Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib. Charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor.
about
Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domainIdentification of the regulatory elements of the human von Willebrand factor for binding to platelet GPIb. Importance of structural integrity of the regions flanked by the CYS1272-CYS1458 disulfide bondCrystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutationsA pH-regulated dimeric bouquet in the structure of von Willebrand factorCrystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrinAn isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domainCrystal structure of the platelet glycoprotein Ib(alpha) N-terminal domain reveals an unmasking mechanism for receptor activationCrystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 FabSubunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome.Assembly of Weibel-Palade body-like tubules from N-terminal domains of von Willebrand factorPlatelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF.Platelet adhesion involves a novel interaction between vimentin and von Willebrand factor under high shear stressAn HMM-based algorithm for evaluating rates of receptor-ligand binding kinetics from thermal fluctuation data.Measurement of the binding forces between von Willebrand factor and variants of platelet glycoprotein Ibalpha using optical tweezers.O-linked glycosylation and functional incompatibility of porcine von Willebrand factor for human platelet GPIb receptors.Targeting von Willebrand factor and platelet glycoprotein Ib receptor.An optimized fluorogenic ADAMTS13 assay with increased sensitivity for the investigation of patients with thrombotic thrombocytopenic purpura.Flow-induced beta-hairpin folding of the glycoprotein Ibalpha beta-switchThe molecular biology of von Willebrand disease.GPIbα-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease.Phylogenetic and functional analysis of histidine residues essential for pH-dependent multimerization of von Willebrand factor.Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloproteaseN-terminal flanking region of A1 domain in von Willebrand factor stabilizes structure of A1A2A3 complex and modulates platelet activation under shear stress.Two Cys residues essential for von Willebrand factor multimer assembly in the Golgi.Binding of platelet glycoprotein Ibalpha to von Willebrand factor domain A1 stimulates the cleavage of the adjacent domain A2 by ADAMTS13.A mechanism for localized dynamics-driven affinity regulation of the binding of von Willebrand factor to platelet glycoprotein Ibα.The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von Willebrand factor to platelet glycoprotein Ibα.Accelerated clearance alone explains ultra-large multimers in von Willebrand disease VicenzaShielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V.Conformational changes in the A1 domain of von Willebrand factor modulating the interaction with platelet glycoprotein Ibalpha.New Concepts and Mechanisms of Platelet Activation Signaling.A biophysical view on von Willebrand factor activation.A discrete site modulates activation of I domains. Application to integrin alphaMbeta2.von Willebrand factor: biological function and molecular defects.Modeling and functional analysis of the interaction between von Willebrand factor A1 domain and glycoprotein Ibalpha.Cloning of the cDNA for murine von Willebrand factor and identification of orthologous genes reveals the extent of conservation among diverse species.Identification of amino acid residues responsible for von Willebrand factor binding to sulfatide by charged-to-alanine-scanning mutagenesis.A new mutation, S1285F, within the A1 loop of von Willebrand factor induces a conformational change in A1 loop with abnormal binding to platelet GPIb and botrocetin causing type 2M von Willebrand disease.Identification of the amino acid residues of the platelet glycoprotein Ib (GPIb) essential for the von Willebrand factor binding by clustered charged-to-alanine scanning mutagenesis.Impact of O-linked glycosylation of the VWF-A1-domain flanking regions on platelet interaction.
P2860
Q22253890-F824CE36-8E45-41EC-854E-8360E582E8C0Q24293697-D955C1D9-986C-4904-A6AD-E3336B9B128BQ24319306-70CFB67B-7B7B-4518-91A7-7B0083D2F4FAQ24324184-AA9DBAD4-22CF-4EE2-8FB0-B32CE782DCC5Q24563636-2DBAB1E4-5B2A-4D08-9C02-1BCC629BDD39Q27627500-CFAA62AA-FF5D-41DB-94D1-822D3D643AE2Q27639267-66CC7D11-58B2-4AE9-A29D-307AE3BC74B6Q27748925-6762D0E2-E6B7-4CE1-A59E-9B27748A46E3Q27931947-B53CC721-A432-4440-8BE2-4B33E60019D7Q30443824-9FB8CCD7-3092-45CA-B016-D6CF301D51FBQ30483148-9E12B672-6245-4E80-931F-F22A4F3C1AF6Q30577008-2A23EE4B-8912-4B9F-8C4C-0BCFDDA8393BQ30618745-4017295D-62B3-4396-B21C-FBED328413D3Q31048172-29FA9463-4820-4BB2-9EEB-1570A58AD97CQ33364143-D32F3B5A-15CD-42B6-9A4C-F813EA2B0F45Q33392975-47459E2C-4F52-4626-A013-7E9599B8EBD5Q33408427-6217613C-D8D2-4D5D-B852-A024ACC2B28DQ34062531-8B9DEB26-75D7-48EE-BE14-4496F55DA202Q34421530-668945DE-CCC4-464F-A8F1-32271D555DABQ34494411-898FE471-82F7-4200-8044-B5688E731550Q35110960-6BEB1C35-ACDA-4034-92E7-4DA9B5239431Q35193294-C43EA686-3321-4F87-9F46-B6716A3D28D9Q35922561-A23F1C36-46B2-456C-A1A2-D192A4E4F653Q36013413-6CCB35E5-7D26-4519-BDC4-F471351B951CQ36986074-13890C46-F3A1-40CA-8E69-C5F20227A4CBQ37168411-219891A7-7846-45F3-AB47-0331B60065D0Q37289199-6BC0E5E8-E2E3-469A-8579-C1BEF922513BQ37393334-0C834E5A-17E6-42A2-A0A0-923C4AF5696BQ38317425-725421AF-E0BD-4542-BB0B-8AD1A33CFE4FQ38359108-45BE98EC-56F6-456D-AA29-AB1D1F26428FQ39147112-B408EC2E-5C45-4EED-9E80-81E3C2352AFCQ39159765-1C09D984-484D-4775-B882-DDFFF3655201Q41150359-C7FC5669-477C-450F-A3E5-05761A7F7B21Q41651628-CB801A6A-433C-4DD7-B93A-67E58E872B85Q41731691-F0FF3A4B-FAFB-44F2-AC9C-58E05471DBE3Q42620255-AFB49440-565C-44C2-B1DD-579CF3A40E2DQ43146191-4C767A00-FDA0-4E6F-81C3-96B9014F6C98Q44316600-F7E4E00E-F9A7-4DA8-BC7D-E2D67617F6DCQ44752490-854B22C6-F94B-46C7-A273-1A4F5966429DQ45192183-AFA63C3C-A59F-45B3-9CB9-0D6801F8C072
P2860
Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib. Charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Identification of amino acid r ...... f human von Willebrand factor.
@en
type
label
Identification of amino acid r ...... f human von Willebrand factor.
@en
prefLabel
Identification of amino acid r ...... f human von Willebrand factor.
@en
P2860
P356
P1476
Identification of amino acid r ...... f human von Willebrand factor.
@en
P2093
Matsushita T
P2860
P304
13406-13414
P356
10.1074/JBC.270.22.13406
P407
P577
1995-06-01T00:00:00Z