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

Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution.

Journal of molecular biology - 26 Jan 2007

Behrsin C D, Bailey M L, Bateman K S, Hamilton K S, Wahl L M, Brandl C J, Shilton B H, Litchfield D W

Abstract excerpt

Pin1 is a phosphorylation-dependent member of the parvulin family of peptidyl-prolyl isomerases exhibiting functional conservation between yeast and man. To perform an unbiased analysis of the regions of Pin1 essential for its functions, we generated libraries of randomly mutated forms of the human Pin1 cDNA and identified functional Pin1 alleles by their ability to complement the Pin1 homolog Ess1 in...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Conserved Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis

Share to NIMA-Interacting Peptidylprolyl Isomerase

Share to Peptidylprolyl Isomerase

Share to Phosphorylation

Share to Protein Conformation

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 17113106
DOI: 10.1016/j.jmb.2006.10.078

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functionally important residues in the peptidyl-prolyl isomerase Pin1 revealed by unigenic evolution.PMID 17113106Read ↗

Activity and Affinity of Pin1 Variants.Semantic proximity Read ↗

The kingdom of the prolyl-isomerase Pin1: The structural and functional convergence and divergence of Pin1Semantic proximity Read ↗

The role of the master cancer regulator Pin1 in the development and treatment of cancerSemantic proximity Read ↗

The structural and functional role of the three tryptophan residues in Pin1.Semantic proximity Read ↗

Targeting carcinogenesis: A role for the prolyl isomerase Pin1?Semantic proximity Read ↗

Functional conservation of phosphorylation-specific prolyl isomerases in plants.Semantic proximity Read ↗

Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1.Semantic proximity Read ↗

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

Prolyl Isomerase Pin1 in Human Cancer: Function, Mechanism, and SignificanceSemantic proximity Read ↗

Pin1 acts catalytically to promote a conformational change in Cdc25.Semantic proximity Read ↗

Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13.Semantic proximity Read ↗

Oncogenic Hijacking of the PIN1 Signaling NetworkSemantic proximity Read ↗

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