Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization of truncated mutants of human microsomal short-chain dehydrogenase/reductase RoDH-4.

Chemico-biological interactions - 1 Feb 2003

Belyaeva Olga V, Chetyrkin Sergei V, Kedishvili Natalia Y

Abstract excerpt

Human NAD(+)-dependent microsomal short-chain dehydrogenase/reductase RoDH-4 oxidizes all-trans-retinol, 13-cis-retinol and 3alpha-hydroxysteroids to corresponding retinaldehydes and 3-ketones. RoDH-4 behaves as an integral membrane protein, but its topology in the membrane is not known. Analysis of RoDH-4 polypeptide using algorithms for secondary structure predictions suggests that RoDH-4 contains four...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alcohol Oxidoreductases
Share to Catalysis
Share to DNA Primers

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Microsomes

Share to Plasmids

Share to Recombinant Proteins

Share to Spodoptera

Share to Subcellular Fractions

Source

Identifiers

PMID: 12604214
DOI: 10.1016/s0009-2797(02)00181-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of truncated mutants of human microsomal short-chain dehydrogenase/reductase RoDH-4.PMID 12604214Read ↗

Elements in the N-terminal signaling sequence that determine cytosolic topology of short-chain dehydrogenases/reductases. Studies with retinol dehydrogenase type 1 and cis-retinol/androgen dehydrogenase type 1.Semantic proximity Read ↗

Molecular cloning and expression analysis of a new gene for short-chain dehydrogenase/reductase 9.Semantic proximity Read ↗

Gene structure and minimal promoter of mouse rdh1.Semantic proximity Read ↗

Characterization of key residues and membrane association domains in retinol dehydrogenase 10.Semantic proximity Read ↗

Structural Insights into the Drosophila melanogaster Retinol Dehydrogenase, a Member of the Short-Chain Dehydrogenase/Reductase Family.Semantic proximity Read ↗

Short‐chain dehydrogenase/reductase (SDR) relationships: A large family with eight clusters common to human, animal, and plant genomesSemantic proximity Read ↗

Redundant and unique roles of retinol dehydrogenases in the mouse retinaSemantic proximity Read ↗

Structure–function of human 3α-hydroxysteroid dehydrogenases: genes and proteinsSemantic proximity Read ↗

Biosynthesis of 9-cis-retinoic acid in vivo. The roles of different retinol dehydrogenases and a structure-activity analysis of microsomal retinol dehydrogenases.Semantic proximity Read ↗

Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde.Semantic proximity Read ↗

The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis.Semantic proximity Read ↗

Evidence that proteosome inhibitors and chemical chaperones can rescue the activity of retinol dehydrogenase 12 mutant T49M.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.