메뉴 건너뛰기




Volumn 70, Issue 1, 1996, Pages 500-510

Fibrinogen Dusart: Electron microscopy of molecules, fibers and clots, and viscoelastic properties of clots

Author keywords

[No Author keywords available]

Indexed keywords

FIBRINOGEN;

EID: 0030068432     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79596-6     Document Type: Article
Times cited : (75)

References (54)
  • 1
    • 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
  • 2
    • 0000673509 scopus 로고
    • Purification of human and bovine fibrinogen
    • Blombäck, B., and M. Blombäck. 1956. Purification of human and bovine fibrinogen. Arkiv Kemi. 10:415-443.
    • (1956) Arkiv Kemi. , vol.10 , pp. 415-443
    • Blombäck, B.1    Blombäck, M.2
  • 4
    • 0019199058 scopus 로고
    • The effect of dextran 70 on the structure of plasma derived fibrin gels
    • Carr, M. E, and D. A. Gabriel. 1980. The effect of dextran 70 on the structure of plasma derived fibrin gels. J. Lab. Clin. Med. 96:985-993.
    • (1980) J. Lab. Clin. Med. , vol.96 , pp. 985-993
    • Carr, M.E.1    Gabriel, D.A.2
  • 5
    • 0026721348 scopus 로고
    • Involvement of the α chain in fibrin clot formation. Effect of monoclonal antibodies
    • Cierniewski, C. S., and A. Z. Budzynski. 1992 Involvement of the α chain in fibrin clot formation. Effect of monoclonal antibodies. Biochemistry. 31:4248-4253.
    • (1992) Biochemistry , vol.31 , pp. 4248-4253
    • Cierniewski, C.S.1    Budzynski, A.Z.2
  • 6
    • 0027517306 scopus 로고
    • Dusart syndrome: A new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure
    • Collet, J. P., J. Soria, M. Mirshahi, M. Hirsch, F. B. Dagonnet, J. Caen, and C. Soria. 1993. Dusart syndrome: a new concept of the relationship between fibrin clot architecture and fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure. Blood. 82:2462-2469.
    • (1993) Blood , vol.82 , pp. 2462-2469
    • Collet, J.P.1    Soria, J.2    Mirshahi, M.3    Hirsch, M.4    Dagonnet, F.B.5    Caen, J.6    Soria, C.7
  • 7
    • 0017069460 scopus 로고
    • Effects of dextran on the molecular structure and tensile behavior of human fibrin
    • Dhall, T. Z., W. A. J. Bryce, and D. P. Dhall. 1976. Effects of dextran on the molecular structure and tensile behavior of human fibrin. Thromb. Haemostasis. 35:737-745.
    • (1976) Thromb. Haemostasis , vol.35 , pp. 737-745
    • Dhall, T.Z.1    Bryce, W.A.J.2    Dhall, D.P.3
  • 9
    • 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
  • 10
    • 0026645829 scopus 로고
    • Fibrin gel network characteristics and coronary heart disease. relations to plasma fibrinogen concentration, acute phase protein, serum lipoproteins and coronary heart disease
    • Fatah, K., A. Hamsten, B. Blombäck. and M. Blombäck. 1992. Fibrin gel network characteristics and coronary heart disease. relations to plasma fibrinogen concentration, acute phase protein, serum lipoproteins and coronary heart disease. Thromb. Haemost. 68:130-135.
    • (1992) Thromb. Haemost. , vol.68 , pp. 130-135
    • Fatah, K.1    Hamsten, A.2    Blombäck, B.3    Blombäck, M.4
  • 11
    • 0345155302 scopus 로고
    • Structure and rheology of fibrin networks
    • O. Kramer, editor. Elsevier, Amsterdam
    • Ferry, J. D. 1988. Structure and rheology of fibrin networks. In Biological and Synthetic Polymer Networks. O. Kramer, editor. Elsevier, Amsterdam. 41-55.
    • (1988) Biological and Synthetic Polymer Networks , pp. 41-55
    • Ferry, J.D.1
  • 12
    • 0018725401 scopus 로고
    • Trinodular structure of fibrinogen: Confirmation by both shadowing and negative-stain electron microscopy
    • Fowler, W. E., and H. P. Erickson. 1979. Trinodular structure of fibrinogen: confirmation by both shadowing and negative-stain electron microscopy. J. Mol. Biol. 134:241-249.
