메뉴 건너뛰기




Volumn 111, Issue 3, 2013, Pages 401-416

Pneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activator

Author keywords

Angiostatin; Phosphoglycerate kinase; Plasminogen; Streptococcus pneumoniae; Tissue type plasminogen activator

Indexed keywords

ANGIOSTATIN; BACTERIAL PROTEIN; PHOSPHOGLYCERATE KINASE; PLASMIN; PLASMINOGEN; RECOMBINANT PROTEIN; TISSUE PLASMINOGEN ACTIVATOR; UROKINASE;

EID: 84897038608     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH13-05-0421     Document Type: Article
Times cited : (36)

References (55)
  • 1
    • 0036009312 scopus 로고    scopus 로고
    • Pneumococcal disease in western Europe: Burden of disease, antibiotic resistance and management
    • Cartwright K. Pneumococcal disease in western Europe: burden of disease, antibiotic resistance and management. Eur J Pediatr 2002; 161: 188-195.
    • (2002) Eur J Pediatr , vol.161 , pp. 188-195
    • Cartwright, K.1
  • 2
    • 40949162838 scopus 로고    scopus 로고
    • The role of Streptococcus pneumoniae virulence factors in host respiratory colonisation and disease
    • Kadioglu A, Weiser JN, Paton JC, et al. The role of Streptococcus pneumoniae virulence factors in host respiratory colonisation and disease. Nat Rev Microbiol 2008; 6: 288-301.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 288-301
    • Kadioglu, A.1    Weiser, J.N.2    Paton, J.C.3
  • 3
    • 32244439999 scopus 로고    scopus 로고
    • Versatility of pneumococcal surface proteins
    • Bergmann S, Hammerschmidt S. Versatility of pneumococcal surface proteins. Microbiology 2006; 152: 295-303.
    • (2006) Microbiology , vol.152 , pp. 295-303
    • Bergmann, S.1    Hammerschmidt, S.2
  • 4
    • 84863561152 scopus 로고    scopus 로고
    • Pneumococcal surface proteins: When the whole is greater than the sum of its parts
    • Pérez-Dorado I, Galan-Bartual S, Hermoso JA. Pneumococcal surface proteins: when the whole is greater than the sum of its parts. Mol Oral Microbiol 2012; 4: 221-245.
    • (2012) Mol Oral Microbiol , vol.4 , pp. 221-245
    • Pérez-Dorado, I.1    Galan-Bartual, S.2    Hermoso, J.A.3
  • 5
    • 23744464766 scopus 로고    scopus 로고
    • The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration
    • Bergmann S, Rohde M, Preissner KT, et al. The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration. Thromb Haemost 2005; 94: 304-311.
    • (2005) Thromb Haemost , vol.94 , pp. 304-311
    • Bergmann, S.1    Rohde, M.2    Preissner, K.T.3
  • 6
    • 34548667697 scopus 로고    scopus 로고
    • Fibrinolysis and host response in bacterial infections
    • Bergmann S, Hammerschmidt S. Fibrinolysis and host response in bacterial infections. Thromb Haemost 2007; 98: 512-520.
    • (2007) Thromb Haemost , vol.98 , pp. 512-520
    • Bergmann, S.1    Hammerschmidt, S.2
  • 7
    • 0023882218 scopus 로고
    • Plasminogen: A brief introduction into its biochemistry and function
    • Miyashita C, Wenzel E, Heiden M. Plasminogen: a brief introduction into its biochemistry and function. Haemostasis 1988; 18 (Suppl 1): 7-13.
    • (1988) Haemostasis , vol.18 , Issue.SUPPL. 1 , pp. 7-13
    • Miyashita, C.1    Wenzel, E.2    Heiden, M.3
  • 8
    • 19944432677 scopus 로고    scopus 로고
    • Angiostatin is a novel anti-inflammatory factor by inhibiting leukocyte recruitment
    • Chavakis T, Athanasopoulos A, Rhee JS, et al. Angiostatin is a novel anti-inflammatory factor by inhibiting leukocyte recruitment. Blood 2005; 105: 1036-1043.
