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Article

Selective modulation of protein C affinity for EPCR and phospholipids by Gla domain mutation.

The FEBS journal - 1 Jan 2005

Preston Roger J S, Villegas-Mendez Ana, Sun Yong-Hui, Hermida José, Simioni Paolo, Philippou Helen, Dahlbäck Björn, Lane David A

Abstract excerpt

Uniquely amongst vitamin K-dependent coagulation proteins, protein C interacts via its Gla domain both with a receptor, the endothelial cell protein C receptor (EPCR), and with phospholipids. We have studied naturally occurring and recombinant protein C Gla domain variants for soluble (s)EPCR binding, cell surface activation to activated protein C (APC) by the thrombin-thrombomodulin complex, and phospholipid...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 15634335
DOI: 10.1111/j.1432-1033.2004.04401.x

Genes

APC

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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.

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