The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
Bile acid biosynthesis
Abstract
To conclude, the last several years have seen a resurgence of interest in the biosynthesis of bile acids. This focus has come about due to the central roles that these molecules play in cholesterol and fat metabolism and due to recent advances in their chemistry, biochemistry, and molecular biology. The application of probes generated by these methodologies has begun to generate novel insight into bile acid metabolism, regulation, and genetics. The next several years should be equally exciting.
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In the citing paper
“AKR1D1 acts as the sole Δ4-3-ketosteroid-5β-reductase (steroid 5β-reductase) in humans”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [20]
In the citing paper
“This configuration introduces a 90° bend into the planar steroid and introduces amphipathic properties into the sterol which is essential for emulsification of fats and cholesterol”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [20]
In the citing paper
“AKR1D1, catalyzes the NADPH dependent reduction of the C4-C5 double bond in Δ4 ketosteroids to form A/B cis-ring junction”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [20]
In the citing paper
“Subsequent steps in bile acid biosynthesis include side chain oxidation and truncation, and conjugation of the bile acid with taurine or glycine”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [20]
In the citing paper
“AKR1D1 catalyzes 5β-reduction of bile acid precursors 7α-hydroxy-4-cholestene-3-one and 7α,12α-dihydroxy-4-cholestene-3-one to yield 7α-hydroxy-5β-cholestan-3-one and 7α,12α-dihydroxy-5β-cholestan-3-one, respectively and AKR1C4 catalyzes the further reduction of 3-keto group”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [20]
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Metadata
- Authors
- Russell, D. W., & Setchell, K. D. R.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Cincinnati Children's Hospital Medical Center (US)
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1992-05-01
- Volume
- 31
- Issue
- 20
- Pages
- 4737-4749
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2053916731
- Cited by
- 819
- References
- 104
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 11 · 2023: 27 · 2022: 14 · 2021: 24 · 2020: 24 · 2019: 17 · 2018: 15 · 2017: 27 · 2016: 15 · 2015: 15 · 2014: 19 · 2013: 22 · 2012: 21
- FWCI
- 28.69
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-20948, P01HL020948)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Keywords
- bile acid synthesis, bile acids, cholesterol metabolism, fat metabolism
- MeSH terms
- Animals, Bile Acids and Salts, Humans
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