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Article

An allosteric disulfide bond is involved in enhanced activation of factor XI by protein disulfide isomerase.

Journal of thrombosis and haemostasis : JTH - 1 Nov 2016

Zucker M, Seligsohn U, Yeheskel A, Mor-Cohen R

Abstract excerpt

Essentials Reduction of three disulfide bonds in factor (F) XI enhances chromogenic substrate cleavage. We measured FXI activity upon reduction and identified a bond involved in the enhanced activity. Reduction of FXI augments FIX cleavage, probably by faster conversion of FXI to FXIa. The Cys362-Cys482 disulfide bond is responsible for FXI enhanced activation upon its reduction. SUMMARY: Background Reduction of...

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Identifiers

PMID: 27575053
DOI: 10.1111/jth.13488

Provenance

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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