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Collagen + H2O
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DREQAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRA + H2O
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i.e. VWF74 peptide, a pseudo-wild-type peptide von Willebrand factor 74, VWF74, encompassing the von Willebrand factor, VWF, A2 domain sequence 1596-1669
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fluorescence resonance energy transfer substrate-von Willebrand factor 73 + H2O
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fluorescent resonance energy transfer-von Willebrand factor 73 + H2O
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FRET-VWF115 peptide + H2O
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von Willebrand factor-derived peptide substrate comprising residues 1554-1668
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FRET-VWF73 + H2O
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fluorogenic von Willebrand factor-derived peptide substrate. The distal C-terminal domains of ADAMTS13 are not necessary for the cleavage of the VWF73-based peptide substrate
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FRETS-rVWF71 + H2O
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substrate based on von Willebrand factor residues Gln1599-Arg1668, with an N-terminal Gly and with mutations N1610C and K1617R. The N-terminus is modified with IRDye QC-1 Nhydroxysuccinimide ester, and Cys1610 is modified with DyLight 633 maleimide
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FRETS-von Willebrand factor 73 + H2O
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FRETS-vWF73 + H2O
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a fluorogenic von Willebrand factor-derived peptide substrate
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FRETS-VWF73 peptide + H2O
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fluorogenic von Willebrand factor-derived peptide substrate
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FRETSVWF73 + H2O
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a von Willebrand factor-derived fluorescein-labeled peptide substrate
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FRETSVWF73 peptide + H2O
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a von Willebrand factor-derived fluorescein-labeled peptide substrate
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GST-von Willebrand factor 73 + H2O
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contains residues Asp1596-Arg1668 from von Willebrand factor domain A2
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HRPH-A2-B
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HRPH-A2-B is a derivative of von Willebrand factor 73, consisting of a HRP conjugate of a biotinylated von Willebrand factor 78 sequence
cleavage of Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275
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large von Willebrand factor multimer + H2O
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recombinant human VWF73 peptide + H2O
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ultra-large von Willebrand factor + H2O
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ultra-large von Willebrand factor multimer + H2O
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von Willebrand factor + H2O
2 peptides
von Willebrand factor + H2O
2 peptides of 140 kD and 65 kD
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cleavage of peptide bond Tyr842-Met843
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
von Willebrand factor + H2O
2 peptides of 176 kD and 140 kD
von Willebrand factor + H2O
?
von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
von Willebrand factor + H2O
von Willebrand factor fragments
von Willebrand factor 115 (1554-1668) + H2O
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A2 domain fragment
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von Willebrand factor 115 + H2O
10000 Da fragment of von Willebrand factor 115 + 7000 Da fragment of von Willebrand factor 115
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von Willebrand factor is cleaved at the Tyr1605-Met1606 bond in the von Willebrand factor A2 domain
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von Willebrand factor 115-A3 (1554-1874) + H2O
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A2 domain fragment
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von Willebrand factor 73 + H2O
7722 Da peptide + ?
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von Willebrand factor 73 + H2O
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minimal substrate cleavable by ADAMTS-13
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von Willebrand factor 76 (1593-1668) + H2O
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A2 domain fragment
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VWF115 + H2O
10 kDa VWF115 fragment + 7 kDa VWF115 fragment
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VWFA2 domain fragment, spanning von Willebrand factor residues 1554-1668, generation of 2 cleavage products of 10 kDa and 7 kDa
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VWF115 D1614A mutant + H2O
10 kDa VWF115 fragment + 7 kDa VWF115 fragment
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Asp1614 VWFA2 domain fragment, spanning von Willebrand factor residues 1554-1668, generation of 2 cleavage products of 10 kDa and 7 kDa
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VWF73 peptide + H2O
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von Willebrand factor-derived peptide substrate
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VWF73 region of von Willebrand factor + H2O
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with this minimal substrate urea is not required for cleavage, minimal substrate for ADAMTS-13
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VWFA2 peptide + H2O
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substrate based on a 78-amino acid sequence corresponding to the sequence Leu1591-Arg1668 of the von Willebrand factor A2 domain
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VWFA2 peptide + H2O
VWFA2 peptide fragments
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A2 domain fragment of von Willebrand factor, cleavage of oxidized or nonoxidized VWFA2 peptide by ADAMTS13, cleavage of the Tyr1605-Met(O)1606 peptide bond by ADAMTS13, overview
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additional information
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FRETS-von Willebrand factor 73 + H2O
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FRETS-von Willebrand factor 73 + H2O
