PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31393047-2 2019 Additionally, ADAMTS13 is thought to regulate lateral association of VWF multimers to form fibrillar structures through its free thiols. Sulfhydryl Compounds 129-135 von Willebrand factor Homo sapiens 69-72 33075181-0 2021 Blocking Von Willebrand Factor Free-Thiols inhibits binding to collagen under high and pathological shear stress. Sulfhydryl Compounds 36-42 von Willebrand factor Homo sapiens 9-30 33075181-1 2021 BACKGROUND: Von Willebrand Factor (VWF) contains a number of free thiols, the majority of which are located in its C-domains, and these have been shown to alter VWF function, However, the impact of free-thiols on function following acute exposure of VWF to collagen under high and pathological shear stress has not been determined. Sulfhydryl Compounds 66-72 von Willebrand factor Homo sapiens 12-33 33075181-1 2021 BACKGROUND: Von Willebrand Factor (VWF) contains a number of free thiols, the majority of which are located in its C-domains, and these have been shown to alter VWF function, However, the impact of free-thiols on function following acute exposure of VWF to collagen under high and pathological shear stress has not been determined. Sulfhydryl Compounds 66-72 von Willebrand factor Homo sapiens 35-38 33075181-1 2021 BACKGROUND: Von Willebrand Factor (VWF) contains a number of free thiols, the majority of which are located in its C-domains, and these have been shown to alter VWF function, However, the impact of free-thiols on function following acute exposure of VWF to collagen under high and pathological shear stress has not been determined. Sulfhydryl Compounds 66-72 von Willebrand factor Homo sapiens 161-164 33075181-1 2021 BACKGROUND: Von Willebrand Factor (VWF) contains a number of free thiols, the majority of which are located in its C-domains, and these have been shown to alter VWF function, However, the impact of free-thiols on function following acute exposure of VWF to collagen under high and pathological shear stress has not been determined. Sulfhydryl Compounds 66-72 von Willebrand factor Homo sapiens 161-164 33075181-1 2021 BACKGROUND: Von Willebrand Factor (VWF) contains a number of free thiols, the majority of which are located in its C-domains, and these have been shown to alter VWF function, However, the impact of free-thiols on function following acute exposure of VWF to collagen under high and pathological shear stress has not been determined. Sulfhydryl Compounds 203-209 von Willebrand factor Homo sapiens 12-33 33075181-1 2021 BACKGROUND: Von Willebrand Factor (VWF) contains a number of free thiols, the majority of which are located in its C-domains, and these have been shown to alter VWF function, However, the impact of free-thiols on function following acute exposure of VWF to collagen under high and pathological shear stress has not been determined. Sulfhydryl Compounds 203-209 von Willebrand factor Homo sapiens 35-38 33075181-4 2021 RESULTS: Blockade of VWF free-thiols reduced VWF mediated platelet capture to collagen in a shear dependent manner, with platelet capture virtually abolished above 5000s-1 and in regions of stenosis in microfluidic channels. Sulfhydryl Compounds 30-36 von Willebrand factor Homo sapiens 21-24 33075181-4 2021 RESULTS: Blockade of VWF free-thiols reduced VWF mediated platelet capture to collagen in a shear dependent manner, with platelet capture virtually abolished above 5000s-1 and in regions of stenosis in microfluidic channels. Sulfhydryl Compounds 30-36 von Willebrand factor Homo sapiens 45-48 33075181-6 2021 AFM measurements showed that thiol-blockade reduced the life-time and strength of the VWF-collagen bond. Sulfhydryl Compounds 29-34 von Willebrand factor Homo sapiens 86-89 33075181-7 2021 Pulling simulations of the VWF-C4 domain demonstrated that with one or two reduced disulphide bonds the C4 domain has increased flexibility and the propensity to undergo free-thiol exchange. Sulfhydryl Compounds 175-180 von Willebrand factor Homo sapiens 27-30 33075181-8 2021 CONCLUSIONS: We conclude that free-thiols in the C-domains of VWF enhance the flexibility of the molecule and enable it to