[HTML][HTML] Shear‐induced unfolding activates von Willebrand factor A2 domain for proteolysis
C Baldauf, R Schneppenheim, W Stacklies… - Journal of Thrombosis …, 2009 - Elsevier
Background: To avoid pathological platelet aggregation by von Willebrand factor (VWF),
VWF multimers are regulated in size and reactivity for adhesion by ADAMTS13‐mediated
proteolysis in a shear flow dependent manner. Objective and methods: We examined
whether tensile stress in VWF under shear flow activates the VWF A2 domain for cleavage
by ADAMTS13 using molecular dynamics simulations. We generated a full length mutant
VWF featuring a homologous disulfide bond in A2 (N1493C and C1670S), in an attempt to …
VWF multimers are regulated in size and reactivity for adhesion by ADAMTS13‐mediated
proteolysis in a shear flow dependent manner. Objective and methods: We examined
whether tensile stress in VWF under shear flow activates the VWF A2 domain for cleavage
by ADAMTS13 using molecular dynamics simulations. We generated a full length mutant
VWF featuring a homologous disulfide bond in A2 (N1493C and C1670S), in an attempt to …
