메뉴 건너뛰기




Volumn 77, Issue 5, 1999, Pages 2813-2826

Structural origins of fibrin clot rheology

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 13A; BLOOD CLOTTING INHIBITOR; CALCIUM ION; FIBRIN; FIBRINOGEN; THROMBIN;

EID: 0032729622     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77113-4     Document Type: Article
Times cited : (467)

References (94)
  • 1
    • 0011842032 scopus 로고
    • Size and shape of fibrinogen. 1. Electron microscopy of the hydrated molecule
    • Bachmann, L., W. W. Schmitt-Fumian, R. Hammel, and K. Lederer. 1975. Size and shape of fibrinogen. 1. Electron microscopy of the hydrated molecule. Makromol. Chem. 176:2603-2618.
    • (1975) Makromol. Chem. , vol.176 , pp. 2603-2618
    • Bachmann, L.1    Schmitt-Fumian, W.W.2    Hammel, R.3    Lederer, K.4
  • 2
    • 0028926219 scopus 로고
    • Three-dimensional reconstruction of fibrin clot networks from stereoscopic intermediate voltage electron microscope images and analysis of branching
    • Baradet, T. C., J. C. Haselgrove, and J. W. Weisel. 1995. Three-dimensional reconstruction of fibrin clot networks from stereoscopic intermediate voltage electron microscope images and analysis of branching. Biophys. J. 68:1551-1560.
    • (1995) Biophys. J. , vol.68 , pp. 1551-1560
    • Baradet, T.C.1    Haselgrove, J.C.2    Weisel, J.W.3
  • 4
    • 0018129207 scopus 로고
    • A two-step fibrinogen-fibrin transition in blood coagulation
    • Blomback, B., B. Hessel, D. Hogg, and L. Therkildsen. 1978. A two-step fibrinogen-fibrin transition in blood coagulation. Nature (Lond.). 275: 501-505.
    • (1978) Nature (Lond.) , vol.275 , pp. 501-505
    • Blomback, B.1    Hessel, B.2    Hogg, D.3    Therkildsen, L.4
  • 5
    • 0020042713 scopus 로고
    • Fibrin gel structure and clotting time
    • Blomback, B., and M. Okada. 1982. Fibrin gel structure and clotting time. Thromb. Haemostasis. 25:51-70.
    • (1982) Thromb. Haemostasis , vol.25 , pp. 51-70
    • Blomback, B.1    Okada, M.2
  • 6
    • 0021146257 scopus 로고
    • Fibrin gels as biological filters and interfaces
    • Blomback, B., M. Okada, B. Forslind, and U. Larsson. 1984. Fibrin gels as biological filters and interfaces. Biorheology. 21:93-104.
    • (1984) Biorheology , vol.21 , pp. 93-104
    • Blomback, B.1    Okada, M.2    Forslind, B.3    Larsson, U.4
  • 7
    • 0015304822 scopus 로고
    • Acceleration of fibrin polymerization by calcium ions
    • Boyer, M. H., J. R. Shainoff, and O. D. Ratnoff. 1972. Acceleration of fibrin polymerization by calcium ions. Blood. 39:382-387.
    • (1972) Blood , vol.39 , pp. 382-387
    • Boyer, M.H.1    Shainoff, J.R.2    Ratnoff, O.D.3
  • 8
    • 0018133275 scopus 로고
    • Fibrin formation: Effect of calcium ions
    • Brass, E. P., W. B. Forman, R. V. Edwards, and O. Lindan. 1978. Fibrin formation: effect of calcium ions. Blood. 52:654-658.
    • (1978) Blood , vol.52 , pp. 654-658
    • Brass, E.P.1    Forman, W.B.2    Edwards, R.V.3    Lindan, O.4
  • 9
    • 0016366236 scopus 로고
    • Thrombelastographic patterns of ancrod and thrombin fibrin formation and dissolution
    • Caprini, J. A., H. C. Kwaan, L. Zuckerman, and R. Verduin. 1974. Thrombelastographic patterns of ancrod and thrombin fibrin formation and dissolution. Thromb. Res. 4:199-217.
    • (1974) Thromb. Res. , vol.4 , pp. 199-217
    • Caprini, J.A.1    Kwaan, H.C.2    Zuckerman, L.3    Verduin, R.4
  • 10
    • 0023903071 scopus 로고
    • Fibrin formed in plasma is composed of fibers more massive than those formed from purified fibrinogen
    • Carr, M. E. 1988. Fibrin formed in plasma is composed of fibers more massive than those formed from purified fibrinogen. Thromb. Haemostasis. 59:535-539.