    • (2005) Blood , vol.105 , pp. 1036-1043
    • Chavakis, T.1    Athanasopoulos, A.2    Rhee, J.S.3
  • 9
    • 0030741447 scopus 로고    scopus 로고
    • Impaired clot lysis by rt-PA catalysed mini-plasminogen activation
    • Duboscq C, Genoud V, Parborell MF, et al. Impaired clot lysis by rt-PA catalysed mini-plasminogen activation. Thromb Res 1997; 86: 505-513.
    • (1997) Thromb Res , vol.86 , pp. 505-513
    • Duboscq, C.1    Genoud, V.2    Parborell, M.F.3
  • 11
    • 0037069281 scopus 로고    scopus 로고
    • Role of the urokinase plasminogen activator system in patients with bacterial meningitis
    • Winkler F, Kastenbauer S, Koedel U, et al. Role of the urokinase plasminogen activator system in patients with bacterial meningitis. Neurology 2002; 59: 1350-1355.
    • (2002) Neurology , vol.59 , pp. 1350-1355
    • Winkler, F.1    Kastenbauer, S.2    Koedel, U.3
  • 12
    • 66449112507 scopus 로고    scopus 로고
    • Enolase from Paracoccidioides brasiliensis: Isolation and identification as a fibronectin-binding protein
    • Donofrio FC, Calil AC, Miranda ET, et al. Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein. J Med Microbiol 2009; 58: 706-713.
    • (2009) J Med Microbiol , vol.58 , pp. 706-713
    • Donofrio, F.C.1    Calil, A.C.2    Miranda, E.T.3
  • 13
    • 2542425761 scopus 로고    scopus 로고
    • Identification of enolase as a lamininbinding protein on the surface of Staphylococcus aureus
    • Carneiro CR, Postol E, Nomizo R, et al. Identification of enolase as a lamininbinding protein on the surface of Staphylococcus aureus. Microbes Infect 2004; 6: 604-608.
    • (2004) Microbes Infect , vol.6 , pp. 604-608
    • Carneiro, C.R.1    Postol, E.2    Nomizo, R.3
  • 14
    • 0034931519 scopus 로고    scopus 로고
    • alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann S, Rohde M, Chhatwal GS, et al. alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 2001; 40: 1273-1287.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3
  • 15
    • 0036176205 scopus 로고    scopus 로고
    • Identification of major outer surface proteins of Streptococcus agalactiae
    • Hughes MJ, Moore JC, Lane JD, et al. Identification of major outer surface proteins of Streptococcus agalactiae. Infect Immun 2002; 70: 1254-1259.
    • (2002) Infect Immun , vol.70 , pp. 1254-1259
    • Hughes, M.J.1    Moore, J.C.2    Lane, J.D.3
  • 16
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation
    • Bernstein BE, Michels PA, Hol WG. Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. Nature 1997; 385: 275-278.
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.2    Hol, W.G.3
  • 17
    • 0029897963 scopus 로고    scopus 로고
    • Folding and functional complementation of engineered fragments from yeast phosphoglycerate kinase
    • Pecorari F, Guilbert C, Minard P, et al. Folding and functional complementation of engineered fragments from yeast phosphoglycerate kinase. Biochemistry 1996; 35: 3465-3476.
    • (1996) Biochemistry , vol.35 , pp. 3465-3476
    • Pecorari, F.1    Guilbert, C.2    Minard, P.3
  • 18
    • 61949389320 scopus 로고    scopus 로고
    • Integrin-linked kinase is required for vitronectin-mediated internalisation of Streptococcus pneumoniae by host cells
    • Bergmann S, Lang A, Rohde M, et al. Integrin-linked kinase is required for vitronectin-mediated internalisation of Streptococcus pneumoniae by host cells. J Cell Sci 2009; 122: 256-267.
