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Referencias:

• Mosesson, M.W., Fibrinogen and fibrin polymerization and functions (1999) Blood Coagul Fibrinolysis, 10 (SUPPL. 1), pp. S45-S48
• Erickson, H.P., Fowler, W.E., Electron microscopy of fibrinogen, its plasmic fragments and polymers (1983) Ann N Y Acad Sci, 408, pp. 146-163
• Weisel, J.W., Stauffacher, C.V., Bullitt, E., Cohen, C., A model for fibrinogen: Domains and sequence (1985) Science, 230, pp. 1388-1391
• Fu, Y., Grieninger, G., Fib420: A normal human variant of fibrinogen with two extended chains (1994) Proc Natl Acad Sci USA, 91, p. 2625
• Nieuwenhuizen, W., Biochemistry and measurement of fibrinogen (1995) Eur Heart J, 16, pp. 6-10
• Spraggon, G., Applegate, D., Everse, S.J., Zhang, J.Z., Verapandian, L., Redman, C., Crystal structure of a recombinant alphaEC domain from human fibrinogen-420 (1998) Proc Natl Acad Sci USA, 95 (16), pp. 9099-9104
• Mosesson, M.W., Fibrinogen gamma chain functions (2003) J Thromb Haemost, 1 (2), pp. 231-238
• Wolfenstein-Todel, C., Mosesson, M.W., Human plasma fibrinogen heterogeneity: Evidence for an extended carboxil-terminal sequence in a normal gamma chain variant (γ′) (1980) Proc Natl Acad Sci USA, 77, pp. 5069-5073
• Siebenlist, K.R., Meh, D.A., Mosesson, M.W., Plasma factor XIII binds specifically to fibrinogen molecules containing γ′ chain (1996) Biochemistry, 35, pp. 10448-10453
• Mosesson, M.W., Siebenlist, K.R., Hernandez, I., Wall, J.S., Hainfeld, J.F., Fibrinogen assembly and crosslinking on a fibrin fragment E template (2002) Thromb Haemost, 87 (4), pp. 651-658
• Mosesson, M.W., Fibrinogen and fibrin structure and functions (2005) J Thromb Haemost, 3 (8), pp. 1894-1904
• Kaminski, M., Siebenlist, K.R., Mosesson, M.W., Evidence for thrombin enhancement of fibrin polymerization that is independent of its catalytic activity (1991) J Lab Clin Med, 117, pp. 218-225
• Lorand, L., Factor XIII: Structure, activation and interaction with fibrinogen and fibrin (2001) Ann NY Acad Sci, 936, pp. 291-311
• Tsurupa, G., Medved, L., Identification and characterization of novel t-PA and plasminogen-binding sites within fibrin(ogen) alpha C-domains (2001) Biochemistry, 40, pp. 801-808
• Farrell, D.H., Thiagarajan, P., Chung, D.W., Davie, E.W., Role of fibrinogen alpha and gamma chain sites in platelet aggregation (1992) Proc Natl Acad Sci USA, 89, pp. 10729-10732
• Dejana, E., Zanetti, A., Conforti, L.G., Biochemical and functional characteristics of fibrinogen interaction with endothelial cells (1988) Haemostasis, 18, pp. 262-270
• Pereira, M., Rybarczyk, B.J., Odrljin, T.M., Hocking, D.C., Sottile, J., Simpson-Haidaris, P.J., The incorporation of fibrinogen into extracellular matrix is dependent on active assembly of a fibronectin matrix (2002) J Cell Sci, 115 (PART 3), pp. 609-617
• Mosesson, M.W., Siebenlist, K.R., Meh, D.A., The structure and biological features of fibrinogen and fibrin (2001) Ann N Y Acad Sci, 936, pp. 11-30
• Weisel, J.W., Fibrinogen and fibrin (2005) Adv Protein Chem, 70, pp. 247-299
• Sahni, A., Khorana, A.A., Baggs, R.B., Peng, H., Francis, C.W., FGF-2 binding to fibrin(ogen) is required for augmented angiogenesis (2006) Blood, 107 (1), pp. 126-131
• Shiose, S., Hata, Y., Noda, Y., Sassa, Y., Takeda, A., Yoshikawa, H., Fibrinogen stimulates in vitro angiogenesis by choroidal endothelial cells via autocrine VEGF (2004) Graefes Arch Clin Exp Ophthalmol, 242 (9), pp. 777-783
• Sahni, A., Sahni, S.K., Francis, C.W., Endothelial cell activation by IL-1beta in the presence of fibrinogen requires alphavbeta3 (2005) Arterioscler Thromb Vasc Biol, 25 (10), pp. 2222-2227
• Medved, L., Nieuwenhuizen, W., Molecular mechanisms of initiation of fibrinolysis by fibrin (2003) Thromb Haemost, 89, pp. 409-419
