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

R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays.

FEBS letters - 29 Jan 1999

Scholz C, Maier P, Dolinski K, Heitman J, Schmid F X

Abstract excerpt

Previously we reported that the R73A and H144Q variants of the yeast cyclophilin Cpr3 were virtually inactive in a protease-coupled peptide assay, but retained activity as catalysts of a proline-limited protein folding reaction [Scholz, C. et al. (1997) FEBS Lett. 414, 69-73]. A reinvestigation revealed that in fact these two mutations strongly decrease the prolyl isomerase activity of Cpr3 in both the peptide...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Chromatography
Share to Chymotrypsin

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

Share to Circular Dichroism

Share to Cyclosporine

Share to Histidine

Share to Peptidylprolyl Isomerase

Share to Tacrolimus

Source

Identifiers

PMID: 10025965
DOI: 10.1016/s0014-5793(98)01735-9

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

R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays.PMID 10025965Read ↗

Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate.Semantic proximity Read ↗

Yeast cyclophilin-related gene encodes a nonessential second peptidyl-prolyl cis-trans isomerase associated with the secretory pathway.Semantic proximity Read ↗

Retarded protein folding of the human Z-type α₁-antitrypsin variant is suppressed by Cpr2p.Semantic proximity Read ↗

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

[Correlation between structure and function of peptidyl-prolyl isomerase].Semantic proximity Read ↗

A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding.Semantic proximity Read ↗

The unfolded-protein-response element discriminates misfolding induced by different mutant pro-sequences of yeast carboxypeptidase Y.Semantic proximity Read ↗

The proline-rich motif of the proDer p 3 allergen propeptide is crucial for protease-protease interaction.Semantic proximity Read ↗

Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions.Semantic proximity Read ↗

Characterization of folding intermediates using prolyl isomerase.Semantic proximity Read ↗

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

Use of CPY and its derivatives to study protein quality control in various cell compartments.Semantic proximity Read ↗

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