withstand high shear forces following collagen binding, demonstrating a previously unrecognised role for VWF free-thiols. Sulfhydryl Compounds 35-41 von Willebrand factor Homo sapiens 62-65 33075181-8 2021 CONCLUSIONS: We conclude that free-thiols in the C-domains of VWF enhance the flexibility of the molecule and enable it to withstand high shear forces following collagen binding, demonstrating a previously unrecognised role for VWF free-thiols. Sulfhydryl Compounds 35-41 von Willebrand factor Homo sapiens 228-231 33075181-8 2021 CONCLUSIONS: We conclude that free-thiols in the C-domains of VWF enhance the flexibility of the molecule and enable it to withstand high shear forces following collagen binding, demonstrating a previously unrecognised role for VWF free-thiols. Sulfhydryl Compounds 237-243 von Willebrand factor Homo sapiens 62-65 33075181-8 2021 CONCLUSIONS: We conclude that free-thiols in the C-domains of VWF enhance the flexibility of the molecule and enable it to withstand high shear forces following collagen binding, demonstrating a previously unrecognised role for VWF free-thiols. Sulfhydryl Compounds 237-243 von Willebrand factor Homo sapiens 228-231 31393047-12 2019 CONCLUSIONS: Our results suggest that a dynamic network of free thiols in ADAMTS13 undergoing intra- and inter-molecular redox reactions may add another layer of regulation to VWF function under various conditions. Sulfhydryl Compounds 64-70 von Willebrand factor Homo sapiens 176-179 26581637-0 2016 Free thiol groups in von Willebrand factor (VWF) are required for its full function under physiological flow conditions. Sulfhydryl Compounds 5-10 von Willebrand factor Homo sapiens 44-47 26581637-1 2016 INTRODUCTION: von Willebrand factor (VWF) is rich in cysteine; next to important structural disulfide bonds, free thiol groups are present. Sulfhydryl Compounds 114-119 von Willebrand factor Homo sapiens 37-40 26581637-2 2016 Free thiols on the surface of plasmatic VWF have been shown to play a role in VWF self-association and in platelet binding under pathologically high levels of shear stress. Sulfhydryl Compounds 5-11 von Willebrand factor Homo sapiens 40-43 26581637-2 2016 Free thiols on the surface of plasmatic VWF have been shown to play a role in VWF self-association and in platelet binding under pathologically high levels of shear stress. Sulfhydryl Compounds 5-11 von Willebrand factor Homo sapiens 78-81 26581637-3 2016 The present study explores the role of VWF free thiol groups under physiological levels of shear stress and in interactions with collagen and platelet-GPIbalpha receptor. Sulfhydryl Compounds 48-53 von Willebrand factor Homo sapiens 39-42 26581637-6 2016 RESULTS: Blockade of free thiol groups significantly reduced VWF-mediated platelet recruitment to collagen under physiological flow conditions. Sulfhydryl Compounds 26-31 von Willebrand factor Homo sapiens 61-64 26581637-10 2016 CONCLUSIONS: This study shows a significant contribution of free thiol groups in VWF to the mediation of platelet adhesion under physiological shear stress conditions. Sulfhydryl Compounds 65-70 von Willebrand factor Homo sapiens 81-84 26581637-11 2016 The free thiol groups are shown to be involved in VWF binding to both collagen III and platelet GP1b receptor. Sulfhydryl Compounds 9-14 von Willebrand factor Homo sapiens 50-53 24008159-6 2013 Recombinant human FH reduced large soluble vWF multimers in a free thiol-dependent reaction that was not inhibited by a variety of protease inhibitors. Sulfhydryl Compounds 67-72 von Willebrand factor Homo sapiens 43-46 24283831-1 2014 BACKGROUND: von Willebrand factor (VWF) contains free thiols that mass spectroscopy has located to nine cysteines: two in the D3 domain (Cys889 and Cys898) and seven in the C domains (Cys2448, Cys2451, Cys2453, Cys2490, Cys2491, Cys2528, and Cys2533) (J Biol Chem, 7, 2007, 35604; Blood, 118, 5312). Sulfhydryl Compounds 54-60 von Willebrand factor Homo sapiens 12-33 24283831-1 2014 BACKGROUND: von Willebrand factor (VWF) contains free thiols that mass spectroscopy has located to nine cysteines: two in the D3 domain (Cys889 and Cys898) and seven in the C domains (Cys2448, Cys2451, Cys2453, Cys2490, Cys2491, Cys2528, and Cys2533) (J Biol Chem, 7, 2007, 35604; Blood, 118, 5312). Sulfhydryl Compounds 54-60 von Willebrand factor Homo sapiens 35-38 24283831-2 2014 It has been suggested that these free thiols function to regulate the self-association of VWF through thiol-disulfide exchange (J Biol Chem, 7, 2007, 35604; Blood, 118, 5312). Sulfhydryl Compounds 38-44 von Willebrand factor Homo sapiens 90-93 24283831-2 2014 It has been suggested that these free thiols function to regulate the self-association of VWF through thiol-disulfide exchange (J Biol Chem, 7, 2007, 35604; Blood, 118, 5312). Sulfhydryl Compounds 38-43 von Willebrand factor Homo sapiens 90-93 24283831-10 2014 CONCLUSIONS: These data suggest: first, that pairing of cysteines implicated in free thiol exchange is essential for correct folding of the VWF molecule, and unpairing must occur following exit from the ER or secretion from the cell; and second, that intact C domains are essential for efficient VWF secretion and must interact in the ER. Sulfhydryl Compounds 85-90 von Willebrand factor Homo sapiens 140-143 24283831-10 2014 CONCLUSIONS: These data suggest: first, that pairing of cysteines implicated in free thiol exchange is essential for correct folding of the VWF molecule, and unpairing must occur following exit from the ER or secretion from the cell; and second, that intact C domains are essential for efficient VWF secretion and must interact in the ER. Sulfhydryl Compounds 85-90 von Willebrand factor Homo sapiens 296-299 21911836-3 2011 Fiber formation has been shown to involve thiol/disulfide exchange between VWF molecules. Sulfhydryl Compounds 42-47 von Willebrand factor Homo sapiens 75-78 23067373-4 2012 The self-association of vWF is also supported by a rapidly expanding reservoir of novel evidences that the thiol/disulfide exchange regulates vWF multimer size in the blood circulation. Sulfhydryl Compounds 107-112 von Willebrand factor Homo sapiens 24-27 23067373-4 2012 The self-association of vWF is also supported by a rapidly expanding reservoir of novel evidences that the thiol/disulfide exchange regulates vWF multimer size in the blood circulation. Sulfhydryl Compounds 107-112 von Willebrand factor Homo sapiens 142-145 20979592-10 2010 CONCLUSIONS: Given the importance of thiol oxidoreductases in thrombus formation, we provide preliminary evidence that the thiol-dependent interaction of beta(2) GPI with VWF may contribute to the redox regulation of platelet adhesion. Sulfhydryl Compounds 37-42 von Willebrand factor Homo sapiens 171-174 20946172-2 2010 This functional difference may be attributed to thiols exposed on the surface of plasma-type VWF multimers, but not on ULVWF multimers. Sulfhydryl Compounds 48-54 von Willebrand factor Homo sapiens 93-96 20946172-3 2010 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 33-39 von Willebrand factor Homo sapiens 102-105 20946172-3 2010 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 33-39 von Willebrand factor Homo sapiens 137-140 20946172-4 2010 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 118-123 von Willebrand factor Homo sapiens 146-149 20946172-6 2010 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 175-180 von Willebrand factor Homo sapiens 117-120 20946172-7 2010 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 9-14 von Willebrand factor Homo sapiens 53-56 11413189-5 2001 Incubation of purified TSP-1 with vWF resulted in formation of thiol-dependent complexes of TSP-1 and vWF, generation of new thiols in vWF, and reduction in the average multimer size of vWF. Sulfhydryl Compounds 63-68 von Willebrand factor Homo sapiens 34-37 11413189-5 2001 Incubation of purified TSP-1 with vWF resulted in formation of thiol-dependent complexes of TSP-1 and vWF, generation of new thiols in vWF, and reduction in the average multimer size of vWF. Sulfhydryl Compounds 63-68 von Willebrand factor Homo sapiens 102-105 11413189-5 2001 Incubation of purified TSP-1 with vWF resulted in formation of thiol-dependent complexes of TSP-1 and vWF, generation of new thiols in vWF, and reduction in the average multimer size of vWF. Sulfhydryl Compounds 63-68 von Willebrand factor