Short CommunicationMapping of a Novel Human Carbonyl Reductase, CBR3, and Ribosomal Pseudogenes to Human Chromosome 21q22.2☆
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Cited by (35)
Long non-coding RNA: A newly deciphered "code" in prostate cancer
2016, Cancer LettersRegulation of human carbonyl reductase 1 (CBR1, SDR21C1) gene by transcription factor Nrf2
2013, Chemico-Biological InteractionsExpression of human carbonyl reductase 3 (CBR3; SDR21C2) is inducible by pro-inflammatory stimuli
2012, Biochemical and Biophysical Research CommunicationsCitation Excerpt :So far, three carbonyl reductases (CBRs) have been identified in humans (CBR1 [SDR21C1], CBR3 [SDR21C2] and CBR4 [SDR45C1]) all of which belong to the short-chain dehydrogenase/reductase (SDR) superfamily [2]. Since the identification of CBR3 in 1998 [3] some progress has been made with regard to its tissue-specific distribution, but still the understanding of its molecular function is incomplete [4]. Although being considered an enzyme in the reductive metabolism of anthracyclines such as doxorubicin and daunorubicin [5,6], the poor catalytic efficiencies for other tested carbonyl compounds imply that the expected function of CBR3 in xenobiotic carbonyl metabolism is very unlikely [7,8].
Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis
2009, Chemico-Biological InteractionsCitation Excerpt :The regulation of CBR1 is described in Ref. [18]. In contrast, CBR3 was discovered only recently, its gene has been identified in 1998 [19] and its physiological role is still unknown. Thanks to the availability of experimentally determined structures of the enzymes, the comparison of the catalytic clefts could shed light on the different substrate specificity.
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Sequence data from this article have been deposited with the DDBJ, EMBL, and GenBank Data Libraries under Accession Nos. AB003151 and AB004848–AB004854.
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