The natural occurrence of human fibrinogen variants disrupting inter-chain disulfide bonds (AαCys36Gly, AαCys36Arg and AαCys45Tyr) confirms the role of N-terminal Aα disulfide bonds in protein assembly and secretion

Analyses of site-directed fibrinogen mutants expressed in several recombinant models have previously shown that both inter- and intra-chain disulfide bonds are critical for fibrinogen assembly and secretion. Four naturally occurring mutations on AαCys36 and AαCys45 residues are reported here to be a...

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Main Authors:	Michel Hanss, Catherine Pouymayou, Marie-Thérèse Blouch, Franck Lellouche, Patrick Ffrench, Robert Rousson, Jean-François Abgrall, Pierre-Emmanuel Morange, Florence Quélin, Philippe de Mazancourt
Format:	Artigo
Language:	Inglês
Published:	Ferrata Storti Foundation 2011-08-01
Series:	Haematologica
Online Access:	https://haematologica.org/article/view/6051
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