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Volumn 92, Issue 7, 1998, Pages 2195-2212

γ-chain dysfibrinogenemias: Molecular structure-function relationships of naturally occurring mutations in the γ chain of human fibrinogen

Author keywords

[No Author keywords available]

Indexed keywords

FIBRINOGEN;

EID: 0032189655     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v92.7.2195     Document Type: Review
Times cited : (91)

References (200)
  • 2
    • 0027326001 scopus 로고
    • Human fibrinogen - Structural variants and functional sites
    • Henschen AH: Human fibrinogen - structural variants and functional sites. Thromb Haemost 70:42, 1993
    • (1993) Thromb Haemost , vol.70 , pp. 42
    • Henschen, A.H.1
  • 3
    • 0000426762 scopus 로고
    • Fibrinogen and fibrin
    • Bloom F, Forbes CD, Thomas DP, Tuddenham EGD (eds). Edinburgh, UK, Churchill Livingstone
    • Doolittle RF: Fibrinogen and fibrin, in Bloom F, Forbes CD, Thomas DP, Tuddenham EGD (eds): Haemostasis and Thrombosis, vol 1. Edinburgh, UK, Churchill Livingstone, 1994, p 491
    • (1994) Haemostasis and Thrombosis , vol.1 , pp. 491
    • Doolittle, R.F.1
  • 5
    • 0030199185 scopus 로고    scopus 로고
    • Fibrinogen and fibrin-proteins with complex roles in hemostasis and thrombosis
    • Blombäck B: Fibrinogen and fibrin-proteins with complex roles in hemostasis and thrombosis. Thromb Res 83:1, 1996
    • (1996) Thromb Res , vol.83 , pp. 1
    • Blombäck, B.1
  • 6
    • 0030803827 scopus 로고    scopus 로고
    • Fibrinogen and fibrin polymerization: Appraisal of the binding events that accompany fibrin generation and fibrin clot assembly
    • Mosesson M: Fibrinogen and fibrin polymerization: Appraisal of the binding events that accompany fibrin generation and fibrin clot assembly. Blood Coagul Fibrinol 8:257, 1997
    • (1997) Blood Coagul Fibrinol , vol.8 , pp. 257
    • Mosesson, M.1
  • 7
    • 0001567645 scopus 로고
    • Les produits de dégradation du fibrinogène humain par la plasmine. 1-Séparation et propriétés physico-chimiques
    • Nussenweig V, Seligmann M, Pelmont J, Grabar P: Les produits de dégradation du fibrinogène humain par la plasmine. 1-Séparation et propriétés physico-chimiques. Ann Inst Pasteur 100:377, 1961
    • (1961) Ann Inst Pasteur , vol.100 , pp. 377
    • Nussenweig, V.1    Seligmann, M.2    Pelmont, J.3    Grabar, P.4
  • 8
    • 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 YI, Gorkun OV, Medved LV, Nieuwenhuizen W, Weisel JW: 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, 1993
    • (1993) J Biol Chem , vol.268 , pp. 13577
    • Veklich, Y.I.1    Gorkun, O.V.2    Medved, L.V.3    Nieuwenhuizen, W.4    Weisel, J.W.5
  • 11
    • 0040119537 scopus 로고
    • Evidence for four different polymerization sites involved in human fibrin formation
    • Olexa SA, Budzynski AZ: Evidence for four different polymerization sites involved in human fibrin formation. Proc Natl Acad Sci USA 77:1374, 1980
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1374
    • Olexa, S.A.1    Budzynski, A.Z.2
  • 12
    • 1842385256 scopus 로고
    • Synthetic peptide probes on the location of fibrin polymerization sites
    • Doolittle RF, Laudano AP: Synthetic peptide probes on the location of fibrin polymerization sites. Protides Biological Fluids 28:311, 1980
    • (1980) Protides Biological Fluids , vol.28 , pp. 311
    • Doolittle, R.F.1    Laudano, A.P.2
  • 13
    • 0025136902 scopus 로고
    • Location of the binding site "b" for lateral polymerization of fibrin
    • Hasegawa N, Sasaki S: Location of the binding site "b" for lateral polymerization of fibrin. Thromb Res 57:183, 1990
    • (1990) Thromb Res , vol.57 , pp. 183
    • Hasegawa, N.1    Sasaki, S.2
  • 15
    • 70449217162 scopus 로고
    • Coagulation studies on "Reptilase", an extract of the venom from Bothrops jararaca
    • Blombäck B, Blombäck M, Nilsson IM: Coagulation studies on "Reptilase", an extract of the venom from Bothrops jararaca. Thromb Diath Haemor 1:76, 1957
    • (1957) Thromb Diath Haemor , vol.1 , pp. 76
    • Blombäck, B.1    Blombäck, M.2    Nilsson, I.M.3
  • 16
    • 0001156062 scopus 로고
    • Cofibrins and fibrin-intermediates as indicators of thrombin activity in vivo
    • Shainoff JR, Page IH: Cofibrins and fibrin-intermediates as indicators of thrombin activity in vivo. Circ Res 8:1013, 1960
    • (1960) Circ Res , vol.8 , pp. 1013
    • Shainoff, J.R.1    Page, I.H.2
  • 17
    • 0020645318 scopus 로고
    • Fibrinopeptide B in fibrin assembly and metabolism: Physiologic significance in delayed release of the peptide
    • Shainoff JR, Dardik BN: Fibrinopeptide B in fibrin assembly and metabolism: Physiologic significance in delayed release of the peptide. Ann NY Acad Sci 408:254, 1983
    • (1983) Ann NY Acad Sci , vol.408 , pp. 254
    • Shainoff, J.R.1    Dardik, B.N.2
  • 18
    • 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 JW, Veklich Y, Gorkun O: 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, 1993
    • (1993) J Mol Biol , vol.232 , pp. 285
    • Weisel, J.W.1    Veklich, Y.2    Gorkun, O.3
  • 19
    • 0000096019 scopus 로고
    • Transpeptidation mechanism in blood clotting
    • Lorand L, Konishi K, Jacobsen A: Transpeptidation mechanism in blood clotting. Nature 194:1148, 1962
    • (1962) Nature , vol.194 , pp. 1148
    • Lorand, L.1    Konishi, K.2    Jacobsen, A.3
  • 20
    • 0014428478 scopus 로고
    • Cross-link in fibrin polymerized by factor XIII: ε-(γ-glutamyl)lysine
    • Pisano JJ, Finlayson JS, Peyton MP: Cross-link in fibrin polymerized by factor XIII: ε-(γ-glutamyl)lysine. Science 160:892, 1968
    • (1968) Science , vol.160 , pp. 892
    • Pisano, J.J.1    Finlayson, J.S.2    Peyton, M.P.3
  • 22
    • 0015237796 scopus 로고
    • γ-γ cross-linking sites in human and bovine fibrin
    • Chen R, Doolittle RF: γ-γ cross-linking sites in human and bovine fibrin. Biochemistry 10:4487, 1971
    • (1971) Biochemistry , vol.10 , pp. 4487
    • Chen, R.1    Doolittle, R.F.2
  • 23
    • 0027131783 scopus 로고
    • Localization of the crosslinking site of GPRVVERHK in the γ-chain of human fibrinogen
    • Cierniewski CS, Budzynski AZ: Localization of the crosslinking site of GPRVVERHK in the γ-chain of human fibrinogen. Eur J Biochem 218:321, 1993
    • (1993) Eur J Biochem , vol.218 , pp. 321
    • Cierniewski, C.S.1    Budzynski, A.Z.2
  • 24
    • 3543099944 scopus 로고
    • Crosslinking of human fibrin: Evidence for intermolecular crosslinking involving α-chains
    • McDonagh RP, McDonagh J, Blombäck M, Blombäck B: Crosslinking of human fibrin: Evidence for intermolecular crosslinking involving α-chains. FEBS Lett 14:33, 1971
    • (1971) FEBS Lett , vol.14 , pp. 33
    • McDonagh, R.P.1    McDonagh, J.2    Blombäck, M.3    Blombäck, B.4
  • 25
    • 0018567763 scopus 로고
    • Amino acid sequence studies on the a chain of human fibrinogen. Exact location of cross-linking acceptor sites
    • Cottrell B A, Strong DD, Watt KW, Doolittle RF: Amino acid sequence studies on the a chain of human fibrinogen. Exact location of cross-linking acceptor sites. Biochemistry 18:5405, 1979
    • (1979) Biochemistry , vol.18 , pp. 5405
    • Cottrell, B.A.1    Strong, D.D.2    Watt, K.W.3    Doolittle, R.F.4
  • 26
    • 0029932912 scopus 로고    scopus 로고
    • Factor XIIIa-catalyzed cross-linking of recombinant αC fragments of human fibrinogen
    • Matsuka YV, Medved LV, Migliorini MM, Ingham KC: Factor XIIIa-catalyzed cross-linking of recombinant αC fragments of human fibrinogen. Biochemistry 35:5810, 1996
    • (1996) Biochemistry , vol.35 , pp. 5810
    • Matsuka, Y.V.1    Medved, L.V.2    Migliorini, M.M.3    Ingham, K.C.4
  • 27
    • 0029784197 scopus 로고    scopus 로고
    • Identification of the a chain lysine donor sites involved in factor XIIIa fibrin cross-linking
    • Sobel JH, Gawinowicz MA: Identification of the a chain lysine donor sites involved in factor XIIIa fibrin cross-linking. J Biol Chem 271:19288, 1996
    • (1996) J Biol Chem , vol.271 , pp. 19288
    • Sobel, J.H.1    Gawinowicz, M.A.2
  • 28
    • 0014817348 scopus 로고
    • Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin
    • McKee PA, Mattock P, Hill RL: Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc Natl Acad Sci USA 66:738, 1970
    • (1970) Proc Natl Acad Sci USA , vol.66 , pp. 738
