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Article

Functional conservation of phosphorylation-specific prolyl isomerases in plants.

The Journal of biological chemistry - 27 Apr 2001

Yao J L, Kops O, Lu P J, Lu K P

Abstract excerpt

The phosphorylation-specific peptidyl prolyl cis/trans isomerase (PPIase) Pin1 in humans and its homologues in yeast and animal species play an important role in cell cycle regulation. These PPIases consist of an NH(2)-terminal WW domain that binds to specific phosphoserine- or phosphothreonine-proline motifs present in a subset of phosphoproteins and a COOH-terminal PPIase domain that specifically isomerizes the...

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Identifiers

PMID: 11118438
DOI: 10.1074/jbc.M007006200

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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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Research trail→

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Functional conservation of phosphorylation-specific prolyl isomerases in plants.PMID 11118438Read ↗

The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins.Semantic proximity Read ↗

Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis.Semantic proximity Read ↗

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

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

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

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

Binding of phosphatase inhibitor-2 to prolyl isomerase Pin1 modifies specificity for mitotic phosphoproteins.Semantic proximity Read ↗

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

PIN1 is an E2F target gene essential for Neu/Ras-induced transformation of mammary epithelial cells.Semantic proximity Read ↗

Small molecules targeting Pin1 as potent anticancer drugsSemantic proximity Read ↗

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