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GST-VWF73 + H2O
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labeled von Willebrand factor-derived peptide substrate
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GST-VWF73 + H2O
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labeled von Willebrand factor-derived peptide substrate. The distal C-terminal domains of ADAMTS13 are not necessary for the cleavage of the VWF73-based peptide substrate
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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proteins + H2O
peptides
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enzyme is involved in thrombotic thrombocytopenic purpura
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proteins + H2O
peptides
enzyme is involved in thrombotic thrombocytopenic purpura
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von Willebrand factor + H2O
2 peptides
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cleavage of peptide bond Tyr842-Met843
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von Willebrand factor + H2O
2 peptides
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cleavage site is located in the A2 domain of the substrate, cleavage of peptide bond Tyr842-Met843
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von Willebrand factor + H2O
2 peptides
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large multimeric complexes are reduced to smaller ones, cleavage of peptide bond Tyr842-Met843
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von Willebrand factor + H2O
2 peptides
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rapid physiological process that occurs on endothelial surfaces, reduced activity results in thrombotic thrombocytopenic pupura
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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ADAMTS13 cleaves von Willebrand factor at the Y1605/M1606 peptide bond in the A2 domain. Mutant substrates L1603Q, L1603R, Y1605D, L1603R/Y1605N, Y1605N/M1606T, Y1605R/M1606T are resistant to cleavage. Mutant substrates R1597W, M1606T and I1616N are less efficiently cleaved than wild-type
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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cleavage of the peptide bond Tyr842-Met843 within the A2 domain
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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cleavage of the peptide bond Tyr842-Met843 within the A2 domain
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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cleavage of the peptide bond Tyr842-Met843 within the A2 domain
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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specific cleavage of the peptide bond Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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cleavage of the peptide bond Tyr842-Met843 within the A2 domain, enzyme deficiency causes lethal thrombotic thrombocytopenic purpura
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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either congenital or acquired defects of the enzyme lead to thrombotic thromcytopenic purpura, cleavage of the peptide bond bond Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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large multimeric substrate, cleavage of the peptide bond Tyr842-Met843 within the A2 domain
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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protein from plasma of patients suffering type I von Willebrand disease is more susceptible to proteolysis by the enzyme due to amino acid polymorphism heterozygous at position Tyr/Cys1584, phenotypic parameters, cleavage of the peptide bond Tyr842-Met843 within the A2 domain
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von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
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complete proteolysis is observed at 37°C in the presence of BaCl2 while about 25% von Willebrand factor still binds to collagen when BaCl2 supplementation is omitted. Proteolysis kinetics at 22°C and 4°C is slower but complete
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von Willebrand factor + H2O
2 peptides of 176 kD and 140 kD
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large multimeric complexes are reduced to smaller ones, cleavage of peptide bond Tyr842-Met843 in the vWFdomain A2
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von Willebrand factor + H2O
2 peptides of 176 kD and 140 kD
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large multimeric complexes are reduced to smaller ones, cleavage of peptide bond Tyr842-Met843 in the vWFdomain A2
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von Willebrand factor + H2O
2 peptides of 176 kD and 140 kD
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rapid physiological process that occurs on endothelial surfaces, activity is reduced by 87-100% in patients with thrombotic thrombocytopenic pupura
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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669524, 677437, 678918, 678964, 679396, 680535, 680695, 681661, 681662, 681663, 682523, 682525, 682898, 682901, 682939, 710826, 710827, 711086, 711559, 711564, 711565, 711569, 711571, 711572, 711575, 711576, 711809, 712568, 713079, 713189, 713533, 713534, 713536, 719881, 720367, 720833, 753897, 754157, 754522, 755583 -
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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specific for
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von Willebrand factor + H2O
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cleavage of peptide bond Tyr842-Met843, native and recombinant enzyme
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von Willebrand factor + H2O
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cleavage of peptide bond Tyr842-Met843, large hemostatically active multimers are cleaved to smaller less active forms, increased proteolytic degradation in patients suffering from von Willebrand disease typ 2A
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von Willebrand factor + H2O
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cleavage of peptide bond Tyr842-Met843, rapid degradation of multimers to smaller fragments, decreased activity results in bone marrow transplant-associated thrombotic microangiopathy and thrombotic thrombocytopenic pupura
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von Willebrand factor + H2O
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decrease of the multimeric pattern of enzyme and decreased activity results in bone marrow transplant-associated thrombotid microangiopathy