    • (1979) J. Mol. Biol. , vol.134 , pp. 241-249
    • Fowler, W.E.1    Erickson, H.P.2
  • 13
    • 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
  • 14
    • 85031226487 scopus 로고
    • Heterozygous Aα16Arg→Cys dysfibrinogenemia: Characterization of mutant molecule rich isolates
    • Galanakis, D. K. 1991. Heterozygous Aα16Arg→Cys dysfibrinogenemia: characterization of mutant molecule rich isolates. Thromb. Haemostasis. 65:899a.
    • (1991) Thromb. Haemostasis , vol.65
    • Galanakis, D.K.1
  • 15
    • 0020957672 scopus 로고
    • Fibrinogen Louisville: An Aα16Arg→His defect which forms no hybrid molecules in heterozygous individuals and inhibits aggregation of normal fibrin monomers
    • Galanakis, D. K., A. Henschen, M. Keeling, and M. Kehl. 1983. Fibrinogen Louisville: an Aα16Arg→His defect which forms no hybrid molecules in heterozygous individuals and inhibits aggregation of normal fibrin monomers. Ann. NY Acad. Sci. 408:644-648.
    • (1983) Ann. NY Acad. Sci. , vol.408 , pp. 644-648
    • Galanakis, D.K.1    Henschen, A.2    Keeling, M.3    Kehl, M.4
  • 16
    • 0024315774 scopus 로고
    • Fibrinogen Stony Brook, a heterozygous Aα16Arg→Cys dysfibrinogenemia: Evaluation of diminished platelet aggregation support and of enhanced inhibition of fibrin assembly
    • Galanakis, D. K., A. Henschen, E. I. Peerschke, and M. Kehl. 1989. Fibrinogen Stony Brook, a heterozygous Aα16Arg→Cys dysfibrinogenemia: evaluation of diminished platelet aggregation support and of enhanced inhibition of fibrin assembly. J. Clin. Invest. 84:295-304.
    • (1989) J. Clin. Invest. , vol.84 , pp. 295-304
    • Galanakis, D.K.1    Henschen, A.2    Peerschke, E.I.3    Kehl, M.4
  • 17
    • 85031223319 scopus 로고
    • Fibrinogen Stony Brook II: A heterozygously transmitted peptide A defect. Evidence that most mutant molecules are homodimers
    • Galanakis, D. K., and M. Hultin. 1990 Fibrinogen Stony Brook II: A heterozygously transmitted peptide A defect. Evidence that most mutant molecules are homodimers. Blood. 76:421a.
    • (1990) Blood , vol.76
    • Galanakis, D.K.1    Hultin, M.2
  • 18
    • 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
  • 20
    • 0025136902 scopus 로고
    • Location of the binding site "b" for lateral polymerization of fibrin
    • Hasegawa, N., and S. Sasaki. 1990. Location of the binding site "b" for lateral polymerization of fibrin. Thromb. Res. 57:183-195.
    • (1990) Thromb. Res. , vol.57 , pp. 183-195
    • Hasegawa, N.1    Sasaki, S.2
  • 21
    • 0021965212 scopus 로고
    • Polymerization properties of two normally circulating fibrinogens, HMW and LMW. Evidence that the COOH-terminal end of the α-chain is of importance for fibrin polymerization
    • Holm, B., F. Brosstad, P. Kierulf, and H. C. Godal. 1985. Polymerization properties of two normally circulating fibrinogens, HMW and LMW. Evidence that the COOH-terminal end of the α-chain is of importance for fibrin polymerization. Thromb. Res. 39:595-606.
    • (1985) Thromb. Res. , vol.39 , pp. 595-606
    • Holm, B.1    Brosstad, F.2    Kierulf, P.3    Godal, H.C.4
  • 22
    • 0020472522 scopus 로고
    • Kinetics of the activation of plasminogen by human tissue plasminogen activator
    • Hoylaerts, M., D. C. Rijken, H. R. Lijnen, and D. Collen. 1982. Kinetics of the activation of plasminogen by human tissue plasminogen activator. J. Biol. Chem. 257:2912-2919.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2912-2919
    • Hoylaerts, M.1    Rijken, D.C.2    Lijnen, H.R.3    Collen, D.4
  • 23
    • 0026017781 scopus 로고
    • A torsion pendulum for measurement of the viscoelasticity of biopolymers and its application to actin networks
    • Janmey, P. A. 1991. A torsion pendulum for measurement of the viscoelasticity of biopolymers and its application to actin networks. J. Biochem Biophys. Methods. 22:41-53.
