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Volumn 45, Issue 6, 2006, Pages 1870-1880

Factor XIIIa mediated attachment of S. aureus fibronectin-binding protein A (FnbA) to fibrin: Identification of Gln103 as a major cross-linking site

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARBOXYLIC ACIDS; CHEMICAL BONDS; CHEMICAL REACTIONS;

EID: 32344449744     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0521240     Document Type: Article
Times cited : (6)

References (50)
  • 1
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy, F. D. (1998) Staphylococcus aureus infections, N. Engl. J. Med. 339, 520-532.
    • (1998) N. Engl. J. Med. , vol.339 , pp. 520-532
    • Lowy, F.D.1
  • 2
    • 0027960065 scopus 로고
    • MSCRAMM-mediated adherence of microorganisms to host tissues
    • Patti, J. M., Allen, B. L., McGavin, M. J., and Hook, M. (1994) MSCRAMM-mediated adherence of microorganisms to host tissues, Annu. Rev. Microbiol. 48, 585-617.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 585-617
    • Patti, J.M.1    Allen, B.L.2    McGavin, M.J.3    Hook, M.4
  • 3
    • 0028334112 scopus 로고
    • Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus
    • McDevitt, D., Francois, P., Vaudaux, P., and Foster, T. J. (1994) Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus, Mol. Microbiol. 11, 237-248.
    • (1994) Mol. Microbiol. , vol.11 , pp. 237-248
    • McDevitt, D.1    Francois, P.2    Vaudaux, P.3    Foster, T.J.4
  • 4
    • 15444353754 scopus 로고    scopus 로고
    • Clumping factor B (C1fB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus
    • Ni Eidhin, D., Perkins, S., Francois, P., Vaudaux, P., Hook, M., and Foster, T. J. (1998) Clumping factor B (C1fB), a new surface-located fibrinogen-binding adhesin of Staphylococcus aureus, Mol. Microbiol. 30, 245-257.
    • (1998) Mol. Microbiol. , vol.30 , pp. 245-257
    • Ni Eidhin, D.1    Perkins, S.2    Francois, P.3    Vaudaux, P.4    Hook, M.5    Foster, T.J.6
  • 5
    • 0034607985 scopus 로고    scopus 로고
    • The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that binds to fibrinogen
    • Wann, E. R., Gurusiddappa, S., and Hook, M. (2000) The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that binds to fibrinogen, J. Biol. Chem. 275, 13863-13871.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13863-13871
    • Wann, E.R.1    Gurusiddappa, S.2    Hook, M.3
  • 6
    • 0000535851 scopus 로고
    • Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: Use of this peptide sequence in the synthesis of biologically active peptides
    • Signas, C., Raucci, G., Jonsson, K., Lindgren, P. E., Anantharamaiah, G. M., Hook, M., and Lindberg, M. (1989) Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: Use of this peptide sequence in the synthesis of biologically active peptides, Proc. Natl. Acad. Sci. U.S.A. 86, 699-703.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 699-703
    • Signas, C.1    Raucci, G.2    Jonsson, K.3    Lindgren, P.E.4    Anantharamaiah, G.M.5    Hook, M.6    Lindberg, M.7
  • 7
    • 0023654797 scopus 로고
    • Isolation and characterization of a fibronectin receptor from Staphylococcus aureus
    • Froman, G., Switalski, L. M., Speziale, P., and Hook, M. (1987) Isolation and characterization of a fibronectin receptor from Staphylococcus aureus, J. Biol. Chem. 262, 6564-6571.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6564-6571
    • Froman, G.1    Switalski, L.M.2    Speziale, P.3    Hook, M.4
  • 8
    • 0027397984 scopus 로고
    • A collagen receptor on Staphylococcus aureus strains isolated from patients with septic arthritis mediates adhesion to cartilage
    • Switalski, L. M., Patti, J. M., Butcher, W., Gristina, A. G., Speziale, P., and Hook, M. (1993) A collagen receptor on Staphylococcus aureus strains isolated from patients with septic arthritis mediates adhesion to cartilage, Mol. Microbiol. 7, 99-107.
