메뉴 건너뛰기




Volumn 103, Issue 11, 2004, Pages 4157-4163

Substitution of the γ-chain Asn308 disturbs the D:D interface affecting fibrin polymerization, fibrinopeptide B release, and FXIIIa-catalyzed cross-linking

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARAGINE; BLOOD CLOTTING FACTOR 13A; CALCIUM; FIBRIN; FIBRINOGEN; FIBRINOPEPTIDE B; ISOLEUCINE; LYSINE; POLYMER; THROMBIN;

EID: 2542445312     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-12-4296     Document Type: Article
Times cited : (10)

References (51)
  • 1
    • 0030199185 scopus 로고    scopus 로고
    • Fibrinogen and fibrin-proteins with complex roles in hemostasis and thrombosis
    • Blomback B. Fibrinogen and fibrin-proteins with complex roles in hemostasis and thrombosis. Thromb Res. 1996;83:1-75.
    • (1996) Thromb Res , vol.83 , pp. 1-75
    • Blomback, B.1
  • 2
    • 0021118122 scopus 로고
    • Fibrinogen and fibrin
    • Doolittle RF. Fibrinogen and fibrin. Ann Rev Biochem. 1984;53:195-229.
    • (1984) Ann Rev Biochem , vol.53 , pp. 195-229
    • Doolittle, R.F.1
  • 3
    • 0027379584 scopus 로고
    • Carboxyl-terminal portions of the alpha 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 alpha chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated αC fragments on polymerization. J Biol Chem. 1993;268:13577-13585.
    • (1993) J Biol Chem , vol.268 , pp. 13577-13585
    • Veklich, Y.I.1    Gorkun, O.V.2    Medved, L.V.3    Nieuwenhuizen, W.4    Weisel, J.W.5
  • 4
    • 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, Cote 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 U S A. 1997;94:7176-7181.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7176-7181
    • Pratt, K.P.1    Cote, H.C.F.2    Chung, D.W.3    Stenkamp, R.E.4    Davie, E.W.5
  • 5
    • 0032537486 scopus 로고    scopus 로고
    • Crystal structure of fragment double-D from human fibrin with two different bound ligands
    • Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF. Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry. 1998;37:8637-8642.
    • (1998) Biochemistry , vol.37 , pp. 8637-8642
    • Everse, S.J.1    Spraggon, G.2    Veerapandian, L.3    Riley, M.4    Doolittle, R.F.5
  • 6
    • 0037044194 scopus 로고    scopus 로고
    • 2.8 Å crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site
    • Kostelansky MS, Betts L, Gorkun OV, Lord ST. 2.8 Å crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site. Biochemistry. 2002;41:12124-12132.
    • (2002) Biochemistry , vol.41 , pp. 12124-12132
    • Kostelansky, M.S.1    Betts, L.2    Gorkun, O.V.3    Lord, S.T.4
  • 7
    • 0015304822 scopus 로고
    • Acceleration of fibrin polymerization by calcium ions
    • Boyer MH, Shainoff JR, Ratnoff OD. Acceleration of fibrin polymerization by calcium ions. Blood. 1972;39:382-387.
    • (1972) Blood , vol.39 , pp. 382-387
    • Boyer, M.H.1    Shainoff, J.R.2    Ratnoff, O.D.3
  • 8
    • 0018129207 scopus 로고
    • A two-step fibrinogen-fibrin transition in blood coagulation
    • Blomback B, Hessel B, Hogg D, Therkildsen L. A two-step fibrinogen-fibrin transition in blood coagulation. Nature. 1978;275:501-505.
    • (1978) Nature , vol.275 , pp. 501-505
    • Blomback, B.1    Hessel, B.2    Hogg, D.3    Therkildsen, L.4
  • 9
    • 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
  • 10
    • 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 U S A. 1980;77:1374-1378.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 1374-1378
    • Olexa, S.A.1    Budzynski, A.Z.2
  • 11
    • 0030848486 scopus 로고    scopus 로고
    • Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
    • Spraggon G, Everse S, 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.2    Doolittle, R.F.3
  • 12
    • 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. 1983;72:1034-1041.
    • (1983) J Clin Invest , vol.72 , pp. 1034-1041
    • Matsuda, M.1    Baba, M.2    Morimoto, K.3    Nakamikawa, C.4
  • 13
    • 0029111701 scopus 로고
    • The role of fibrinogen D-domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ275 Arg → Cys)
    • Mosesson M, Siebenlist K, DiOrio J, Matsuda M, Hainfeld JF, Wall JS. The role of fibrinogen D-domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ275 Arg → Cys). J Clin Invest. 1995;96:1053-1058.