    • (1988) Thromb. Haemostasis , vol.59 , pp. 535-539
    • Carr, M.E.1
  • 11
    • 0029100827 scopus 로고
    • Effect of fibrin structure on plasmin-mediated dissolution of plasma clots
    • Carr, M. E., and B. M. Alving. 1995. Effect of fibrin structure on plasmin-mediated dissolution of plasma clots. Blood Coagul. Fibrinolysis. 6:567-573.
    • (1995) Blood Coagul. Fibrinolysis , vol.6 , pp. 567-573
    • Carr, M.E.1    Alving, B.M.2
  • 12
    • 0028953090 scopus 로고
    • Fibrin structure and concentration alter clot elastic modulus but do not alter platelet mediated force development
    • Carr, M. E., and S. L. Carr. 1995. Fibrin structure and concentration alter clot elastic modulus but do not alter platelet mediated force development. Blood Coagul. Fibrinolysis. 6:79-86.
    • (1995) Blood Coagul. Fibrinolysis , vol.6 , pp. 79-86
    • Carr, M.E.1    Carr, S.L.2
  • 13
    • 0022924149 scopus 로고
    • 2+ on the structure of reptilase-derived and thrombin-derived fibrin gels
    • 2+ on the structure of reptilase-derived and thrombin-derived fibrin gels. Biochem. J. 239:513-516.
    • (1986) Biochem. J. , vol.239 , pp. 513-516
    • Carr, M.E.1    Gabriel, D.A.2    McDonagh, J.3
  • 14
    • 0023583663 scopus 로고
    • Influence of factor XIII and fibronectin on fiber size and density in thrombin-induced fibrin gels
    • Carr, M. E., D. A. Gabriel, and J. McDonagh. 1987. Influence of factor XIII and fibronectin on fiber size and density in thrombin-induced fibrin gels. J. Lab. Clin. Med. 110:747-752.
    • (1987) J. Lab. Clin. Med. , vol.110 , pp. 747-752
    • Carr, M.E.1    Gabriel, D.A.2    McDonagh, J.3
  • 15
    • 0017910967 scopus 로고
    • Size and density of fibrin fibers from turbidity
    • Carr, M. E., and J. Hermans. 1978. Size and density of fibrin fibers from turbidity. Macromolecules. 11:46-50.
    • (1978) Macromolecules , vol.11 , pp. 46-50
    • Carr, M.E.1    Hermans, J.2
  • 16
    • 0017601513 scopus 로고
    • Mass-length ratio of fibrin fibers from gel permeation and light scattering
    • Carr, M. E., L. L. Shen, and J. Hermans. 1977. Mass-length ratio of fibrin fibers from gel permeation and light scattering. Biopolymers. 16:1-15.
    • (1977) Biopolymers , vol.16 , pp. 1-15
    • Carr, M.E.1    Shen, L.L.2    Hermans, J.3
  • 17
    • 0014531411 scopus 로고
    • Identification of the polypeptide chains involved in the cross-linking of fibrin
    • Chen, R., and R. F. Doolittle. 1969. Identification of the polypeptide chains involved in the cross-linking of fibrin. Proc. Natl. Acad. Sci. USA. 63:420-427.
    • (1969) Proc. Natl. Acad. Sci. USA. , vol.63 , pp. 420-427
    • Chen, R.1    Doolittle, R.F.2
  • 18
    • 33947290263 scopus 로고
    • γ-γ Cross-linking sites in human and bovine fibrin
    • Chen, R., and R. F. Doolittle. 1971. γ-γ Cross-linking sites in human and bovine fibrin. Biochemistry. 10:4486-4491.
    • (1971) Biochemistry , vol.10 , pp. 4486-4491
    • Chen, R.1    Doolittle, R.F.2
  • 19
    • 0024443424 scopus 로고
    • Fibrinogen sialic acid residues are low affinity calcium binding sites that influence fibrin assembly
    • Dang, C. V., C. K. Shin, W. R. Bell, C. Nagaswami, and J. W. Weisel. 1989. Fibrinogen sialic acid residues are low affinity calcium binding sites that influence fibrin assembly. J. biol. Chem. 264:15104-15108.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15104-15108
    • Dang, C.V.1    Shin, C.K.2    Bell, W.R.3    Nagaswami, C.4    Weisel, J.W.5
  • 20
    • 0018996782 scopus 로고
    • Nonlinear elasticity of rodlike macromolecules in condensed state
    • Doi, M., and N. Y. Kuzuu. 1980. Nonlinear elasticity of rodlike macromolecules in condensed state. J. Polym. Sci., Polym. Phys. Ed. 18: 409-419.
    • (1980) J. Polym. Sci., Polym. Phys. Ed. , vol.18 , pp. 409-419
    • Doi, M.1    Kuzuu, N.Y.2
  • 21
    • 0015208063 scopus 로고
    • Hybrid fibrin: Proof of the intermolecular nature of γ-γ cross-linking units
    • Doolittle, R. F., R. Chen, and F. Lau. 1971. Hybrid fibrin: proof of the intermolecular nature of γ-γ cross-linking units. Biochem. Biophys. Res. Commun. 44:94-100.