    • (1993) Mol. Microbiol. , vol.7 , pp. 99-107
    • Switalski, L.M.1    Patti, J.M.2    Butcher, W.3    Gristina, A.G.4    Speziale, P.5    Hook, M.6
  • 9
    • 0346220010 scopus 로고    scopus 로고
    • Staphylococcus aureus fibronectin-binding protein serves as a substrate for coagulation factor XIIIa: Evidence for factor XIIIa-catalyzed covalent cross-linking to fibronectin and fibrin
    • Matsuka, Y. V., Anderson, T. E., Milner-Fish, T., Ooi, P., and Baker, S. (2003) Staphylococcus aureus fibronectin-binding protein serves as a substrate for coagulation factor XIIIa: Evidence for factor XIIIa-catalyzed covalent cross-linking to fibronectin and fibrin, Biochemistry 42, 14643-14652.
    • (2003) Biochemistry , vol.42 , pp. 14643-14652
    • Matsuka, Y.V.1    Anderson, T.E.2    Milner-Fish, T.3    Ooi, P.4    Baker, S.5
  • 10
    • 0028318420 scopus 로고
    • Interaction of N-terminal fragments of fibronectin with synthetic and recombinant D motifs from its binding protein on Staphylococcus aureus studied using fluorescence anisotropy
    • Huff, S., Matsuka, Y. V., McGavin, M. J., and Ingham, K. C. (1994) Interaction of N-terminal fragments of fibronectin with synthetic and recombinant D motifs from its binding protein on Staphylococcus aureus studied using fluorescence anisotropy, J. Biol. Chem. 269, 15563-15570.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15563-15570
    • Huff, S.1    Matsuka, Y.V.2    McGavin, M.J.3    Ingham, K.C.4
  • 11
    • 0026334144 scopus 로고
    • Two different genes encode fibronectin-binding proteins in Staphylococcus aureus: The complete nucleotide sequence and characterization of the second gene
    • Jonsson, K., Signas, C., Muller, H.-P., and Lindberg, M. (1991) Two different genes encode fibronectin-binding proteins in Staphylococcus aureus: the complete nucleotide sequence and characterization of the second gene, Eur. J. Biochem. 202, 1041-1048.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1041-1048
    • Jonsson, K.1    Signas, C.2    Muller, H.-P.3    Lindberg, M.4
  • 12
    • 0034972479 scopus 로고    scopus 로고
    • Factor XIII: Structure, activation, and interactions with fibrinogen and fibrin
    • Lorand, L. (2001) Factor XIII: structure, activation, and interactions with fibrinogen and fibrin, Ann. N.Y. Acad. Sci. 936, 291-311.
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 291-311
    • Lorand, L.1
  • 13
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Cross-linking enzymes with pleiotropic functions
    • Lorand, L., and Graham, R. M. (2003) Transglutaminases: cross-linking enzymes with pleiotropic functions, Nature 4, 140-156.
    • (2003) Nature , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 14
    • 33947290263 scopus 로고
    • γ-γ Cross-linking sites in human and bovine fibrin
    • Chen, R., and Doolittle, R. F. (1971) γ-γ Cross-linking sites in human and bovine fibrin, Biochemistry 10, 4486-4491.
    • (1971) Biochemistry , vol.10 , pp. 4486-4491
    • Chen, R.1    Doolittle, R.F.2
  • 15
    • 0018567763 scopus 로고
    • Amino acid sequence studies on the α-chain of human fibrinogen. Exact location of cross-linking acceptor sites
    • Cottrell, B. A., Strong, D. D., Watt, K. W. K., and Doolittle, R. F. (1979) Amino acid sequence studies on the α-chain of human fibrinogen. Exact location of cross-linking acceptor sites, Biochemistry 18, 5405-5410.
