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Mechanisms by which von Willebrand disease mutations destabilize the A2 domain.
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Mechanisms by which von Willebrand disease mutations destabilize the A2 domain.
Xu AJ, Springer TA. Mechanisms by which von Willebrand disease mutations destabilize the A2 domain. J Biol Chem. 2013 Mar 01; 288(9):6317-24.
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PubMed
subject areas
Amino Acid Substitution
Calcium
Hot Temperature
Humans
Mutation, Missense
Protein Folding
Protein Stability
Protein Structure, Secondary
Protein Structure, Tertiary
von Willebrand Diseases
von Willebrand Factor
authors with profiles
Timothy Alan Springer, Ph.D.