메뉴 건너뛰기




Volumn 82, Issue 2, 1999, Pages 277-282

Structural studies of fibrinolysis by electron and light microscopy

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIN; FIBRINOGEN; PLASMIN; PLASMINOGEN; TISSUE PLASMINOGEN ACTIVATOR;

EID: 0032718245     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1615843     Document Type: Conference Paper
Times cited : (60)

References (35)
  • 1
    • 0019165924 scopus 로고
    • Plasmic degradation of crosslinked fibrin. Characterization of new macromolecular soluble complexes and a model of their structure
    • Francis CW, Marder VJ, Barlow GH. Plasmic degradation of crosslinked fibrin. Characterization of new macromolecular soluble complexes and a model of their structure. J Clin Invest. 1980;66:1033-1043.
    • (1980) J Clin Invest , vol.66 , pp. 1033-1043
    • Francis, C.W.1    Marder, V.J.2    Barlow, G.H.3
  • 2
    • 0020025365 scopus 로고
    • A molecular model of plasmic degradation of crosslinked fibrin
    • Francis CW, Marder VJ. A molecular model of plasmic degradation of crosslinked fibrin. Semin Thromb Hemost. 1982;8:25-35.
    • (1982) Semin Thromb Hemost , vol.8 , pp. 25-35
    • Francis, C.W.1    Marder, V.J.2
  • 4
    • 0027332737 scopus 로고
    • Determination of the topology of factor XIIIa-induced fibrin gamma-chain cross-links by electron microscopy of ligated fragments
    • Weisel JW, Francis CW, Nagaswami C, Marder VJ. Determination of the topology of factor XIIIa-induced fibrin gamma-chain cross-links by electron microscopy of ligated fragments. J Biol Chem. 1993;268:26618-26624.
    • (1993) J Biol Chem , vol.268 , pp. 26618-26624
    • Weisel, J.W.1    Francis, C.W.2    Nagaswami, C.3    Marder, V.J.4
  • 5
    • 0030848486 scopus 로고    scopus 로고
    • Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
    • Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature. 1997;389:455-462.
    • (1997) Nature , vol.389 , pp. 455-462
    • Spraggon, G.1    Everse, S.J.2    Doolittle, R.F.3
  • 7
    • 0026491075 scopus 로고
    • The effect of fibrin structure on fibrinolysis
    • Gabriel DA, Muga K, Boothroyd EM. The effect of fibrin structure on fibrinolysis. J Biol Chem. 1992;267:24259-24263.
    • (1992) J Biol Chem , vol.267 , pp. 24259-24263
    • Gabriel, D.A.1    Muga, K.2    Boothroyd, E.M.3
  • 8
    • 0029100827 scopus 로고
    • Effect of fibrin structure on plasmin-mediated dissolution of plasma clots
    • Carr ME, Alving BM. Effect of fibrin structure on plasmin-mediated dissolution of plasma clots. Blood Coagul Fibrinolysis. 1995;6:567-573.
    • (1995) Blood Coagul Fibrinolysis , vol.6 , pp. 567-573
    • Carr, M.E.1    Alving, B.M.2
  • 9
    • 0029562794 scopus 로고
    • The effect of acetylsalicylic acid on fibrin gel lysis by tissue plasminogen activator
    • Williams S, Fatah K, Ivert T, Blombäck M. The effect of acetylsalicylic acid on fibrin gel lysis by tissue plasminogen activator. Blood Coagul Fibrinolysis. 1995;6:718-725.
    • (1995) Blood Coagul Fibrinolysis , vol.6 , pp. 718-725
    • Williams, S.1    Fatah, K.2    Ivert, T.3    Blombäck, M.4
  • 10
    • 0030997702 scopus 로고    scopus 로고
    • Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation
    • Kolev K, Tenekedjiev K, Komorowicz E, Machovich R. Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation. J Biol Chem. 1997;272:13666-13675.