    • (1995) J Clin Invest , vol.96 , pp. 1053-1058
    • Mosesson, M.1    Siebenlist, K.2    DiOrio, J.3    Matsuda, M.4    Hainfeld, J.F.5    Wall, J.S.6
  • 14
    • 0017680149 scopus 로고
    • The ε-(γ-glutamyl) lysine crosslink and the catalytic role of transglutaminases
    • Folk JE, Finlayson JS. The ε-(γ-glutamyl) lysine crosslink and the catalytic role of transglutaminases. Adv Prot Chem. 1977;31:1-133.
    • (1977) Adv Prot Chem , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 15
    • 1842292129 scopus 로고    scopus 로고
    • The polymerization pocket "a" within the carboxyterminal region of the γ chain of human fibrinogen is adjacent to but independent from the calcium binding site
    • Cote HCF, Pratt KP, Davie EW, Chung DW. The polymerization pocket "a" within the carboxyterminal region of the γ chain of human fibrinogen is adjacent to but independent from the calcium binding site. J Biol Chem. 1997;272:23792-23798.
    • (1997) J Biol Chem , vol.272 , pp. 23792-23798
    • Cote, H.C.F.1    Pratt, K.P.2    Davie, E.W.3    Chung, D.W.4
  • 16
    • 0033537698 scopus 로고    scopus 로고
    • Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Proamide
    • Everse SJ, Spraggon G, Veerapandian L, Doolittle RF. Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Proamide. Biochemistry. 1999;38:2941-2946.
    • (1999) Biochemistry , vol.38 , pp. 2941-2946
    • Everse, S.J.1    Spraggon, G.2    Veerapandian, L.3    Doolittle, R.F.4
  • 17
    • 0141832851 scopus 로고    scopus 로고
    • X-ray crystallographic studies of fibrinogen and fibrin
    • Doolittle RF. X-ray crystallographic studies of fibrinogen and fibrin. J Thromb Haemost. 2003;1:1559-1565.
    • (2003) J Thromb Haemost , vol.1 , pp. 1559-1565
    • Doolittle, R.F.1
  • 18
    • 0021696927 scopus 로고
    • Genetically abnormal fibrinogens-strategies for structure elucidation, including fibrinopeptide analysis
    • Henschen A, Kehl M, Southan C. Genetically abnormal fibrinogens-strategies for structure elucidation, including fibrinopeptide analysis. Curr Probl Clin Biochem. 1984;14:273-320.
    • (1984) Curr Probl Clin Biochem , vol.14 , pp. 273-320
    • Henschen, A.1    Kehl, M.2    Southan, C.3
  • 19
    • 0032189655 scopus 로고    scopus 로고
    • γ-chain dysfibrinogenemias: Molecular structure-function relationships of naturally occurring mutations in the γ chain of human fibrinogen
    • Cote HCF, Lord ST, Pratt KP. γ-Chain dysfibrinogenemias: molecular structure-function relationships of naturally occurring mutations in the γ chain of human fibrinogen. Blood. 1998;92:2195-2212.
    • (1998) Blood , vol.92 , pp. 2195-2212
    • Cote, H.C.F.1    Lord, S.T.2    Pratt, K.P.3
  • 20
    • 0032723366 scopus 로고    scopus 로고
    • Structure and function of fibrinogen: Insights from dysfibrinogens
    • Matsuda M, Sugo T, Yoshida N, et al. Structure and function of fibrinogen: insights from dysfibrinogens. Thromb Haemost. 1999;82:283-290.
    • (1999) Thromb Haemost , vol.82 , pp. 283-290
    • Matsuda, M.1    Sugo, T.2    Yoshida, N.3
  • 21
    • 0031903388 scopus 로고    scopus 로고
    • A three-dimensional consideration of variant human fibrinogens
    • Everse SJ, Spraggon G, Doolittle, RF. A three-dimensional consideration of variant human fibrinogens. Thromb Haemost. 1998;80:1-9.
    • (1998) Thromb Haemost , vol.80 , pp. 1-9
    • Everse, S.J.1    Spraggon, G.2    Doolittle, R.F.3
  • 22
    • 0025239558 scopus 로고
    • Polymerization defect of fibrinogen Baltimore III due to a γAsn308 → lle mutation
    • Bantia S, Bell WR, Dang CV. Polymerization defect of fibrinogen Baltimore III due to a γAsn308 → lle mutation. Blood. 1990;75:1659-1663.