    • McKee, P.A.1    Mattock, P.2    Hill, R.L.3
  • 29
    • 0020596436 scopus 로고
    • Contribution of fibrin stabilization to clot strength. Supplementation of factor XIII-deficient plasma with the purified zymogen
    • Shen L, Lorand L: Contribution of fibrin stabilization to clot strength. Supplementation of factor XIII-deficient plasma with the purified zymogen. J Clin Invest 71:1336, 1983
    • (1983) J Clin Invest , vol.71 , pp. 1336
    • Shen, L.1    Lorand, L.2
  • 31
    • 0023939414 scopus 로고
    • Increased resistance to plasmic degradation of fibrin with highly crosslinked α-polymer chains formed at high factor XIII concentrations
    • Francis CW, Marder VJ: Increased resistance to plasmic degradation of fibrin with highly crosslinked α-polymer chains formed at high factor XIII concentrations. Blood 71:1361, 1988
    • (1988) Blood , vol.71 , pp. 1361
    • Francis, C.W.1    Marder, V.J.2
  • 32
    • 0027993303 scopus 로고
    • Progressive cross-linking of fibrin γ chains increases resistance to fibrinolysis
    • Siebenlist KR, Mosesson MW: Progressive cross-linking of fibrin γ chains increases resistance to fibrinolysis. J Biol Chem 269:28414, 1994
    • (1994) J Biol Chem , vol.269 , pp. 28414
    • Siebenlist, K.R.1    Mosesson, M.W.2
  • 33
    • 0017847923 scopus 로고
    • Molecular mechanism of physiological fibrinolysis
    • Wiman B, Collen D: Molecular mechanism of physiological fibrinolysis. Nature 272:549, 1978
    • (1978) Nature , vol.272 , pp. 549
    • Wiman, B.1    Collen, D.2
  • 34
    • 0020472522 scopus 로고
    • Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin
    • Hoylaerts M, Rijken DC, Lijnen HR, Collen D: Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J Biol Chem 257:2912, 1982
    • (1982) J Biol Chem , vol.257 , pp. 2912
    • Hoylaerts, M.1    Rijken, D.C.2    Lijnen, H.R.3    Collen, D.4
  • 35
    • 0019987224 scopus 로고
    • Studies on the kinetics of plasminogen activation by tissue plasminogen activator
    • Ranby M: Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim Biophys Acta 704:461, 1982
    • (1982) Biochim Biophys Acta , vol.704 , pp. 461
    • Ranby, M.1
  • 36
    • 0025642709 scopus 로고
    • The role of fragment X polymers in the fibrin enhancement of tissue plasminogen activator-catalyzed plasmin formation
    • Suenson E, Bjerrum P, Holm A, Lind B, Meldal M, Seimer J, Petersen LC: The role of fragment X polymers in the fibrin enhancement of tissue plasminogen activator-catalyzed plasmin formation. J Biol Chem 265:22228, 1990
    • (1990) J Biol Chem , vol.265 , pp. 22228
    • Suenson, E.1    Bjerrum, P.2    Holm, A.3    Lind, B.4    Meldal, M.5    Seimer, J.6    Petersen, L.C.7
  • 37
    • 0027937766 scopus 로고
    • Fibrin structures during tissue-type plasminogen activator-mediated fibrinolysis studied by laser light scattering: Relation to fibrin enhancement of plasminogen activation
    • Bauer R, Hansen SL, Jones G, Suenson E, Thorsen S, Ogendal L: Fibrin structures during tissue-type plasminogen activator-mediated fibrinolysis studied by laser light scattering: Relation to fibrin enhancement of plasminogen activation. Eur Biophys J 23:239, 1994
    • (1994) Eur Biophys J , vol.23 , pp. 239
    • Bauer, R.1    Hansen, S.L.2    Jones, G.3    Suenson, E.4    Thorsen, S.5    Ogendal, L.6
  • 39
    • 0023267687 scopus 로고
    • Fibrinogen induces adhesion, spreading, and microfilament organization of human endothelial cells in vitro
    • Dejana E, Colella S, Languino LR, Balconi G, Corbascio GC, Marchisio PC: Fibrinogen induces adhesion, spreading, and microfilament organization of human endothelial cells in vitro. J Cell Biol 104:1403, 1987
    • (1987) J Cell Biol , vol.104 , pp. 1403
    • Dejana, E.1    Colella, S.2    Languino, L.R.3    Balconi, G.4    Corbascio, G.C.5    Marchisio, P.C.6
  • 40
    • 0024247053 scopus 로고
    • Biochemical and functional characteristics of fibrinogen interaction with endothelial cells
    • Dejana E, Zanetti A, Conforti G: Biochemical and functional characteristics of fibrinogen interaction with endothelial cells. Haemostasis 18:262, 1988
    • (1988) Haemostasis , vol.18 , pp. 262
    • Dejana, E.1    Zanetti, A.2    Conforti, G.3
  • 42
    • 0029957939 scopus 로고    scopus 로고
    • Fibrinogen mediates leukocyte-endothelium bridging in vivo at low shear forces
    • Sriramarao P, Languino LR, Altieri DC: Fibrinogen mediates leukocyte-endothelium bridging in vivo at low shear forces. Blood 88:3416, 1996
    • (1996) Blood , vol.88 , pp. 3416
    • Sriramarao, P.1    Languino, L.R.2    Altieri, D.C.3
  • 44
    • 0024109978 scopus 로고
    • Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen
    • Altieri DC, Bader R, Mannucci PM, Edgington TS: Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen. J Cell Biol 107:1893, 1988
    • (1988) J Cell Biol , vol.107 , pp. 1893
    • Altieri, D.C.1    Bader, R.2    Mannucci, P.M.3    Edgington, T.S.4
  • 46
    • 0023694736 scopus 로고
    • Fibrinogen association with human monocytes: Evidence for constitutive expression of fibrinogen receptors and for involvement of Mac-1 (CD18, CR3) in the binding
    • Trezzini C, Jungi TW, Kuhnert P, Peterhans E: Fibrinogen association with human monocytes: Evidence for constitutive expression of fibrinogen receptors and for involvement of Mac-1 (CD18, CR3) in the binding. Biochem Biophys Res Commun 156:477, 1988
    • (1988) Biochem Biophys Res Commun , vol.156 , pp. 477
    • Trezzini, C.1    Jungi, T.W.2    Kuhnert, P.3    Peterhans, E.4
  • 48
    • 0029822772 scopus 로고    scopus 로고
    • Fibulin-1 mediates platelet adhesion via a bridge of fibrinogen
    • Godyna S, Diaz Ricart M, Argraves WS: Fibulin-1 mediates platelet adhesion via a bridge of fibrinogen. Blood 88:2569, 1996
    • (1996) Blood , vol.88 , pp. 2569
    • Godyna, S.1    Diaz Ricart, M.2    Argraves, W.S.3
  • 50
    • 0022399546 scopus 로고
    • Characterization of peptides cleaved by plasmin from the C-terminal polymerization domain of human fibrinogen
    • Southan C, Thompson E, Panico M, Etienne T, Morris HR, Lane DA: Characterization of peptides cleaved by plasmin from the C-terminal polymerization domain of human fibrinogen. J Biol Chem 260:13095, 1985
    • (1985) J Biol Chem , vol.260 , pp. 13095
    • Southan, C.1    Thompson, E.2    Panico, M.3    Etienne, T.4    Morris, H.R.5    Lane, D.A.6
  • 51
    • 0022263169 scopus 로고
    • Localization of a fibrinogen calcium binding site between γ-subunit positions 311 and 336 by terbium fluorescence
    • Dang CV, Ebert RF, Bell WR; Localization of a fibrinogen calcium binding site between γ-subunit positions 311 and 336 by terbium fluorescence. J Biol Chem 260:9713, 1985
    • (1985) J Biol Chem , vol.260 , pp. 9713
    • Dang, C.V.1    Ebert, R.F.2    Bell, W.R.3
  • 52
    • 0022461520 scopus 로고
    • Localization of segments essential for polymerization and for calcium binding in the γ-chain of human fibrinogen
    • Váradi A, Scheraga HA: Localization of segments essential for polymerization and for calcium binding in the γ-chain of human fibrinogen. Biochemistry 25:519, 1986
    • (1986) Biochemistry , vol.25 , pp. 519
    • Váradi, A.1    Scheraga, H.A.2
  • 53
    • 0026576175 scopus 로고
    • Photoaffinity labeling of the primary fibrin polymerization site: Isolation and characterization of a labeled cyanogen bromide fragment corresponding to γ-chain residues 337-379
    • Shimizu A, Nagel GM, Doolittle RF: Photoaffinity labeling of the primary fibrin polymerization site: isolation and characterization of a labeled cyanogen bromide fragment corresponding to γ-chain residues 337-379. Proc Natl Acad Sci USA 89:2888, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2888
    • Shimizu, A.1    Nagel, G.M.2    Doolittle, R.F.3
  • 54
    • 0026594383 scopus 로고
    • Photoaffinity labeling of the primary fibrin polymerization site: Localization of the label to γ-chain Tyr-363
    • Yamazumi K, Doolittle RF: Photoaffinity labeling of the primary fibrin polymerization site: localization of the label to γ-chain Tyr-363. Proc Natl Acad Sci USA 89:2893, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2893
    • Yamazumi, K.1    Doolittle, R.F.2
  • 56
    • 0030738474 scopus 로고    scopus 로고
