Evidence map›Paper›PMID 21051590›Full record

ReviewEndocrine reviews2011

The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders.

Walter L Miller, Richard J Auchus

Erratum issuedOpen access · bronzeAbstract readReview
In one paragraph

Review in Endocrine reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1,012 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
1,012citing papers in PubMed, 2 pooled it
62.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1,012 citing papers in PubMed, 2 syntheses or guidelines pooled it, 2,357 citations in OpenAlex.

  1. When bad turns good: a systematic review on cholesterol and LDL in longitudinal patient cohorts with Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Pooled it
  2. 17α-Hydroxylase/17,20-lyase Deficiency (17-OHD): A Meta-analysis of Reported Cases.The Journal of clinical endocrinology and metabolism · 2025
    Pooled it
  3. Trial
  4. Review
  5. Serum androgen profile of elite athletes.The Journal of clinical endocrinology and metabolism · 2026
    Article
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  15. Review
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  19. Approach to the patient: investigation of postmenopausal androgen excess.The Journal of clinical endocrinology and metabolism · 2026
    Review
  20. Article

952 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Walter L MillerDistinguished Professor of Pediatrics, University of California San Francisco, San Francisco, California 94143-0978, USA. wlmlab@ucsf.edu
Richard J Auchus
The University of Texas Southwestern Medical Center · USUniversity of California, San Francisco · US

Funding

Molecular Biology of Steroidogenic ProteinsR01DK037922 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MILLER, WALTER L. · 1987 to 2011
$2.8M
NIDDK NIH HHS R01 DK037922
6 · The paper itself

Abstract

Steroidogenesis entails processes by which cholesterol is converted to biologically active steroid hormones. Whereas most endocrine texts discuss adrenal, ovarian, testicular, placental, and other steroidogenic processes in a gland-specific fashion, steroidogenesis is better understood as a single process that is repeated in each gland with cell-type-specific variations on a single theme. Thus, understanding steroidogenesis is rooted in an understanding of the biochemistry of the various steroidogenic enzymes and cofactors and the genes that encode them. The first and rate-limiting step in steroidogenesis is the conversion of cholesterol to pregnenolone by a single enzyme, P450scc (CYP11A1), but this enzymatically complex step is subject to multiple regulatory mechanisms, yielding finely tuned quantitative regulation. Qualitative regulation determining the type of steroid to be produced is mediated by many enzymes and cofactors. Steroidogenic enzymes fall into two groups: cytochrome P450 enzymes and hydroxysteroid dehydrogenases. A cytochrome P450 may be either type 1 (in mitochondria) or type 2 (in endoplasmic reticulum), and a hydroxysteroid dehydrogenase may belong to either the aldo-keto reductase or short-chain dehydrogenase/reductase families. The activities of these enzymes are modulated by posttranslational modifications and by cofactors, especially electron-donating redox partners. The elucidation of the precise roles of these various enzymes and cofactors has been greatly facilitated by identifying the genetic bases of rare disorders of steroidogenesis. Some enzymes not principally involved in steroidogenesis may also catalyze extraglandular steroidogenesis, modulating the phenotype expected to result from some mutations. Understanding steroidogenesis is of fundamental importance to understanding disorders of sexual differentiation, reproduction, fertility, hypertension, obesity, and physiological homeostasis.

Indexed as

Adrenal GlandsAnimalsCholesterolElectron TransportFemaleGonadsHumansMaleMiceMitochondriaPhosphoproteinsPregnenoloneRatsSteroidogenic Acute Regulatory ProteinSteroidsCholesterolPhosphoproteinsPregnenoloneSteroidogenic Acute Regulatory ProteinSteroids

Identifiers

PMID21051590
PMCPMC3365799
OpenAlexW2009171847

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.