VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13.
about
ADAMTS13 substrate recognition of von Willebrand factor A2 domainPathophysiology of thrombotic thrombocytopenic purpuraMultiple domains of ADAMTS13 are targeted by autoantibodies against ADAMTS13 in patients with acquired idiopathic thrombotic thrombocytopenic purpuraPathogenesis of thrombotic microangiopathiesADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural OverviewCalcium modulates force sensing by the von Willebrand factor A2 domainIdentification of strain-specific variants of mouse Adamts13 gene encoding von Willebrand factor-cleaving proteaseShigatoxin triggers thrombotic thrombocytopenic purpura in genetically susceptible ADAMTS13-deficient mice.Attack of the acronyms: TTP, VWF, ADAMTS-13 and SELDI-TOF-MS.A rapid test for the diagnosis of thrombotic thrombocytopenic purpura using surface enhanced laser desorption/ionization time-of-flight (SELDI-TOF)-mass spectrometry.FRETS-VWF73, a first fluorogenic substrate for ADAMTS13 assay.Thrombotic thrombocytopenic purpura and its diagnosis.von Willebrand factor: two sides of a coin.Molecular biology of ADAMTS13 and diagnostic utility of ADAMTS13 proteolytic activity and inhibitor assays.A rapid enzyme-linked assay for ADAMTS-13.Inhibitory autoantibodies against ADAMTS-13 in patients with thrombotic thrombocytopenic purpura bind ADAMTS-13 protease and may accelerate its clearance in vivo.ADAMTS13 phenotype in plasma from normal individuals and patients with thrombotic thrombocytopenic purpuraNormal levels of ADAMTS13 and factor H are present in the pharmaceutically licensed plasma for transfusion (Octaplas) and in the universally applicable plasma (Uniplas) in development.The clinical utility of ADAMTS13 activity, antigen and autoantibody assays in thrombotic thrombocytopenic purpura.Degradation of circulating von Willebrand factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy.The distal carboxyl-terminal domains of ADAMTS13 are required for regulation of in vivo thrombus formation.Correction of murine ADAMTS13 deficiency by hematopoietic progenitor cell-mediated gene therapyEscherichia coli-derived von Willebrand factor-A2 domain fluorescence/Förster resonance energy transfer proteins that quantify ADAMTS13 activity.A shear-based assay for assessing plasma ADAMTS13 activity and inhibitors in patients with thrombotic thrombocytopenic purpuraResidues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domainCrystal structure and enzymatic activity of an ADAMTS-13 mutant with the East Asian-specific P475S polymorphism.Stability of relevant plasma protein activities in cryosupernatant plasma units during refrigerated storage for up to 5 days postthaw.Impact of severe ADAMTS13 deficiency on clinical presentation and outcomes in patients with thrombotic microangiopathies: the experience of the Harvard TMA Research Collaborative.Bortezomib in the treatment of refractory thrombotic thrombocytopenic purpura.Treatment with or without plasma exchange for patients with acquired thrombotic microangiopathy not associated with severe ADAMTS13 deficiency: a propensity score-matched study.Diagnostic and treatment guidelines for thrombotic thrombocytopenic purpura (TTP) 2017 in Japan.Amino acid residues Arg(659), Arg(660), and Tyr(661) in the spacer domain of ADAMTS13 are critical for cleavage of von Willebrand factor.A conformation-sensitive monoclonal antibody against the A2 domain of von Willebrand factor reduces its proteolysis by ADAMTS13Unraveling the scissile bond: how ADAMTS13 recognizes and cleaves von Willebrand factor.Pathologic mechanisms of type 1 VWD mutations R1205H and Y1584C through in vitro and in vivo mouse models.Why Do We Need ADAMTS13?Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13).Characterization of a core binding site for ADAMTS-13 in the A2 domain of von Willebrand factor.Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloproteaseProbing ADAMTS13 substrate specificity using phage display
P2860
Q24338203-A733CF96-89E8-47DB-A547-4A81E719366DQ24614117-D35534FD-CBF1-4C14-93CC-8A1FE4C73EA1Q24620546-C7411264-B1DF-4F98-92B8-A1D3B2FFD964Q24658043-FC774615-88E3-4DB8-A279-455EBADD1FA6Q26747656-CC9A8C4E-1731-4531-A711-FA170A259FB0Q27670774-C94D863E-402A-4281-A514-EA52C6542A0DQ28588904-F0998696-047C-4313-A996-6DB7B9F53FA5Q28594414-1D419F3D-15C8-4AA9-B1EC-473CD07A61EDQ33231921-D9BA487B-0092-429A-8E2B-750F85BA6637Q33231922-536D1B4D-1F5B-4793-A4FB-6686AA935506Q33365643-C8D1B299-BB07-4E63-8F91-F2FC6798FDAAQ33366296-0BE0B73B-E746-4596-B784-A215A0A6CC5EQ33367858-BFF28982-FDDB-4E8C-AAB5-379201BE7C27Q33369765-B3883102-6A8A-4642-9041-1674BA90A830Q33369893-C04DD5A6-6989-4DB7-9FE4-DBF969FA7071Q33372115-73B250AE-043D-4827-A2C7-52C462BEFA2BQ33373698-87A2A23B-96C3-472B-A541-6740ECB39E8AQ33374478-A0478524-A807-424C-8909-2B2F907CAC3BQ33374597-226900BE-B01D-4DC9-A860-3F9F0895436BQ33378594-05B98F7F-CB98-4784-82F1-E4FCD72565ACQ33382570-CC47B39A-8703-44EF-AA97-2066146C18F7Q33382766-EAC1A7F1-22F9-453E-B2BF-12658330577AQ33393227-975B2C74-F645-4477-8348-ADB025CA7A1BQ33393728-04345C61-42F3-40B3-A491-D51E880FD62FQ33395978-43B03E0B-D92B-4B51-A16B-7410767568BFQ33407332-B3E90D1E-6A15-4AD2-82E4-34D6F80ACD2EQ33407886-4DEEBCC4-A79E-43AB-999D-BAFEEE631E54Q33425489-F53569DD-556C-4DE9-B3B0-294BF3C7BD3AQ33430998-8954B107-AB5C-46D7-A59F-CF5377DA36C2Q33432547-59990AF0-24B2-40D2-8B47-2188AE95880FQ33442170-609A1659-8E25-4235-8897-951EBFC4EE1DQ33747303-B7BAA341-CF8D-4DB3-8BB4-32A33EEC7977Q33968288-9734AB71-784D-44AB-BB47-929DEB0E8657Q34196324-84E86BC9-EB43-4A82-BDEA-68FF9C766084Q34923853-46D9F00B-47F9-46E1-BE1C-F04B08A5453CQ35062975-B7407D46-A2D5-4F60-9A95-CA08D6D784FFQ35105077-EFAEB776-9005-441A-B8F2-6C5ECBB5746AQ35165568-F85F32EE-68B2-47D6-B886-8798D8D57636Q35193294-9EAAF3BA-A51A-4D7F-8E32-61240FA9DE95Q35596768-95EDE116-BF07-4325-ABB6-81B5D2A44B51
P2860
VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13.
description
2003 nî lūn-bûn
@nan
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
VWF73, a region from D1596 to ...... nimal substrate for ADAMTS-13.
@ast
VWF73, a region from D1596 to ...... nimal substrate for ADAMTS-13.
@en
type
label
VWF73, a region from D1596 to ...... nimal substrate for ADAMTS-13.
@ast
VWF73, a region from D1596 to ...... nimal substrate for ADAMTS-13.
@en
prefLabel
VWF73, a region from D1596 to ...... nimal substrate for ADAMTS-13.
@ast
VWF73, a region from D1596 to ...... nimal substrate for ADAMTS-13.
@en
P2093
P1433
P1476
VWF73, a region from D1596 to ...... nimal substrate for ADAMTS-13.
@en
P2093
Koichi Kokame
Masanori Matsumoto
Toshiyuki Miyata
Yoshihiro Fujimura
P304
P356
10.1182/BLOOD-2003-08-2861
P407
P577
2003-09-25T00:00:00Z