Title : Covalent regulation of ULVWF string formation and elongation on endothelial cells under flow conditions.

Pub. Date : 2008 Jul

PMID : 18433456






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The presence of thiols in ULVWF and plasma VWF multimers was determined by maleimide-PEO(2)-Biotin labeling and thiol-chromatography. Sulfhydryl Compounds von Willebrand factor Homo sapiens
2 The presence of thiols in ULVWF and plasma VWF multimers was determined by maleimide-PEO(2)-Biotin labeling and thiol-chromatography. Sulfhydryl Compounds von Willebrand factor Homo sapiens
3 The formation and propagation of ULVWF strings were dose-dependently reduced by blocking thiols on VWF with NEM, indicating that ULVWF strings are formed by the covalent association of perfused VWF to ULVWF anchored to endothelial cells. Sulfhydryl Compounds von Willebrand factor Homo sapiens
4 The formation and propagation of ULVWF strings were dose-dependently reduced by blocking thiols on VWF with NEM, indicating that ULVWF strings are formed by the covalent association of perfused VWF to ULVWF anchored to endothelial cells. Sulfhydryl Compounds von Willebrand factor Homo sapiens
5 The association is made possible by the presence of free thiols in VWF multimers and by the ability of (UL) VWF to covalently re-multimerize. Sulfhydryl Compounds von Willebrand factor Homo sapiens