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Article

An engineered fibrinogen variant AαQ328,366P does not polymerise normally, but retains the ability to form α cross-links.

Thrombosis and haemostasis - 1 Feb 2013

Park Rojin, Ping Lifang, Song Jaewoo, Seo Joo-Young, Choi Tae-Youn, Choi Jong-Rak, Gorkun Oleg V, Lord Susan T

Abstract excerpt

A fibrin clot is stabilised through the formation of factor XIIIa-catalysed intermolecular ε-lysyl-γ-glutamyl covalent cross-links between α chains to form α polymers and between γ chains to form γ dimers. In a previous study we characterised fibrinogen Seoul II, a heterozygous dysfibrinogen in which a cross-linking acceptor site in Aα chain, Gln328, was replaced with Pro (AαQ328P). Following on the previous...

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PMID: 23224113
DOI: 10.1160/TH12-08-0609

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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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