    • (1997) J Biol Chem , vol.272 , pp. 13666-13675
    • Kolev, K.1    Tenekedjiev, K.2    Komorowicz, E.3    Machovich, R.4
  • 11
    • 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 JP, Soria J, Mirshahi M, Hirsch M, Dagonnet FB, Caen J, Soria C. Dusart syndrome. A new concept of the relationship between fibrin clot architecture and fibrin clot degradability: Hypofibrinolysis related to an abnormal clot structure. Blood. 1993;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
  • 12
    • 0030068432 scopus 로고    scopus 로고
    • Fibrinogen Dusart: Electron microscopy of molecules, fibers and clots and viscoelastic measurements
    • Collet J-P, Woodhead JL, Soria J, Soria C, Mirshahi M, Caen JP, Weisel JW. Fibrinogen Dusart: Electron microscopy of molecules, fibers and clots and viscoelastic measurements. Biophys J. 1996;70:500-510.
    • (1996) Biophys J , vol.70 , pp. 500-510
    • Collet, J.-P.1    Woodhead, J.L.2    Soria, J.3    Soria, C.4    Mirshahi, M.5    Caen, J.P.6    Weisel, J.W.7
  • 13
    • 0028051450 scopus 로고
    • A correlation between thrombotic disease and a specific fibrinogen abnormality (A alpha 554 Arg → cys) in two unrelated kindred, Dusart and Chapel Hill III
    • Wada Y, Lord ST, A correlation between thrombotic disease and a specific fibrinogen abnormality (A alpha 554 Arg → Cys) in two unrelated kindred, Dusart and Chapel Hill III. Blood. 1994;84:3709-3714.
    • (1994) Blood , vol.84 , pp. 3709-3714
    • Wada, Y.1    Lord, S.T.2
  • 14
    • 0030273580 scopus 로고    scopus 로고
    • The structure-function relationship of hereditary dysfibrinogens
    • Matsuda M. The structure-function relationship of hereditary dysfibrinogens. Int J Hematol. 1996;64:167-179.
    • (1996) Int J Hematol , vol.64 , pp. 167-179
    • Matsuda, M.1
  • 15
    • 0032189655 scopus 로고    scopus 로고
    • Gamma-chain dysfibrinogenemias: Molecular structure-function relationships of naturally occurring mutations in the gamma chain of human fibrinogen
    • Cote HC, Lord ST, Pratt KP. Gamma-Chain dysfibrinogenemias: Molecular structure-function relationships of naturally occurring mutations in the gamma chain of human fibrinogen. Blood. 1998;92:2195-2212.
    • (1998) Blood , vol.92 , pp. 2195-2212
    • Cote, H.C.1    Lord, S.T.2    Pratt, K.P.3
  • 16
    • 0020645325 scopus 로고
    • Plasmin degradation of cross-linked fibrin
    • Marder VJ, Francis CW. Plasmin degradation of cross-linked fibrin. Ann NY Acad Sci. 1982;408:397-406.
    • (1982) Ann NY Acad Sci , vol.408 , pp. 397-406
    • Marder, V.J.1    Francis, C.W.2
  • 17
    • 0029131436 scopus 로고
    • Superficial accumulation of plasminogen during plasma clot lysis
    • Sakharov DV, Rijken DC. Superficial accumulation of plasminogen during plasma clot lysis. Circulation. 1995;92:1883-1890.
    • (1995) Circulation , vol.92 , pp. 1883-1890
    • Sakharov, D.V.1    Rijken, D.C.2
  • 18
    • 0030068051 scopus 로고    scopus 로고
    • Rearrangements of the fibrin network and spatial distribution of fibrinolytic components during plasma clot lysis. Study with confocal microscopy
    • Sakharov DV, Nagelkerke JF, Rijken DC. Rearrangements of the fibrin network and spatial distribution of fibrinolytic components during plasma clot lysis. Study with confocal microscopy. J Biol Chem. 1996;271:2133-2138.
