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A High Affinity Interaction of Plasminogen with Fibrin Is Not Essential for Efficient Activation by Tissue-type Plasminogen Activator

Fibrin (Fn) enhances plasminogen (Pg) activation by tissue-type plasminogen activator (tPA) by serving as a template onto which Pg and tPA assemble. To explore the contribution of the Pg/Fn interaction to Fn cofactor activity, Pg variants were generated and their affinities for Fn were determined us...

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書誌詳細
主要な著者: Kim, Paul Y., Tieu, Long D., Stafford, Alan R., Fredenburgh, James C., Weitz, Jeffrey I.
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Biochemistry and Molecular Biology 2012
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC3281636/
https://ncbi.nlm.nih.gov/pubmed/22187433
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.317719
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