ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions.
By Jing-fei Dong, J. Moake, L. Nolasco, Aubrey Bernardo, W. Arceneaux, C. Shrimpton, Alicia J. Schade, L. McIntire, K. Fujikawa, José A. López. Blood, 2002
905 citations recorded by the source corpus.
Subfields: Hematology, Immunology
View Paper: https://www.semanticscholar.org/paper/63dae1243422c0c9f31ec2fbb9e5403cbc0031ea
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Citations in the corpus
- ADAMTS13 and von Willebrand Factor in Thrombotic Thrombocytopenic Purpura (2015, background): “Human recombinant ADAMTS13 was quickly expressed in transfected cell lines as a 195-kDa protein, capable of cleaving soluble multimeric VWF (19, 20) and endothelium-released and anchored ULVWF strings (21).”
- Platelet-neutrophil-interactions: linking hemostasis and inflammation. (2007, background): “The presentation of UL vWF multimers induces platelet adhesion to the GPIb/IX/V complex and aggregation.(38)”
- In vitro microvessels for the study of angiogenesis and thrombosis (2012, background): “VWF is a protein that can be released from endothelial Weibel–Palade bodies (WPBs) and assemble into fibers on the endothelial surface upon endothelial activation (34) under flow.”