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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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Bibliografiset tiedot
Päätekijät: Tischer, Alexander, Madde, Pranathi, Blancas-Mejia, Luis. M., Auton, Matthew
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2013
Aiheet:
Linkit: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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