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Effects of Limiting Extension at the αIIb Genu on Ligand Binding to Integrin αIIbβ3

Structural data of integrin αIIbβ3 have been interpreted as supporting a model in which: 1) the receptor exists primarily in a “bent,” low affinity conformation on unactivated platelets and 2) activation induces an extended, high affinity conformation prior to, or following, ligand binding. Previous...

詳細記述

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書誌詳細
主要な著者: Blue, Robert, Li, Jihong, Steinberger, Jonathan, Murcia, Marta, Filizola, Marta, Coller, Barry S.
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Biochemistry and Molecular Biology 2010
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2878525/
https://ncbi.nlm.nih.gov/pubmed/20363746
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.107763
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