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von Willebrand factor + H2O
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enzyme deficiency causes lethal thrombotic thrombocytopenic purpura, cleavage of peptide bond Tyr1605-Met1606 resulting in limited platelet accumulation in microvascular thrombi (Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275)
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von Willebrand factor + H2O
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the cleavage site is exposed to the enzyme by conformational changes due to shear stress in the plasma, decrease of the multimeric pattern of enzyme and decreased activity results in bone marrow transplant-associated thrombotic microangiopathy, cleavage of peptide bond Tyr842-Met843, large hemostatically active multimers are cleaved to smaller less active forms, increased proteolytic degradation in patients suffering von Willebrand disease typ 2A
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von Willebrand factor + H2O
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cleavage of Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275
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von Willebrand factor + H2O
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important role for Asp1614 and surrounding charged residues in the binding and cleavage of the von Willebrand factor A2 domain
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von Willebrand factor + H2O
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VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13
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von Willebrand factor + H2O
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ADAMTS13 cleaves at the peptide bond Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275
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von Willebrand factor + H2O
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ADAMTS13 cleaves the bond Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275
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von Willebrand factor + H2O
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amino acid position C1584 is necessary for enhanced von Willebrand factor proteolysis by ADAMTS13
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von Willebrand factor + H2O
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ADAMTS13 efficiently cleaves only the Tyr842-Met843 bond within the central A2 domain of multimeric von Willebrand factor (i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275)
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von Willebrand factor + H2O
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ADAMTS13 efficiently cleaves only the Tyr842-Met843 bond within the central A2 domain of multimeric von Willebrand factor (i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275). This specificity depends in part on binding of the noncatalytic ADAMTS13 spacer domain to the C-terminal alpha-helix of von Willebrand factor domain A2. By kinetic analysis of recombinant ADAMTS13 constructs, it is shown that the first thrombospondin-1, Cys-rich, and spacer domains of ADAMTS13 interact with segments of von Willebrand factor domain A2 between Gln1624 and Arg1668 (in von Willebrand factor UniProt Id P04275), and together these exosite interactions increase the rate of substrate cleavage by at least approximately 300fold. Specific recognition of von Willebrand factor depends on cooperative, modular contacts between several ADAMTS13 domains and discrete segments of von Willebrand factor domain A2. Specification of the cleavage site depends on sequences flanking the scissile bond between positions P9 (Arg1597) and P18' (Ile1623)
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von Willebrand factor + H2O
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all alterations examined in the Y1605-M1606 cleavage site greatly reduce the cleavability of von Willebrand factor by ADAMTS13. Greatest cleavage resistance is observed in Y1605A/M1606A. Y1605H and M1606L show a loss of cleavability in the recombinant full-length von Willebrand factor assay, suggesting that an aromatic ring at 1605 is critical for ADAMTS13 recognition. The G1643S polymorphism shows increased cleavage, suggesting a type 2A von Willebrand factor phenotype, while D1472H, Q1571H and P1601T show slightly decreased ADAMTS13 cleavage. A-domain changes in von Willebrand factor alter ADAMTS13-mediated proteolysis
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von Willebrand factor + H2O
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a catalysis-deficient ADAMTS13 P475S mutant does not show VWF-induced changes in conformation
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von Willebrand factor + H2O
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ADAMTS13 cleaves ultra-large von Willebrand factor multimers
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von Willebrand factor + H2O
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cleavage of ultra-large multimers
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von Willebrand factor + H2O
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force-induced von Willebrand factor A2 domain unfolding of the substrate facilitates cleavage, using single VWF A1A2A3 tridomain polypeptides, structural destabilization of A1A2A3 was induced by 5- to 80-pN forces
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von Willebrand factor + H2O
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persistently elevated levels of von Willebrand factor in plasma during and after liver transplantation, while plasma levels of ADAMTS13 dropp during transplantation
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von Willebrand factor + H2O
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specific cleavage of ultra-large von Willebrand factor multimers
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von Willebrand factor + H2O
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cleaving of ultra-large multimers between residues Tyr842 and Met843 in the central A2 domain, the TSP-1 domain of ADAMTS13 is required for interaction with the extracellular matrix and the substrate, as well as the CUB domains, that are also essential for intracellular trafficking
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von Willebrand factor + H2O
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i.e. VWF, a large glycoprotein secreted by vascular endothelial cells as multimers
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von Willebrand factor + H2O
