Role of the alpha C domains of fibrin in clot formation.
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The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosisCrystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolutionNMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen αC-Domain Fragment †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 levelTransglutaminase-catalyzed crosslinking of the Aalpha and gamma constituent chains in fibrinogenPolyphosphate delays fibrin polymerisation and alters the mechanical properties of the fibrin network.Polymerization of rod-like macromolecular monomers studied by stopped-flow, multiangle light scattering: set-up, data processing, and application to fibrin formation.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.Structure, stability, and interaction of the fibrin(ogen) alphaC-domainsFibrinogen Dusart: electron microscopy of molecules, fibers and clots, and viscoelastic properties of clots.Cl- regulates the structure of the fibrin clot.Structural origins of fibrin clot rheologyThe molecular origins of the mechanical properties of fibrin.The minor form alpha' chain from lamprey fibrinogen is rapidly crosslinked during clotting.Evaluation of fibrinogen self-assembly: role of its αC region.Molecular mechanisms affecting fibrin structure and stability.Fibrinogen nanofibril growth and self-assembly on Au (1,1,1) surface in the absence of thrombin.Substitution of the human αC region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibersA model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptidesThe complementary aggregation sites of fibrin investigated through examination of polymers of fibrinogen with fragment E.On the mechanism of αC polymer formation in fibrin.The assembly of nonadhesive fibrinogen matrices depends on the αC regions of the fibrinogen molecule.Neutrophil interaction with the hemostatic system contributes to liver injury in rats cotreated with lipopolysaccharide and ranitidineSubmillisecond elastic recoil reveals molecular origins of fibrin fiber mechanics.Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR.Post-translational oxidative modification of fibrinogen is associated with coagulopathy after traumatic injury.The relationship between the fibrinogen D domain self-association/cross-linking site (gammaXL) and the fibrinogen Dusart abnormality (Aalpha R554C-albumin): clues to thrombophilia in the "Dusart syndrome".Sculpting the blank slate: how fibrin's support of vascularization can inspire biomaterial designStructural properties of fracture haematoma: current status and future clinical implications.Structural hierarchy governs fibrin gel mechanicsMulti-scale strain-stiffening of semiflexible bundle networks.Elimination of coagulation factor XIII from fibrinogen preparations.Identification of the Staphylococcus aureus MSCRAMM clumping factor B (ClfB) binding site in the alphaC-domain of human fibrinogenThe alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis.A modular fibrinogen model that captures the stress-strain behavior of fibrin fibers.Novel Aalpha chain truncation (fibrinogen Perth) resulting in low expression and impaired fibrinogen polymerization.Effect of fibrinogen, fibrin, and fibrin degradation products on transendothelial migration of leukocytes.Functional analysis of recombinant Bbeta15C and Bbeta15A fibrinogens demonstrates that Bbeta15G residue plays important roles in FPB release and in lateral aggregation of protofibrils.
P2860
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P2860
Role of the alpha C domains of fibrin in clot formation.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh-hant
name
Role of the alpha C domains of fibrin in clot formation.
@en
Role of the alpha C domains of fibrin in clot formation.
@nl
type
label
Role of the alpha C domains of fibrin in clot formation.
@en
Role of the alpha C domains of fibrin in clot formation.
@nl
prefLabel
Role of the alpha C domains of fibrin in clot formation.
@en
Role of the alpha C domains of fibrin in clot formation.
@nl
P2093
P356
P1433
P1476
Role of the alpha C domains of fibrin in clot formation
@en
P2093
A H Henschen
J W Weisel
Y I Veklich
P304
P356
10.1021/BI00188A031
P407
P577
1994-06-01T00:00:00Z