    • The primary fibrin polymerization pocket: Three-dimensional structure of a 30-kDa C-terminal γ chain fragment complexed with the peptide Gly-Pro-Arg-Pro
    • Pratt KP, Côté HCF, Chung DW, Stenkamp RE, Davie EW: The primary fibrin polymerization pocket: Three-dimensional structure of a 30-kDa C-terminal γ chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci USA 94:7176, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7176
    • Pratt, K.P.1    Côté, H.C.F.2    Chung, D.W.3    Stenkamp, R.E.4    Davie, E.W.5
  • 57
    • 0020694167 scopus 로고
    • Recognition site for the platelet receptor is present on the 15-residue carboxy-terminal fragment of the γ chain of human fibrinogen and is not involved in the fibrin polymerization reaction
    • Kloczewiak M, Timmons S, Hawiger J: Recognition site for the platelet receptor is present on the 15-residue carboxy-terminal fragment of the γ chain of human fibrinogen and is not involved in the fibrin polymerization reaction. Thromb Res 29:249, 1983
    • (1983) Thromb Res , vol.29 , pp. 249
    • Kloczewiak, M.1    Timmons, S.2    Hawiger, J.3
  • 58
    • 0021319857 scopus 로고
    • Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the γ chain
    • Kloczewiak M, Timmons S, Lukas TJ, Hawiger J: Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the γ chain. Biochemistry 23:1767, 1984
    • (1984) Biochemistry , vol.23 , pp. 1767
    • Kloczewiak, M.1    Timmons, S.2    Lukas, T.J.3    Hawiger, J.4
  • 59
    • 0026476184 scopus 로고
    • The residues AGDV of recombinant γ chains of human fibrinogen must be carboxy-terminal to support human platelet aggregation
    • Hettasch JM, Bolyard MG, Lord ST: The residues AGDV of recombinant γ chains of human fibrinogen must be carboxy-terminal to support human platelet aggregation. Thromb Haemost 68:701, 1992
    • (1992) Thromb Haemost , vol.68 , pp. 701
    • Hettasch, J.M.1    Bolyard, M.G.2    Lord, S.T.3
  • 60
    • 0029978277 scopus 로고    scopus 로고
    • Dissecting clot retraction and platelet aggregation. Clot retraction does not require an intact fibrinogen γ chain C terminus
    • Rooney MM, Parise LV, Lord ST: Dissecting clot retraction and platelet aggregation. Clot retraction does not require an intact fibrinogen γ chain C terminus. J Biol Chem 271:8553, 1996
    • (1996) J Biol Chem , vol.271 , pp. 8553
    • Rooney, M.M.1    Parise, L.V.2    Lord, S.T.3
  • 61
    • 0024381372 scopus 로고
    • Low-affinity interaction of fibrinogen carboxy-gamma terminus with human monocytes induces an oxidative burst and modulates effector functions
    • Trezzini C, Jungi TW, Maly FE, Vittoz M, Peterhans E: Low-affinity interaction of fibrinogen carboxy-gamma terminus with human monocytes induces an oxidative burst and modulates effector functions. Biochem Biophys Res Commun 165:7, 1989
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 7
    • Trezzini, C.1    Jungi, T.W.2    Maly, F.E.3    Vittoz, M.4    Peterhans, E.5
  • 63
    • 0030990983 scopus 로고    scopus 로고
    • Domain structure and functional activity of the recombinant human fibrinogen γ-module (γ148-411)
    • Medved L, Litvinovich S, Ugarova T, Matsuka Y, Ingham K: Domain structure and functional activity of the recombinant human fibrinogen γ-module (γ148-411). Biochemistry 36:4685, 1997
    • (1997) Biochemistry , vol.36 , pp. 4685
    • Medved, L.1    Litvinovich, S.2    Ugarova, T.3    Matsuka, Y.4    Ingham, K.5
  • 64
    • 0020539513 scopus 로고
    • Location of plasminogen-binding sites in human fibrin(ogen)
    • Váradi A, Patthy L: Location of plasminogen-binding sites in human fibrin(ogen). Biochemistry 22:2440, 1983
    • (1983) Biochemistry , vol.22 , pp. 2440
    • Váradi, A.1    Patthy, L.2
  • 66
    • 0026521641 scopus 로고
    • Localization in the fibrinogen γ-chain of a new site that is involved in the acceleration of the tissue-type plasmmogen activator-catalysed activation of plasminogen
    • Yonekawa O, Voskuilen M, Nieuwenhuizen W: Localization in the fibrinogen γ-chain of a new site that is involved in the acceleration of the tissue-type plasmmogen activator-catalysed activation of plasminogen. Biochem J 283:187, 1992
    • (1992) Biochem J , vol.283 , pp. 187
    • Yonekawa, O.1    Voskuilen, M.2    Nieuwenhuizen, W.3
  • 67
    • 0027459457 scopus 로고
    • Initial interaction between fibrin and tissue plasminogen activator (t-PA). the Gly-Pro-Arg-Pro binding site on fibrin(ogen) is important for t-PA activity
    • Kaczmarek E, Lee MH, McDonagh J: Initial interaction between fibrin and tissue plasminogen activator (t-PA). The Gly-Pro-Arg-Pro binding site on fibrin(ogen) is important for t-PA activity. J Biol Chem 268:2474, 1993
    • (1993) J Biol Chem , vol.268 , pp. 2474
    • Kaczmarek, E.1    Lee, M.H.2    McDonagh, J.3
  • 68
    • 0028104076 scopus 로고
    • Sites in fibrin involved in the acceleration of plasminogen activation by t-PA. Possible role of fibrin polymerisation
    • Nieuwenhuizen W: Sites in fibrin involved in the acceleration of plasminogen activation by t-PA. Possible role of fibrin polymerisation. Thromb Res 75:343, 1994
    • (1994) Thromb Res , vol.75 , pp. 343
    • Nieuwenhuizen, W.1
  • 70
    • 0023644095 scopus 로고
    • Fibrinogen and risk of cardiovascular disease. the Framingham Study
    • Kannel WB, Wolf PA, Castelli WP, D'Agostino RB: Fibrinogen and risk of cardiovascular disease. The Framingham Study. JAMA 258:1183, 1987
    • (1987) JAMA , vol.258 , pp. 1183
    • Kannel, W.B.1    Wolf, P.A.2    Castelli, W.P.3    D'Agostino, R.B.4
  • 72
    • 0028123725 scopus 로고
    • Fibrinogen: An important risk factor for atherothrombotic diseases
    • Ernst E: Fibrinogen: An important risk factor for atherothrombotic diseases. Ann Med 26:15, 1994
    • (1994) Ann Med , vol.26 , pp. 15
    • Ernst, E.1
  • 73
    • 0027996501 scopus 로고
    • Fibrinogen: A major new risk factor for cardiovascular disease. A review of the literature
    • de la Serna G: Fibrinogen: A major new risk factor for cardiovascular disease. A review of the literature. J Fam Pract 39:468, 1994
    • (1994) J Fam Pract , vol.39 , pp. 468
    • De la Serna, G.1
  • 74
    • 0028085216 scopus 로고
    • Fibrinogen: Its emerging role as a cardiovascular risk factor
    • Ernst E: Fibrinogen: Its emerging role as a cardiovascular risk factor. Angiology 45:87, 1994
    • (1994) Angiology , vol.45 , pp. 87
    • Ernst, E.1
  • 75
    • 0026645829 scopus 로고
    • Fibrin gel network characteristics and coronary heart disease: Relations to plasma fibrinogen concentration, acute phase protein, serum lipoproteins and coronary atherosclerosis
    • Fatah K, Hamsten A, Blombäck B, Blombäck M: Fibrin gel network characteristics and coronary heart disease: Relations to plasma fibrinogen concentration, acute phase protein, serum lipoproteins and coronary atherosclerosis. Thromb Haemost 68:130, 1992
    • (1992) Thromb Haemost , vol.68 , pp. 130
    • Fatah, K.1    Hamsten, A.2    Blombäck, B.3    Blombäck, M.4
  • 76
    • 0023941118 scopus 로고
    • Erythrocyte aggregation and cardiovascular risk factors
    • Dintenfass L: Erythrocyte aggregation and cardiovascular risk factors. Clin Hemorheol 8:237, 1988
    • (1988) Clin Hemorheol , vol.8 , pp. 237
    • Dintenfass, L.1
  • 77
    • 0027965921 scopus 로고
    • Fibrin in human plasma: Gel architectures governed by rate and nature of fibrinogen activation
    • Blombäck B, Carlsson K, Fatah K, Hessel B, Procyk R: Fibrin in human plasma: Gel architectures governed by rate and nature of fibrinogen activation. Thromb Res 75:521, 1994
    • (1994) Thromb Res , vol.75 , pp. 521
    • Blombäck, B.1    Carlsson, K.2    Fatah, K.3    Hessel, B.4    Procyk, R.5
  • 78
    • 0026759420 scopus 로고
    • Fibrinogen anomalies and disease. A clinical update
    • Galanakis DK: Fibrinogen anomalies and disease. A clinical update. Hematol Oncol Clin North Am 6:1171, 1992
    • (1992) Hematol Oncol Clin North Am , vol.6 , pp. 1171
    • Galanakis, D.K.1
  • 80
    • 0027143945 scopus 로고
    • A review of the hypercoagulable state
    • Eby CS: A review of the hypercoagulable state. Hematol Oncol Clin North Am 7:1121, 1993
    • (1993) Hematol Oncol Clin North Am , vol.7 , pp. 1121
    • Eby, C.S.1
  • 81
    • 0027729107 scopus 로고
    • Hypercoagulable states
    • Nachman RL, Silverstein R: Hypercoagulable states. Ann Intern Med 119:819, 1993 [see comments in Ann Intern Med 119:819, 1993]
