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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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| 主要な著者: | , , , , , , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
Ferrata Storti Foundation
2011
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| 主題: | |
| オンライン･アクセス: | 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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