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

Proline isomerases function during heat shock.

Proceedings of the National Academy of Sciences of the United States of America - 15 Jun 1993

Sykes K, Gething M J, Sambrook J

Abstract excerpt

The cyclophilins (CYPs) and FK506 binding proteins (FKBPs) are two families of distinct proline isomerases that are targets for a number of clinically important immunosuppressive drugs. Members of both families catalyze cis/trans isomerization of peptidyl-prolyl bonds, which can be a rate-limiting step during protein folding in vitro and in vivo. We demonstrate in Saccharomyces cerevisiae that heat shock causes a...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Base Sequence
Share to Cloning, Molecular

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

Share to Genotype

Share to Kinetics

Share to Molecular Sequence Data

Share to Promoter Regions, Genetic

Share to RNA, Messenger

Source

Open in PubMed Open full text

Identifiers

PMID: 7685914
DOI: 10.1073/pnas.90.12.5853
PMCID: PMC46821

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

Proline isomerases function during heat shock.PMID 7685914Read ↗

Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation.Semantic proximity Read ↗

Hmo1p, a high mobility group 1/2 homolog, genetically and physically interacts with the yeast FKBP12 prolyl isomerase.Semantic proximity Read ↗

Functions of FKBP12 and mitochondrial cyclophilin active site residues in vitro and in vivo in Saccharomyces cerevisiae.Semantic proximity Read ↗

Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae.Semantic proximity Read ↗

Cold Shock Induces the Synthesis of Stress Proteins in Human KeratinocytesSemantic proximity Read ↗

Cyclophilin A and FKBP12 Interact with YY1 and Alter Its Transcriptional ActivitySemantic proximity Read ↗

Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.Semantic proximity Read ↗

Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD.Semantic proximity Read ↗

Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function.Semantic proximity Read ↗

The yeast FKS1 gene encodes a novel membrane protein, mutations in which confer FK506 and cyclosporin A hypersensitivity and calcineurin-dependent growth.Semantic proximity Read ↗

Mouse FKBP23 mediates conformer-specific functions of BiP by catalyzing Pro117 cis/trans isomerization.Semantic proximity Read ↗

Insights from yeast into whether the inhibition of heat shock transcription factor (Hsf1) by rapamycin can prevent the Hsf1 activation that results from treatment with an Hsp90 inhibitor.Semantic proximity Read ↗

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