    • (1991) J. Biochem Biophys. Methods , vol.22 , pp. 41-53
    • Janmey, P.A.1
  • 24
    • 0025765110 scopus 로고
    • Viscoelastic properties of vimentin compared with other filamentous biopolymer networks
    • Janmey, P. A., U. Euteneuer, P. Traub, and M. Schliwa. 1991. Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J. Cell. Biol. 113:155-160
    • (1991) J. Cell. Biol. , vol.113 , pp. 155-160
    • Janmey, P.A.1    Euteneuer, U.2    Traub, P.3    Schliwa, M.4
  • 25
    • 0026785207 scopus 로고
    • Fibrinogen Marburg: A homozygous case of dysfibrinogenemia, lacking amino acids Aα 461-610 (Lys 461 AAA →stop TAA)
    • Koopman, J., F. Haverkate, J Grimbergen, R. Egbring, and S. T. Lord. 1992. Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids Aα 461-610 (Lys 461 AAA →stop TAA). Blond. 80:1972-1979.
    • (1992) Blond , vol.80 , pp. 1972-1979
    • Koopman, J.1    Haverkate, F.2    Grimbergen, J.3    Egbring, R.4    Lord, S.T.5
  • 27
    • 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
  • 28
    • 0027217672 scopus 로고
    • Anticoagulant function of a 24-Kd fragment isolated from human fibrinogen Aα chains
    • Lau, H. K. F. 1993. Anticoagulant function of a 24-Kd fragment isolated from human fibrinogen Aα chains. Blood. 81:3277-3284.
    • (1993) Blood , vol.81 , pp. 3277-3284
    • Lau, H.K.F.1
  • 30
    • 0021341834 scopus 로고
    • Dysfibrinogenemia (fibrinogen Dusart) associated with impaired enhancement of plasminogen activation
    • Lijnen, H. R , J Soria, C. Soria, D. Collen, and J. P. Caen. 1984. Dysfibrinogenemia (fibrinogen Dusart) associated with impaired enhancement of plasminogen activation. Thromb. Haemostasis. 51:108-109.
    • (1984) Thromb. Haemostasis , vol.51 , pp. 108-109
    • Lijnen, H.R.1    Soria, J.2    Soria, C.3    Collen, D.4    Caen, J.P.5
  • 32
    • 0002768703 scopus 로고
    • Suppression of plasminogen binding to fibrin by high fibrinogen: A mechanism for how high fibrinogen enhances the risk of thrombosis
    • McDonagh, J. 1994. Suppression of plasminogen binding to fibrin by high fibrinogen: a mechanism for how high fibrinogen enhances the risk of thrombosis. Sanofi Assoc. Thromb. Res. 4:I-XX.
    • (1994) Sanofi Assoc. Thromb. Res. , vol.4
    • McDonagh, J.1
  • 33
    • 0021905372 scopus 로고
    • The role of fibrinogen α C-domains in the fibrin assembly process
    • Medved', L. V., O. V. Gorkun, V. F. Manyakov, and V. A. Belitser. 1985. The role of fibrinogen α C-domains in the fibrin assembly process. FEBS Lett. 181:109-112.
    • (1985) FEBS Lett. , vol.181 , pp. 109-112
    • Medved', L.V.1    Gorkun, O.V.2    Manyakov, V.F.3    Belitser, V.A.4
  • 34
    • 0025679015 scopus 로고
    • Electron microscope investigation of the early stages of fibrin assembly. Twisted protofibrils and fibers
    • Medved', L., T. Ugarova, Y. Veklich, N. Lukinova, and J. Weisel. 1990, Electron microscope investigation of the early stages of fibrin assembly. Twisted protofibrils and fibers. J. Mol. Blol. 216:503-509.
