Pub. Date : 2010 Dec
PMID : 20946172
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | This functional difference may be attributed to thiols exposed on the surface of plasma-type VWF multimers, but not on ULVWF multimers. | Sulfhydryl Compounds | von Willebrand factor | Homo sapiens |
| 2 | Shear stress induces the exposed thiols to form disulfide bonds between laterally apposed plasma-type VWF multimers, leading to enhanced VWF binding to platelets. | Sulfhydryl Compounds | von Willebrand factor | Homo sapiens |
| 3 | Shear stress induces the exposed thiols to form disulfide bonds between laterally apposed plasma-type VWF multimers, leading to enhanced VWF binding to platelets. | Sulfhydryl Compounds | von Willebrand factor | Homo sapiens |
| 4 | OBJECTIVES: We tested a hypothesis that ADAMTS-13 has a disulfide bond reducing activity that regulates shear-induced thiol-disulfide exchange of VWF. | Sulfhydryl Compounds | von Willebrand factor | Homo sapiens |
| 5 | RESULTS: ADAMTS-13 contains a disulfide bond reducing activity that primarily targets disulfide bonds in plasma-type VWF multimers induced by high shear stress or formed with thiol beads, but not disulfide bonds in native multimeric structures. | Sulfhydryl Compounds | von Willebrand factor | Homo sapiens |
| 6 | Cysteine thiols targeted by this activity are in the VWF C-domain and are known to participate in shear-induced thiol-disulfide exchange. | Sulfhydryl Compounds | von Willebrand factor | Homo sapiens |