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

Identification of Eukaryotic Parvulin Homologues: A New Subfamily of Peptidylprolyl cis–trans Isomerases

1 Jun 1999

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Galectins and Cancer Biology
Share to Peptidase Inhibition and Analysis
Share to Signaling Pathways in Disease

Source

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

Identifiers

PMID: 10364457
DOI: 10.1006/bbrc.1999.0828

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

Identification of Eukaryotic Parvulin Homologues: A New Subfamily of Peptidylprolyl cis–trans IsomerasesPMID 10364457Read ↗

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

Identification and comparative analysis of the peptidyl‐prolyl <i>cis/trans</i> isomerase repertoires of <i>H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe</i>Semantic proximity Read ↗

Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiationSemantic proximity Read ↗

A novel plant peptidyl-prolyl-cis-trans-isomerase (PPIase): cDNA cloning, structural analysis, enzymatic activity and expressionSemantic proximity Read ↗

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

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

Parvulin (Par14), a Peptidyl-Prolyl cis-trans Isomerase, Is a Novel rRNA Processing Factor That Evolved in the Metazoan LineageSemantic proximity Read ↗

Confirmation of the existence of a third family among peptidyl‐prolyl <i>cis/trans</i> isomerases Amino acid sequence and recombinant production of parvulinSemantic proximity Read ↗

Pin1 and Par14 Peptidyl Prolyl Isomerase Inhibitors Block Cell ProliferationSemantic proximity Read ↗

Biological Function of Pin1 in Vivo and Its Inhibitors for Preclinical Study: Early Development, Current Strategies, and Future DirectionsSemantic proximity Read ↗

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

Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14.Semantic proximity Read ↗

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