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- W2157764784 abstract "Significance The blood protein von Willebrand factor (VWF) is required for platelets to stop bleeding at sites of injury, and the metalloprotease ADAMTS13 limits platelet adhesion by cleaving VWF only when flowing blood stretches it, especially within a growing thrombus. This feedback inhibition is essential because ADAMTS13 deficiency causes fatal microvascular thrombosis. How ADAMTS13 recognizes VWF so specifically is not understood. We now find that ADAMTS13 is folded roughly in half so that its distal domains inhibit the metalloprotease domain. VWF relieves this autoinhibition and promotes its own destruction by allosterically activating ADAMTS13. Thus, VWF is both a substrate and a cofactor in this critical regulatory process." @default.
- W2157764784 created "2016-06-24" @default.
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- W2157764784 date "2014-12-15" @default.
- W2157764784 modified "2023-10-11" @default.
- W2157764784 title "Allosteric activation of ADAMTS13 by von Willebrand factor" @default.
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- W2157764784 doi "https://doi.org/10.1073/pnas.1413282112" @default.
- W2157764784 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4284596" @default.
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