Biology:SORD
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Sorbitol dehydrogenase is an enzyme that in humans is encoded by the SORD gene.[1][2]
References
- ↑ "Structural organization of the human sorbitol dehydrogenase gene (SORD)". Genomics 26 (1): 55–62. Jul 1995. doi:10.1016/0888-7543(95)80082-W. PMID 7782086. https://zenodo.org/record/1258603.
- ↑ "Entrez Gene: SORD sorbitol dehydrogenase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6652.
Further reading
- "Sorbitol dehydrogenase: structure, function and ligand design.". Curr. Med. Chem. 11 (4): 465–76. 2004. doi:10.2174/0929867043455927. PMID 14965227.
- "Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme.". Eur. J. Biochem. 186 (3): 543–50. 1990. doi:10.1111/j.1432-1033.1989.tb15240.x. PMID 2691249.
- "Aldose metabolism in developing human fetal brain and liver.". Experientia 40 (12): 1420–2. 1985. doi:10.1007/BF01951922. PMID 6439573.
- "Cloning, sequencing, and determination of the sites of expression of mouse sorbitol dehydrogenase cDNA.". Eur. J. Biochem. 230 (3): 1059–65. 1995. doi:10.1111/j.1432-1033.1995.tb20656.x. PMID 7601136.
- "The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization.". Genomics 21 (2): 354–8. 1994. doi:10.1006/geno.1994.1276. PMID 8088829.
- "Membrane-bound sorbitol dehydrogenase in human red blood cells. Studies in normal subjects and in enzyme-deficient subjects with congenital cataracts.". J. Inherit. Metab. Dis. 16 (1): 67–72. 1993. doi:10.1007/BF00711317. PMID 8487505.
- "Identification and characterisation of a sequence related to human sorbitol dehydrogenase.". Eur. J. Biochem. 245 (3): 760–7. 1997. doi:10.1111/j.1432-1033.1997.00760.x. PMID 9183016.
- "Structural and evolutionary characterization of the human sorbitol dehydrogenase gene duplication.". Mamm. Genome 9 (12): 1042–8. 1999. doi:10.1007/s003359900922. PMID 9880675.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Expression, purification and preliminary crystallographic analysis of human sorbitol dehydrogenase.". Acta Crystallogr. D 59 (Pt 3): 558–60. 2003. doi:10.1107/S0907444903000441. PMID 12595725.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. 2004. doi:10.1038/nbt810. PMID 12665801.
- "X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase.". Structure 11 (9): 1071–85. 2004. doi:10.1016/S0969-2126(03)00167-9. PMID 12962626.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin.". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. 2005. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Catalytic mechanism of Zn2+-dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu154-->Cys forms of yeast xylitol dehydrogenase". Biochem. J. 404 (3): 421–9. 2007. doi:10.1042/BJ20061384. PMID 17343568.
External links
- Overview of all the structural information available in the PDB for UniProt: Q00796 (Sorbitol dehydrogenase) at the PDBe-KB.