    • (1971) Biochem. Biophys. Res. Commun. , vol.44 , pp. 94-100
    • Doolittle, R.F.1    Chen, R.2    Lau, F.3
  • 22
    • 0015426046 scopus 로고
    • Equilibria in the fibrinogen-fibrin conversion. IX. Effects of calcium ions on the reversible polymerization of fibrin monomer
    • Endres, G. F., and H. A. Scheraga, 1972. Equilibria in the fibrinogen-fibrin conversion. IX. Effects of calcium ions on the reversible polymerization of fibrin monomer. Arch. Biochem. Biophys. 153:266-278.
    • (1972) Arch. Biochem. Biophys. , vol.153 , pp. 266-278
    • Endres, G.F.1    Scheraga, H.A.2
  • 23
    • 0020645311 scopus 로고
    • Electron microscopy of fibrinogen, its plasmic fragments and small polymers
    • Erickson, H. P., and W. E. Fowler. 1983. Electron microscopy of fibrinogen, its plasmic fragments and small polymers. Ann. NY Acad. Sci. 408:146-163.
    • (1983) Ann. NY Acad. Sci. , vol.408 , pp. 146-163
    • Erickson, H.P.1    Fowler, W.E.2
  • 24
    • 0019306559 scopus 로고
    • Electron microscopy of negatively stained and unstained fibrinogen
    • Estis, L. F., and R. H. Haschemeyer. 1980. Electron microscopy of negatively stained and unstained fibrinogen. Proc. Natl. Acad. Sci. USA. 77:3139-3143.
    • (1980) Proc. Natl. Acad. Sci. USA. , vol.77 , pp. 3139-3143
    • Estis, L.F.1    Haschemeyer, R.H.2
  • 25
    • 0002879442 scopus 로고
    • Human thrombins
    • R. L. Lundblad, J. W. Fenton, II, and K. G. Mann, editors. Ann Arbor Science, Ann Arbor, Michigan
    • Fenton, J. W., II, B. H. Landis, D. A. Walz, and J. S. Finlayson. 1977. Human thrombins. In Chemistry and Biology of Thrombin. R. L. Lundblad, J. W. Fenton, II, and K. G. Mann, editors. Ann Arbor Science, Ann Arbor, Michigan. 43-70.
    • (1977) Chemistry and Biology of Thrombin , pp. 43-70
    • Fenton J.W. II1    Landis, B.H.2    Walz, D.A.3    Finlayson, J.S.4
  • 27
    • 0345052707 scopus 로고
    • The conversion of fibrinogen to fibrin. VII. Rigidity and stress relaxation of fibrin clots; effects of calcium
    • Ferry, J. D., M. Miller, and S. Shulman. 1951. The conversion of fibrinogen to fibrin. VII. Rigidity and stress relaxation of fibrin clots; effects of calcium. Arch. Biochem. Biophys. 34:424-436.
    • (1951) Arch. Biochem. Biophys. , vol.34 , pp. 424-436
    • Ferry, J.D.1    Miller, M.2    Shulman, S.3
  • 28
    • 0001454124 scopus 로고
    • Preparation and properties of serum and plasma proteins. IX. Human fibrin in the form of an elastic film
    • Ferry, J. D., and P. R. Morrison. 1947. Preparation and properties of serum and plasma proteins. IX. Human fibrin in the form of an elastic film. J. Am. Chem. Soc. 69:400-409.
    • (1947) J. Am. Chem. Soc. , vol.69 , pp. 400-409
    • Ferry, J.D.1    Morrison, P.R.2
  • 31
  • 32
    • 0015903468 scopus 로고
    • The dynamic rigidity of fibrin gels
    • Fukada, E., and M. Kaibara. 1973. The dynamic rigidity of fibrin gels. Biorheology. 10:129-138.
    • (1973) Biorheology , vol.10 , pp. 129-138
    • Fukada, E.1    Kaibara, M.2
  • 33
    • 0026491075 scopus 로고
    • The effect of fibrin structure on fibrinolysis
    • Gabriel, D. A., K. Muga, and E. M. Boothroyd. 1992. The effect of fibrin structure on fibrinolysis. J. Biol. Chem. 267:24259-24263.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24259-24263
    • Gabriel, D.A.1    Muga, K.2    Boothroyd, E.M.3
  • 34
    • 0016274342 scopus 로고
    • Rheology of fibrin clots. II. Linear viscoelastic behavior in shear creep
    • Gerth, C., W. W. Roberts, and J. D. Ferry. 1974. Rheology of fibrin clots. II. Linear viscoelastic behavior in shear creep. Biophys. Chem. 2:208-217.