    • (1990) Blood , vol.75 , pp. 1659-1663
    • Bantia, S.1    Bell, W.R.2    Dang, C.V.3
  • 23
    • 0029831998 scopus 로고    scopus 로고
    • Fibrinogen Matsumoto II: γ308 Asn → Lys (AAT → AAG) mutation associated with bleeding tendency
    • Okumura N, Furihata K, Terasawa F, Ishikawa S, Ueno I, Katsuyama T. Fibrinogen Matsumoto II: γ308 Asn → Lys (AAT → AAG) mutation associated with bleeding tendency. Br J Haematol. 1996;94:526-528.
    • (1996) Br J Haematol , vol.94 , pp. 526-528
    • Okumura, N.1    Furihata, K.2    Terasawa, F.3    Ishikawa, S.4    Ueno, I.5    Katsuyama, T.6
  • 24
    • 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. 1988;263:13848-13856.
    • (1988) J Biol Chem , vol.263 , pp. 13848-13856
    • Yoshida, N.1    Terukina, S.2    Okuma, M.3    Moroi, M.4    Aoki, N.5    Matsuda, M.6
  • 26
    • 0034116650 scopus 로고    scopus 로고
    • A functional assay suggests that heterodimers exist in two C-terminal γ-chain dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV
    • Hogan KA, Lord ST, Okumura N, et al. A functional assay suggests that heterodimers exist in two C-terminal γ-chain dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV. Thromb Haemost. 2000;83:592-597.
    • (2000) Thromb Haemost , vol.83 , pp. 592-597
    • Hogan, K.A.1    Lord, S.T.2    Okumura, N.3
  • 27
    • 0037104676 scopus 로고    scopus 로고
    • Evidence that heterodimers exist in the fibrinogen Matsumoto II (γ308N → K) proband and participate in fibrin fiber formation
    • Okumura N, Terasawa F, Fujita K, Fujihara N, Tozuka M, Koh C-S. Evidence that heterodimers exist in the fibrinogen Matsumoto II (γ308N → K) proband and participate in fibrin fiber formation. Thromb Res. 2002;107:157-162.
    • (2002) Thromb Res , vol.107 , pp. 157-162
    • Okumura, N.1    Terasawa, F.2    Fujita, K.3    Fujihara, N.4    Tozuka, M.5    Koh, C.-S.6
  • 28
    • 0034974358 scopus 로고    scopus 로고
    • Insight from studies with recombinant fibrinogens
    • Lord ST, Gorkun OV. Insight from studies with recombinant fibrinogens. Ann N Y Acad Sci. 2001;936:101-116.
    • (2001) Ann N Y Acad Sci , vol.936 , pp. 101-116
    • Lord, S.T.1    Gorkun, O.V.2
  • 29
    • 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. 1996;75:887-891.
    • (1996) Thromb Haemost , vol.75 , pp. 887-891
    • Okumura, N.1    Furihata, K.2    Terasawa, F.3    Nakagoshi, R.4    Ueno, I.5    Katsuyama, T.6
  • 30
    • 0030998485 scopus 로고    scopus 로고
    • The conversion of fibrinogen to fibrin: Recombinant fibrinogen typifies plasma fibrinogen
    • Gorkun OV, Veklich YI, Weisel JW, Lord ST. The conversion of fibrinogen to fibrin: recombinant fibrinogen typifies plasma fibrinogen. Blood. 1997;89:4407-4414.
    • (1997) Blood , vol.89 , pp. 4407-4414
    • Gorkun, O.V.1    Veklich, Y.I.2    Weisel, J.W.3    Lord, S.T.4
  • 31
    • 0033931595 scopus 로고    scopus 로고
    • Difference in electrophoretic mobility and plasmic digestion profile between four recombinant fibrinogens, γ308K, γ308I, γ308A, and wild type (γ308N)
    • Okumura N, Terasawa F, Fujita K, Tozuka M, Ota H, Katsuyama T. Difference in electrophoretic mobility and plasmic digestion profile between four recombinant fibrinogens, γ308K, γ308I, γ308A, and wild type (γ308N). Electrophoresis. 2000;21:2309-2315.
