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

Crosstalk of prolyl isomerases, Pin1/Ess1, and cyclophilin A.

Biochemical and biophysical research communications - 23 Nov 2001

Fujimori F, Gunji W, Kikuchi J, Mogi T, Ohashi Y, Makino T, Oyama A, Okuhara K, Uchida T, Murakami Y

Abstract excerpt

Previous studies have indicated that Ess1/Pin1, a gene in the parvulin family of peptidyl-prolyl isomerases (PPIases), plays an important role in regulating the G(2)/M transition of the cell cycle by binding cell-cycle-regulating proteins in eukaryotic cells. Although the ess1 gene has been consi...

Read the complete abstract on PubMed

Topics

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

Share to Cell Cycle
Share to Cyclophilin A
Share to DNA, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to G1 Phase

Share to Genes, Fungal

Share to NIMA-Interacting Peptidylprolyl Isomerase

Share to Peptidylprolyl Isomerase

Share to RNA, Fungal

Source

Identifiers

PMID: 11708797
DOI: 10.1006/bbrc.2001.5925

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-11708797-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crosstalk of prolyl isomerases, Pin1/Ess1, and cyclophilin A.PMID 11708797Read ↗

The Ess1 prolyl isomerase is required for growth and morphogenetic switching in Candida albicans.Semantic proximity Read ↗

The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery.Semantic proximity Read ↗

Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G(0) arrest.Semantic proximity Read ↗

The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.Semantic proximity Read ↗

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

Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.Semantic proximity Read ↗

The Ess1 prolyl isomerase is dispensable for growth but required for virulence in Cryptococcus neoformans.Semantic proximity Read ↗

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

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

Prolyl isomerase Pin1 in metabolic reprogramming of cancer cellsSemantic proximity Read ↗

A role for Pin1 in mammalian germ cell development and spermatogenesis.Semantic proximity Read ↗

Cyclophilin A peptidyl-prolyl isomerase activity promotes ZPR1 nuclear export.Semantic proximity Read ↗

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