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CBR1 protein, human
Known as:
carbonyl reductase 1, human
, Prostaglandin-E(2) 9-Reductase
, 15-Hydroxyprostaglandin Dehydrogenase
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Carbonyl reductase [NADPH] 1 (277 aa, ~30 kDa) is encoded by the human CBR1 gene. This protein plays a role in the reduction of carbonyl compounds.
National Institutes of Health
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Related topics
Related topics
11 relations
Broader (2)
Alcohol Oxidoreductases
carbonyl reductase (NADPH)
Arachidonic Acid Metabolism Pathway
CBR1 gene
Drug Metabolism Induction
Eicosanoid Modulation
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2017
Highly Cited
2017
Enzymatic synthesis of an ezetimibe intermediate using carbonyl reductase coupled with glucose dehydrogenase in an aqueous-organic solvent system.
Zhi-qiang Liu
,
Silin Dong
,
+5 authors
Yuguo Zheng
Bioresource Technology
2017
Corpus ID: 38623500
Review
2007
Review
2007
Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology.
U. Oppermann
Annual Review of Pharmacology and Toxicology
2007
Corpus ID: 13349196
Carbonyl groups are frequently found in endogenous or xenobiotic compounds. Reactive carbonyls, formed during lipid peroxidation…
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Highly Cited
2006
Highly Cited
2006
15-hydroxyprostaglandin dehydrogenase is a tumor suppressor of human breast cancer.
I. Wolf
,
J. O'kelly
,
+6 authors
H. Koeffler
Cancer Research
2006
Corpus ID: 27665723
Prostaglandin E(2) plays a growth-stimulatory role in breast cancer, and the rate-limiting enzyme in its synthesis…
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Review
2006
Review
2006
Multiplicity of mammalian reductases for xenobiotic carbonyl compounds.
T. Matsunaga
,
S. Shintani
,
A. Harã
Drug Metabolism and Pharmacokinetics
2006
Corpus ID: 25388312
A variety of carbonyl compounds are present in foods, environmental pollutants, and drugs. These xenobiotic carbonyl compounds…
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Review
2006
Review
2006
NAD+-linked 15-hydroxyprostaglandin dehydrogenase: structure and biological functions.
H. Tai
,
H. Cho
,
M. Tong
,
Y. Ding
Current pharmaceutical design
2006
Corpus ID: 45328903
NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase (15-PGDH) catalyzes the oxidation of 15(S)-hydroxyl group of prostaglandins…
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Highly Cited
1997
Highly Cited
1997
Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family.
N. Tanaka
,
T. Nonaka
,
M. Nakanishi
,
Y. Deyashiki
,
A. Harã
,
Y. Mitsui
Structure
1997
Corpus ID: 9255697
Highly Cited
1995
Highly Cited
1995
Purification and partial characterization of an aldo-keto reductase from Saccharomyces cerevisiae
A. Kuhn
,
C. van Zyl
,
A. van Tonder
,
B. Prior
Applied and Environmental Microbiology
1995
Corpus ID: 25633386
A cytosolic aldo-keto reductase was purified from Saccharomyces cerevisiae ATCC 26602 to homogeneity by affinity chromatography…
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Highly Cited
1995
Highly Cited
1995
Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase and aldehyde reductase of human liver.
Y. Miyabe
,
Y. Deyashiki
,
+7 authors
Kazuya Matsuura
Biochemical Pharmacology
1995
Corpus ID: 35962937
Highly Cited
1992
Highly Cited
1992
Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase.
Minoru Tanaka
,
S. Ohno
,
S. Adachi
,
S. Nakajin
,
M. Shinoda
,
Yoshitaka Nagahama
Journal of Biological Chemistry
1992
Corpus ID: 43839812
Highly Cited
1981
Highly Cited
1981
Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase.
B. Wermuth
Journal of Biological Chemistry
1981
Corpus ID: 23393981
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