    • (1990) J. Mol. Blol. , vol.216 , pp. 503-509
    • Medved', L.1    Ugarova, T.2    Veklich, Y.3    Lukinova, N.4    Weisel, J.5
  • 35
    • 0014143974 scopus 로고
    • Human fibrinogen of relatively high solubility. Comparative biophysical, biochemical, and biological studies with fibrinogen of lower solubility
    • Mosesson, M. W , N. Alkjaersig, B. Sweet, and S. Sherry. 1967. Human fibrinogen of relatively high solubility. Comparative biophysical, biochemical, and biological studies with fibrinogen of lower solubility. Biochemistry. 6:3279-3287.
    • (1967) Biochemistry , vol.6 , pp. 3279-3287
    • Mosesson, M.W.1    Alkjaersig, N.2    Sweet, B.3    Sherry, S.4
  • 36
    • 0017189690 scopus 로고
    • Rheology of fibrin clots. III. Sheer 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. Sheer 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
  • 37
    • 84955027173 scopus 로고
    • A torsion pendulum for dynamic creep measurements of soft viscoelastic materials
    • Plazek, D. J., M. N. Vrancken, and J. W. Berge. 1958 A torsion pendulum for dynamic creep measurements of soft viscoelastic materials. Trans. Soc. Rheol. 2:39-51.
    • (1958) Trans. Soc. Rheol. , vol.2 , pp. 39-51
    • Plazek, D.J.1    Vrancken, M.N.2    Berge, J.W.3
  • 38
    • 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
  • 39
    • 0015594187 scopus 로고
    • Viscoelastic properties of fibrin clots
    • Roberts, W. W., L. Lorand, and L. F. Mockros. 1973 Viscoelastic properties of fibrin clots. Biorheolagy. 10:29-42.
    • (1973) Biorheolagy , vol.10 , pp. 29-42
    • Roberts, W.W.1    Lorand, L.2    Mockros, L.F.3
  • 40
    • 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
  • 41
    • 0027476203 scopus 로고
    • The polymerization of fibrinogen Dusart (Aα 554 Arg → Cys) after removal of carboxy terminal regions of the Aα-chains
    • Siebenlist, K. R., M. W. Mosesson, J. P. DiOrio, J. Soria, C. Soria, and J. P. Caen. 1993. The polymerization of fibrinogen Dusart (Aα 554 Arg → Cys) after removal of carboxy terminal regions of the Aα-chains. Blood Coagul. Fibrinolysis 4:61-65.
    • (1993) Blood Coagul. Fibrinolysis , vol.4 , pp. 61-65
    • Siebenlist, K.R.1    Mosesson, M.W.2    DiOrio, J.P.3    Soria, J.4    Soria, C.5    Caen, J.P.6
  • 42
    • 0023941028 scopus 로고
    • Fibrinogen Birmingham: A heterozygous dysfibrinogenemia (Aα Arg16 → His) containing heterodimeric molecules
    • Siebenlist, K. R., J. T. Prchal, and M. W. Mosesson. 1988. Fibrinogen Birmingham: a heterozygous dysfibrinogenemia (Aα Arg16 → His) containing heterodimeric molecules. Blood. 71:613-618.
    • (1988) Blood , vol.71 , pp. 613-618
    • Siebenlist, K.R.1    Prchal, J.T.2    Mosesson, M.W.3
  • 43
    • 0021113788 scopus 로고
    • Electron microscopic studies of fibrinogen structure: Historical perspectives and recent experiments
    • Slayter, H. S 1983. Electron microscopic studies of fibrinogen structure: historical perspectives and recent experiments. Ann. NY Acad. Sci. 408:131-45.
    • (1983) Ann. NY Acad. Sci. , vol.408 , pp. 131-145
    • Slayter, H.S.1
  • 44
    • 0020596374 scopus 로고
    • A new type of congenital dysfibrinogenemia with defective fibrin lysis: Dusart syndrome, possible relation to thrombosis
    • Soria, J., C. Soria, and J. P. Caen. 1983. A new type of congenital dysfibrinogenemia with defective fibrin lysis: Dusart syndrome, possible relation to thrombosis. Brit. J Haematol. 53:575-586.
