Evidence map›Paper›PMID 21621639›Full record

ReviewBiochimica et biophysica acta2012

Physiological insights into all-trans-retinoic acid biosynthesis.

Joseph L Napoli

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 206 papers.

0numbers the graph read from it
0cells of the map it votes in
206citing papers in PubMed
–field-weighted citation impact
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

206 citing papers in PubMed.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Retinoic acid signaling and metabolism in heart failure.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Joseph L NapoliUniversity of California, Berkeley, CA, USA. jna@berkeley.edu

Funding

RETINAL DEHYDROGENASESR01AG013566 · NIA · UNIVERSITY OF CALIFORNIA BERKELEY · PI NAPOLI, JOSEPH L · 1995 to 2009
$2.9M
Ethanol effects on retinoic acid function in embryo hippocampusR01AA017927 · NIAAA · UNIVERSITY OF CALIFORNIA BERKELEY · PI NAPOLI, JOSEPH L · 2009 to 2015
$2.4M
Biosynthesis of 9-cis-retinoic acid/retinol homeostasisR01DK047839 · NIDDK · UNIVERSITY OF CALIFORNIA BERKELEY · PI NAPOLI, JOSEPH L · 1994 to 2007
$2.2M
RETINOID METABOLISMR01DK036870 · NIDDK · UNIVERSITY OF CALIFORNIA BERKELEY · PI NAPOLI, JOSEPH L · 1986 to 2007
$2.1M
Function of 9-cis-retinoic acidR01DK090522 · NIDDK · UNIVERSITY OF CALIFORNIA BERKELEY · PI NAPOLI, JOSEPH L · 2011 to 2014
$1.3M
NIAAA NIH HHS R01 AA017927NIA NIH HHS R01 AG013566NIDDK NIH HHS R01 DK036870NIDDK NIH HHS R01 DK047839NIDDK NIH HHS R01 DK090522
6 · The paper itself

Abstract

All-trans-retinoic acid (atRA) provides essential support to diverse biological systems and physiological processes. Epithelial differentiation and its relationship to cancer, and embryogenesis have typified intense areas of interest into atRA function. Recently, however, interest in atRA action in the nervous system, the immune system, energy balance and obesity has increased considerably, especially concerning postnatal function. atRA action depends on atRA biosynthesis: defects in retinoid-dependent processes increasingly relate to defects in atRA biogenesis. Considerable evidence indicates that physiological atRA biosynthesis occurs via a regulated process, consisting of a complex interaction of retinoid binding-proteins and retinoid recognizing enzymes. An accrual of biochemical, physiological and genetic data have identified specific functional outcomes for the retinol dehydrogenases, RDH1, RDH10, and DHRS9, as physiological catalysts of the first step in atRA biosynthesis, and for the retinal dehydrogenases RALDH1, RALDH2, and RALDH3, as catalysts of the second and irreversible step. Each of these enzymes associates with explicit biological processes mediated by atRA. Redundancy occurs, but seems limited. Cumulative data support a model of interactions among these enzymes with retinoid binding-proteins, with feedback regulation and/or control by atRA via modulating gene expression of multiple participants. The ratio apo-CRBP1/holo-CRBP1 participates by influencing retinol flux into and out of storage as retinyl esters, thereby modulating substrate to support atRA biosynthesis. atRA biosynthesis requires the presence of both an RDH and an RALDH: conversely, absence of one isozyme of either step does not indicate lack of atRA biosynthesis at the site. This article is part of a Special Issue entitled: Retinoid and Lipid Metabolism.

Indexed as

Alcohol OxidoreductasesAldehyde DehydrogenaseAnimalsHomeostasisHumansHydroxysteroid DehydrogenasesMiceRatsReceptors, Retinoic AcidRetinol-Binding ProteinsTretinoinAlcohol OxidoreductasesAldehyde DehydrogenaseHydroxysteroid DehydrogenasesReceptors, Retinoic AcidRetinol-Binding Proteinsretinol dehydrogenaseTretinoin

Identifiers

PMID21621639
PMCPMC3179567

What OpenQuestion holds

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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.