    • (1974) Biophys. Chem. , vol.2 , pp. 208-217
    • Gerth, C.1    Roberts, W.W.2    Ferry, J.D.3
  • 35
    • 0020625071 scopus 로고
    • Effects of cross-linking on the rigidity and proteolytic susceptibility of human fibrin clots
    • Gladner, J. A., and R. Nossal. 1983. Effects of cross-linking on the rigidity and proteolytic susceptibility of human fibrin clots. Thromb. Res. 30: 273-288.
    • (1983) Thromb. Res. , vol.30 , pp. 273-288
    • Gladner, J.A.1    Nossal, R.2
  • 36
    • 0016701444 scopus 로고
    • Rheological properties of fibrin clots. Effects of fibrinogen concentration, factor XIII deficiency, and factor XIII inhibition
    • Glover, C. J., L. V. McIntire, C. H. Brown, and E. A. Natelson. 1975. Rheological properties of fibrin clots. Effects of fibrinogen concentration, factor XIII deficiency, and factor XIII inhibition. J. Lab. Clin. Med. 86:644-656.
    • (1975) J. Lab. Clin. Med. , vol.86 , pp. 644-656
    • Glover, C.J.1    McIntire, L.V.2    Brown, C.H.3    Natelson, E.A.4
  • 41
    • 70249091771 scopus 로고
    • The fibrinogen molecule: Its size, shape, and mode of polymerization
    • Hall, C. E., and H. S. Slayter. 1959. The fibrinogen molecule: its size, shape, and mode of polymerization. J. Biophys. Biochem. Cytol. 5:11-17.
    • (1959) J. Biophys. Biochem. Cytol. , vol.5 , pp. 11-17
    • Hall, C.E.1    Slayter, H.S.2
  • 42
    • 0019210979 scopus 로고
    • Fibrin assembly: A comparison of electron microscopic and light scattering results
    • Hantgan, R. R., W. Fowler, H. Erickson, and J. Hermans. 1980. Fibrin assembly: a comparison of electron microscopic and light scattering results. Thromb. Haemostasis. 44:119-124.
    • (1980) Thromb. Haemostasis , vol.44 , pp. 119-124
    • Hantgan, R.R.1    Fowler, W.2    Erickson, H.3    Hermans, J.4
  • 43
    • 0018597469 scopus 로고
    • Assembly of fibrin
    • Hantgan, R. R., and J. Hermans. 1979. Assembly of fibrin. J. Biol Chem. 254:11272-11281.
    • (1979) J. Biol Chem. , vol.254 , pp. 11272-11281
    • Hantgan, R.R.1    Hermans, J.2
  • 45
    • 0020645319 scopus 로고
    • Calcium ion functions in fibrinogen conversion to fibrin
    • Hardy, J. J., N. A. Carrell, and J. McDonagh. 1983. Calcium ion functions in fibrinogen conversion to fibrin. Ann. NY Acad. Sci. 408:279-287.
    • (1983) Ann. NY Acad. Sci. , vol.408 , pp. 279-287
    • Hardy, J.J.1    Carrell, N.A.2    McDonagh, J.3
  • 46
    • 0032527073 scopus 로고    scopus 로고
    • Effects of fibrin micromorphology and density on neurite growth from dorsal root ganglia cultured within three-dimensional fibrin gels
    • Herbert, C. B., C. Nagaswami, G. D. Bittner, J. A. Hubbell, and J. W. Weisel. 1998. Effects of fibrin micromorphology and density on neurite growth from dorsal root ganglia cultured within three-dimensional fibrin gels. J. Biomed. Mater. Res. 40:551-559.
    • (1998) J. Biomed. Mater. Res. , vol.40 , pp. 551-559
    • Herbert, C.B.1    Nagaswami, C.2    Bittner, G.D.3    Hubbell, J.A.4    Weisel, J.W.5
  • 47
    • 0020734317 scopus 로고
    • Rheology of fibrin clots. Vi. Stress relaxation, creep, and differential dynamic modulus of fine clots in large shearing deformations
    • Janmey, P. A., E. J. Amis, and J. D. Ferry. 1983. Rheology of fibrin clots. VI. Stress relaxation, creep, and differential dynamic modulus of fine clots in large shearing deformations. J. Rheol. 27:135-153.
    • (1983) J. Rheol. , vol.27 , pp. 135-153
    • Janmey, P.A.1    Amis, E.J.2    Ferry, J.D.3
  • 48
    • 0015592072 scopus 로고
    • Dynamic viscoelastic study of the formation of fibrin networks in fibrinogen-thrombin systems and plasma
    • Kaibara, M. 1973. Dynamic viscoelastic study of the formation of fibrin networks in fibrinogen-thrombin systems and plasma. Biorheology. 10: 61-73.