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identification of ADAMTS13 peptide sequences binding to von Willebrand factor, overview
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von Willebrand factor + H2O
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recombinant substrate stably expressed in HEK293 cells, the ADAMTS13 metalloprotease domain cleaves the von Willebrand factor A2 domain at the Y1605-M1606 scissile bond
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von Willebrand factor + H2O
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substrate is FRET-VWF73
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von Willebrand factor + H2O
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the S119-W262 H-bond in the ADAMTS13 metalloprotease domain is crucial for maximal turnover
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von Willebrand factor + H2O
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wild-type plasma-derived substrate of human origin, and substrate modified by alpha2-3,6,8,9-neuraminidase from Arthrobacter ureafaciens removing alpha2-3- and alpha2-6-linked sialic acid, and treatment with PNGase F to remove complex N-linked glycan structures. alpha2-6-linked sialic acid increases von Willebrand factor proteolysis by ADAMTS13 through a conformational mechanism, overview
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von Willebrand factor + H2O
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ADAMTS-13 has thiol reductase activity limited towards von Willebrand factor
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von Willebrand factor + H2O
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ADAMTS13 specifically cleaves von Willbrand factor A2 domain between Tyr1605 and Met1606
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von Willebrand factor + H2O
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cleavage occurs at strand beta4 (Tyr1605-Met1606) in the structural core of the A2 domain. Ca2+ binding stabilizes the A2 domain and impedes its unfolding, and consequently protects it from cleavage by ADAMTS13
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von Willebrand factor + H2O
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the disulfide-bond-reducing activity of ADAMTS-13 prevents covalent lateral association and increased platelet adherence of plasma-type von Willebrand factor multimers induced by high fluid shear stress
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von Willebrand factor + H2O
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von Willebrand factor A2 domain unfolding is required for proteolysis by ADAMTS13, the ADAMTS13 cleavage site is at Tyr1605-Met1606
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von Willebrand factor + H2O
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von Willebrand factor + H2O
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specific cleavage of ultra-large von Willebrand factor multimers
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von Willebrand factor + H2O
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von Willebrand factor is also susceptible to cleavage by ADAMTS13 when incorporated in a thrombus
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von Willebrand factor + H2O
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substrate of human origin
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von Willebrand factor + H2O
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. Very low activity with recombinant human substrate in vitro, comparison to other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. The guinea pig ADAMTS13 shows no activity with the recombinant human substrate in vitro, comparison to other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS-13 cleavage of von Willebrand factor strings secreted from stimulated and unstimulated HUVECs occurs at the position 1605-6 of the von Willebrand factor A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS-13 cleaves the Tyr1605-Met1606 bond in the VWF A2 domain, mechanisms of VWF recognition, cleavage analysis and kinetics under static and flow conditions, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS-13 cleaves von Willebrand factor (VWF) exclusively at the Tyr1605-Met1606 peptide bond in the A2 domain
LC-MS product identification
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS-13 cleavage of HUVEC-secreted von Willebrand factor strings at Y1605-6M sites of the von Willebrand factor A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS-13 cleaves the Tyr1605-Met1606 bond in the VWF A2 domain, mechanisms of VWF recognition. One ADAMTS13 binding site of VWF is located in the region of VWF spanning residues 1874 to 2813, which includes the VWF D4 domain, interacts with the C-terminal domains of ADAMTS13, interaction occurs even when VWF is in static conditions, globular and with the VWF A2 domain hidden. The binding site may participate as the initial step of a multistep interaction ultimately leading to proteolysis of VWF byADAMTS13
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. Comparison of the activity with human recombinan substrate in vitro with enzymes from other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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binding of all the proximal noncatalytic domains of ADAMTS13 to von Willebrand factor is necessary to position the active site of ADAMTS13 to the scissile bond, Tyr1605-Met1606, on von Willebrand factor, resulting in productive cleavage. The metalloprotease domain of ADAMTS13 alone is ineffective in cleaving von Willebrand factor, linear relationship between the domains of ADAMTS13 and von Willebrand factor proteolysis. All the proximal noncatalytic domains of ADAMTS13 are required for productive engagement with von Willebrand factor-A2 domain at least under static/denaturing conditions
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. Activity with the recombinant human substrate in vitro, comparison to other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. The wild-type mouse ADAMTS13 shows no activity with the recombinant human substrate in vitro, comparison to other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. The rabbit ADAMTS13 shows activity similar to the human ADAMTS13 with the recombinant human substrate in vitro, comparison to other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. The rat ADAMTS13 shows no activity with the recombinant human substrate in vitro, comparison to other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain
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von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond within the central A2 domain. Very low activity with recombinant human substrate in vitro, comparison to other mammal enzymes, overview
