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Article

Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa.

Thrombosis and haemostasis - 3 Jul 2014

Wakabayashi H, Wintermute J M, Fay P J

Abstract excerpt

FVIIIa is labile due to the dissociation of A2 subunit. Previously, we introduced hydrophobic mutations at select A1/A2/A3 subunit interfaces yielding more stable FVIII(a) variants. Separately we showed that altering the sequence flanking the primary FXa cleavage site in FVIIIa (Arg336) yielded reduced rates of proteolytic inactivation of FVIIIa. In this study we prepared the FXa-cleavage resistant mutant...

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Source

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Identifiers

PMID: 24599523
DOI: 10.1160/TH13-10-0918
PMCID: PMC4470385

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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