Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
about
The dysfibrinogenaemiasFibrin-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.Fibrinogen variant B D432A has normal polymerization but does not bind knob"B"Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule levelAn integrated study of fibrinogen during blood coagulation.Polymerization of rod-like macromolecular monomers studied by stopped-flow, multiangle light scattering: set-up, data processing, and application to fibrin formation.Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled.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.Influence of cellular and plasma procoagulant activity on the fibrin networkThrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow.Nanoscale probing reveals that reduced stiffness of clots from fibrinogen lacking 42 N-terminal Bbeta-chain residues is due to the formation of abnormal oligomersFibrinogen Dusart: electron microscopy of molecules, fibers and clots, and viscoelastic properties of clots.Three-dimensional reconstruction of fibrin clot networks from stereoscopic intermediate voltage electron microscope images and analysis of branchingCl- regulates the structure of the fibrin clot.Clots of beta-fibrin. Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptidesTwisting of fibrin fibers limits their radial growthNanostructure of the fibrin clot.Fibrinopeptides A and B release in the process of surface fibrin formation.Thrombin-dependent Incorporation of von Willebrand Factor into a Fibrin Network.Experimental and imaging techniques for examining fibrin clot structures in normal and diseased states.Endothelial cell spreading on fibrin requires fibrinopeptide B cleavage and amino acid residues 15-42 of the beta chain.Mice expressing a mutant form of fibrinogen that cannot support fibrin formation exhibit compromised antimicrobial host defense.Dynamic imaging of fibrin network formation correlated with other measures of polymerization.Neprilysin Inhibits Coagulation through Proteolytic Inactivation of FibrinogenPROBING αIIbβ3: LIGAND INTERACTIONS BY DYNAMIC FORCE SPECTROSCOPY AND SURFACE PLASMON RESONANCE.Viscoelasticity and Ultrastructure in Coagulation and Inflammation: Two Diverse Techniques, One Conclusion.Binding of alpha-thrombin to fibrin depends on the quality of the fibrin network.Engineering fibrin matrices: the engagement of polymerization pockets through fibrin knob technology for the delivery and retention of therapeutic proteins.Allosteric effects potentiating the release of the second fibrinopeptide A from fibrinogen by thrombin.Novel Aalpha chain truncation (fibrinogen Perth) resulting in low expression and impaired fibrinogen polymerization.Fibrinogen Mahdia: A congenitally abnormal fibrinogen characterized by defective fibrin polymerization.Nonuniform Internal Structure of Fibrin Fibers: Protein Density and Bond Density Strongly Decrease with Increasing Diameter.Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the gamma chain of firbinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation.Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition for cofactor sites on thrombin determines its fate.Calix[4]arene methylenebisphosphonic acids as inhibitors of fibrin polymerization.
P2860
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P2860
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
description
1986 nî lūn-bûn
@nan
1986 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@ast
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@en
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@nl
type
label
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@ast
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@en
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@nl
prefLabel
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@ast
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@en
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@nl
P2860
P1433
P1476
Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides.
@en
P2093
J W Weisel
P2860
P304
P356
10.1016/S0006-3495(86)83552-4
P407
P577
1986-12-01T00:00:00Z