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Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition

Tissue inhibitors of metalloproteinases (TIMPs) are natural inhibitors of matrix metalloproteinases (MMPs), enzymes that contribute to cancer and many inflammatory and degenerative diseases. The TIMP N-terminal domain binds and inhibits an MMP catalytic domain, but the role of the TIMP C-terminal do...

詳細記述

保存先:
書誌詳細
出版年:J Biol Chem
主要な著者: Raeeszadeh-Sarmazdeh, Maryam, Greene, Kerrie A., Sankaran, Banumathi, Downey, Gregory P., Radisky, Derek C., Radisky, Evette S.
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Biochemistry and Molecular Biology 2019
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC6579469/
https://ncbi.nlm.nih.gov/pubmed/31040180
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.008321
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