AKR1B1

Aldo-keto reductase family 1, member B1 (aldose reductase), also known as AKR1B1, is a human gene.

PBB_Summary
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summary_text = This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member catalyzes the reduction of a number of aldehydes, including the aldehyde form of glucose, and is thereby implicated in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. There are a few putative pseudogenes for this gene, and one of them has been confirmed and mapped to chromosome 3.cite web | title = Entrez Gene: AKR1B1 aldo-keto reductase family 1, member B1 (aldose reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=231| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Borhani DW, Harter TM, Petrash JM |title=The crystal structure of the aldose reductase.NADPH binary complex. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24841–7 |year= 1992 |pmid= 1447221 |doi=
*cite journal | author=Wilson DK, Bohren KM, Gabbay KH, Quiocho FA |title=An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. |journal=Science |volume=257 |issue= 5066 |pages= 81–4 |year= 1992 |pmid= 1621098 |doi=10.1126/science.1621098
*cite journal | author=Graham A, Heath P, Morten JE, Markham AF |title=The human aldose reductase gene maps to chromosome region 7q35. |journal=Hum. Genet. |volume=86 |issue= 5 |pages= 509–14 |year= 1991 |pmid= 1901827 |doi=10.1007/BF00194644
*cite journal | author=Graham A, Brown L, Hedge PJ, "et al." |title=Structure of the human aldose reductase gene. |journal=J. Biol. Chem. |volume=266 |issue= 11 |pages= 6872–7 |year= 1991 |pmid= 1901857 |doi=
*cite journal | author=Grundmann U, Bohn H, Obermeier R, Amann E |title=Cloning and prokaryotic expression of a biologically active human placental aldose reductase. |journal=DNA Cell Biol. |volume=9 |issue= 3 |pages= 149–57 |year= 1990 |pmid= 2111143 |doi=
*cite journal | author=Nishimura C, Matsuura Y, Kokai Y, "et al." |title=Cloning and expression of human aldose reductase. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 9788–92 |year= 1990 |pmid= 2112546 |doi=
*cite journal | author=Morjana NA, Lyons C, Flynn TG |title=Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. |journal=J. Biol. Chem. |volume=264 |issue= 5 |pages= 2912–9 |year= 1989 |pmid= 2492527 |doi=
*cite journal | author=Bohren KM, Bullock B, Wermuth B, Gabbay KH |title=The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. |journal=J. Biol. Chem. |volume=264 |issue= 16 |pages= 9547–51 |year= 1989 |pmid= 2498333 |doi=
*cite journal | author=Chung S, LaMendola J |title=Cloning and sequence determination of human placental aldose reductase gene. |journal=J. Biol. Chem. |volume=264 |issue= 25 |pages= 14775–7 |year= 1989 |pmid= 2504709 |doi=
*cite journal | author=Graham A, Hedge PJ, Powell SJ, "et al." |title=Nucleotide sequence of cDNA for human aldose reductase. |journal=Nucleic Acids Res. |volume=17 |issue= 20 |pages= 8368 |year= 1989 |pmid= 2510130 |doi=10.1093/nar/17.20.8368
*cite journal | author=Akagi Y, Kador PF, Kuwabara T, Kinoshita JH |title=Aldose reductase localization in human retinal mural cells. |journal=Invest. Ophthalmol. Vis. Sci. |volume=24 |issue= 11 |pages= 1516–9 |year= 1984 |pmid= 6417042 |doi=
*cite journal | author=Ko BC, Lam KS, Wat NM, Chung SS |title=An (A-C)n dinucleotide repeat polymorphic marker at the 5' end of the aldose reductase gene is associated with early-onset diabetic retinopathy in NIDDM patients. |journal=Diabetes |volume=44 |issue= 7 |pages= 727–32 |year= 1995 |pmid= 7789640 |doi=10.2337/diabetes.44.7.727
*cite journal | author=Wilson DK, Tarle I, Petrash JM, Quiocho FA |title=Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 21 |pages= 9847–51 |year= 1993 |pmid= 8234324 |doi=10.1073/pnas.90.21.9847
*cite journal | author=Tarle I, Borhani DW, Wilson DK, "et al." |title=Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110. |journal=J. Biol. Chem. |volume=268 |issue= 34 |pages= 25687–93 |year= 1994 |pmid= 8245005 |doi=
*cite journal | author=Robinson B, Hunsaker LA, Stangebye LA, Vander Jagt DL |title=Aldose and aldehyde reductases from human kidney cortex and medulla. |journal=Biochim. Biophys. Acta |volume=1203 |issue= 2 |pages= 260–6 |year= 1994 |pmid= 8268209 |doi=
*cite journal | author=Jaquinod M, Potier N, Klarskov K, "et al." |title=Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes. |journal=Eur. J. Biochem. |volume=218 |issue= 3 |pages= 893–903 |year= 1994 |pmid= 8281941 |doi=10.1111/j.1432-1033.1993.tb18445.x
*cite journal | author=Liu SQ, Bhatnagar A, Ansari NH, Srivastava SK |title=Identification of the reactive cysteine residue in human placenta aldose reductase. |journal=Biochim. Biophys. Acta |volume=1164 |issue= 3 |pages= 268–72 |year= 1993 |pmid= 8343525 |doi=
*cite journal | author=Nishimura C, Furue M, Ito T, "et al." |title=Quantitative determination of human aldose reductase by enzyme-linked immunosorbent assay. Immunoassay of human aldose reductase. |journal=Biochem. Pharmacol. |volume=46 |issue= 1 |pages= 21–8 |year= 1993 |pmid= 8347133 |doi=10.1016/0006-2952(93)90343-U
*cite journal | author=Sato S, Lin LR, Reddy VN, Kador PF |title=Aldose reductase in human retinal pigment epithelial cells. |journal=Exp. Eye Res. |volume=57 |issue= 2 |pages= 235–41 |year= 1993 |pmid= 8405190 |doi= 10.1006/exer.1993.1119
*cite journal | author=Ferraretto A, Negri A, Giuliani A, "et al." |title=Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress. |journal=Biochim. Biophys. Acta |volume=1175 |issue= 3 |pages= 283–8 |year= 1993 |pmid= 8435445 |doi=10.1016/0167-4889(93)90218-E

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