    • (1979) Biochemistry , vol.18 , pp. 5405-5410
    • Cottrell, B.A.1    Strong, D.D.2    Watt, K.W.K.3    Doolittle, R.F.4
  • 16
    • 0030728644 scopus 로고    scopus 로고
    • Cross-linking of fibronectin to C-terminal fragments of the fibrinogen α-chain by factor XIIIa
    • Matsuka, Y., Migliorini, M., and Ingham, K. (1997) Cross-linking of fibronectin to C-terminal fragments of the fibrinogen α-chain by factor XIIIa, J. Protein Chem. 16, 739-745.
    • (1997) J. Protein Chem. , vol.16 , pp. 739-745
    • Matsuka, Y.1    Migliorini, M.2    Ingham, K.3
  • 17
    • 0020645335 scopus 로고
    • Specificity of fibronectin-fibrin cross-linking
    • Mosher, D. F., and Johnson, R. B. (1983) Specificity of fibronectin-fibrin cross-linking, Ann. N.Y. Acad. Sci. 408, 583-593.
    • (1983) Ann. N.Y. Acad. Sci. , vol.408 , pp. 583-593
    • Mosher, D.F.1    Johnson, R.B.2
  • 18
    • 0034637513 scopus 로고    scopus 로고
    • Cross-linking of plasminogen activator inhibitor 2 and α2-antiplasmin to fibrin(ogen)
    • Ritchie, H., Lawrie, L. C., Crombie, P. W., Mosesson, M. W., and Booth, N. A. (2000) Cross-linking of plasminogen activator inhibitor 2 and α2-antiplasmin to fibrin(ogen), J. Biol. Chem. 275, 24915-24920.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24915-24920
    • Ritchie, H.1    Lawrie, L.C.2    Crombie, P.W.3    Mosesson, M.W.4    Booth, N.A.5
  • 19
    • 0034964394 scopus 로고    scopus 로고
    • Characterization of cross-linking sites in fibrinogen for plasminogen activator inhibitor 2 (PAI-2)
    • Ritchie, H., Lawrie, L. C., Mosesson, M. W., and Booth, N. A. (2001) Characterization of cross-linking sites in fibrinogen for plasminogen activator inhibitor 2 (PAI-2), Ann. N.Y. Acad. Sci. 936, 215-218.
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 215-218
    • Ritchie, H.1    Lawrie, L.C.2    Mosesson, M.W.3    Booth, N.A.4
  • 20
    • 0019781878 scopus 로고
    • Cross-linking of α2-plasmin inhibitor and fibrin by fibrin-stabilizing factor
    • Tamaki, T., and Aoki, N. (1981) Cross-linking of α2-plasmin inhibitor and fibrin by fibrin-stabilizing factor, Biochim. Biophys. Acta 661, 280-286.
    • (1981) Biochim. Biophys. Acta , vol.661 , pp. 280-286
    • Tamaki, T.1    Aoki, N.2
  • 21
    • 0022979474 scopus 로고
    • Cross-linking site in fibrinogen for α2-plasmin inhibitor
    • Kimura, S., and Aoki, N. (1986) Cross-linking site in fibrinogen for α2-plasmin inhibitor, J. Biol. Chem. 261, 15591-15595.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15591-15595
    • Kimura, S.1    Aoki, N.2
  • 22
    • 0036682920 scopus 로고    scopus 로고
    • Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms
    • Ariens, R. A. S., Lai, T.-S., Weisel, J. W., Greenberg, C. S., and Grant, P. J. (2002) Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms, Blood 100, 743-754.