• Hettasch JM, Greenberg CS. Fibrin formation and stabilization. In: Thrombosis and Hemorrhage. 2° ed. Baltimore (Maryland, EUA): Lozcalzo J and Schafer AI Eds.; 1998. p. 129-154; Gorkun, O.V., Veklich, Y.I., Medved, L.V., Henschen, A.H., Weisel, J.W., Role of the αC domains of fibrin in clot formation (1994) Biochemistry, 33, pp. 6986-6997
• Siebenlist, K.R., Meh, D.A., Mosesson, M.W., Protransglutaminase (Factor XIII) mediated cross-linking of fibrinogen and fibrin (2001) Thromb Haemost, 86, pp. 1221-1228
• Blombäck, B., Carlsson, K., Hessel, B., Liljeborg, A., Procyc, R., Aslund, N., Native fibrin gel networks observed by 3 D microscopy, permeation and turbidity (1989) Biochim Biophys Acta, 997, pp. 96-110
• Lauricella, A.M., Quintana, I., Kordich, L., Effect of homocysteine thiol group on fibrin networks: Another possible mechanism of harm (2002) Thromb Res, 107, pp. 75-79
• Collet, J.P., Park, D., Lesty, C., Soria, J., Soria, C., Montalescot, G., Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed. Dynamic and structural approaches by confocal microscopy (2000) Arterioscler Thromb Vasc Biol, 20, pp. 1354-1361
• Weisel, J., Veklich, Y., Collet, J., Francis, C., Structural studies of fibrinolysis by electron and light microscopy (1999) Thromb Haemost, 82 (2), pp. 277-282
• Lukacova, D., Matsueda, G.R., Haber, E., Reed, G.L., Inhibition of factor XIII activation by an anti-peptide monoclonal antibody (1991) Biochemistry, 30 (42), pp. 10164-10170
• Mosesson, M.W., Hernandez, I., Siebenlist, K.R., Evidence that catalytically-inactivated thrombin forms non-covalently linked dimers that bridge between fibrin/fibrinogen fibers and enhance fibrin polymerization (2004) Biophys Chem, 110 (1-2), pp. 93-100
• Scheiner, T., Jirouskova, M., Nagaswami, C., Coller, B.S., Weisel, J.W., A monoclonal antibody to the fibrinogen gamma-chain alters fibrin clot structure and its properties by producing short, thin fibers arranged in bundles (2003) J Thromb Haemost, 1 (12), pp. 2594-2602
• Lee, K.N., Jackson, K.W., Christiansen, V.J., Chung, K.H., McKee, P.A., A novel plasma proteinase α2-antiplasmin inhibition of fibrin digestion (2004) Blood, 103 (10), pp. 3783-3788
• Vaziri, N.D., Kennedy, S.C., Kennedy, M., Gonzalez, E., Coagulation, fibrinolytic, and inhibitory proteins in acute myocardial infarction and angina pectoris (1994) Am J Med, 96 (6), p. 571
• Kaijzel, E.L., Koolwijk, P., van Erck, M.G., van Hinsbergh, V.W., de Maat, M.P., Molecular weight fibrinogen variants determine angiogenesis rate in a fibrin matrix in vitro and in vivo (2006) J Thromb Haemost, 4 (9), pp. 1975-1981
• Siebenlist, K.R., Mosesson, M.W., Hernandez, I., Bush, L.A., Di Cera, E., Shainoff, J.R., Studies on the basis for the properties of fibrin produced from fibrinogen-containing gamma' chains (2005) Blood, 106 (8), pp. 2730-2736
• Hamano, A., Mimuro, J., Aoshima, M., Itoh, T., Kitamura, N., Nishinarita, S., Thrombophilic dysfibrinogen Tokyo V with the amino acid substitution of gammaAla327Thr: Formation of fragile but fibrinolysis-resistant fibrin clots and its relevance to arterial thromboembolism (2004) Blood, 103 (8), pp. 3045-3050
• Marchi, R., Carvajal, Z., Meyer, M., Soria, J., Ruiz-Saez, A., Arocha-Pinango, C.L., Fibrinogen Guarenas, an abnormal fibrinogen with an Aalpha-chain truncation due to a nonsense mutation at Aalpha 467 Glu (GAA) - >stop (TAA) (2006) Thromb Res, 118 (5), pp. 637-650
• Hessel B, Silveira AM, Carlsson K, Oksa H, Rasi V, Vahtera E. Fibrinogenemia Tampere. A dysfibrinogenemia with defective gelation and thromboembolic disease. Thromb Res 1995; 78 (4): 323-39; Sugo, T., Endo, H., Matsuda, M., Ohmori, T., Madoiwa, S., Mimuro, J., A classification of the fibrin network structures formed from the hereditary dysfibrinogens (2006) J Thromb Haemost, 4 (8), pp. 1738-1746
• Blombäck, B., Banerjee, D., Carlsson, K., Hamsten, A., Hessel, B., Procyk, R., Silveira, A., Native fibrin gel networks and factors influencing their formation in health and disease (1990) Adv Exp Med Biol, 281, pp. 1-23