    • (1973) Biorheology , vol.10 , pp. 61-73
    • Kaibara, M.1
  • 49
    • 0014772838 scopus 로고
    • Dynamic viscoelastic study for the structure of fibrin networks in the clots of blood and plasma
    • Kaibara, M., and E. Fukada. 1970. Dynamic viscoelastic study for the structure of fibrin networks in the clots of blood and plasma. Biorheology. 6:329-339.
    • (1970) Biorheology , vol.6 , pp. 329-339
    • Kaibara, M.1    Fukada, E.2
  • 50
    • 0015171319 scopus 로고
    • The influence of the concentration of thrombin and the dynamic viscoelasticity of clotting blood and fibrinogen-thrombin systems
    • Kaibara, M., and E. Fukada. 1971. The influence of the concentration of thrombin and the dynamic viscoelasticity of clotting blood and fibrinogen-thrombin systems. Biorheology. 8:139-147.
    • (1971) Biorheology , vol.8 , pp. 139-147
    • Kaibara, M.1    Fukada, E.2
  • 51
    • 0017357934 scopus 로고
    • Fibrin digestion by thrombin. Comparison with plasmin-digested fibrinogen
    • Kang, E. P., and D. C. Triantaphyllopoulos. 1977a. Fibrin digestion by thrombin. Comparison with plasmin-digested fibrinogen. Biochim. Biophys. Acta. 490:403-442.
    • (1977) Biochim. Biophys. Acta , vol.490 , pp. 403-442
    • Kang, E.P.1    Triantaphyllopoulos, D.C.2
  • 52
    • 0017667467 scopus 로고
    • Fibrin digestion by thrombin. The significance of the arginyl and lysyl bonds
    • Kang, E. P., and D. C. Triantaphyllopoulos. 1977b. Fibrin digestion by thrombin. The significance of the arginyl and lysyl bonds. Thromb. Res. 11:403-415.
    • (1977) Thromb. Res. , vol.11 , pp. 403-415
    • Kang, E.P.1    Triantaphyllopoulos, D.C.2
  • 53
    • 33845382806 scopus 로고
    • Nonparametric estimation from incomplete observations
    • Kaplan, E. L., and P. Meier. 1958. Nonparametric estimation from incomplete observations. J. Am. Stat. Assoc. 53:457-481.
    • (1958) J. Am. Stat. Assoc. , vol.53 , pp. 457-481
    • Kaplan, E.L.1    Meier, P.2
  • 54
    • 0030997702 scopus 로고    scopus 로고
    • Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation
    • Kolev, K., K. Tenekedjiev, E. Komorowicz, and R. Machovich. 1997. Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation. J. Biol. Chem. 272: 13606-13675.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13606-13675
    • Kolev, K.1    Tenekedjiev, K.2    Komorowicz, E.3    Machovich, R.4
  • 55
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 56
    • 0023752048 scopus 로고
    • Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers
    • Langer, B. G., J. W. Weisel, P. A. Dinauer, C. Nagaswami, and W. R. Bell. 1988. Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers. J. Biol. Chem. 263: 15056-15063.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15056-15063
    • Langer, B.G.1    Weisel, J.W.2    Dinauer, P.A.3    Nagaswami, C.4    Bell, W.R.5
  • 57
    • 0019870106 scopus 로고
    • Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen
    • Laudano, A. P., and R. F. Doolittle. 1981. Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen. Science (Wash. DC). 212:457-459.
    • (1981) Science (Wash. DC) , vol.212 , pp. 457-459
    • Laudano, A.P.1    Doolittle, R.F.2
  • 58
    • 0002162129 scopus 로고
    • Activation of the fibrin stabilization factor of plasma by thrombin
    • Lorand, L., and K. Konishi. 1964. Activation of the fibrin stabilization factor of plasma by thrombin. Arch. Biochem. Biophys. 105:58-67.
    • (1964) Arch. Biochem. Biophys. , vol.105 , pp. 58-67
    • Lorand, L.1    Konishi, K.2
  • 60
    • 0020155199 scopus 로고
    • Experimental determinations of crosslink densities
    • Mark, J. E. 1982. Experimental determinations of crosslink densities. Rubber Chem. Technol. 55:762-768.
    • (1982) Rubber Chem. Technol. , vol.55 , pp. 762-768
    • Mark, J.E.1
  • 61
    • 0023906018 scopus 로고
    • Elasticity of fibrin and protofibrin gels is differentially modulated by calcium and zinc
    • Marx, G. 1988. Elasticity of fibrin and protofibrin gels is differentially modulated by calcium and zinc. Thromb. Haemostasis. 59:500-503.
    • (1988) Thromb. Haemostasis , vol.59 , pp. 500-503
    • Marx, G.1
  • 62
    • 0014430557 scopus 로고
    • The identification of isopeptide cross-links in insoluble fibrin
    • Matacic, S., and A. G. Loewy. 1968. The identification of isopeptide cross-links in insoluble fibrin. Biochem. Biophys. Res. Commun. 30: 356-362.