    • (2000) Electrophoresis , vol.21 , pp. 2309-2315
    • Okumura, N.1    Terasawa, F.2    Fujita, K.3    Tozuka, M.4    Ota, H.5    Katsuyama, T.6
  • 32
    • 0014223584 scopus 로고
    • Physicochemical studies of bovine fibrinogen, IV: Ultraviolet absorption and its relation to the structure of the molecule
    • Mihalyi E. Physicochemical studies of bovine fibrinogen, IV: ultraviolet absorption and its relation to the structure of the molecule. Biochemistry. 1968;7:208-223.
    • (1968) Biochemistry , vol.7 , pp. 208-223
    • Mihalyi, E.1
  • 33
    • 0020682254 scopus 로고
    • Inhibition of fibrin polymerization by fragment D is affected by calcium, Gly-Pro-Arg and Gly-His-Arg
    • Furlan M, Rupp C, Beck EA. Inhibition of fibrin polymerization by fragment D is affected by calcium, Gly-Pro-Arg and Gly-His-Arg. Biochim Biophys Acta. 1983;742:25-32.
    • (1983) Biochim Biophys Acta , vol.742 , pp. 25-32
    • Furlan, M.1    Rupp, C.2    Beck, E.A.3
  • 34
    • 0027524307 scopus 로고
    • Quantifying thrombin-catalyzed release of fibrinopeptides from fibrinogen using high-performance liquid chromatography
    • Ng AS, Lewis SD, Shafer JA. Quantifying thrombin-catalyzed release of fibrinopeptides from fibrinogen using high-performance liquid chromatography. Methods Enzymol. 1993;222:341-358.
    • (1993) Methods Enzymol , vol.222 , pp. 341-358
    • Ng, A.S.1    Lewis, S.D.2    Shafer, J.A.3
  • 35
    • 0030048726 scopus 로고    scopus 로고
    • Strategy for recombinant multichain protein synthesis: Fibrinogen Bβ-chain variants as thrombin substrates
    • Lord ST, Strickland E, Jayjock E. Strategy for recombinant multichain protein synthesis: fibrinogen Bβ-chain variants as thrombin substrates. Biochemistry. 1996;35:2342-2348.
    • (1996) Biochemistry , vol.35 , pp. 2342-2348
    • Lord, S.T.1    Strickland, E.2    Jayjock, E.3
  • 36
    • 0024331906 scopus 로고
    • Fibrinogen Kyoto 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. 1989;74:2681-2687.
    • (1989) Blood , vol.74 , pp. 2681-2687
    • Terukina, S.1    Yamazumi, K.2    Okamoto, K.3    Yamashita, H.4    Ito, Y.5    Matsuda III, M.6
  • 37
    • 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). 1989;105:10-14.
    • (1989) J Biochem (Tokyo) , vol.105 , pp. 10-14
    • Miyata, T.1    Furukawa, K.2    Iwanaga, S.3    Takamatsu, J.4    Saito, H.5
  • 38
    • 0027952782 scopus 로고
    • Effect of calcium on the mobility of γ-chain from fibrinogen Osaka V on sodium dodecyl sulfate-polyacrytamide gel electrophoresis
    • Yoshida N, Hirata H, Imaoka S, Matsuda M, Yamazumi K, Asakura S. Effect of calcium on the mobility of γ-chain from fibrinogen Osaka V on sodium dodecyl sulfate-polyacrytamide gel electrophoresis. Thromb Res. 1994;73:79-82.
    • (1994) Thromb Res , vol.73 , pp. 79-82
    • Yoshida, N.1    Hirata, H.2    Imaoka, S.3    Matsuda, M.4    Yamazumi, K.5    Asakura, S.6
  • 39
    • 0034625408 scopus 로고    scopus 로고
    • Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the γ chain of fibrinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation
    • Hogan KA, Gorkun OV, Lounes KC, et al. Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the γ chain of fibrinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation. J Biol Chem. 2000;275:17778-17785.
    • (2000) J Biol Chem , vol.275 , pp. 17778-17785
    • Hogan, K.A.1    Gorkun, O.V.2    Lounes, K.C.3
  • 40
    • 0025816449 scopus 로고
    • A congenitally 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, Briet E, Lord ST. A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain gene, causing defective calcium binding and impaired fibrin polymerization. J Biol Chem. 1991;266:13456-13461.