    • (1993) Ann Intern Med , vol.119 , pp. 819
    • Nachman, R.L.1    Silverstein, R.2
  • 82
    • 0027729107 scopus 로고
    • see comments
    • Nachman RL, Silverstein R: Hypercoagulable states. Ann Intern Med 119:819, 1993 [see comments in Ann Intern Med 119:819, 1993]
    • (1993) Ann Intern Med , vol.119 , pp. 819
  • 83
    • 0028291573 scopus 로고
    • Evaluation of mild bleeding disorders and easy bruising
    • Sham RL, Francis CW: Evaluation of mild bleeding disorders and easy bruising. Blood Rev 8:98, 1994
    • (1994) Blood Rev , vol.8 , pp. 98
    • Sham, R.L.1    Francis, C.W.2
  • 84
    • 0028577799 scopus 로고
    • Hypercoagulable states: Molecular genetics to clinical practice
    • Schafer AI: Hypercoagulable states: Molecular genetics to clinical practice. Lancet 344:1739, 1994
    • (1994) Lancet , vol.344 , pp. 1739
    • Schafer, A.I.1
  • 85
    • 0028877613 scopus 로고
    • Familial dysfibrinogenemia and thrombophilia. Report on a study of the SSC Subcommittee on Fibrinogen
    • Haverkate F, Samama M: Familial dysfibrinogenemia and thrombophilia. Report on a study of the SSC Subcommittee on Fibrinogen. Thromb Haemost 73:151, 1995
    • (1995) Thromb Haemost , vol.73 , pp. 151
    • Haverkate, F.1    Samama, M.2
  • 86
    • 0030850123 scopus 로고    scopus 로고
    • Risk factors for venous thrombosis: Prevalence, risk, and interaction
    • Rosendaal FR: Risk factors for venous thrombosis: Prevalence, risk, and interaction. Semin Hematol 34:171, 1997
    • (1997) Semin Hematol , vol.34 , pp. 171
    • Rosendaal, F.R.1
  • 88
    • 0002012682 scopus 로고
    • Hereditary variants of human fibrinogens
    • Bloom F, Forbes CD, Thomas DP, Tuddenham EGD (eds). Edinburgh, UK, Churchill Livingstone
    • Koopman J, Haverkate F: Hereditary variants of human fibrinogens, in Bloom F, Forbes CD, Thomas DP, Tuddenham EGD (eds): Haemostasis and Thrombosis, vol 1. Edinburgh, UK, Churchill Livingstone, 1994, p 515
    • (1994) Haemostasis and Thrombosis , vol.1 , pp. 515
    • Koopman, J.1    Haverkate, F.2
  • 90
    • 70249091771 scopus 로고
    • The fibrinogen molecule: Its size, shape, and mode of polymerization
    • Hall C, Slayter H: The fibrinogen molecule: Its size, shape, and mode of polymerization. J Biophys Biochem Cyt 5:11, 1959
    • (1959) J Biophys Biochem Cyt , vol.5 , pp. 11
    • Hall, C.1    Slayter, H.2
  • 91
    • 0001033839 scopus 로고
    • Axial period of fibrinogen and fibrin
    • Stryer L, Cohen C, Langridge R: Axial period of fibrinogen and fibrin. Nature 197:793, 1963
    • (1963) Nature , vol.197 , pp. 793
    • Stryer, L.1    Cohen, C.2    Langridge, R.3
  • 92
    • 0016396449 scopus 로고
    • Crystallisation of a modified ribrinogen
    • Cohen C, Tooney NM: Crystallisation of a modified ribrinogen. Nature 251:659, 1974
    • (1974) Nature , vol.251 , pp. 659
    • Cohen, C.1    Tooney, N.M.2
  • 93
    • 0018222289 scopus 로고
    • Crystals of modified fibrinogen: Size, shape and packing of molecules
    • Weisel JW, Warren SG, Cohen C: Crystals of modified fibrinogen: Size, shape and packing of molecules. J Mol Biol 126:159, 1978
    • (1978) J Mol Biol , vol.126 , pp. 159
    • Weisel, J.W.1    Warren, S.G.2    Cohen, C.3
  • 94
    • 0018725401 scopus 로고
    • Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy
    • Fowler WE, Erickson HP: Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy. J Mol Biol 134:241, 1979
    • (1979) J Mol Biol , vol.134 , pp. 241
    • Fowler, W.E.1    Erickson, H.P.2
  • 98
    • 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 389:455, 1997
    • (1997) Nature , vol.389 , pp. 455
    • Spraggon, G.1    Everse, S.J.2    Doolittle, R.F.3
  • 99
    • 1842292129 scopus 로고    scopus 로고
    • The polymerization pocket "a" within the carboxyl-terminal region of the γ chain of human fibrinogen is adjacent to but independent from the calcium-binding site
    • Ĉté HCF, Pratt KP, Davie EW, Chung DW: The polymerization pocket "a" within the carboxyl-terminal region of the γ chain of human fibrinogen is adjacent to but independent from the calcium-binding site. J Biol Chem 272:23792, 1997
    • (1997) J Biol Chem , vol.272 , pp. 23792
    • Ĉté, H.C.F.1    Pratt, K.P.2    Davie, E.W.3    Chung, D.W.4
  • 100
    • 0027055525 scopus 로고
    • A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives
    • Doolittle RF: A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives. Protein Sci 1:1563, 1992
    • (1992) Protein Sci , vol.1 , pp. 1563
    • Doolittle, R.F.1
  • 101
    • 0029111701 scopus 로고
    • The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and ribrinogen Tokyo II (γ275 Arg → Cys)
    • Mosesson MW, Siebenlist KR, DiOrio JP, Matsuda M, Hainfeld JF, Wall JS: The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and ribrinogen Tokyo II (γ275 Arg → Cys). J Clin Invest 96:1053, 1995
    • (1995) J Clin Invest , vol.96 , pp. 1053
    • Mosesson, M.W.1    Siebenlist, K.R.2    DiOrio, J.P.3    Matsuda, M.4    Hainfeld, J.F.5    Wall, J.S.6
  • 103
    • 0025195067 scopus 로고
    • 1H NMR sequential assignments and secondary structure analysis of human fibrinogen γ-chain C-terminal residues 385-411
    • Mayo KH, Burke C, Lindon JN, Kloczewiak M: 1H NMR sequential assignments and secondary structure analysis of human fibrinogen γ-chain C-terminal residues 385-411, Biochemistry 29:3277, 1990
    • (1990) Biochemistry , vol.29 , pp. 3277
    • Mayo, K.H.1    Burke, C.2    Lindon, J.N.3    Kloczewiak, M.4
  • 104
    • 0026483948 scopus 로고
    • A β-turn is present in the 392-411 segment of the human fibrinogen γ-chain. Effects of structural changes in this segment on affinity to antibody 4A5
    • Blumenstein M, Matsueda GR, Tiffimons S, Hawiger J: A β-turn is present in the 392-411 segment of the human fibrinogen γ-chain. Effects of structural changes in this segment on affinity to antibody 4A5. Biochemistry 31:10692, 1992
    • (1992) Biochemistry , vol.31 , pp. 10692
    • Blumenstein, M.1    Matsueda, G.R.2    Tiffimons, S.3    Hawiger, J.4
  • 105
    • 0028135357 scopus 로고
    • Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen γ chain obtained by carrier protein-driven crystallization
    • Donahue JP, Patel H, Anderson WF, Hawiger J: Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen γ chain obtained by carrier protein-driven crystallization. Proc Natl Acad Sci USA 91:12178, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12178
    • Donahue, J.P.1    Patel, H.2    Anderson, W.F.3    Hawiger, J.4
  • 106
    • 0028894964 scopus 로고
    • Effect of pH on the conformation and backbone dynamics of a 27-residue peptide in trifluorethanol. An NMR and CD study
    • Fan F, Mayo KH: Effect of pH on the conformation and backbone dynamics of a 27-residue peptide in trifluorethanol. An NMR and CD study. J Biol Chem 270:24693, 1995
    • (1995) J Biol Chem , vol.270 , pp. 24693
    • Fan, F.1    Mayo, K.H.2
  • 107
    • 0029971737 scopus 로고    scopus 로고
    • Integrin receptor GPIIb/IIIa bound state conformation of the fibrinogen γ-chain C-terminal peptide 400-411: NMR and transfer NOE studies
    • Mayo KH, Fan F, Beavers MP, Eckardt A, Keane P, Hoekstra WJ, Andrade-Gordon P: Integrin receptor GPIIb/IIIa bound state conformation of the fibrinogen γ-chain C-terminal peptide 400-411: NMR and transfer NOE studies. Biochemistry 35:4434, 1996
    • (1996) Biochemistry , vol.35 , pp. 4434
    • Mayo, K.H.1    Fan, F.2    Beavers, M.P.3    Eckardt, A.4    Keane, P.5    Hoekstra, W.J.6    Andrade-Gordon, P.7
  • 108
    • 0024396651 scopus 로고
    • The normal and morbid biology of fibrinogen
    • Dang CV, Bell WR, Shuman M: The normal and morbid biology of fibrinogen. Am J Med 87:567, 1989
    • (1989) Am J Med , vol.87 , pp. 567
    • Dang, C.V.1    Bell, W.R.2    Shuman, M.3
  • 109
    • 0025167430 scopus 로고
    • Molecular abnormalities of fibrinogen - The present status of structure elucidation
    • Matsuda M, Iwanaga S, Takada A, Henschen A (eds). Amsterdam, The Netherlands, Elsevier
    • Matsuda M, Yoshida N, Terukina S, Yamazumi K, Maekawa H: Molecular abnormalities of fibrinogen - The present status of structure elucidation, in Matsuda M, Iwanaga S, Takada A, Henschen A (eds): Fibrinogen 4. Current Basic and Clinical aspects. Amsterdam, The Netherlands, Elsevier, 1990, p 139