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von Willebrand factor + H2O
von Willebrand factor fragments
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von Willebrand factor + H2O
von Willebrand factor fragments
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond
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von Willebrand factor + H2O
von Willebrand factor fragments
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ADAMTS13 cleaves von Willebrand factor to smaller less-active forms
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von Willebrand factor + H2O
von Willebrand factor fragments
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ADAMTS13 specifically cleaves von Willebrand factor multimers at the site of the Tyr1605-Met1606 bond of the VWF-A2 domain
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von Willebrand factor + H2O
von Willebrand factor fragments
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cleavage at the Tyr1605-Met1606 bond within the van Willebrand factor A2 domain
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von Willebrand factor + H2O
von Willebrand factor fragments
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cleavage can also occur at the surface of endothelial cells. ADAMTS13 that is prebound to endothelial cells exhibits increased proteolysis of VWF as compared with ADAMTS13 present only in solution. Thus, cleavage of VWF occurs mainly at the endothelial cell surface
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von Willebrand factor + H2O
von Willebrand factor fragments
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cleavage of ultra large von Willebrand multimers into smaller fragments
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von Willebrand factor + H2O
von Willebrand factor fragments
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specific cleavage of the long strings of ultra-large von Willebrand factor multimers
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von Willebrand factor + H2O
von Willebrand factor fragments
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ADAMTS13 cleaves von Willebrand factor at the Tyr1605-Met1606 bond. The ADAMTS13 spacer domain is required for cleavage of von Willebrand factor, role of the amino acid residues Arg659, Arg660, and Tyr661 of theADAMTS13 spacer domain in substrate recognition, sequence comparisons and kinetics, detailed overview
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von Willebrand factor + H2O
von Willebrand factor fragments
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cleavage of the Tyr1605-Met(O)1606 peptide bond by ADAMTS13
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von Willebrand factor + H2O
von Willebrand factor fragments
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specific cleavage of the long strings of ultra-large von Willebrand factor multimers. The specificity of ADAMTS13 for proteolysis of von Willebrand factor is facilitated by multiple cooperative contacts that bind ADAMTS13 to von Willebrand factor
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von Willebrand factor + H2O
von Willebrand factor fragments
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ADAMTS13 cleaves von Willebrand factor to smaller less-active forms
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VWF115 + H2O
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a von Willebrand factor-derived peptide substrate, comprising amino acid residues 1554-1668 of von Willebrand factor
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VWF115 + H2O
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von Willebrand factor A2 domain fragment, residues 1554-1668
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additional information
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differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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additional information
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differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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additional information
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no activity with human fibrinogen, bovine serum albumin, and calf skin collagen
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additional information
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pro-von Willebrand factor is cleaved by pro-ADAMTS13 and by ADAMTS13
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additional information
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does not cleave GST-von Willebrand factor 64 which lacks 9 aa residues (E1660APDLVLQR1668)
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additional information
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PNGase-treated von Willebrand factor is more succeptible to proteolysis by ADAMTS13 and binds with increased affinity
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additional information
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ADAMTS13 binds to CD36, a transmembrane protein of endothelial cells and platelets, i.e. glycoprotein IV, not diminishing the proteolytic activity of ADAMTS13, but providing an anchor for ADAMTS13 on the surface of endothelial cells and platelets
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additional information
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ADAMTS13 contains eight thrombospondin type 1 repeats and binds to CD36, a transmembrane protein present on endothelial cells and platelets. CD36 also binds to thrombospondin-2 via three thrombospondin type 1 repeats in a manner competitive to ADAMTS13, overview
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additional information
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MDTCS domain modelling and substrate recognition mode analysis, overview
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additional information
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proteolysis can occur only once VWF has been unraveled from its globular conformation, either by high fluid shear stress in vivo or in the presence of denaturants in vitro, conditions that are able to promote the exposure of the VWF scissile bond
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additional information
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removal of newly released ultralarge-von Willebrand factor strings or bundles anchored on endothelial cells by ADAMTS13 occurs rapidly and efficiently in the presence and in the absence of fluid shear stress, suggesting that the cell-bound ultra large-von Willebrand factor polymers may be preferred substrates for ADAMTS13
