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

Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1.

Structure (London, England : 1993) - 1 Dec 2015

Wang Xingsheng, Mahoney Brendan J, Zhang Meiling, Zintsmaster John S, Peng Jeffrey W

Abstract excerpt

Pin1 is a modular peptidyl-prolyl isomerase specific for phosphorylated Ser/Thr-Pro (pS/T-P) motifs, typically within intrinsically disordered regions of signaling proteins. Pin1 consists of two flexibly linked domains: an N-terminal WW domain for substrate binding and a larger C-terminal peptidyl-prolyl isomerase (PPIase) domain. Previous studies showed that binding of phosphopeptide substrates to Pin1 could...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Amino Acid Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to NIMA-Interacting Peptidylprolyl Isomerase

Share to Peptidylprolyl Isomerase

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 26602185
DOI: 10.1016/j.str.2015.08.019
PMCID: PMC4670574

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1.PMID 26602185Read ↗

Activity and Affinity of Pin1 Variants.Semantic proximity Read ↗

Dynamic Allostery Modulates Catalytic Activity by Modifying the Hydrogen Bonding Network in the Catalytic Site of Human Pin1.Semantic proximity Read ↗

Extended Impact of Pin1 Catalytic Loop Phosphorylation Revealed by S71E Phosphomimetic.Semantic proximity Read ↗

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

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

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

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

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

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

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

Oncogenic Hijacking of the PIN1 Signaling NetworkSemantic proximity Read ↗

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

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