    • (1968) Biochem. Biophys. Res. Commun. , vol.30 , pp. 356-362
    • Matacic, S.1    Loewy, A.G.2
  • 63
    • 0014817348 scopus 로고
    • Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin
    • McKee, P. A., P. Mattock, and R. L. Hill. 1970. Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc. Nad. Acad. Sci. USA. 66:738-744.
    • (1970) Proc. Nad. Acad. Sci. USA , vol.66 , pp. 738-744
    • McKee, P.A.1    Mattock, P.2    Hill, R.L.3
  • 64
    • 0014223584 scopus 로고
    • Physicochemical studies of bovine fibrinogen. IV. Ultraviolet absorption and its relation to the structure of the molecule
    • Mihalyi, E. 1968. Physicochemical studies of bovine fibrinogen. IV. Ultraviolet absorption and its relation to the structure of the molecule. Biochemistry. 7:208-223.
    • (1968) Biochemistry , vol.7 , pp. 208-223
    • Mihalyi, E.1
  • 65
    • 0023864593 scopus 로고
    • Clotting of bovine fibrinogen. Calcium binding to fibrin during clotting and its dependence on release of fibrinopeptide B
    • Mihalyi, E. 1988. Clotting of bovine fibrinogen. Calcium binding to fibrin during clotting and its dependence on release of fibrinopeptide B. Biochemistry. 27:967-976.
    • (1988) Biochemistry , vol.27 , pp. 967-976
    • Mihalyi, E.1
  • 66
    • 0016198707 scopus 로고
    • Viscoelastic properties of ligation-inhibited fibrin clots
    • Mockros, L. F., W. W. Roberts, and L. Lorand. 1974. Viscoelastic properties of ligation-inhibited fibrin clots. Biophys. Chem. 2:164-169.
    • (1974) Biophys. Chem. , vol.2 , pp. 164-169
    • Mockros, L.F.1    Roberts, W.W.2    Lorand, L.3
  • 67
    • 0027247825 scopus 로고
    • Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction
    • Mosesson, M. W., J. P. DiOrio, K. R. Siebenlist, J. S. Wall, and J. F. Hainfeld. 1993. Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction. Blood. 82: 1517-1521.
    • (1993) Blood , vol.82 , pp. 1517-1521
    • Mosesson, M.W.1    Diorio, J.P.2    Siebenlist, K.R.3    Wall, J.S.4    Hainfeld, J.F.5
  • 68
    • 0004782883 scopus 로고
    • Identification of covalently linked trimeric and tetrameric D domains in cross-linked fibrin
    • Mosesson, M. W., K. R. Siebenlist, D. L. Amrani, and J. P. DiOrio. 1989. Identification of covalently linked trimeric and tetrameric D domains in cross-linked fibrin. Proc. Natl. Acad. Sci. USA. 86:1113-1117.
    • (1989) Proc. Natl. Acad. Sci. USA. , vol.86 , pp. 1113-1117
    • Mosesson, M.W.1    Siebenlist, K.R.2    Amrani, D.L.3    DiOrio, J.P.4
  • 69
    • 0021590812 scopus 로고
    • Electron microscopy of fine fibrin clots and fine and coarse fibrin films. Observations of fibers in cross-section and in deformed states
    • Muller, M. F., H. Ris, and J. D. Ferry. 1984. Electron microscopy of fine fibrin clots and fine and coarse fibrin films. Observations of fibers in cross-section and in deformed states. J. Mol. Biol. 174:369-384.
    • (1984) J. Mol. Biol. , vol.174 , pp. 369-384
    • Muller, M.F.1    Ris, H.2    Ferry, J.D.3
  • 70
    • 0025607863 scopus 로고
    • Cross-linked Aαγ chain hybrids serve as unique markers for ftbrinogen polymerized by tissue transglutaminase
    • Murthy, S. N. P., and L. Lorand. 1990. Cross-linked Aαγ chain hybrids serve as unique markers for ftbrinogen polymerized by tissue transglutaminase. Proc. Natl. Acad. Sci. USA. 87:9679-9682.
    • (1990) Proc. Natl. Acad. Sci. USA. , vol.87 , pp. 9679-9682
    • Murthy, S.N.P.1    Lorand, L.2
  • 71
    • 0017189690 scopus 로고
    • Rheology of fibrin clots. III. Shear creep and creep recovery of fine ligated and coarse unligated clots
    • Nelb, G. W., C. Gerth, J. D. Ferry, and L. Lorand. 1976. Rheology of fibrin clots. III. Shear creep and creep recovery of fine ligated and coarse unligated clots. Biophys. Chem. 5:377-387.