    • (1996) J Biol Chem , vol.271 , pp. 2133-2138
    • Sakharov, D.V.1    Nagelkerke, J.F.2    Rijken, D.C.3
  • 19
    • 0027410344 scopus 로고
    • Regulation of fibrinolysis by platelet-released plasminogen activator inhibitor 1: Light scattering and ultrastructural examination of lysis of a model platelet-fibrin thrombus
    • Braaten JV, Handt S, Jerome WG, Kirkpatrick J, Lewis JC, Hantgan RR. Regulation of fibrinolysis by platelet-released plasminogen activator inhibitor 1: Light scattering and ultrastructural examination of lysis of a model platelet-fibrin thrombus. Blood. 1993;81:1290-1299.
    • (1993) Blood , vol.81 , pp. 1290-1299
    • Braaten, J.V.1    Handt, S.2    Jerome, W.G.3    Kirkpatrick, J.4    Lewis, J.C.5    Hantgan, R.R.6
  • 20
    • 0027141112 scopus 로고
    • Inner clot diffusion and permeation during fibrinolysis
    • Diamond SL, Anand S. Inner clot diffusion and permeation during fibrinolysis. Biophys J. 1993;65:2622-2643.
    • (1993) Biophys J , vol.65 , pp. 2622-2643
    • Diamond, S.L.1    Anand, S.2
  • 21
    • 0032535294 scopus 로고    scopus 로고
    • Structural studies of fibrinolysis by electron microscopy
    • Veklich Y, Francis CW, White J, Weisel JW. Structural studies of fibrinolysis by electron microscopy. Blood. 1998;92:4721-4729.
    • (1998) Blood , vol.92 , pp. 4721-4729
    • Veklich, Y.1    Francis, C.W.2    White, J.3    Weisel, J.W.4
  • 22
    • 0022967224 scopus 로고
    • Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides
    • Weisel JW. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys J. 1986;50:1079-1093.
    • (1986) Biophys J , vol.50 , pp. 1079-1093
    • Weisel, J.W.1
  • 23
    • 0017703122 scopus 로고
    • Early events in the plasmin digestion of fibrinogen and fibrin. Effects of plasmin on fibrin polymerization
    • Shen LL, McDonagh RP, McDonagh J, Hermans J. Early events in the plasmin digestion of fibrinogen and fibrin. Effects of plasmin on fibrin polymerization. J Biol Chem. 1977;252:6184-6189.
    • (1977) J Biol Chem , vol.252 , pp. 6184-6189
    • Shen, L.L.1    McDonagh, R.P.2    McDonagh, J.3    Hermans, J.4
  • 24
    • 0028147599 scopus 로고
    • Interactions of plasminogen and polymerizing fibrin and its derivatives monitored with a photoaffinity cross-linker and electron microscopy
    • Weisel JW, Nagaswami C, Korsholm B, Petersen LC, Suenson E. Interactions of plasminogen and polymerizing fibrin and its derivatives monitored with a photoaffinity cross-linker and electron microscopy. J Mol Biol. 1994;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
  • 25
    • 0025907705 scopus 로고
    • Dependence of blood clot lysis on the mode of transport of urokinase into the clot-A magnetic resonance imaging study in vitro
    • Blinc A, Planinsic G, Keber D, Jarh O, Lahajnar G, Zidansek A, Demsar, F. Dependence of blood clot lysis on the mode of transport of urokinase into the clot-A magnetic resonance imaging study in vitro. Thromb Haemost. 1991;65:549-552.
    • (1991) Thromb Haemost , vol.65 , pp. 549-552
    • Blinc, A.1    Planinsic, G.2    Keber, D.3    Jarh, O.4    Lahajnar, G.5    Zidansek, A.6    Demsar, F.7
  • 26
    • 0019210979 scopus 로고
    • Fibrin assembly: A comparison of electron microscopic and light scattering results
    • Hantgan R, Fowler W, Erickson H, Hermans J. Fibrin assembly: A comparison of electron microscopic and light scattering results. Thromb Haemost. 1980;44:119-124.