    • (2009) J Cell Sci , vol.122 , pp. 256-267
    • Bergmann, S.1    Lang, A.2    Rohde, M.3
  • 19
    • 0030329981 scopus 로고    scopus 로고
    • SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
    • Frank R, Overwin H. SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Methods Mol Biol 1996; 66: 149-169.
    • (1996) Methods Mol Biol , vol.66 , pp. 149-169
    • Frank, R.1    Overwin, H.2
  • 20
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Bergmann S, Wild D, Diekmann O, et al. Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol Microbiol 2003; 49: 411-423.
    • (2003) Mol Microbiol , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3
  • 21
    • 80955135594 scopus 로고    scopus 로고
    • Crystallisation and preliminary X-ray diffraction analysis of phosphoglycerate kinase from Streptococcus pneumoniae
    • Bernardo-Garcia N, Bartual SG, Fulde M, et al. Crystallisation and preliminary X-ray diffraction analysis of phosphoglycerate kinase from Streptococcus pneumoniae. Acta Crystallogr Sect F Struct Biol Cryst Commun 2011; 67: 1285-1289.
    • (2011) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.67 , pp. 1285-1289
    • Bernardo-Garcia, N.1    Bartual, S.G.2    Fulde, M.3
  • 22
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie AG. The integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 2006; 62: 48-57.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 23
    • 0031573453 scopus 로고    scopus 로고
    • Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability
    • Auerbach G, Huber R, Grättinger M, et al. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure 1997; 5: 1475-1483.
    • (1997) Structure , vol.5 , pp. 1475-1483
    • Auerbach, G.1    Huber, R.2    Grättinger, M.3
  • 24
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Pythonbased system for macromolecular structure solution
    • Adams PD, Afonine PV, Bunkoczi G, et al. PHENIX: a comprehensive Pythonbased system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 2010; 66: 213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkoczi, G.3
  • 25
  • 26
    • 48449105393 scopus 로고    scopus 로고
    • The Rosetta Dock server for local protein-protein docking
    • Lyskov S, Gray JJ. The Rosetta Dock server for local protein-protein docking. Nucleic Acids Res 2008; 36: W233-238.
    • (2008) Nucleic Acids Res , vol.36
    • Lyskov, S.1    Gray, J.J.2
  • 27
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan Y, Wu C, Chowdhury S, et al. A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem 2003; 24: 1999-2012.
    • (2003) J Comput Chem , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3
  • 28
    • 2442480826 scopus 로고    scopus 로고
    • Distinguish protein decoys by using a scoring function based on a new AMBER force field. Short molecular dynamincs simulations, and the generalized born solvent model
    • Lee MC, Duan Y. Distinguish protein decoys by using a scoring function based on a new AMBER force field. Short molecular dynamincs simulations, and the generalized born solvent model. Proteins 2004; 55: 620-634.
    • (2004) Proteins , vol.55 , pp. 620-634
    • Lee, M.C.1    Duan, Y.2
  • 29
    • 23444454552 scopus 로고    scopus 로고
    • The Amber biomolecular simulation programs
    • Case DA, Cheatham TE 3rd, Darden T, et al. The Amber biomolecular simulation programs. J Comput Chem 2005; 26: 1668-1688.
    • (2005) J Comput Chem , vol.26 , pp. 1668-1688
    • Case, D.A.1    Cheatham III, T.E.2    Darden, T.3
  • 30
    • 34247266546 scopus 로고    scopus 로고
    • A new implicit solvent model for protein-ligand docking
    • Morreale A, Gil-Redondo R, Ortiz AR. A new implicit solvent model for protein-ligand docking. Proteins 2007; 67: 606-616.
    • (2007) Proteins , vol.67 , pp. 606-616
    • Morreale, A.1    Gil-Redondo, R.2    Ortiz, A.R.3
  • 31
    • 77954040065 scopus 로고    scopus 로고
    • Molecular characterisation of pneumococcal isolates from pets and laboratory animals
    • van der Linden M, Al-Lahham A, Nicklas W, et al. Molecular characterisation of pneumococcal isolates from pets and laboratory animals. PLoS One 2009; 4: e8286.