    • (1990) Fibrinogen 4. Current Basic and Clinical Aspects , pp. 139
    • Matsuda, M.1    Yoshida, N.2    Terukina, S.3    Yamazumi, K.4    Maekawa, H.5
  • 110
    • 0027724649 scopus 로고
    • Inherited dysfibrinogenemia: Emerging abnormal structure associations with pathologic and nonpathologic dysfunctions
    • Galanakis DK: Inherited dysfibrinogenemia: Emerging abnormal structure associations with pathologic and nonpathologic dysfunctions. Semin Thromb Hemost 19:386, 1993
    • (1993) Semin Thromb Hemost , vol.19 , pp. 386
    • Galanakis, D.K.1
  • 111
    • 0030273580 scopus 로고    scopus 로고
    • The structure-function relationship of hereditary dysfibrinogens
    • Matsuda M: The structure-function relationship of hereditary dysfibrinogens. Int J Hematol 64:167, 1996
    • (1996) Int J Hematol , vol.64 , pp. 167
    • Matsuda, M.1
  • 114
    • 0023755597 scopus 로고
    • Substitution of γ Arg-275 by Cys in an abnormal fibrinogen, "fibrinogen Osaka II." Evidence for a unique solitary cystine structure at the mutation site
    • Terukina S, Matsuda M, Hirata H, Takeda Y, Miyata T, Takao T, Shimonishi Y: Substitution of γ Arg-275 by Cys in an abnormal fibrinogen, "fibrinogen Osaka II." Evidence for a unique solitary cystine structure at the mutation site. J Biol Chem 263:13579, 1988
    • (1988) J Biol Chem , vol.263 , pp. 13579
    • Terukina, S.1    Matsuda, M.2    Hirata, H.3    Takeda, Y.4    Miyata, T.5    Takao, T.6    Shimonishi, Y.7
  • 115
    • 0023860974 scopus 로고
    • An apparently higher molecular weight γ-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of γ arginine-275 by cysteine
    • Yoshida N, Ota K, Moroi M, Matsuda M: An apparently higher molecular weight γ-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of γ arginine-275 by cysteine. Blood 71:480, 1988
    • (1988) Blood , vol.71 , pp. 480
    • Yoshida, N.1    Ota, K.2    Moroi, M.3    Matsuda, M.4
  • 116
    • 0000792704 scopus 로고
    • Two abnormal fibrinogens designated as Osaka II and Morioka with a hitherto unidentified amino acid substitution; γArg-275 by Cys
    • Terukina S, Matsuda M, Yoshida N, Yamazumi K, Takeda Y, Takano T: Two abnormal fibrinogens designated as Osaka II and Morioka with a hitherto unidentified amino acid substitution; γArg-275 by Cys (abstr). Thromb Haemost 58:515, 1987
    • (1987) Thromb Haemost , vol.58 , pp. 515
    • Terukina, S.1    Matsuda, M.2    Yoshida, N.3    Yamazumi, K.4    Takeda, Y.5    Takano, T.6
  • 117
    • 0021846230 scopus 로고
    • Fibrinogen Baltimore IV: Congenital dysfibrinogenemia with delayed fibrin monomer polymerization
    • Ebert RF, Bell WR: Fibrinogen Baltimore IV: Congenital dysfibrinogenemia with delayed fibrin monomer polymerization. Thromb Res 38:121, 1985
    • (1985) Thromb Res , vol.38 , pp. 121
    • Ebert, R.F.1    Bell, W.R.2
  • 118
    • 0024421560 scopus 로고
    • Fibrinogen Baltimore IV: Congenital dysfibrinogenemia with a γ275 (Arg → Cys) substitution
    • Schmelzer CH, Ebert RF, Bell WR: Fibrinogen Baltimore IV: Congenital dysfibrinogenemia with a γ275 (Arg → Cys) substitution. Thromb Res 56:307, 1989
    • (1989) Thromb Res , vol.56 , pp. 307
    • Schmelzer, C.H.1    Ebert, R.F.2    Bell, W.R.3
  • 119
    • 0021070892 scopus 로고
    • "Fibrinogen Tokyo II". An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules
    • Matsuda M, Baba M, Morimoto K, Nakamikawa C: "Fibrinogen Tokyo II". An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules. J Clin Invest 72:1034, 1983
    • (1983) J Clin Invest , vol.72 , pp. 1034
    • Matsuda, M.1    Baba, M.2    Morimoto, K.3    Nakamikawa, C.4
  • 121
    • 0029026342 scopus 로고
    • Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (γArg 275 → His) and Villajoyosa (γArg 275 → Cys)
    • Borrell M, Garí M, Coll I, Vallvé C, Tirado I, Soria JM, Sala N, Muñoz C, Oliver A, García A, Fontcuberta J: Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (γArg 275 → His) and Villajoyosa (γArg 275 → Cys). Blood Coagul Fibrinol 6:198, 1995
    • (1995) Blood Coagul Fibrinol , vol.6 , pp. 198
    • Borrell, M.1    Garí, M.2    Coll, I.3    Vallvé, C.4    Tirado, I.5    Soria, J.M.6    Sala, N.7    Muñoz, C.8    Oliver, A.9    García, A.10    Fontcuberta, J.11
  • 122
    • 0018619910 scopus 로고
    • Anticlotting properties of fragments D from human fibrinogen and fibrin
    • Haverkate F, Timan G, Nieuwenhuizen W: Anticlotting properties of fragments D from human fibrinogen and fibrin. Eur J Clin Invest 9:253, 1979
    • (1979) Eur J Clin Invest , vol.9 , pp. 253
    • Haverkate, F.1    Timan, G.2    Nieuwenhuizen, W.3
  • 123
    • 0000744717 scopus 로고    scopus 로고
    • Thrombophilia associated with dysfibrinogenemia [fibrinogen Cedar Rapids (γR275C)] and a heterozygous factor V Leiden defect
    • abstr, suppl
    • Mosesson MW, Siebenlist KR, Olson JD: Thrombophilia associated with dysfibrinogenemia [fibrinogen Cedar Rapids (γR275C)] and a heterozygous factor V Leiden defect. Thromb Haemost OC-1560:382, 1997 (abstr, suppl)
    • (1997) Thromb Haemost , vol.OC-1560 , pp. 382
    • Mosesson, M.W.1    Siebenlist, K.R.2    Olson, J.D.3
  • 126
    • 0030850713 scopus 로고    scopus 로고
    • Resistance to activated protein C as risk factor for thrombosis: Molecular mechanisms, laboratory investigation, and clinical management
    • Dahlback B: Resistance to activated protein C as risk factor for thrombosis: Molecular mechanisms, laboratory investigation, and clinical management. Semin Hematol 34:217, 1997
    • (1997) Semin Hematol , vol.34 , pp. 217
    • Dahlback, B.1
  • 128
    • 0026440134 scopus 로고
    • Heterozygous abnormal fibrinogen Osaka III with the replacement of γ arginine-275 by histidine has an apparently higher molecular weight γ-chain variant
    • Yoshida N, Imaoka S, Hirata H, Matsuda M, Asakura S: Heterozygous abnormal fibrinogen Osaka III with the replacement of γ arginine-275 by histidine has an apparently higher molecular weight γ-chain variant. Thromb Haemost 68:534, 1992
    • (1992) Thromb Haemost , vol.68 , pp. 534
    • Yoshida, N.1    Imaoka, S.2    Hirata, H.3    Matsuda, M.4    Asakura, S.5
  • 129
    • 0030066680 scopus 로고    scopus 로고
    • Fibrinogen Claro - Another dysfunctional fibrinogen variant with γ275 arginine → histidine substitution
    • published erratum appears in Thromb Res 82:107, 1996
    • Steinmann C, Jungo M, Beck EA, Lämmle B, Furlan M: Fibrinogen Claro - Another dysfunctional fibrinogen variant with γ275 arginine → histidine substitution [published erratum appears in Thromb Res 82:107, 1996]. Thromb Res 81:145, 1996
    • (1996) Thromb Res , vol.81 , pp. 145
    • Steinmann, C.1    Jungo, M.2    Beck, E.A.3    Lämmle, B.4    Furlan, M.5
  • 130
    • 0024213684 scopus 로고
    • Normal plasmic cleavage of the γ-chain variant of "fibrinogen Saga" with an Arg-275 to His substitution
    • Yamazumi K, Terukina S, Onohara S, Matsuda M: Normal plasmic cleavage of the γ-chain variant of "fibrinogen Saga" with an Arg-275 to His substitution. Thromb Haemost 60:476, 1988
    • (1988) Thromb Haemost , vol.60 , pp. 476
    • Yamazumi, K.1    Terukina, S.2    Onohara, S.3    Matsuda, M.4
  • 133
    • 0017686536 scopus 로고
    • Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D
    • Haverkate F, Timan G: Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D. Thromb Res 10:803, 1977
    • (1977) Thromb Res , vol.10 , pp. 803
    • Haverkate, F.1    Timan, G.2
  • 134
    • 0013844775 scopus 로고
    • A new inherited coagulation disorder caused by an abnormal fibrinogen ('Fibrinogen Baltimore')
    • Beck EA, Charache P, Jackson DP: A new inherited coagulation disorder caused by an abnormal fibrinogen ('Fibrinogen Baltimore'). Nature 208:143, 1965
    • (1965) Nature , vol.208 , pp. 143
    • Beck, E.A.1    Charache, P.2    Jackson, D.P.3
  • 135
    • 0014576618 scopus 로고
    • Chromatographic, ultracentrifugal, and related studies of fibrinogen "Baltimore"
    • Mosesson MW, Beck EA: Chromatographic, ultracentrifugal, and related studies of fibrinogen "Baltimore." J Clin Invest 48:1656, 1969
    • (1969) J Clin Invest , vol.48 , pp. 1656
    • Mosesson, M.W.1    Beck, E.A.2
  • 136
    • 0015123423 scopus 로고
    • Functional evaluation of an inherited abnormal fibrinogen: Fibrinogen "Baltimore."
