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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Detalhes bibliográficos
Main Authors: Hanss, Michel, Pouymayou, Catherine, Blouch, Marie-Thérèse, Lellouche, Franck, Ffrench, Patrick, Rousson, Robert, Abgrall, Jean-François, Morange, Pierre-Emmanuel, Quélin, Florence, de Mazancourt, Philippe
Formato: Artigo
Idioma:Inglês
Publicado em: Ferrata Storti Foundation 2011
Assuntos:
Brief Reports
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3148918/
https://ncbi.nlm.nih.gov/pubmed/21459789
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3324/haematol.2010.029801
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