosteric mechanism in human UDP-alpha-D-glucose 6-dehydrogenase (UGDH) based on an easily acquired and identifiable structural attribute: packing defects in the protein core. PMID: 21595445
14. UGDH can regulate cell motility through the production of glycosaminoglycans PMID: 20691680
15. Results support the UGDH content in prostatic acini as a novel candidate biomarker that may complement the development of a multi-biomarker panel for detecting PC within the tumor adjacent field on a histologically normal biopsy specimen. PMID: 19676054
16. UGDH core promoter has a role in up- and down-regulation of UGDH after TGF-beta stimulation and in hypoxic conditions PMID: 12682078
17. role of Cys-276 as a catalytic residue; Lys-279 is likely to have a role in positioning active site residues and in maintaining the hexameric quaternary structure PMID: 15044486
18. Gly-13 plays an important role for efficient binding of NAD(+) to human UDP-glucose dehydrogenase PMID: 15247292
19. C276 plays an important role for efficient binding of UDP-glucose to hUGDH PMID: 15898741
20. Our results indicate that the region from nucleotide position -486 to -632 relative to the start of the small transcript contains positive regulatory elements that contribute to gene expression. PMID: 16002992
21. report the presence of an inhibitory cis-element in the distal region of the UGDH promoter that interacts with putative transcriptional repressors for the negative regulation of the UGDH gene PMID: 16495656
22. UGDH was purified and crystallized, and diffraction data proposes that the biological unit of UGDH is a tetramer. PMID: 17073734
23. Alteration of lysine 220 to alanine, histidine, or arginine significantly impaired enzyme function. PMID: 17209547
24. Results suggest that UGDH Ala222 and Ser233 play an important role in maintaining the hexameric structure and the reduced binding affinities for substrates are attributable to its altered subunit communication. PMID: 17927902
25. This demonstrates that the UGDH transcript and protein quantities, the enzyme activity, and glycosaminoglycan contents increase in LMP2A overexpressed human embryonic kidney 293 (HEK293) cells. PMID: 18717819
26. perturbation caused by the mutation of a residue at a considerably distant location from the oligomeric interfaces is preferentially distributed throughout specific sites, especially the large flexible regions in the UGDH structure PMID: 19358821

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HGNC: 12525

OMIM: 603370

KEGG: hsa:7358

STRING: 9606.ENSP00000319501

UniGene: Hs.572518