    • (1991) J Biol Chem , vol.266 , pp. 13456-13461
    • Koopman, J.1    Haverkate, F.2    Briet, E.3    Lord, S.T.4
  • 41
    • 0037093093 scopus 로고    scopus 로고
    • Fibrinogen Hillsborough: A novel γGly309Asp dysfibrinogen with impaired clotting
    • Mullin JL, Brennan SO, Ganly PS, George PM. Fibrinogen Hillsborough: a novel γGly309Asp dysfibrinogen with impaired clotting. Blood. 2002;99:3597-3601.
    • (2002) Blood , vol.99 , pp. 3597-3601
    • Mullin, J.L.1    Brennan, S.O.2    Ganly, P.S.3    George, P.M.4
  • 43
    • 0022354752 scopus 로고
    • Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin
    • Lewis SD, Shields PP, Shafer JA. Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin. J Biol Chem. 1985;260:10192-10199.
    • (1985) J Biol Chem , vol.260 , pp. 10192-10199
    • Lewis, S.D.1    Shields, P.P.2    Shafer, J.A.3
  • 44
    • 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, Muller-Berghaus G. Thrombin-induced fibrinopeptide B release from normal and variant fibrinogens: influence of inhibitors of fibrin polymerization. Biochim Biophy Acta. 1988;965:169-175.
    • (1988) Biochim Biophy Acta , vol.965 , pp. 169-175
    • Ruf, W.1    Bender, A.2    Lane, D.A.3    Preissner, K.T.4    Selmayr, E.5    Muller-Berghaus, G.6
  • 45
    • 0029847710 scopus 로고    scopus 로고
    • Novel aspects of blood coagulation factor XIII, I: Structure, distribution, activation, and function
    • Muszbek L, Adany R, Mikkola H. Novel aspects of blood coagulation factor XIII, I: structure, distribution, activation, and function. Crit Rev Clin Lab Sci. 1996;33:357-421.
    • (1996) Crit Rev Clin Lab Sci , vol.33 , pp. 357-421
    • Muszbek, L.1    Adany, R.2    Mikkola, H.3
  • 46
    • 0036682920 scopus 로고    scopus 로고
    • Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms
    • Ariëns RA, Lai T-S, Weisel JW, Greenberg CS, Grant PJ. Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms. Blood. 2002;100:743-754.
    • (2002) Blood , vol.100 , pp. 743-754
    • Ariëns, R.A.1    Lai, T.-S.2    Weisel, J.W.3    Greenberg, C.S.4    Grant, P.J.5
  • 47
    • 0014817348 scopus 로고
    • Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin
    • McKee PA, Mattock P, Hill R. Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc Natl Acad Sci U S A. 1970;66:738-744.
    • (1970) Proc Natl Acad Sci U S A , vol.66 , pp. 738-744
    • McKee, P.A.1    Mattock, P.2    Hill, R.3
  • 48
    • 0016759666 scopus 로고
    • Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa)
    • Kanaide H, Shainoff JR. Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa). J Lab Clin Med. 1975;85:574-597.
    • (1975) J Lab Clin Med , vol.85 , pp. 574-597
    • Kanaide, H.1    Shainoff, J.R.2
  • 49
    • 0030725658 scopus 로고    scopus 로고
    • Severely impaired polymerization of recombinant fibrinogen γy-364Asp → His, the substitution discovered in a heterozygous individual
    • Okumura N, Gorkun OV, Lord ST. Severely impaired polymerization of recombinant fibrinogen γy-364Asp → His, the substitution discovered in a heterozygous individual. J Biol Chem. 1997;47:29596-29601
    • (1997) J Biol Chem , vol.47 , pp. 29596-29601
    • Okumura, N.1    Gorkun, O.V.2    Lord, S.T.3
  • 50
    • 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. 1988;51:251-258.
    • (1988) Thromb Res , vol.51 , pp. 251-258
    • Ebert, R.F.1    Bell, W.R.2
  • 51
    • 0034964282 scopus 로고    scopus 로고
    • Structure and properties of clots form fibrinogen Bicetre II (γ308Asn → Lys). Increased permeability due to a larger pores, thicker fibers and decreased rigidity
    • Marchi R, Loyau S, Angles-Cano E, Weisel JW. Structure and properties of clots form fibrinogen Bicetre II (γ308Asn → Lys). Increased permeability due to a larger pores, thicker fibers and decreased rigidity. Ann N Y Acad Sci. 2001;936:125-128.
    • (2001) Ann N Y Acad Sci , vol.936 , pp. 125-128
    • Marchi, R.1    Loyau, S.2    Angles-Cano, E.3    Weisel, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.