The DOI matches its Crossref record; 93 of the 101 references it cites were found in a registry or an index.
17beta-hydroxysteroid dehydrogenase (HSD)/17-ketosteroid reductase (KSR) family; nomenclature and main characteristics of the 17HSD/KSR enzymes
Open accessAbstract
A number of enzymes possessing 17beta-hydroxysteroid dehydrogenase/17-ketosteroid reductase (17HSD/KSR) activities have been described and cloned, but their nomenclature needs specification. To clarify the present situation, descriptions of the eight cloned 17HSD/KSRs are given and guidelines for the classification of novel 17HSD/KSR enzymes are presented.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“There are at least 14 human 17HSD isoforms; these isoforms vary widely in size, structure, substrate specificity, cofactor utilization, and physiological functions (502).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [502]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The widespread tissue distribution and broad substrate specificity of 17HSD2 suggests that its role in human physiology is to protect tissues from excessive exposure to active steroid hormones by oxidation to inactive 17-ketosteroids (502).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [502]
Experimental — accuracy not yet measuredIn the citing paper
“Estrone undergoes 16α-hydroxylation and HSD17B1 catalyzed reduction, while 17β-estradiol only requires 16α-hydroxylation [[311], [312], [313], [314]].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [311]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
JOURNAL OF CLINICAL ENDOCRINOLOGY AND METABOLISM
Hoskins, R. G. (1953) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-13-4-473 · Cited by 3,780
Proceedings of the National Academy of Sciences, USA.
Ochoa, S. (1996) · Current Biology · doi:10.1016/s0960-9822(09)00431-x · Cited by 2,783
Molecular and cellular endocrinology
(1995) · Journal of Endocrinology · doi:10.1677/joe.0.147so19 · Cited by 1,986
Short-chain dehydrogenases/reductases (SDR)
Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzàlez‐Duarte, R., Jeffery, J., & Ghosh, D. (1995) · Biochemistry · doi:10.1021/bi00018a001 · Cited by 1,241
The Journal of Steroid Biochemistry and Molecular Biology
(2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(11)00143-9 · Cited by 1,233
Male pseudohermaphroditism caused by mutations of testicular 17β-hydroxysteroid dehydrogenase 3
Geissler, W. M., Davis, D. L., Wu, L., Bradshaw, K. D., Patel, S., Mendonca, B. B., Elliston, K. O., Wilson, J. D., Russell, D. W., & Andersson, S. (1994) · Nature Genetics · doi:10.1038/ng0594-34 · Cited by 570
The key role of 17β-hydroxysteroid dehydrogenases in sex steroid biology
Labrie, F., Luu-The, V., Lin, S.-X., Claude, L., Simard, J., Breton, R., & Bélanger, A. (1997) · Steroids · doi:10.1016/s0039-128x(96)00174-2 · Cited by 480
Self-citationJournal of Histochemistry and Cytochemistry
(1953) · Nature · doi:10.1038/172232b0 · Cited by 471
Molecular Endocrinology of Hydroxysteroid Dehydrogenases
Penning, T. M. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0302 · Cited by 439
Wu, L., Einstein, M., Geissler, W. M., Chan, H. K., Elliston, K. O., & Andersson, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31480-7 · Cited by 437
Research works printed but not linked: 2
- [57]57. Maxwell MM, Nearing J & Aziz N 1995 Ke 6 gene. Sequence and organization and aberrant regulation in murine polycystic kidney disease. Journal of Biological Chemistry 270 25213-25219.
- [64]64. Mustonen MVJ, Poutanen MH, Isomaa VV, Vihko PT & Vihko RK 1997b Cloning of mouse 17 -hydroxysteroid dehydrogenase type 2, and analysing expression of the mRNAs for types 1, 2, 3, 4 and 5 in mouse embryos and adult tissues. Biochemical Journal 325 199-205.
Cited by
Sorted by citations
Items 301–309 of 309
Ridden, A. D. (2013) · UC Research Repository (University of Canterbury) · doi:10.26021/6519
Metadata
- Authors
- Peltoketo, H., Luu-The, V, Simard, J., & Adamski, J.
- Affiliations
- University of Oulu (FI)
- Centre hospitalier de l'Université Laval (CA)
- Helmholtz Munich (DE)
- Venue
- Journal of Molecular Endocrinology
- Publisher
- Bioscientifica
- Published
- 1999-08-01
- Volume
- 23
- Issue
- 1
- Pages
- 1-11
- ISSN
- 0952-5041 (ISSN-L)
- 1479-6813
- OpenAlex
- W2116838171
- Semantic Scholar
- 09af775fcb4aa1e427eb5e859c6ee8074a5ccf34
- Cited by
- 302
- References
- 101
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 3 · 2021: 2 · 2020: 7 · 2019: 4 · 2018: 3 · 2017: 5 · 2016: 8 · 2015: 11 · 2014: 9 · 2013: 6 · 2012: 8
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Molecular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- World Health Organization
- Deutsche Forschungsgemeinschaft
- Medical Research Council Canada
- Medical Research Council
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Sexual Differentiation and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Keywords
- 17β-hydroxysteroid dehydrogenase, enzyme nomenclature, enzyme classification, steroid metabolism
- MeSH terms
- Animals, Humans, Terminology as Topic, 17-Hydroxysteroid Dehydrogenases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