    • (1976) Biophys. Chem. , vol.5 , pp. 377-387
    • Nelb, G.W.1    Gerth, C.2    Ferry, J.D.3    Lorand, L.4
  • 72
    • 0019830051 scopus 로고
    • Rheology of fibrin clots. V. Shear modulus, creep, and creep recovery of fine unligated clots
    • Nelb, G. W., G. W. Kamykowski, and J. D. Ferry. 1981. Rheology of fibrin clots. V. Shear modulus, creep, and creep recovery of fine unligated clots. Biophys. Chem. 13:15-23.
    • (1981) Biophys. Chem. , vol.13 , pp. 15-23
    • Nelb, G.W.1    Kamykowski, G.W.2    Ferry, J.D.3
  • 73
    • 0020664856 scopus 로고
    • Calcium and fibrin gel structure
    • Okada, M., and B. Blomback. 1983. Calcium and fibrin gel structure. Thromb. Res. 29:269-280.
    • (1983) Thromb. Res. , vol.29 , pp. 269-280
    • Okada, M.1    Blomback, B.2
  • 74
    • 0014428478 scopus 로고
    • Cross-link in fibrin polymerized by factor XIII: ∈(γ-glutamyl)lysine
    • Pisano, J. J., J. S. Finlayson, and M. P. Peyton. 1968. Cross-link in fibrin polymerized by factor XIII: ∈(γ-glutamyl)lysine. Science (Wash. DC). 160:892-893.
    • (1968) Science (Wash. DC) , vol.160 , pp. 892-893
    • Pisano, J.J.1    Finlayson, J.S.2    Peyton, M.P.3
  • 75
    • 0345484347 scopus 로고
    • Accelerating effect of calcium and other cations on conversion of fibrinogen to fibrin
    • Ratnoff, O. D., and A. M. Potts. 1954. Accelerating effect of calcium and other cations on conversion of fibrinogen to fibrin. J. Clin. Invest. 33:206-210.
    • (1954) J. Clin. Invest. , vol.33 , pp. 206-210
    • Ratnoff, O.D.1    Potts, A.M.2
  • 76
    • 0015971058 scopus 로고
    • Rheology of fibrin clots. I. Dynamic viscoelastic properties and fluid permeation
    • Roberts, W. W., O. Kramer, R. W. Rosser, F. H. M. Nestler, and J. D. Ferry. 1974. Rheology of fibrin clots. I. Dynamic viscoelastic properties and fluid permeation. Biophys. Chem. 1:152-160.
    • (1974) Biophys. Chem. , vol.1 , pp. 152-160
    • Roberts, W.W.1    Kramer, O.2    Rosser, R.W.3    Nestler, F.H.M.4    Ferry, J.D.5
  • 77
    • 0015594187 scopus 로고
    • Viscoelastic properties of fibrin clots
    • Roberts, W. W., L. L. Lorand, and L. F. Mockros. 1973. Viscoelastic properties of fibrin clots. Biorheology. 10:29-42.
    • (1973) Biorheology , vol.10 , pp. 29-42
    • Roberts, W.W.1    Lorand, L.L.2    Mockros, L.F.3
  • 78
    • 0345052703 scopus 로고
    • Accelerating effect of calcium on the fibrinogen-fibrin transformation
    • Rosenfeld, G., and B. Janszky. 1952. Accelerating effect of calcium on the fibrinogen-fibrin transformation. Science (Wash. DC). 116:36-37.
    • (1952) Science (Wash. DC) , vol.116 , pp. 36-37
    • Rosenfeld, G.1    Janszky, B.2
  • 79
    • 0017396636 scopus 로고
    • Rheology of fibrin clots. IV. Darcy constants and fiber thickness
    • Rosser, R. W., W. W. Roberts, and J. D. Ferry. 1977. Rheology of fibrin clots. IV. Darcy constants and fiber thickness. Biophys. Chem. 7:153-157.
    • (1977) Biophys. Chem. , vol.7 , pp. 153-157
    • Rosser, R.W.1    Roberts, W.W.2    Ferry, J.D.3
  • 80
    • 0015092656 scopus 로고
    • The effect of fibrin-stabilizing factor on the subunit structure of human fibrin
    • Schwartz, M. L., S. V. Pizzo, R. L. Hill, and P. A. McKee. 1971. The effect of fibrin-stabilizing factor on the subunit structure of human fibrin. J. Clin. Invest. 50:1506-1513.
    • (1971) J. Clin. Invest. , vol.50 , pp. 1506-1513
    • Schwartz, M.L.1    Pizzo, S.V.2    Hill, R.L.3    McKee, P.A.4
  • 81
    • 0027970345 scopus 로고
    • Changes in clot deformability-a possible explanation for the epidemiological association between plasma fibrinogen concentration and myocardial infarction
    • Scrutton, M. C., S. B. Ross-Murphy, G. M. Bennett, Y. Stirling, and T. W. Meade. 1994. Changes in clot deformability-a possible explanation for the epidemiological association between plasma fibrinogen concentration and myocardial infarction. Blood Coagul. Fibrinolysis. 5:719-723.
