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1 ing mediated by natural B-knobs exposed in a fibrin monomer.
2 25)I-labeled VEGF- and Sepharose-immobilized fibrin monomer.
3 in and fibrinogen or by the reassociation of fibrin monomers.
4 ide or isopeptide bond that ligates adjacent fibrin monomers.
5 thrombin was normal in rate and amount, but fibrin monomer aggregation was grossly disturbed, especi
8 ough the introduction of cross-links between fibrin monomers and through cross-linking of proteins wi
9 ion of fibrinogen, (3) the polymerization of fibrin monomers, and (4) FXIIIa-catalyzed cross-link for
11 hat the C domains of VWF and the E domain of fibrin monomers are involved in the incorporation of VWF
13 then by approximately 50% of the length of a fibrin monomer before rupture of the 'A-a' interaction.
14 nto self-aggregating, fully coagulable alpha-fibrin monomers, but the fibrin precursor with one site
15 n precursor because it is converted to alpha-fibrin monomer faster than fibrinogen converts to monome
16 ere prepared, and their abilities to inhibit fibrin monomers from repolymerizing were compared in tur
18 ptide bonds between noncovalently associated fibrin monomers in the final stages of the blood coagula
19 or XIIIa (FXIIIa) catalyzed cross-linking of fibrin monomers, is currently still a challenge in medic
20 study we found proof for binding of VWF to a fibrin monomer layer during the process of fibrinogen-to
23 cular markers thrombin/antithrombin, soluble fibrin monomer, protein C, and activated protein C/inhib
24 gulation, soluble fibrinogen is converted to fibrin monomers that polymerize to form an insoluble clo
26 f knobs 'A' and 'B' in the central nodule of fibrin monomer to complementary holes 'a' and 'b' in the
27 profibrin forms soluble complexes with alpha-fibrin monomer under conditions in which it and fibrin p
29 First, thrombin cleaves fibrinogen producing fibrin monomers, which polymerize and serve as a templat
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