    • (2002) Blood , vol.100 , pp. 743-754
    • Ariens, R.A.S.1    Lai, T.-S.2    Weisel, J.W.3    Greenberg, C.S.4    Grant, P.J.5
  • 23
    • 0028027240 scopus 로고
    • Residue Gin-30 of human erythrocyte anion transporter is a prime site for reaction with intrinsic transglutaminase
    • Murthy, S. N. P., Wilson, J., Zhang, Y., and Lorand, L. (1994) Residue Gin-30 of human erythrocyte anion transporter is a prime site for reaction with intrinsic transglutaminase, J. Biol. Chem. 269, 22907-22911.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22907-22911
    • Murthy, S.N.P.1    Wilson, J.2    Zhang, Y.3    Lorand, L.4
  • 24
    • 0025195103 scopus 로고
    • Labeling of ε-lysine cross-linking sites in proteins with peptide substrates of factor XIIIa and transglutaminase
    • Parameswaran, K., Velasco, P., Wilson, J., and Lorand, L. (1990) Labeling of ε-lysine cross-linking sites in proteins with peptide substrates of factor XIIIa and transglutaminase, Proc. Natl. Acad. Sci. U.S.A. 87, 8472-8475.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8472-8475
    • Parameswaran, K.1    Velasco, P.2    Wilson, J.3    Lorand, L.4
  • 25
    • 4644237859 scopus 로고    scopus 로고
    • Identification of factor XIIIa-reactive glutamine acceptor and lysine donor sites within fibronectin-binding protein (FnbA) from Staphylococcus aureus
    • Anderson, E. T., Fletcher, L., Severin, A., Murphy, E., Baker, S. M., and Matsuka, Y. V. (2004) Identification of factor XIIIa-reactive glutamine acceptor and lysine donor sites within fibronectin-binding protein (FnbA) from Staphylococcus aureus, Biochemistry 43, 11842-11852.
    • (2004) Biochemistry , vol.43 , pp. 11842-11852
    • Anderson, E.T.1    Fletcher, L.2    Severin, A.3    Murphy, E.4    Baker, S.M.5    Matsuka, Y.V.6
  • 26
    • 0019775733 scopus 로고
    • Fluorescent labeling of the carbohydrate moieties of human chorionic gonadotropin and α1-acid glycoprotein
    • Ingham, K., and Brew, S. (1981) Fluorescent labeling of the carbohydrate moieties of human chorionic gonadotropin and α1-acid glycoprotein, Biochim. Biophys. Acta 670, 181-189.
    • (1981) Biochim. Biophys. Acta , vol.670 , pp. 181-189
    • Ingham, K.1    Brew, S.2
  • 27
    • 0029161613 scopus 로고
    • Identification of factor-XIIIa-reactive glutaminyl residues in the propolypeptide of bovine von Willebrand factor
    • Takagi, J., Aoyama, T., Ueki, S., Ohba, H., Saito, Y., and Lorand, L. (1995) Identification of factor-XIIIa-reactive glutaminyl residues in the propolypeptide of bovine von Willebrand factor, Eur. J. Biochem. 232, 773-777.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 773-777
    • Takagi, J.1    Aoyama, T.2    Ueki, S.3    Ohba, H.4    Saito, Y.5    Lorand, L.6
  • 28
    • 0017910967 scopus 로고
    • Size and density of fibrin fibers from turbidity
    • Carr, M. E., and Hermans, J. (1978) Size and density of fibrin fibers from turbidity, Macromolecules 11, 46-50.
    • (1978) Macromolecules , vol.11 , pp. 46-50
    • Carr, M.E.1    Hermans, J.2
  • 29
    • 0026771894 scopus 로고
    • Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: Clot structure and assembly are kinetically controlled
    • Weisel, J. W., and Nagaswami, C. (1992) Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled, Biophys. J. 63, 111-128.
    • (1992) Biophys. J. , vol.63 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 30
    • 0024357241 scopus 로고
    • Reduced adherence to traumatized rat heart valves by a low-fibronectin-binding mutant of Staphylococcus aureus
    • Kuypers, J. M., and Proctor, R. A. (1989) Reduced adherence to traumatized rat heart valves by a low-fibronectin-binding mutant of Staphylococcus aureus, Infect. Immun. 57, 2306-2312.
