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Article

Functional characterization of two novel parvulins in Trypanosoma brucei.

FEBS letters - 2 Jul 2010

Goh Jian Yuan, Lai Cheng-Yu, Tan Luuan Chin, Yang Daiwen, He Cynthia Y, Liou Yih-Cherng

Abstract excerpt

Parvulins belong to a family of peptidyl-prolyl cis/trans isomerases (PPIases) that catalyze the cis/trans conformations of prolyl-peptidyl bonds. Herein, we characterized two novel parvulins, TbPIN1 and TbPAR42, in Trypanosoma brucei. TbPIN1, a 115 amino-acid protein, contains a single PPIase domain but lacks the N-terminal WW domain. Using NMR spectroscopy, TbPIN1 was found to exhibit PPIase activity toward a...

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Identifiers

PMID: 20466001
DOI: 10.1016/j.febslet.2010.04.077

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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.

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