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A molten globule intermediate of the Von Willebrand Factor A1 domain firmly tethers platelets under shear flow
Clinical mutations in patients diagnosed with Type 2A von Willebrand disease (vWD) have been identified that break the single disulfide bond linking N- and C-termini in the vWF A1 domain. We have modeled the effect of these mutations on the disulfide-bonded structure of A1 by reducing and carboxy-am...
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| Hoofdauteurs: | , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2013
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4006108/ https://ncbi.nlm.nih.gov/pubmed/24265179 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/prot.24464 |
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