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additional information
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thrombospondin1 and ADAMTS13 form complexes together in cells and in direct protein binding assays
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additional information
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thrombospondin1 and ADAMTS13 form complexes together in cells and in direct protein binding assays
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additional information
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ADAMTS 13 activity measurement using a collagen binding assay
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additional information
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binding specificities of wild-type ADAMTS13 and ADAMTS13-RYY to von Willebrand factor115, von Willebrand factor106, and full-length von Willebrand factor, overview
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additional information
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construction of substrate peptides VWF Asp1596-Ala1669, i.e. VWF74, VWF Asp1596-Ala1669 containing nitrotyrosine, i.e. VWF74-NT, or methionine sulfoxide, i.e. VWF74-MetSO, at position 1605 or 1606, respectively. VWF74 oxidized by peroxynitrite undergoes a severe impairment of its hydrolysis. Likewise, VWF74-MetSO is minimally hydrolyzed, whereas VWF74-NT is hydrolyzed only slightly more efficiently than VWF74, overview
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additional information
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differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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additional information
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molecular modeling of ADAMTS13 metalloprotease domain using its sequence homology to adamalysin II and the crystal structure
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additional information
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proteolysis can occur only once VWF has been unraveled from its globular conformation, either by high fluid shear stress in vivo or in the presence of denaturants in vitro, conditions that are able to promote the exposure of the VWF scissile bond. The ADAMTS13 C-terminal distal domains (TSP5-CUB) bind to a novel binding site in the C-terminal region of VWF, spanning residues 1874-2813 and including the VWF D4 domain, which, critically, is constitutively exposed on the surface of VWF in solution without flow. C-terminal VWF fragments, as well as an antibody specifically directed toward the VWF D4 domain, inhibit VWF proteolysis by ADAMTS13 under shear conditions
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additional information
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role for ADAMTS13 disintegrin-like domains in substrate recognition and proteolysis, homology modeling, overview. Residues Arg349, Leu350, and Val352 are predicted to form a cluster on the surface of the ADAMTS13 disintegrin-like domain immediately adjacent to the active-site cleft
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additional information
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structure-function analysis, overview
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additional information
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the positively charged Arg349 on ADAMTS13 appears to directly interact with the negatively charged Asp1614 on the von Willebrand factor-A2 domain. This seemingly weak interaction between the disintegrin and VWF-A2 appears to be essential for efficient catalysis of von Willebrand factor under static/denaturing conditions. Molecular modeling of the involvement of the disintegrin domain of ADAMTS13 in von Willebrand factor processing, overview
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additional information
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plasmin cleaves and ultimately inactivates the enzyme
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additional information
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plasmin cleaves and ultimately inactivates the enzyme
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additional information
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the enzyme cleaves a susceptible tyrosine-methionine bond located between amino acids 9 and 10 in a synthetic 77 amino acid substrate. Amino acid 3 is a glutamic acid residue to which the fluorescent 2-(N-methylamino)benzoyl group is covalently bonded. Amino acid 13 is a glycine residue to which the quenching agent 2,4 dinitrophenol is attached. Upon cleavage of the tyrosine-methionine bond, the quenching effect of the 2,4 dinitrophenol is reduced, and excitation of-(N-methylamino)benzoyl results in fluorescent emission measured at 440 nm
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additional information
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differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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additional information
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important role for ADAMTS13 in preventing excessive spontaneous Weibel-Palade body secretion, and in the regulation of leukocyte adhesion and extravasation during inflammation
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additional information
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assay on the fluorogenic substrate FRETS-vWF73
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additional information
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no activity in von Willebrand factor-deficient or ADAMTS13-deficient mice with the recombinant substrate of human origin. Differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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additional information
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differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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additional information
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differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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additional information
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differences in susceptibility to cleavage of recombinant von Willebrand factor by different species need to be considered when interpreting the physiology of human recombinant von Willebrand factor from results of tests in animal models
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