    • (2009) PLoS One , vol.4
    • van der Linden, M.1    Al-Lahham, A.2    Nicklas, W.3
  • 32
    • 5144224570 scopus 로고    scopus 로고
    • Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: Crystal structure and evaluation of plasmin(ogen)-binding sites
    • Ehinger S, Schubert WD, Bergmann S, et al. Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites. J Mol Biol 2004; 343: 997-1005.
    • (2004) J Mol Biol , vol.343 , pp. 997-1005
    • Ehinger, S.1    Schubert, W.D.2    Bergmann, S.3
  • 33
    • 84861117698 scopus 로고    scopus 로고
    • The X-ray crystal structure of full-length human plasminogen
    • Law RH, Caradoc-Davies T, Cowieson N, et al. The X-ray crystal structure of full-length human plasminogen. Cell Rep 2012; 1: 185-190.
    • (2012) Cell Rep , vol.1 , pp. 185-190
    • Law, R.H.1    Caradoc-Davies, T.2    Cowieson, N.3
  • 34
    • 0026528807 scopus 로고
    • Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution
    • de Vos AM, Ultsch MH, Kelley RF, et al. Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution. Biochemistry 1992; 31: 270-279.
    • (1992) Biochemistry , vol.31 , pp. 270-279
    • de Vos, A.M.1    Ultsch, M.H.2    Kelley, R.F.3
  • 35
    • 31944447012 scopus 로고    scopus 로고
    • Structure of human urokinase plasminogen activator in complex with its receptor
    • Huai Q, Mazar AP, Kuo A, et al. Structure of human urokinase plasminogen activator in complex with its receptor. Science 2006; 311: 656-659.
    • (2006) Science , vol.311 , pp. 656-659
    • Huai, Q.1    Mazar, A.P.2    Kuo, A.3
  • 36
    • 0028169064 scopus 로고
    • Binding of tissue-type plasminogen activator (t-PA) to Neisseria meningitidis and Haemophilus influenzae
    • Ullberg M, Wiman B, Kronvall G. Binding of tissue-type plasminogen activator (t-PA) to Neisseria meningitidis and Haemophilus influenzae. FEMS Immunol Med Microbiol 1994; 9: 171-177.
    • (1994) FEMS Immunol Med Microbiol , vol.9 , pp. 171-177
    • Ullberg, M.1    Wiman, B.2    Kronvall, G.3
  • 37
    • 0037053441 scopus 로고    scopus 로고
    • The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin
    • Abad MC, Arni RK, Grella DK, et al. The X-ray crystallographic structure of the angiogenesis inhibitor angiostatin. J Mol Biol 2002; 318: 1009-1017.
    • (2002) J Mol Biol , vol.318 , pp. 1009-1017
    • Abad, M.C.1    Arni, R.K.2    Grella, D.K.3
  • 38
    • 42949153528 scopus 로고    scopus 로고
    • Plasminogen binding by oral streptococci from dental plaque and inflammatory lesions
    • Kinnby B, Booth NA, Svensater G. Plasminogen binding by oral streptococci from dental plaque and inflammatory lesions. Microbiology 2008; 154: 924-931.
    • (2008) Microbiology , vol.154 , pp. 924-931
    • Kinnby, B.1    Booth, N.A.2    Svensater, G.3
  • 39
    • 79960929092 scopus 로고    scopus 로고
    • Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin
    • Boone TJ, Burnham CA, Tyrrell GJ. Binding of group B streptococcal phosphoglycerate kinase to plasminogen and actin. Microb Pathog 2011; 51: 255-261.
    • (2011) Microb Pathog , vol.51 , pp. 255-261
    • Boone, T.J.1    Burnham, C.A.2    Tyrrell, G.J.3
  • 40
    • 84865259227 scopus 로고    scopus 로고
    • Identification of the actin and plasminogen binding regions of group B streptococcal phosphoglycerate kinase
    • Boone TJ, Tyrrell GJ. Identification of the actin and plasminogen binding regions of group B streptococcal phosphoglycerate kinase. J Biol Chem 2012; 287: 29035-29044.