    • Beck EA, Shainoff JR, Vogel A, Jackson DP: Functional evaluation of an inherited abnormal fibrinogen: Fibrinogen "Baltimore." J Clin Invest 50:1874, 1971
    • (1971) J Clin Invest , vol.50 , pp. 1874
    • Beck, E.A.1    Shainoff, J.R.2    Vogel, A.3    Jackson, D.P.4
  • 137
    • 0016582508 scopus 로고
    • Defective ex-polymerization in the conversion of fibrinogen Baltimore to fibrin
    • Brown CH, Crowe MF: Defective ex-polymerization in the conversion of fibrinogen Baltimore to fibrin. J Clin Invest 55:1190, 1975
    • (1975) J Clin Invest , vol.55 , pp. 1190
    • Brown, C.H.1    Crowe, M.F.2
  • 138
    • 0025220990 scopus 로고
    • Fibrinogen Baltimore I: Polymerization defect associated with a γ292Gly → Val (GGC→GTC) mutation
    • Bantia S, Mane SM, Bell WR, Dang CV: Fibrinogen Baltimore I: Polymerization defect associated with a γ292Gly → Val (GGC→GTC) mutation. Blood 76:2279, 1990
    • (1990) Blood , vol.76 , pp. 2279
    • Bantia, S.1    Mane, S.M.2    Bell, W.R.3    Dang, C.V.4
  • 140
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics of proteins in solution
    • Wesson L, Eisenberg D: Atomic solvation parameters applied to molecular dynamics of proteins in solution. Protein Sci 1:227, 1992
    • (1992) Protein Sci , vol.1 , pp. 227
    • Wesson, L.1    Eisenberg, D.2
  • 141
    • 0023686606 scopus 로고
    • Fibrinogen Baltimore III: Congenital dysfibrinogenemia with a shortened γ-subunit
    • Ebert RF, Bell WR: Fibrinogen Baltimore III: Congenital dysfibrinogenemia with a shortened γ-subunit. Thromb Res 51:251, 1988
    • (1988) Thromb Res , vol.51 , pp. 251
    • Ebert, R.F.1    Bell, W.R.2
  • 142
    • 0025239558 scopus 로고
    • Polymerization defect of fibrinogen Baltimore III due to a γ Asn308 → Ile mutation
    • Bantia S, Bell WR, Dang CV: Polymerization defect of fibrinogen Baltimore III due to a γ Asn308 → Ile mutation. Blood 75:1659, 1990
    • (1990) Blood , vol.75 , pp. 1659
    • Bantia, S.1    Bell, W.R.2    Dang, C.V.3
  • 143
    • 0022515261 scopus 로고
    • A lower molecular weight γ-chain variant in a congenital abnormal fibrinogen (Kyoto)
    • Yoshida N, Okuma M, Moroi M, Matsuda M: A lower molecular weight γ-chain variant in a congenital abnormal fibrinogen (Kyoto). Blood 68:703, 1986
    • (1986) Blood , vol.68 , pp. 703
    • Yoshida, N.1    Okuma, M.2    Moroi, M.3    Matsuda, M.4
  • 144
    • 0023731893 scopus 로고
    • Characterization of an apparently lower molecular weight γ-chain variant in fibrinogen Kyoto I. the replacement of γ-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site
    • Yoshida N, Terukina S, Okuma M, Moroi M, Aoki N, Matsuda M: Characterization of an apparently lower molecular weight γ-chain variant in fibrinogen Kyoto I. The replacement of γ-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site. J Biol Chem 263:13848, 1988
    • (1988) J Biol Chem , vol.263 , pp. 13848
    • Yoshida, N.1    Terukina, S.2    Okuma, M.3    Moroi, M.4    Aoki, N.5    Matsuda, M.6
  • 147
    • 0024559787 scopus 로고
    • A γ methionine-310 to threonine substitution and consequent N-glycosylation at γ asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi
    • Yamazumi K, Shimura K, Terukina S, Takahashi N, Matsuda M: A γ methionine-310 to threonine substitution and consequent N-glycosylation at γ asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi. J Clin Invest 83:1590, 1989
    • (1989) J Clin Invest , vol.83 , pp. 1590
    • Yamazumi, K.1    Shimura, K.2    Terukina, S.3    Takahashi, N.4    Matsuda, M.5
  • 148
    • 0025495682 scopus 로고
    • Delayed intermolecular γ-chain cross-linking by factor XHIa in fibrinogen Asahi characterized by a γ-Met-310 to Thr substitution with an N-glycosylated γ-Asn-308
    • Yamazumi K, Shimura K, Maekawa H, Muramatsu S, Terukina S, Matsuda M: Delayed intermolecular γ-chain cross-linking by factor XHIa in fibrinogen Asahi characterized by a γ-Met-310 to Thr substitution with an N-glycosylated γ-Asn-308. Blood Coagul Fibrinol 1:557, 1990
    • (1990) Blood Coagul Fibrinol , vol.1 , pp. 557
    • Yamazumi, K.1    Shimura, K.2    Maekawa, H.3    Muramatsu, S.4    Terukina, S.5    Matsuda, M.6
  • 149
    • 0024443424 scopus 로고
    • Fibrinogen sialic acid residues are low affinity calcium-binding sites that influence fibrin assembly
    • Dang CV, Shin CK, Bell WR, Nagaswami C, Weisel JW: Fibrinogen sialic acid residues are low affinity calcium-binding sites that influence fibrin assembly. J Biol Chem 264:15104, 1989
    • (1989) J Biol Chem , vol.264 , pp. 15104
    • Dang, C.V.1    Shin, C.K.2    Bell, W.R.3    Nagaswami, C.4    Weisel, J.W.5
  • 150
    • 0017400243 scopus 로고
    • Functional and metabolic properties of human asialofibrinogen
    • Martinez J, Palascak J, Peters C: Functional and metabolic properties of human asialofibrinogen. J Lab Clin Med 89:367, 1977
    • (1977) J Lab Clin Med , vol.89 , pp. 367
    • Martinez, J.1    Palascak, J.2    Peters, C.3
  • 151
    • 0023752048 scopus 로고
    • Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers
    • Langer BG, Weisel JW, Dinauer PA, Nagaswami C, Bell WR: Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers. J Biol Chem 263:15056, 1988
    • (1988) J Biol Chem , vol.263 , pp. 15056
    • Langer, B.G.1    Weisel, J.W.2    Dinauer, P.A.3    Nagaswami, C.4    Bell, W.R.5
  • 152
    • 11944269286 scopus 로고
    • Fibrinogen Lima: A homozygous dysfibrinogen with an Aα-arginine-141 to serine substitution associated with extra N-glycosylation at Aα-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator
    • Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, Arocha-Pinango CL, Rodriguez S, Nagy H, Perez-Requejo JL, Matsuda M: Fibrinogen Lima: A homozygous dysfibrinogen with an Aα-arginine-141 to serine substitution associated with extra N-glycosylation at Aα-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator. J Clin Invest 90:67, 1992
    • (1992) J Clin Invest , vol.90 , pp. 67
    • Maekawa, H.1    Yamazumi, K.2    Muramatsu, S.3    Kaneko, M.4    Hirata, H.5    Takahashi, N.6    Arocha-Pinango, C.L.7    Rodriguez, S.8    Nagy, H.9    Perez-Requejo, J.L.10    Matsuda, M.11
  • 153
    • 0025816449 scopus 로고
    • A congenially abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain gene, causing defective calcium binding and impaired fibrin polymerization
    • Koopman J, Haverkate F, Briët E, Lord ST: A congenially abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain gene, causing defective calcium binding and impaired fibrin polymerization. J Biol Chem 266:13456, 1991
    • (1991) J Biol Chem , vol.266 , pp. 13456
    • Koopman, J.1    Haverkate, F.2    Briët, E.3    Lord, S.T.4
  • 155
    • 0020261202 scopus 로고
    • Comparative studies on the structures of the carbohydrate moieties of human fibrinogen and abnormal fibrinogen Nagoya
    • Mizuochi T, Taniguchi T, Asami Y, Takamatsu J, Okude M, Iwanaga S, Kobata A: Comparative studies on the structures of the carbohydrate moieties of human fibrinogen and abnormal fibrinogen Nagoya. J Biochem Tokyo 92:283, 1982
    • (1982) J Biochem Tokyo , vol.92 , pp. 283
    • Mizuochi, T.1    Taniguchi, T.2    Asami, Y.3    Takamatsu, J.4    Okude, M.5    Iwanaga, S.6    Kobata, A.7
  • 156
