A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid (Q28575114)

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English	A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid	scientific journal article

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scholarly article

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PubMed

PubMed publication ID

7832787

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31 January 2017

title

A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid (English)

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PubMed

PubMed publication ID

7832787

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31 January 2017

main subject

tretinoin

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author name string

J. Labrecque

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1

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PubMed

PubMed publication ID

7832787

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31 January 2017

F. Dumas

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2

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PubMed

PubMed publication ID

7832787

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31 January 2017

A. Lacroix

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3

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PubMed

PubMed publication ID

7832787

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31 January 2017

P. V. Bhat

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4

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PubMed

PubMed publication ID

7832787

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31 January 2017

language of work or name

English

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publication date

15 January 1995

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PubMed

PubMed publication ID

7832787

retrieved

31 January 2017

published in

Biochemical Journal

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PubMed

PubMed publication ID

7832787

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31 January 2017

volume

305 ( Pt 2)

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PubMed

PubMed publication ID

7832787

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31 January 2017

page(s)

681–684

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PubMed

PubMed publication ID

7832787

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31 January 2017

cites work

Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes

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The visual cycle operates via an isomerase acting on all-trans retinol in the pigment epithelium

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17 March 2017

Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro

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Identification of a receptor for the morphogen retinoic acid

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Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats

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A third human retinoic acid receptor, hRAR-gamma

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Nuclear receptor that identifies a novel retinoic acid response pathway

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Characterization of three RXR genes that mediate the action of 9-cis retinoic acid

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PubMed Central

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9-cis retinoic acid is a high affinity ligand for the retinoid X receptor

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9-Cis retinoic acid stereoisomer binds and activates the nuclear receptor RXRα

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A human retinoic acid receptor which belongs to the family of nuclear receptors

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Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme

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Evidence for a lecithin-retinol acyltransferase activity in the rat small intestine

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Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine

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Isolation and characterization of a cytosolic aldehyde dehydrogenase-encoding cDNA from mouse liver

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9-cis-retinoic acid is a natural antagonist for the retinoic acid receptor response pathway

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Isoelectric focusing studies of aldehyde dehydrogenases from mouse tissues: variant phenotypes of liver, stomach and testis isozymes.

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Properties of retinal-oxidizing enzyme activity in rat kidney

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Specificity of cellular retinol-binding protein for compounds with vitamin A activity

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Purification and partial characterization of a rat kidney aldehyde dehydrogenase that oxidizes retinal to retinoic acid

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27 November 2018

Radioimmunochemical determination of cellular retinol- and cellular retinoic acid-binding proteins in cytosols of rat tissues

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27 November 2018

Effect of 2-alkanols on the separation of geometric isomers of retinol in non-aqueous high-performance liquid chromatography

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7832787

retrieved

12 December 2020

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Rat liver aldehyde dehydrogenase. II. Isolation and characterization of four inducible isozymes

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Identification and spatial distribution of retinoids in the developing chick limb bud

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Binding specificities of cellular retinol-binding protein and cellular retinol-binding protein, type II

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Enzymatic oxidation of all-trans retinal to retinoic acid in rat tissues

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Esterification by rat liver microsomes of retinol bound to cellular retinol-binding protein

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Isoenzymes of alcohol dehydrogenase in retinoid metabolism

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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inferred from PubMed ID database lookup

Holocellular retinol binding protein as a substrate for microsomal retinal synthesis

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Purification of retinol dehydrogenase from bovine retinal rod outer segments

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Effects of retinoic acid on the concentrations of radioactive metabolites of retinol in tissues of rats maintained on a retinol-deficient diet

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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The catalytic specificity of liver alcohol dehydrogenase: vitamin A alcohol and vitamin A aldehyde activities

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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A gas-liquid solid phase peptide and protein sequenator

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

based on heuristic

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Identification of the endogenous retinoids associated with three cellular retinoid-binding proteins from bovine retina and retinal pigment epithelium

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7832787

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12 December 2020

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Identifiers

DOI

10.1042/BJ3050681

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2913035

OpenCitations bibliographic resource ID

2913035

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2913035

PMC publication ID

1136415

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PubMed publication ID

7832787

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2913035

ResearchGate publication ID

15366009

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