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

Chlamydomonas Immunophilins and Parvulins: Survey and Critical Assessment of Gene Models

1 Feb 2005

Abstract excerpt

Cis-trans isomerization of the Xaa-Pro bond is an important step in protein folding and a critical determinant of protein structure ([27][1]). Peptidyl-prolyl cis-trans isomerases (PPIases or rotamases) belong to three unrelated families: FK506-binding proteins (FKBPs), cyclophilins, and parvulins.

Read the complete abstract on PubMed

Topics

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

Share to Peptidase Inhibition and Analysis
Share to Signaling Pathways in Disease
Share to Toxin Mechanisms and Immunotoxins

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

Source

Identifiers

PMID: 15701785
DOI: 10.1128/ec.4.2.230-241.2005

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

Chlamydomonas Immunophilins and Parvulins: Survey and Critical Assessment of Gene ModelsPMID 15701785Read ↗

Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic BacteriaSemantic proximity Read ↗

Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases.Semantic proximity Read ↗

Peptidyl-prolyl cis-trans isomerases, cyclophilin, FK506-binding protein, and ninaA: four of a kind.Semantic proximity Read ↗

Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in ArabidopsisSemantic proximity Read ↗

Vaccine potential of bacterial macrophage infectivity potentiator (MIP)-like peptidyl prolylcis/transisomerase (PPIase) proteinsSemantic proximity Read ↗

Genome-wide characterization of peptidyl-prolyl cis–trans isomerases in Penicillium and their regulation by salt stress in a halotolerant P. oxalicumSemantic proximity Read ↗

Microbial Peptidyl-Prolyl <i>cis</i> / <i>trans</i> Isomerases (PPIases): Virulence Factors and Potential Alternative Drug TargetsSemantic proximity Read ↗

Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseasesSemantic proximity Read ↗

Identification and study of Prolyl Oligopeptidases and related sequences in bacterial lineagesSemantic proximity Read ↗

From Drosophila to humans: reflections on the roles of the prolyl isomerases and chaperones, cyclophilins, in cell function and disease.Semantic proximity Read ↗

Identification and comparative analysis of sixteen fungal peptidyl-prolyl cis/trans isomerase repertoiresSemantic proximity Read ↗

Insights into peptidyl-prolyl cis–trans isomerase structure and function in immunocytesSemantic proximity Read ↗

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