    • 0024495774 scopus 로고
    • Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the γ-chain that impairs the polymerization of fibrin monomer
    • Miyata T, Furukawa K, Iwanaga S, Takamatsu J, Saito H: Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the γ-chain that impairs the polymerization of fibrin monomer. J Biochem Tokyo 105:10, 1989
    • (1989) J Biochem Tokyo , vol.105 , pp. 10
    • Miyata, T.1    Furukawa, K.2    Iwanaga, S.3    Takamatsu, J.4    Saito, H.5
  • 157
    • 0022481417 scopus 로고
    • Characterization of fibrinogen Milano I: Amino acid exchange γ330 Asp → Val impairs fibrin polymerization
    • Reber P, Furlan M, Rupp C, Kehl M, Henschen A, Mannucci PM, Beck EA: Characterization of fibrinogen Milano I: Amino acid exchange γ330 Asp → Val impairs fibrin polymerization. Blood 67:1751, 1986
    • (1986) Blood , vol.67 , pp. 1751
    • Reber, P.1    Furlan, M.2    Rupp, C.3    Kehl, M.4    Henschen, A.5    Mannucci, P.M.6    Beck, E.A.7
  • 158
    • 0024331906 scopus 로고
    • Fibrinogen Kyoto III: A congenital dysfibrinogen with a γ aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization
    • Terukina S, Yamazumi K, Okamoto K, Yamashita H, Ito Y, Matsuda M: Fibrinogen Kyoto III: A congenital dysfibrinogen with a γ aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization. Blood 74:2681, 1989
    • (1989) Blood , vol.74 , pp. 2681
    • Terukina, S.1    Yamazumi, K.2    Okamoto, K.3    Yamashita, H.4    Ito, Y.5    Matsuda, M.6
  • 159
    • 0019517552 scopus 로고
    • Fibrinogen Bern I and fibrinogen Bern II: 2 hereditary fibrinogen variants with diverse biochemical properties
    • Rupp C, Kuyas C, Haeberli A, Furlan M, von Fliedner V, Beck EA: Fibrinogen Bern I and fibrinogen Bern II: 2 hereditary fibrinogen variants with diverse biochemical properties. Schweiz Med Wochenschr 111:1543, 1981
    • (1981) Schweiz Med Wochenschr , vol.111 , pp. 1543
    • Rupp, C.1    Kuyas, C.2    Haeberli, A.3    Furlan, M.4    Von Fliedner, V.5    Beck, E.A.6
  • 160
    • 0027482187 scopus 로고
    • Fibrinogen Bern I: Substitution γ 337 Asn → Lys is responsible for defective fibrin monomer polymerization
    • Steinmann C, Reber P, Jungo M, Lammle B, Heinemann G, Wermuth B, Furlan M: Fibrinogen Bern I: Substitution γ 337 Asn → Lys is responsible for defective fibrin monomer polymerization. Blood 82:2104, 1993
    • (1993) Blood , vol.82 , pp. 2104
    • Steinmann, C.1    Reber, P.2    Jungo, M.3    Lammle, B.4    Heinemann, G.5    Wermuth, B.6    Furlan, M.7
  • 161
    • 0000504784 scopus 로고
    • Constitutional and familial abnormal fibrinogen
    • suppl
    • Ménaché D: Constitutional and familial abnormal fibrinogen. Thromb Diath Haemorrh 13:173, 1964 (suppl)
    • (1964) Thromb Diath Haemorrh , vol.13 , pp. 173
    • Ménaché, D.1
  • 162
    • 0016346220 scopus 로고
    • Defect in the gamma polypeptide chain of a congenital abnormal fibrinogen
    • Budzynski AZ, Marder VJ, Ménaché D, Guillin M-C: Defect in the gamma polypeptide chain of a congenital abnormal fibrinogen. Nature 252:66, 1974
    • (1974) Nature , vol.252 , pp. 66
    • Budzynski, A.Z.1    Marder, V.J.2    Ménaché, D.3    Guillin, M.-C.4
  • 163
    • 0017260825 scopus 로고
    • Studies on the structural abnormality of fibrinogen Paris I
    • Mosesson MW, Amrani DL, Ménaché D: Studies on the structural abnormality of fibrinogen Paris I. J Clin Invest 57:782, 1976
    • (1976) J Clin Invest , vol.57 , pp. 782
    • Mosesson, M.W.1    Amrani, D.L.2    Ménaché, D.3
  • 165
    • 0023201012 scopus 로고
    • ADP-induced platelet aggregation depends on the conformation or availability of the terminal gamma chain sequence of fibrinogen. Study of the reactivity of fibrinogen Paris 1
    • Denninger M-H, Jandrot-Perrus M, Elion J, Bertrand O, Homandberg GA, Mosesson MW, Guillin M-C: ADP-induced platelet aggregation depends on the conformation or availability of the terminal gamma chain sequence of fibrinogen. Study of the reactivity of fibrinogen Paris 1. Blood 70:558, 1987
    • (1987) Blood , vol.70 , pp. 558
    • Denninger, M.-H.1    Jandrot-Perrus, M.2    Elion, J.3    Bertrand, O.4    Homandberg, G.A.5    Mosesson, M.W.6    Guillin, M.-C.7
  • 166
    • 0027461540 scopus 로고
    • Paris I dysfibrinogenemia: A point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen γ-chain
    • Rosenberg JB, Newman PJ, Mosesson MW, Guillin M-C, Amrani DL: Paris I dysfibrinogenemia: A point mutation in intron 8 results in insertion of a 15 amino acid sequence in the fibrinogen γ-chain. Thromb Haemost 69:217, 1993
    • (1993) Thromb Haemost , vol.69 , pp. 217
    • Rosenberg, J.B.1    Newman, P.J.2    Mosesson, M.W.3    Guillin, M.-C.4    Amrani, D.L.5
  • 168
    • 0029857493 scopus 로고    scopus 로고
    • Fibrinogen Matsumoto I: A γ364 Asp → His (GAT → CAT) substitution associated with defective fibrin polymerization
    • Okumura N, Furihata K, Terasawa F, Nakagoshi R, Ueno I, Katsuyama T: Fibrinogen Matsumoto I: A γ364 Asp → His (GAT → CAT) substitution associated with defective fibrin polymerization. Thromb Haemost 75:887, 1996
    • (1996) Thromb Haemost , vol.75 , pp. 887
    • Okumura, N.1    Furihata, K.2    Terasawa, F.3    Nakagoshi, R.4    Ueno, I.5    Katsuyama, T.6
  • 169
    • 0029461283 scopus 로고
    • Association of dysfibrinogenemia and thrombosis. Apropos of a family (Fibrinogen Melun) and review of the literature
    • Bentolila S, Samama MM, Conard J, Horellou MH, Ffrench P: Association of dysfibrinogenemia and thrombosis. Apropos of a family (Fibrinogen Melun) and review of the literature. Ann Med Interne Paris 146:575, 1995
    • (1995) Ann Med Interne Paris , vol.146 , pp. 575
    • Bentolila, S.1    Samama, M.M.2    Conard, J.3    Horellou, M.H.4    Ffrench, P.5
  • 170
    • 0030725658 scopus 로고    scopus 로고
    • Severely impaired polymerization of recombinant fibrinogen γ364 Asp → His, the substitution discovered in a heterozygous individual
    • Okumura N, Gorkun OV, Lord ST: Severely impaired polymerization of recombinant fibrinogen γ364 Asp → His, the substitution discovered in a heterozygous individual. J Biol Chem 272:29596, 1997
    • (1997) J Biol Chem , vol.272 , pp. 29596
    • Okumura, N.1    Gorkun, O.V.2    Lord, S.T.3
  • 171
    • 0027024701 scopus 로고
    • The synthetic peptide Gly-Pro-Arg-Pro-amide limits the plasmic digestion of fibrinogen in the same fashion as calcium ion
    • Yamazumi K, Doolittle RF: The synthetic peptide Gly-Pro-Arg-Pro-amide limits the plasmic digestion of fibrinogen in the same fashion as calcium ion. Protein Sci 1:1719, 1992
    • (1992) Protein Sci , vol.1 , pp. 1719
    • Yamazumi, K.1    Doolittle, R.F.2
  • 172
    • 0021806417 scopus 로고
    • Protective effect of divalent cations in the plasmin degradation of fibrinogen
    • Dang CV, Bell WR, Ebert RF, Starksen NF: Protective effect of divalent cations in the plasmin degradation of fibrinogen. Arch Biochem Biophys 238:452, 1985
    • (1985) Arch Biochem Biophys , vol.238 , pp. 452
    • Dang, C.V.1    Bell, W.R.2    Ebert, R.F.3    Starksen, N.F.4
  • 173
    • 0026802038 scopus 로고
    • Characterization of an abnormal fibrinogen Osaka V with the replacement of γ-arginine 375 by glycine. the lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis
    • Yoshida N, Hirata H, Morigami Y, Imaoka S, Matsuda M, Yamazumi K, Asakura S: Characterization of an abnormal fibrinogen Osaka V with the replacement of γ-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis. J Biol Chem 267:2753, 1992
    • (1992) J Biol Chem , vol.267 , pp. 2753
    • Yoshida, N.1    Hirata, H.2    Morigami, Y.3    Imaoka, S.4    Matsuda, M.5    Yamazumi, K.6    Asakura, S.7
  • 174
    • 0017834156 scopus 로고
    • Stabilization of the plasmin digestion products of fibrinogen and fibrin by calcium ions
    • Purves LR, Lindsey GG, Brown G, Franks J: Stabilization of the plasmin digestion products of fibrinogen and fibrin by calcium ions. Thromb Res 12:473, 1978
    • (1978) Thromb Res , vol.12 , pp. 473
    • Purves, L.R.1    Lindsey, G.G.2    Brown, G.3    Franks, J.4
  • 175
    • 0018341686 scopus 로고
    • Calcium-binding properties of human fibrin(ogen) and degradation products
    • Nieuwenhuizen W, Vermond A, Nooijen WJ, Haverkate F: Calcium-binding properties of human fibrin(ogen) and degradation products. FEBS Lett 98:257, 1979
    • (1979) FEBS Lett , vol.98 , pp. 257
    • Nieuwenhuizen, W.1    Vermond, A.2    Nooijen, W.J.3    Haverkate, F.4
  • 176
    • 0020050917 scopus 로고
    • Potential role of the Aα chain in the binding of calcium to human fibrinogen
    • Marguerie G, Ardaillou N: Potential role of the Aα chain in the binding of calcium to human fibrinogen. Biochim Biophys Acta 701:410, 1982
    • (1982) Biochim Biophys Acta , vol.701 , pp. 410
    • Marguerie, G.1    Ardaillou, N.2
  • 178
    • 0030723472 scopus 로고    scopus 로고
    • Fibrinogen Kai sers lautern (γ380 Lys to Asn): A new glycosylated fibrinogen variant with delayed polymerization
    • Ridgway HJ, Brennan SO, Loreth RM, George PM: Fibrinogen Kai sers lautern (γ380 Lys to Asn): A new glycosylated fibrinogen variant with delayed polymerization. Br J Haematol 99:562, 1997
    • (1997) Br J Haematol , vol.99 , pp. 562
    • Ridgway, H.J.1    Brennan, S.O.2    Loreth, R.M.3    George, P.M.4
  • 179
    • 0018126726 scopus 로고
    • Calcium binding to human fibrinogen - Localization of two calcium specific sites
    • Lindsey GG, Brown G, Purves LR: Calcium binding to human fibrinogen - Localization of two calcium specific sites. Thromb Res 13:345, 1978
    • (1978) Thromb Res , vol.13 , pp. 345
    • Lindsey, G.G.1    Brown, G.2    Purves, L.R.3
  • 180
    • 0015304822 scopus 로고
    • Acceleration of fibrin polymerization by calcium ions
    • Boyer MH, Shainoff JR, Ratnoff OD: Acceleration of fibrin polymerization by calcium ions. Blood 39:382, 1972
    • (1972) Blood , vol.39 , pp. 382
    • Boyer, M.H.1    Shainoff, J.R.2    Ratnoff, O.D.3
  • 181
    • 0018886368 scopus 로고
    • Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences
    • Laudano AP, Doolittle RF: Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences. Biochemistry 19:1013, 1980
    • (1980) Biochemistry , vol.19 , pp. 1013
    • Laudano, A.P.1    Doolittle, R.F.2
  • 182
    • 0019870106 scopus 로고
    • Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen
    • Laudano AP, Doolittle RF: Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen. Science 212:457, 1981
    • (1981) Science , vol.212 , pp. 457
    • Laudano, A.P.1    Doolittle, R.F.2
  • 185
    • 3543101090 scopus 로고
    • The structure of the human fibrin gamma-chain crosslink
    • Mosesson MW, Amrani DL, Siebenlist KR, DiOrio JP (eds). Amsterdam, The Netherlands, Elsevier Science
    • Purves L, Purves M: The structure of the human fibrin gamma-chain crosslink, in Mosesson MW, Amrani DL, Siebenlist KR, DiOrio JP (eds): Fibrinogen 3. Biochemistry, Biological Functions, Gene Regulation and Expression. Amsterdam, The Netherlands, Elsevier Science, 1988, p 95
    • (1988) Fibrinogen 3. Biochemistry, Biological Functions, Gene Regulation and Expression , pp. 95
    • Purves, L.1    Purves, M.2
  • 186
    • 0020426405 scopus 로고
    • Localization of a site interacting with human platelet receptor on carboxy-terminal segment of human fibrinogen γ chain
    • Kloczewiak M, Timmons S, Hawiger J: Localization of a site interacting with human platelet receptor on carboxy-terminal segment of human fibrinogen γ chain. Biochem Biophys Res Commun 107:181, 1982
    • (1982) Biochem Biophys Res Commun , vol.107 , pp. 181
    • Kloczewiak, M.1    Timmons, S.2    Hawiger, J.3
  • 188
    • 0026728176 scopus 로고
    • Examination of the platelet membrane glycoprotein IIb-IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy
    • Weisel JW, Nagaswami C, Vilaire G, Bennett JS: Examination of the platelet membrane glycoprotein IIb-IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy. J Biol Chem 267:16637, 1992
    • (1992) J Biol Chem , vol.267 , pp. 16637
    • Weisel, J.W.1    Nagaswami, C.2    Vilaire, G.3    Bennett, J.S.4
  • 189
  • 190
    • 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, 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 82:2462, 1993
    • (1993) Blood , vol.82 , pp. 2462
    • Collet, J.-P.1    Soria, J.2    Mirshahi, M.3    Hirsch, M.4    Dagonnet, F.B.5    Caen, J.6    Soria, C.7
  • 191
    • 0021341834 scopus 로고
    • Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation
    • Lijnen HR, Soria J, Soria C, Collen D, Caen JP: Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation. Thromb Haemost 51:108, 1984
    • (1984) Thromb Haemost , vol.51 , pp. 108
    • Lijnen, H.R.1    Soria, J.2    Soria, C.3    Collen, D.4    Caen, J.P.5
  • 193
    • 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 267:24259, 1992
    • (1992) J Biol Chem , vol.267 , pp. 24259
    • Gabriel, D.A.1    Muga, K.2    Boothroyd, E.M.3
  • 196
    • 0028787376 scopus 로고
    • Dysfibrinogenemia: A case with thrombosis (fibrinogen Richfield) and an overview of the clinical and laboratory spectrum
    • Schorer AE, Singh J, Basara ML: Dysfibrinogenemia: A case with thrombosis (fibrinogen Richfield) and an overview of the clinical and laboratory spectrum. Am J Hematol 50:200, 1995
    • (1995) Am J Hematol , vol.50 , pp. 200
    • Schorer, A.E.1    Singh, J.2    Basara, M.L.3
  • 199
    • 0023932353 scopus 로고
    • Thrombin-induced fibrinopeptide B release from normal and variant fibrinogens: Influence of inhibitors of fibrin polymerization
    • Ruf W, Bender A, Lane DA, Preissner KT, Selmayr E, Müller-Bergbaus G: Thrombin-induced fibrinopeptide B release from normal and variant fibrinogens: Influence of inhibitors of fibrin polymerization. Biochim Biophys Acta 965:169, 1988
    • (1988) Biochim Biophys Acta , vol.965 , pp. 169
    • Ruf, W.1    Bender, A.2    Lane, D.A.3    Preissner, K.T.4    Selmayr, E.5    Müller-Bergbaus, G.6
  • 200
    • 0029808926 scopus 로고    scopus 로고
    • Normal binding of calcium to five fibrinogen variants with mutations in the carboxy terminal part of the γ-chain
    • Furlan M, Stucki B, Steinmann C, Jungo M, Lämmle B: Normal binding of calcium to five fibrinogen variants with mutations in the carboxy terminal part of the γ-chain. Thromb Haemost 76:377, 1996
    • (1996) Thromb Haemost , vol.76 , pp. 377
    • Furlan, M.1    Stucki, B.2    Steinmann, C.3    Jungo, M.4    Lämmle, B.5


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