    • (1989) Infect. Immun. , vol.57 , pp. 2306-2312
    • Kuypers, J.M.1    Proctor, R.A.2
  • 31
    • 0034836914 scopus 로고    scopus 로고
    • Reassessing the role of Staphylococcus aureus clumping factor and fibronectin-binding protein by expression in Lactococcus lactis
    • Que, Y.-A., Francois, P., Haefliger, J.-A., Entenza, J.-M., Vaudaux, P., and Moreillon, P. (2001) Reassessing the role of Staphylococcus aureus clumping factor and fibronectin-binding protein by expression in Lactococcus lactis, Infect. Immun. 69, 6296-6302.
    • (2001) Infect. Immun. , vol.69 , pp. 6296-6302
    • Que, Y.-A.1    Francois, P.2    Haefliger, J.-A.3    Entenza, J.-M.4    Vaudaux, P.5    Moreillon, P.6
  • 33
    • 0020060170 scopus 로고
    • Identification of a region of human fibrinogen interacting with staphylococcal clumping factor
    • Hawiger, J., Timmons, S., Strong, D. D., Cottrel, B. A., Riley, M., and Doolittle, F. R. (1982) Identification of a region of human fibrinogen interacting with staphylococcal clumping factor, Biochemistry 21, 1407-1413.
    • (1982) Biochemistry , vol.21 , pp. 1407-1413
    • Hawiger, J.1    Timmons, S.2    Strong, D.D.3    Cottrel, B.A.4    Riley, M.5    Doolittle, F.R.6
  • 34
    • 12244313428 scopus 로고    scopus 로고
    • A novel variant of the immunoglobulin fold in surface adhesions of Staphylococcus aureus: Crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A
    • Deivanayagam, C. C. S., Wann, E. R., Chen, W., Carson, M., Rajashankar, K. R., Hook, M., and Narayana, S. V. L. (2002) A novel variant of the immunoglobulin fold in surface adhesions of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A, EMBO J. 21, 6660-6672.
    • (2002) EMBO J. , vol.21 , pp. 6660-6672
    • Deivanayagam, C.C.S.1    Wann, E.R.2    Chen, W.3    Carson, M.4    Rajashankar, K.R.5    Hook, M.6    Narayana, S.V.L.7
  • 36
    • 0032767986 scopus 로고    scopus 로고
    • Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells
    • Joh, D., Wann, E. R., Kreikemeyer, B., Speziale, P., and Hook, M. (1999) Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells, Matrix Biol. 18, 211-223.
    • (1999) Matrix Biol. , vol.18 , pp. 211-223
    • Joh, D.1    Wann, E.R.2    Kreikemeyer, B.3    Speziale, P.4    Hook, M.5
  • 37
    • 0035159395 scopus 로고    scopus 로고
    • Protransglutaminase (factor XIII) mediated cross-linking of fibrinogen and fibrin
    • Siebenlist, K. R., Meh, D. A., and Mosesson, M. W. (2001) Protransglutaminase (factor XIII) mediated cross-linking of fibrinogen and fibrin, Thromb. Haemost. 86, 1221-1228.
    • (2001) Thromb. Haemost. , vol.86 , pp. 1221-1228
    • Siebenlist, K.R.1    Meh, D.A.2    Mosesson, M.W.3
  • 39
    • 0030774882 scopus 로고    scopus 로고
    • Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix
    • Corbett, S. A., Lee, L., Wilson, C. L., and Schwarzbauer, J. E. (1997) Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix, J. Biol. Chem. 272, 24999-25005.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24999-25005
    • Corbett, S.A.1    Lee, L.2    Wilson, C.L.3    Schwarzbauer, J.E.4
  • 40
    • 0034531162 scopus 로고    scopus 로고
    • Cross-linking of wild type and mutant α2-antiplasmins to fibrin by activated factor XIII and by tissue transglutaminase
    • Lee, K. N., Lee, C. S., Tae, W. C., Jackson, K. W., Christiansen, V. J., and McKee, P. A. (2000) Cross-linking of wild type and mutant α2-antiplasmins to fibrin by activated factor XIII and by tissue transglutaminase, J. Biol. Chem. 275, 37382-37389.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37382-37389
    • Lee, K.N.1    Lee, C.S.2    Tae, W.C.3    Jackson, K.W.4    Christiansen, V.J.5    McKee, P.A.6
  • 43
    • 0018859015 scopus 로고
    • Structural features of glutamine substrates for human plasma factor XIIIa (activated blood coagulation factor XIII)
    • German, J. J., and Folk, J. E. (1980) Structural features of glutamine substrates for human plasma factor XIIIa (activated blood coagulation factor XIII), J. Biol. Chem. 255, 419-427.