    • (1994) Blood Coagul. Fibrinolysis , vol.5 , pp. 719-723
    • Scrutton, M.C.1    Ross-Murphy, S.B.2    Bennett, G.M.3    Stirling, Y.4    Meade, T.W.5
  • 82
    • 0022368596 scopus 로고
    • Physiological studies on fibrin network structure
    • Shah, G. A., C. H. Nair, and D. P. Dhall. 1985. Physiological studies on fibrin network structure. Thromb. Res. 40:181-188.
    • (1985) Thromb. Res. , vol.40 , pp. 181-188
    • Shah, G.A.1    Nair, C.H.2    Dhall, D.P.3
  • 83
    • 0025735355 scopus 로고
    • Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase
    • Shainoff, J. R., D. A. Urbanic, and P. M. DiBello. 1991. Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase. J. Biol. Chem. 266:6429-6437.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6429-6437
    • Shainoff, J.R.1    Urbanic, D.A.2    DiBello, P.M.3
  • 84
    • 0016703755 scopus 로고
    • Effects of calcium ion and covalent cross-linking on formation and elasticity of fibrin gels
    • Shen, L. L., J. Hermans, J. McDonagh, R. P. McDonagh, and M. Carr. 1975. Effects of calcium ion and covalent cross-linking on formation and elasticity of fibrin gels. Thromb. Res. 6:255-256.
    • (1975) Thromb. Res. , vol.6 , pp. 255-256
    • Shen, L.L.1    Hermans, J.2    McDonagh, J.3    McDonagh, R.P.4    Carr, M.5
  • 85
    • 0020596436 scopus 로고
    • Contribution of fibrin stabilization to clot strength. Supplementation of factor XIII-defitient plasma with the purified zymogen
    • Shen, L. L., and L. Lorand. 1983. Contribution of fibrin stabilization to clot strength. Supplementation of factor XIII-defitient plasma with the purified zymogen. J. Clin. Invest. 71:1336-1341.
    • (1983) J. Clin. Invest. , vol.71 , pp. 1336-1341
    • Shen, L.L.1    Lorand, L.2
  • 86
    • 0015964971 scopus 로고
    • Fibrin gel structure: Influence of calcium and covalent cross-linking on the elasticity
    • Shen, L. L., R. P. McDonagh, J. McDonagh, and J. Hermans. 1974. Fibrin gel structure: influence of calcium and covalent cross-linking on the elasticity. Biochem. Biophys. Res. Common. 56:793-799.
    • (1974) Biochem. Biophys. Res. Common. , vol.56 , pp. 793-799
    • Shen, L.L.1    McDonagh, R.P.2    McDonagh, J.3    Hermans, J.4
  • 87
    • 0026542962 scopus 로고
    • Factors affecting γ-chain multimer formation in cross-linked fibrin
    • Siebenlist, K. R., and M. W. Mosesson. 1992. Factors affecting γ-chain multimer formation in cross-linked fibrin. Biochemistry. 31:936-941.
    • (1992) Biochemistry , vol.31 , pp. 936-941
    • Siebenlist, K.R.1    Mosesson, M.W.2
  • 88
    • 0023775446 scopus 로고
    • Early alpha chain cross-linking in human fibrin preparations
    • Sobel, J. H., C. A. Thibodeau, and R. E. Canfield. 1988. Early alpha chain cross-linking in human fibrin preparations. Thromb. Haemostasis. 60: 153-159.
    • (1988) Thromb. Haemostasis , vol.60 , pp. 153-159
    • Sobel, J.H.1    Thibodeau, C.A.2    Canfield, R.E.3
  • 91
    • 0026771894 scopus 로고
    • Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: Clot structure and assembly are kinetically controlled
    • Weisel, J. W., and C. Nagaswami. 1992. Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled. Biophys. 763:111-128.
    • (1992) Biophys. , vol.763 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 93
    • 0027194661 scopus 로고
    • The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots
    • Weisel, J. W., Y. Veklich, and O. Gorkun. 1993. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots. J. Mol. Biol. 232:285-297.
    • (1993) J. Mol. Biol. , vol.232 , pp. 285-297
    • Weisel, J.W.1    Veklich, Y.2    Gorkun, O.3
  • 94
    • 0019867456 scopus 로고
    • Relations between enzymatic and association reactions in the development of bovine fibrin clot structure
    • Wolfe, J. K., and D. F. Waugh. 1981. Relations between enzymatic and association reactions in the development of bovine fibrin clot structure. Arch. Biochem. Biophys. 211:125-142.
    • (1981) Arch. Biochem. Biophys. , vol.211 , pp. 125-142
    • Wolfe, J.K.1    Waugh, D.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.