Mechanism of integrin activation by disulfide bond reduction.
about
Structure of a Complete Integrin Ectodomain in a Physiologic Resting State and Activation and Deactivation by Applied ForcesStructure of an integrin with an αI domain, complement receptor type 4Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidantsProtection against electrophile and oxidant stress by induction of the phase 2 response: fate of cysteines of the Keap1 sensor modified by inducersProtein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacologyBacitracin reveals a role for multiple thiol isomerases in platelet function.SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling.A critical role for extracellular protein disulfide isomerase during thrombus formation in mice.Cytoskeletal perturbation leads to platelet dysfunction and thrombocytopenia in variant forms of Glanzmann thrombastheniaHigh expression of QSOX1 reduces tumorogenesis, and is associated with a better outcome for breast cancer patientsProtein disulfide isomerase in thrombosis and vascular inflammationFRET detection of cellular alpha4-integrin conformational activation.Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques.A single disulfide bond disruption in the β3 integrin subunit promotes thiol/disulfide exchange, a molecular dynamics study.The role of Nox-mediated oxidation in the regulation of cytoskeletal dynamicsFuture innovations in anti-platelet therapies.Regulation of mature ADAM17 by redox agents for L-selectin sheddingIdentification of nitroxyl-induced modifications in human platelet proteins using a novel mass spectrometric detection method.Control of blood proteins by functional disulfide bonds.Glycoprotein IIb/IIIa inhibitors: an update on the mechanism of action and use of functional testing methods to assess antiplatelet efficacy.Redox-relevant aspects of the extracellular matrix and its cellular contacts via integrinsInhibition of Protein Disulfide Isomerase in Thrombosis.Unique disulfide bonds in epidermal growth factor (EGF) domains of β3 affect structure and function of αIIbβ3 and αvβ3 integrins in different manner.Specific cysteines in beta3 are involved in disulfide bond exchange-dependent and -independent activation of alphaIIbbeta3.Interaction and functional association of protein disulfide isomerase with alphaVbeta3 integrin on endothelial cells.Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP) is a multistep process of intra- and intermolecular disulfide rearrangements.Three-dimensional model of human platelet integrin alphaIIb beta3 in solution obtained by small angle neutron scattering.Critical cysteine residues for regulation of integrin alphaIIbbeta3 are clustered in the epidermal growth factor domains of the beta3 subunit.Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3.Adhesion-induced unclasping of cytoplasmic tails of integrin alpha(IIb)beta3.Preparation of stable maleimide-functionalized au nanoparticles and their use in counting surface ligands.Activation of recombinant alphaIIbbeta3 expressed in Chinese hamster ovary cells exposes different binding sites for fibrinogen or von Willebrand factor: evidence using monoclonal antibodies to alphaIIbbeta3.Agonist-specific structural rearrangements of integrin alpha IIbbeta 3. Confirmation of the bent conformation in platelets at rest and after activation.Activation of integrin alphaIIbbeta3 expressed in Chinese hamster ovary cells is required for interaction with solid-phase von Willebrand factor.Thymidine phosphorylase and 2-deoxyribose stimulate human endothelial cell migration by specific activation of the integrins alpha 5 beta 1 and alpha V beta 3.Conformational regulation of alpha 4 beta 1-integrin affinity by reducing agents. "Inside-out" signaling is independent of and additive to reduction-regulated integrin activation.Systems Biology Approaches to Redox Metabolism in Stress and Disease States.The lateral diffusion and fibrinogen induced clustering of platelet integrin αIIbβ3 reconstituted into physiologically mimetic GUVs
P2860
Q27653293-D6B49C47-578A-41CF-87BC-317E21C5A48BQ27658770-C097E6D6-3E5C-46F5-9FDE-AC599E967636Q28218883-DFB69983-D534-4FBF-8F7B-58911670320AQ29616503-CBFF3362-A199-4A7B-AAE8-53A7545A903FQ30368044-3966F256-8C49-41BC-83B8-54003EC76A5DQ30806590-6F3FCEE8-8D42-49E2-8929-772AC7460AADQ33292562-EF2246D5-66C7-4D2D-899D-A3420872A892Q33320817-992A68B7-1835-41EB-B270-97F1744DDF1CQ33426579-A6F1A3A8-8CE7-4F43-9192-3628FAAFAF6BQ33739290-C1B94FE1-1D37-4298-AAF2-D75A28416112Q33827608-385C2D00-5E95-4E60-99A1-76892DE7697BQ34183992-28EB3F0D-D4BE-4737-A55D-37DEEA1D1381Q34624392-9087C617-94EC-438D-AD31-B5501135B0A9Q34634757-A609FDD0-DD8B-49E8-A8A1-283F860EC228Q36424627-BA2A6C3A-8D78-42B4-89D9-23C57A4FC457Q36753593-74C7E5AF-DAE9-4FFE-B6E1-854C3C5B5A48Q37122083-B3095480-6868-4897-8C12-C843D1709282Q37210656-70559713-0307-4195-B163-2C9CFA7C38ADQ37670056-29DB87E4-36B6-4A8A-8D7D-A105898E9157Q37841572-40950598-FBFA-48DE-A97E-28603EAD34BAQ38138161-4AFF2D5F-C753-4F64-B5B8-9A06734385C6Q38751515-EFE11A17-ACAE-4E4D-9476-0F0620566E49Q39401120-F2B16434-7AEF-49A6-8215-1441D6909C86Q39985185-EC35F540-9B21-41B8-839B-903696FB05CEQ40004042-5484ECFD-9369-4D2A-8B69-20F62EC4508DQ40472377-60E23145-6882-4737-8EA0-3B3FC00DCAC0Q41620098-582047FD-22EB-4339-AB88-CFECD8184890Q41852812-C1041641-D4B2-41F7-8F7A-6E13BC8C29C1Q42423811-CF2853AA-AE0A-4BAB-BABE-9B3EE7FABDACQ42583235-7B9DCE39-7B7C-4B5B-BA47-D0EF5EAE43B4Q43058839-C347263A-AF2B-4703-8C19-68F2895EE0DFQ43889368-B8088782-25DA-40F0-9366-615C2A5C3CAAQ44078626-6F625C47-C12E-4178-9D99-20F5FE3280C2Q44242590-AFC3BB5B-D693-4934-83D1-690073DB6CC6Q44364009-3B87AAFE-AC83-44E8-9D59-7FBD1E840048Q44912917-99A014FB-E31C-43B2-84DA-6AE1C5039FDEQ47420453-38B8523D-4C6C-4534-AC09-D6874BBC6579Q57976978-A81C2919-E25B-44C7-807A-B0DD10323D26
P2860
Mechanism of integrin activation by disulfide bond reduction.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Mechanism of integrin activation by disulfide bond reduction.
@ast
Mechanism of integrin activation by disulfide bond reduction.
@en
type
label
Mechanism of integrin activation by disulfide bond reduction.
@ast
Mechanism of integrin activation by disulfide bond reduction.
@en
prefLabel
Mechanism of integrin activation by disulfide bond reduction.
@ast
Mechanism of integrin activation by disulfide bond reduction.
@en
P356
P1433
P1476
Mechanism of integrin activation by disulfide bond reduction.
@en
P304
P356
10.1021/BI002902I
P407
P577
2001-07-01T00:00:00Z