    • (1980) Thromb Haemost , vol.44 , pp. 119-124
    • Hantgan, R.1    Fowler, W.2    Erickson, H.3    Hermans, J.4
  • 27
    • 0018597469 scopus 로고
    • Assembly of fibrin. A light scattering study
    • Hantgan RR, Hermans J. Assembly of fibrin. A light scattering study. J Biol Chem. 1979;254:11272-11281.
    • (1979) J Biol Chem , vol.254 , pp. 11272-11281
    • Hantgan, R.R.1    Hermans, J.2
  • 28
    • 0026771894 scopus 로고
    • Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: Clot structure and assembly are kinetically controlled
    • Weisel JW, Nagaswami C. Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: Clot structure and assembly are kinetically controlled. Biophys J. 1992;63:111-128.
    • (1992) Biophys J , vol.63 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 29
    • 0023584366 scopus 로고
    • Rapid formation of large molecular weight alpha-polymers in cross-linked fibrin induced by high factor XIII concentrations
    • Francis CW, Marder VJ. Rapid formation of large molecular weight alpha-polymers in cross-linked fibrin induced by high factor XIII concentrations. J Clin Invest. 1987;80:1459-1465.
    • (1987) J Clin Invest , vol.80 , pp. 1459-1465
    • Francis, C.W.1    Marder, V.J.2
  • 30
    • 0009501934 scopus 로고
    • Initial plasmin-degradation of fibrin as the basis of a positive feedback mechanism in fibrinolysis
    • Suenson E, Lützen O, Thorsen S. Initial plasmin-degradation of fibrin as the basis of a positive feedback mechanism in fibrinolysis. Eur J Biochem. 1984;149:193-200.
    • (1984) Eur J Biochem , vol.149 , pp. 193-200
    • Suenson, E.1    Lützen, O.2    Thorsen, S.3
  • 31
    • 0026700846 scopus 로고
    • Positive co-operative binding at two weak lysine-binding sites governs the Glu-plasminogen conformational change
    • Christensen U, Mølgaard L. Positive co-operative binding at two weak lysine-binding sites governs the Glu-plasminogen conformational change. Biochem J. 1992;285:419-425.
    • (1992) Biochem J , vol.285 , pp. 419-425
    • Christensen, U.1    Mølgaard, L.2
  • 32
    • 0028226262 scopus 로고
    • Conformational studies of human plasminogen and plasminogen fragments: Evidence for a novel third conformation of plasminogen
    • Marshall JM, Brown AJ, Ponting CP. Conformational studies of human plasminogen and plasminogen fragments: evidence for a novel third conformation of plasminogen. Biochemistry. 1994;33:3599-3606.
    • (1994) Biochemistry , vol.33 , pp. 3599-3606
    • Marshall, J.M.1    Brown, A.J.2    Ponting, C.P.3
  • 34
    • 0020174684 scopus 로고
    • The binding of plasminogen to fibrin: Evidence for plasminogen-bridging
    • Garman AJ, Smith RAG. The binding of plasminogen to fibrin: Evidence for plasminogen-bridging. Thromb Res. 1982;27:311-320.
    • (1982) Thromb Res , vol.27 , pp. 311-320
    • Garman, A.J.1    Smith, R.A.G.2
  • 35
    • 0025957849 scopus 로고
    • Effect of plasminogen and tissue-type plasminogen activator on fibrin gel structure
    • Petersen LC, Suenson E. Effect of plasminogen and tissue-type plasminogen activator on fibrin gel structure. Fibrinolysis. 1991;5:51-59.
    • (1991) Fibrinolysis , vol.5 , pp. 51-59
    • Petersen, L.C.1    Suenson, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.