• Okada, M., Blombäck, B., Calcium and fibrin gel structure (1983) Thromb Res, 29, pp. 69-280
• Marx, G., Divalent cations induce protofibril gelation (1988) Am J Hemat, 27, pp. 104-109
• Kostelansky, M.S., Betts, L., Gorkun, O.V., Lord, S.T., 2.8 A crystal structures of recombinant fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site (2002) Biochemistry, 41, pp. 12124-12132
• Dang, C.V., Shin, C.K., Bell, W.R., Nagaswami, C., Weisel, J.W., Fibrinogen sialic acid residues are low affinity calcium binding sites that influence fibrin assembly (1989) J Biol Chem, 264 (25), pp. 15104-15108
• Hardy, J.J., Carrell, N.A., McDonagh, J., Calcium ion functions in fibrinogen conversion to fibrin (1983) Ann N Y Acad Sci, 408, pp. 279-287
• Blomback, B., Carlsson, K., Fatah, K., Hessel, B., Procyk, R., Fibrin in human plasma: Gel architecture governed by rate and nature of fibrinogen activation (1994) Thromb Res, 75, pp. 521-538
• Ryan, E.A., Mochros, L.F., Weisel, J.W., Lorand, L., Structural origin of fibrin clot rheology (1999) Biophys J, 77, pp. 2813-2826
• Nair, C.H., Azhar, A., Wilson, J.D., Dhall, D.P., Studies of fibrin network structure in human plasma. Part II. Clinical application: Diabetic and antidiabetic drug (1991) Thromb Res, 64, pp. 477-485
• Jörneskog, G., Egberg, N., Fagrell, B., Fatah, K., Hessel, B., Johnsson, H., Altered properties of the fibrin gel structure in patients with IDDM (1996) Diabetología, 39, pp. 1519-1523
• Martínez, J., MacDonald, K.A., Palascak, J.E., The role of sialic acid in the dysfibrinogenemia associated with leaver disease: Distribution of sialic acid on the constituent chains (1983) Blood, 61, pp. 1196-1202
• Yoshida, Y., Shiiki, H., Iwano, M., Uyama, H., Hamano, K., Nishino, T., Enhanced expression of plasminogen activator inhibitor 1 in patients with nephrotic syndrome (2001) Nephron, 88 (1), pp. 24-29
• Weisel, J., Veklich, Y., Collet, J., Francis, C., Structural studies of fibrinolysis by electron and light microscopy (1999) Thromb Haemost, 82 (2), pp. 277-282
• Collet, J.P., Park, D., Lesty, C., Soria, J., Soria, C., Montalescot, G., Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed. Dynamic and structural approaches by confocal microscopy (2000) Arterioscler Thromb Vasc Biol, 20, pp. 1354-1361
• Kolev, K., Machovich, R., Molecular and cellular modulation of fibrinolysis (2003) Thromb Haemost, 89, pp. 610-621
• Gabriel, D.A., Muga, K., Boothroyd, E.M., The effect of fibrin structure in fibrinolysis (1992) J Biol Chem, 267, pp. 24259-24263
• Sabovic, M., Blinc, A., Biochemical and biophysical conditions for blood clot lysis (2000) Eur J Physiol, 440 (SUPPL.), pp. R134-R136
• Wu, J.H., Siddiqui, K., Diamond, S., Transport phenomena and clot dissolving therapy: An experimental investigation of diffusion-controlled and permeation-enhanced fibrinolysis (1994) Thromb Haemost, 72 (1), pp. 105-112
• Mills, J.D., Ariens, R.A., Mansfield, M.W., Grant, P.J., Altered fibrin clot structure in the healthy relatives of patients with premature coronary artery disease (2002) Circulation, 106 (15), pp. 1938-1942
• Fatah, K., Silveira, A., Tornvall, P., Karpe, F., Blomback, M., Hamsten, A., Proneness to formation of tight and rigid fibrin gel structures in men with myocardial infarction at a young age (1996) Thromb Haemost, 76 (4), pp. 535-540
• Lim BC, Ariens RA, Carter AM, Weisel JW, Grant PJ. Genetic regulation of fibrin structure and function: complex gene-environment interactions may modulate vascular risk. Lancet 2003; 361 (9367): 1424-31. Erratum in: Lancet 2003; 361 (9376): 2250; Lauricella, A.M., Quintana, I.L., Sassetti, B., Castañón, M.M., Kordich, L.C., Influence of homocysteine on fibrin network lysis (2006) Blood Coagul Fibrinol, 17, pp. 181-186

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