Homo sapiens 102-105 11413189-5 2001 Incubation of purified TSP-1 with vWF resulted in formation of thiol-dependent complexes of TSP-1 and vWF, generation of new thiols in vWF, and reduction in the average multimer size of vWF. Sulfhydryl Compounds 63-68 von Willebrand factor Homo sapiens 102-105 11413189-5 2001 Incubation of purified TSP-1 with vWF resulted in formation of thiol-dependent complexes of TSP-1 and vWF, generation of new thiols in vWF, and reduction in the average multimer size of vWF. Sulfhydryl Compounds 125-131 von Willebrand factor Homo sapiens 34-37 11019979-7 2000 Reduction in vWF multimer size was associated with formation of new thiols in vWF and there was no evidence for additional proteolytic processing of vWF. Sulfhydryl Compounds 68-74 von Willebrand factor Homo sapiens 13-16 11019979-7 2000 Reduction in vWF multimer size was associated with formation of new thiols in vWF and there was no evidence for additional proteolytic processing of vWF. Sulfhydryl Compounds 68-74 von Willebrand factor Homo sapiens 78-81 11019979-7 2000 Reduction in vWF multimer size was associated with formation of new thiols in vWF and there was no evidence for additional proteolytic processing of vWF. Sulfhydryl Compounds 68-74 von Willebrand factor Homo sapiens 78-81 11019979-10 2000 In support of this hypothesis, incubation of vWF with the protein reductants, protein disulfide isomerase and thioredoxin, resulted in formation of new thiols in vWF and reduction in the average multimer size of vWF. Sulfhydryl Compounds 152-158 von Willebrand factor Homo sapiens 45-48 11019979-10 2000 In support of this hypothesis, incubation of vWF with the protein reductants, protein disulfide isomerase and thioredoxin, resulted in formation of new thiols in vWF and reduction in the average multimer size of vWF. Sulfhydryl Compounds 152-158 von Willebrand factor Homo sapiens 162-165 11019979-10 2000 In support of this hypothesis, incubation of vWF with the protein reductants, protein disulfide isomerase and thioredoxin, resulted in formation of new thiols in vWF and reduction in the average multimer size of vWF. Sulfhydryl Compounds 152-158 von Willebrand factor Homo sapiens 162-165 18433456-4 2008 The presence of thiols in ULVWF and plasma VWF multimers was determined by maleimide-PEO(2)-Biotin labeling and thiol-chromatography. Sulfhydryl Compounds 16-22 von Willebrand factor Homo sapiens 28-31 18433456-4 2008 The presence of thiols in ULVWF and plasma VWF multimers was determined by maleimide-PEO(2)-Biotin labeling and thiol-chromatography. Sulfhydryl Compounds 16-21 von Willebrand factor Homo sapiens 28-31 18433456-7 2008 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 89-95 von Willebrand factor Homo sapiens 35-38 18433456-7 2008 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 89-95 von Willebrand factor Homo sapiens 99-102 18433456-8 2008 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 57-63 von Willebrand factor Homo sapiens 67-70 17925407-5 2007 In this study, we demonstrate that some of the plasma VWF multimers contain surface-exposed free thiols. Sulfhydryl Compounds 97-103 von Willebrand factor Homo sapiens 54-57 17925407-7 2007 The shear-induced thiol-disulfide exchange increases VWF binding to platelets. Sulfhydryl Compounds 18-23 von Willebrand factor Homo sapiens 53-56 17925407-8 2007 The thiol-disulfide exchange involves some or all of nine cysteine residues (Cys(889), Cys(898), Cys(2448), Cys(2451), Cys(2490), Cys(2491), Cys(2453), Cys(2528), and Cys(2533)) in the D3 and C domains as determined by mass spectrometry of the tryptic VWF peptides. Sulfhydryl Compounds 4-9 von Willebrand factor Homo sapiens 252-255 17925407-9 2007 These results suggest that the thiol-disulfide state may serve as an important structural determinant of VWF adhesion activity and can be modified by fluid shear stress. Sulfhydryl Compounds 31-36 von Willebrand factor Homo sapiens 105-108 12351392-0 2002 The von Willebrand factor-reducing activity of thrombospondin-1 is located in the calcium-binding/C-terminal sequence and requires a free thiol at position 974. Sulfhydryl Compounds 138-143 von Willebrand factor Homo sapiens 4-25