Multi-step fibrinogen binding to the integrin (alpha)IIb(beta)3 detected using force spectroscopy. - Wikidata - wikimedia - TriplyDB

Multi-step fibrinogen binding to the integrin (alpha)IIb(beta)3 detected using force spectroscopy.

Multi-step fibrinogen binding to the integrin (alpha)IIb(beta)3 detected using force spectroscopy.

http://www.wikidata.org/entity/Q33220247

about

Platelets lacking PIP5KIγ have normal integrin activation but impaired cytoskeletal-membrane integrity and adhesion Loss of PIP5KIgamma, unlike other PIP5KI isoforms, impairs the integrity of the membrane cytoskeleton in murine megakaryocytes.Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.Dynamic antibody-binding properties in the pathogenesis of HIT.Distinct specificity and single-molecule kinetics characterize the interaction of pathogenic and non-pathogenic antibodies against platelet factor 4-heparin complexes with platelet factor 4.Anti-platelet factor 4/polyanion antibodies mediate a new mechanism of autoimmunity.Effect of pH and ionic strength on the binding strength of anti-PF4/polyanion antibodies.What is vinculin needed for in platelets?Identification of interacting hot spots in the beta3 integrin stalk using comprehensive interface design Single-molecule adhesion forces and attachment lifetimes of myosin-I phosphoinositide interactions Dissociation of bimolecular αIIbβ3-fibrinogen complex under a constant tensile force.Measurement of the Interaction Between Recombinant I-domain from Integrin alpha 2 beta 1 and a Triple Helical Collagen Peptide with the GFOGER Binding Motif Using Molecular Force Spectroscopy Fibrin serves as a divalent ligand that regulates neutrophil-mediated melanoma cells adhesion to endothelium under shear conditions The Platelet Integrin αIIbβ3 Differentially Interacts with Fibrin Versus Fibrinogen On the mechanism of αC polymer formation in fibrin.Resolving two-dimensional kinetics of the integrin αIIbβ3-fibrinogen interactions using binding-unbinding correlation spectroscopy Optical tweezers for single cells Platelet adhesion: a game of catch and release Studying Molecular Interactions at the Single Bond Level with a Laminar Flow Chamber.Biomechanics of cell adhesion: how force regulates the lifetime of adhesive bonds at the single molecule level.Regulation of integrins in platelets.Engineered isopeptide bond stabilized fibrin inspired nanoscale peptide based sealants for efficient blood clotting.Simulation of aggregating particles in complex flows by the lattice kinetic Monte Carlo method Bimolecular integrin-ligand interactions quantified using peptide-functionalized dextran-coated microparticles.Activation induced morphological changes and integrin αIIbβ3 activity of living platelets.Shear strengthens fibrin: the knob-hole interactions display 'catch-slip' kinetics.Strong Binding of Platelet Integrin αIIbβ3 to Fibrin Clots: Potential Target to Destabilize Thrombi.Targeted molecular dynamics reveals overall common conformational changes upon hybrid domain swing-out in beta3 integrins.Laminin-111-derived peptide conjugated fibrin hydrogel restores salivary gland function.β1-Integrin-Mediated Adhesion Is Lipid-Bilayer Dependent.Single-molecule measurements of the effect of force on Thy-1/αvβ3-integrin interaction using non-purified proteins.Single-Molecule Interactions of a Monoclonal Anti-DNA Antibody with DNA.Mechanistic Basis for the Binding of RGD- and AGDV-Peptides to the Platelet Integrin αIIbβ3.Interaction of integrin alphaIIb beta3 with Fibrinogen Modelling of platelet-fibrin clot formation in flow with a DPD-PDE method.A study of the distribution and density of the VEGFR-2 receptor on glioma microvascular endothelial cell membranes.Molecular Force Sensors: From Fundamental Concepts toward Applications in Cell Biology

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P2860

Multi-step fibrinogen binding to the integrin (alpha)IIb(beta)3 detected using force spectroscopy.

http://www.wikidata.org/entity/Q33220247

description

2005 nî lūn-bûn

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2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Multi-step fibrinogen binding ...... cted using force spectroscopy.

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Multi-step fibrinogen binding ...... cted using force spectroscopy.

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type

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Multi-step fibrinogen binding ...... cted using force spectroscopy.

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Multi-step fibrinogen binding ...... cted using force spectroscopy.

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Multi-step fibrinogen binding ...... cted using force spectroscopy.

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Multi-step fibrinogen binding ...... cted using force spectroscopy.

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BIOPHYSJ.105.061887

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Biophysical Journal

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Multi-step fibrinogen binding ...... cted using force spectroscopy.

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P2093

Henry Shuman

http://www.w3.org/2001/XMLSchema#string

Joel S Bennett

http://www.w3.org/2001/XMLSchema#string

John W Weisel

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Rustem I Litvinov

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P2860

A structural basis for integrin activation by the cytoplasmic tail of the alpha IIb-subunit

A microcantilever device to assess the effect of force on the lifetime of selectin-carbohydrate bonds.

Models for the specific adhesion of cells to cells

The molecular mechanics of P- and L-selectin lectin domains binding to PSGL-1

Two-dimensional tracking of ncd motility by back focal plane interferometry.

Combined laser tweezers and dielectric field cage for the analysis of receptor-ligand interactions on single cells.

Binding strength and activation state of single fibrinogen-integrin pairs on living cells.

Dynamics of the interaction between a fibronectin molecule and a living bacterium under mechanical force.

Advanced optical tweezers for the study of cellular and molecular biomechanics.

Measuring the forces that control protein interactions.

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2824-2834

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10.1529/BIOPHYSJ.105.061887

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2005-07-22T00:00:00Z

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1366781

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