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Article

Prevalent overexpression of prolyl isomerase Pin1 in human cancers.

The American journal of pathology - 1 May 2004

Bao Lere, Kimzey Amy, Sauter Guido, Sowadski Janusz M, Lu Kun Ping, Wang Da-Gong

Abstract excerpt

Phosphorylation of proteins on serine or threonine residues preceding proline (pSer/Thr-Pro) is a major regulatory mechanism in cell proliferation and transformation. Interestingly, the pSer/Thr-Pro motifs in proteins exist in two distinct cis and trans conformations, whose conversion rate is normally reduced on phosphorylation, but is catalyzed specifically by the prolyl isomerase Pin1. Pin1 can catalytically...

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Identifiers

PMID: 15111319
DOI: 10.1016/S0002-9440(10)63731-5
PMCID: PMC1615639

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

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Prevalent overexpression of prolyl isomerase Pin1 in human cancers.PMID 15111319Read ↗

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

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Oncogenic Hijacking of the PIN1 Signaling NetworkSemantic proximity Read ↗

Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function.Semantic proximity Read ↗

Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis.Semantic proximity Read ↗

Targeting Pin1 for Modulation of Cell Motility and Cancer TherapySemantic proximity Read ↗

A novel functional variant (-842G>C) in the PIN1 promoter contributes to decreased risk of squamous cell carcinoma of the head and neck by diminishing the promoter activity.Semantic proximity Read ↗

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