    • (1983) Brit. J Haematol. , vol.53 , pp. 575-586
    • Soria, J.1    Soria, C.2    Caen, J.P.3
  • 45
    • 0027379584 scopus 로고
    • Carboxyl terminal portions of the α chains of fibrinogen and fibrin: Localization by electron microscopy and the effects of isolated αC fragments on polymerization
    • Veklich, Y. I., O. V. Gorkun, L. V. Medved, W. Nieuwenhuizen, and J. W. Weisel. 1993. Carboxyl terminal portions of the α chains of fibrinogen and fibrin: localization by electron microscopy and the effects of isolated αC fragments on polymerization. J. Biol. Chem. 268:13577-13585.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13577-13585
    • Veklich, Y.I.1    Gorkun, O.V.2    Medved, L.V.3    Nieuwenhuizen, W.4    Weisel, J.W.5
  • 46
    • 0028051450 scopus 로고
    • A correlation between thrombotic disease and a specific fibrinogen abnormality (Aα 554 Arg→Cys) in two unrelated kindred, Dusart and Chapel Hill III
    • Wada, Y., and S. T. Lord. 1994. A correlation between thrombotic disease and a specific fibrinogen abnormality (Aα 554 Arg→Cys) in two unrelated kindred, Dusart and Chapel Hill III. Blood. 84:3709-3714.
    • (1994) Blood , vol.84 , pp. 3709-3714
    • Wada, Y.1    Lord, S.T.2
  • 47
    • 0023483395 scopus 로고
    • The electron microscope band pattern of human fibrin: Various stains, lateral order, and carbohydrate localization
    • Weisel, J. W. 1986a. The electron microscope band pattern of human fibrin: various stains, lateral order, and carbohydrate localization J Ultrastruct. Mol. Struct. Res. 96:176-188.
    • (1986) J Ultrastruct. Mol. Struct. Res. , vol.96 , pp. 176-188
    • Weisel, J.W.1
  • 48
    • 0022967224 scopus 로고
    • Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides
    • Weisel, J. W. 1986b. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys. J. 50:1079-1093.
    • (1986) Biophys. J. , vol.50 , pp. 1079-1093
    • Weisel, J.W.1
  • 49
    • 9044227071 scopus 로고
    • Structural studies of lateral aggregation in fibrin assembly
    • M. W. Mosesson, D. L. Amrani, K. R. Siebenlist, and J. P. DiOrio, editors Excerpta Medica, Amsterdam
    • Weisel, J. W. 1988. Structural studies of lateral aggregation in fibrin assembly. In Fibrinogen 3, Biochemistry, Biological Functions, Gene Regulation and Expression, M. W. Mosesson, D. L. Amrani, K. R. Siebenlist, and J. P. DiOrio, editors Excerpta Medica, Amsterdam. 113-116.
    • (1988) Fibrinogen 3, Biochemistry, Biological Functions, Gene Regulation and Expression , pp. 113-116
    • Weisel, J.W.1
  • 50
    • 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. J. 63:111-128.
    • (1992) Biophys. J. , vol.63 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 51
    • 0028147599 scopus 로고
    • Interactions of plasminogen and polymerizing fibrin and its derivatives monitored with a photoaffinity cross-linker and electron microscopy
    • Weisel, J. W., C. Nagaswami, B. Korsholm, L. C. Petersen, and E. Suenson. 1994. Interactions of plasminogen and polymerizing fibrin and its derivatives monitored with a photoaffinity cross-linker and electron microscopy. J. Mol. Biol 235: 1117-1135.
    • (1994) J. Mol. Biol , vol.235 , pp. 1117-1135
    • Weisel, J.W.1    Nagaswami, C.2    Korsholm, B.3    Petersen, L.C.4    Suenson, E.5
  • 53
    • 0022339326 scopus 로고
    • A model for fibrinogen: Domains and sequence
    • Weisel, J. W., C. V. Stauffacher, E. Bullitt, and C. Cohen. 1985. A model for fibrinogen: domains and sequence. Science. 230:1388-1391.
    • (1985) Science , vol.230 , pp. 1388-1391
    • Weisel, J.W.1    Stauffacher, C.V.2    Bullitt, E.3    Cohen, C.4
  • 54
    • 0020645312 scopus 로고
    • Morphology of fibrinogen monomers and of fibrin protofibrils
    • Williams, R. C. 1983. Morphology of fibrinogen monomers and of fibrin protofibrils. Ann. NY Acad. Sci. 408:180-193.
    • (1983) Ann. NY Acad. Sci. , vol.408 , pp. 180-193
    • Williams, R.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.