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Control of VWF A2 domain stability and ADAMTS13 access to the scissile bond of full-length VWF
Rheological shear forces in the blood trigger von Willebrand factor (VWF) unfolding which exposes the Y1605-M1606 scissile bond within the VWF A2 domain for cleavage by ADAMTS13. The VWF A2 domain contains 2 structural features that provide it with stability: a vicinal disulphide bond and a Ca(2+)-b...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
American Society of Hematology
2014
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3990914/ https://ncbi.nlm.nih.gov/pubmed/24558203 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1182/blood-2013-11-538173 |
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