    • (1980) J. Biol. Chem. , vol.255 , pp. 419-427
    • German, J.J.1    Folk, J.E.2
  • 44
    • 0021142637 scopus 로고
    • Structural features of glutamine substrates for transglutaminases. Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme
    • German, J. J., and Folk, J. E. (1984) Structural features of glutamine substrates for transglutaminases. Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme, J. Biol. Chem. 259, 9007-9010.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9007-9010
    • German, J.J.1    Folk, J.E.2
  • 45
    • 0030468786 scopus 로고    scopus 로고
    • Determinants of substrate specificity for factor XIII
    • McDonagh, J., and Fukue, H. (1996) Determinants of substrate specificity for factor XIII, Semin. Thromb. Hemost. 22, 369-376.
    • (1996) Semin. Thromb. Hemost. , vol.22 , pp. 369-376
    • McDonagh, J.1    Fukue, H.2
  • 46
    • 0026569887 scopus 로고
    • Interactions of factor XIII with fibrin as substrate and cofactor
    • Hornyak, T. J., and Shafer, J. A. (1992) Interactions of factor XIII with fibrin as substrate and cofactor, Biochemistry 31, 423-429.
    • (1992) Biochemistry , vol.31 , pp. 423-429
    • Hornyak, T.J.1    Shafer, J.A.2
  • 47
    • 0032892173 scopus 로고    scopus 로고
    • Monocyte plasminogen activator inhibitor 2 (PAI-2) inhibits u-PA-mediated fibrin clot lysis and is cross-linked to fibrin
    • Ritchie, H., Robbie, L. A., Kinghorn, S., Exley, R., and Booth, N. A. (1999) Monocyte plasminogen activator inhibitor 2 (PAI-2) inhibits u-PA-mediated fibrin clot lysis and is cross-linked to fibrin, Thromb. Haemost. 81, 96-103.
    • (1999) Thromb. Haemost. , vol.81 , pp. 96-103
    • Ritchie, H.1    Robbie, L.A.2    Kinghorn, S.3    Exley, R.4    Booth, N.A.5
  • 48
    • 0025213864 scopus 로고
    • Sequence location of a putative transglutaminase cross-linking site in human vitronectin
    • Skorstengaard, K., Halkier, T., Hojrup, P., and Mosher, D. F. (1990) Sequence location of a putative transglutaminase cross-linking site in human vitronectin, FEBS Lett. 262, 269-274.
    • (1990) FEBS Lett. , vol.262 , pp. 269-274
    • Skorstengaard, K.1    Halkier, T.2    Hojrup, P.3    Mosher, D.F.4
  • 49
    • 0032538447 scopus 로고    scopus 로고
    • Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin
    • Valnickova, Z., and Enghild, J. J. (1998) Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin, J. Biol. Chem. 273, 27220-27224.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27220-27224
    • Valnickova, Z.1    Enghild, J.J.2
  • 50
    • 0029932912 scopus 로고    scopus 로고
    • Factor XIIIa-catalyzed cross-linking of recombinant αC fragments of human fibrinogen
    • Matsuka, Y., Medved, L., Migliorini, M., and Ingham, K. (1996) Factor XIIIa-catalyzed cross-linking of recombinant αC fragments of human fibrinogen, Biochemistry 35, 5810-5816.
    • (1996) Biochemistry , vol.35 , pp. 5810-5816
    • Matsuka, Y.1    Medved, L.2    Migliorini, M.3    Ingham, K.4


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