N-linked glycan stabilisation of the VWF A2 domain.
London, United Kingdom. In Blood, Feb 2016
UNASSIGNED: Shear forces in the blood trigger a conformational transition in the VWF A2 domain, from its native folded to an unfolded state, in which the cryptic scissile bond (Y1505-M1606) is exposed and can then be proteolysed by ADAMTS13.
Relevance of ADAMTS13 to liver transplantation and surgery.
Nara, Japan. In World J Hepatol, Aug 2015
A disintegrin-like and metalloproteinase with thrombospondin type-1 motifs 13 (ADAMTS13) specifically cleaves unusually-large von Willebrand factor (VWF) multimers under high shear stress, and down-regulates VWF function to form platelet thrombi.
Pathogenesis of thrombotic microangiopathies.
Philadelphia, United States. In Annu Rev Pathol, 2007
The congenital and idiopathic TTP syndromes are caused primarily by deficiency of ADAMTS13, owing to mutations in the ADAMTS13 gene or autoantibodies that inhibit ADAMTS13 activity.