Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions. - Wikidata - wikimedia - TriplyDB

Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.

Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.

http://www.wikidata.org/entity/Q33255750

about

Mechanisms of fibrin polymerization and clinical implications Fibrin-based biomaterials: modulation of macroscopic properties through rational design at the molecular level.Molecular interference of fibrin's divalent polymerization mechanism enables modulation of multiscale material properties.Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks.Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.Nonparametric density estimation and optimal bandwidth selection for protein unfolding and unbinding data.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.Building better fibrin knob mimics: an investigation of synthetic fibrin knob peptide structures in solution and their dynamic binding with fibrinogen/fibrin holes.The Platelet Integrin αIIbβ3 Differentially Interacts with Fibrin Versus Fibrinogen Nitrated fibrinogen is a biomarker of oxidative stress in venous thromboembolism Thrombus growth and embolism on tissue factor-bearing collagen surfaces under flow: role of thrombin with and without fibrin.Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense.Blood clots are rapidly assembled hemodynamic sensors: flow arrest triggers intraluminal thrombus contraction Side view thrombosis microfluidic device with controllable wall shear rate and transthrombus pressure gradient.Fibrinogen beta-chain tyrosine nitration is a prothrombotic risk factor Molecular mechanisms, thermodynamics, and dissociation kinetics of knob-hole interactions in fibrin.Structural properties of fracture haematoma: current status and future clinical implications.Fibrin Formation, Structure and Properties.Structural hierarchy governs fibrin gel mechanics Structural effects of methionine oxidation on isolated subdomains of human fibrin D and αC regions.Engineering fibrin matrices: the engagement of polymerization pockets through fibrin knob technology for the delivery and retention of therapeutic proteins.Single-platelet nanomechanics measured by high-throughput cytometry.Strong Binding of Platelet Integrin αIIbβ3 to Fibrin Clots: Potential Target to Destabilize Thrombi.Structural Basis of Interfacial Flexibility in Fibrin Oligomers.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.Recombinant fibrinogen reveals the differential roles of α- and γ-chain cross-linking and molecular heterogeneity in fibrin clot strain-stiffening.

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P2860

Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.

http://www.wikidata.org/entity/Q33255750

description

2006 nî lūn-bûn

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2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի օգոստոսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Polymerization of fibrin: Dire ...... al B:b knob-hole interactions.

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Polymerization of fibrin: Dire ...... al B:b knob-hole interactions.

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Polymerization of fibrin: Dire ...... al B:b knob-hole interactions.

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Polymerization of fibrin: Dire ...... al B:b knob-hole interactions.

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Polymerization of fibrin: Dire ...... al B:b knob-hole interactions.

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Polymerization of fibrin: Dire ...... ual B:b knob-hole interactions

@en

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Dennis K Galanakis

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Henry Shuman

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John W Weisel

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Rustem I Litvinov

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P2860

Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide

2.8 A crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site

Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen

Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin

Crystal structure of fragment double-D from human fibrin with two different bound ligands

Interaction of fibrin(ogen) with the endothelial cell receptor VE-cadherin: mapping of the receptor-binding site in the NH2-terminal portions of the fibrin beta chains

Fibrinogen and fibrin

A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine

Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences

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

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130-138

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10.1182/BLOOD-2006-07-033910

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1

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Sergiy Yakovlev

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6849158

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1785071

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