    • (2012) J Biol Chem , vol.287 , pp. 29035-29044
    • Boone, T.J.1    Tyrrell, G.J.2
  • 41
    • 0032486286 scopus 로고    scopus 로고
    • alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi V, Fischetti VA. alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 1998; 273: 14503-14515.
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 42
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: Its role in diseases
    • Pancholi V. Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 2001; 58: 902-920.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 43
    • 38349144290 scopus 로고    scopus 로고
    • The lack of binding of VEK-30, an internal peptide from the group A streptococcal M-like protein, PAM, to murine plasminogen is due to two amino acid replacements in the plasminogen kringle-2 domain
    • Fu Q, Figuera-Losada M, Ploplis VA, et al. The lack of binding of VEK-30, an internal peptide from the group A streptococcal M-like protein, PAM, to murine plasminogen is due to two amino acid replacements in the plasminogen kringle-2 domain. J Biol Chem 2008; 283: 1580-1587.
    • (2008) J Biol Chem , vol.283 , pp. 1580-1587
    • Fu, Q.1    Figuera-Losada, M.2    Ploplis, V.A.3
  • 44
    • 0028348234 scopus 로고
    • The structure of recombinant plasminogen kringle 1 and the fibrin binding site
    • Wu TP, Padmanabhan KP, Tulinsky A. The structure of recombinant plasminogen kringle 1 and the fibrin binding site. Blood Coagul Fibrinolysis 1994; 5: 157-166.
    • (1994) Blood Coagul Fibrinolysis , vol.5 , pp. 157-166
    • Wu, T.P.1    Padmanabhan, K.P.2    Tulinsky, A.3
  • 45
    • 0033619701 scopus 로고    scopus 로고
    • Solution structure and dynamics of the plasminogen kringle 2-AMCHA complex: 3(1)-helix in homologous domains
    • Marti DN, Schaller J, Llinas M. Solution structure and dynamics of the plasminogen kringle 2-AMCHA complex: 3(1)-helix in homologous domains. Biochemistry 1999; 38: 15741-15755.
    • (1999) Biochemistry , vol.38 , pp. 15741-15755
    • Marti, D.N.1    Schaller, J.2    Llinas, M.3
  • 46
    • 77955700229 scopus 로고    scopus 로고
    • Human plasminogen kringle 3: Solution structure, functional insights, phylogenetic landscape
    • Christen MT, Frank P, Schaller J, et al. Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape. Biochemistry 2010; 49: 7131-7150.
    • (2010) Biochemistry , vol.49 , pp. 7131-7150
    • Christen, M.T.1    Frank, P.2    Schaller, J.3
  • 47
    • 0030938277 scopus 로고    scopus 로고
    • Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues
    • Stec B, Yamano A, Whitlow M, et al. Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues. Acta Crystallogr D Biol Crystallogr 1997; 53: 169-178.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 169-178
    • Stec, B.1    Yamano, A.2    Whitlow, M.3
  • 48
    • 0032502267 scopus 로고    scopus 로고
    • Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen
    • Chang Y, Mochalkin I, McCance SG, et al. Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. Biochemistry 1998; 37: 3258-3271.
    • (1998) Biochemistry , vol.37 , pp. 3258-3271
    • Chang, Y.1    Mochalkin, I.2    McCance, S.G.3
  • 49
    • 0020479217 scopus 로고
    • Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4
    • Trexler M, Vali Z, Patthy L. Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4. J Biol Chem 1982; 257: 7401-7406.
    • (1982) J Biol Chem , vol.257 , pp. 7401-7406
    • Trexler, M.1    Vali, Z.2    Patthy, L.3
  • 50
    • 0021739141 scopus 로고
    • The fibrin-binding site of human plasminogen. Arginines 32 and 34 are essential for fibrin affinity of the kringle 1 domain
    • Vali Z, Patthy L. The fibrin-binding site of human plasminogen. Arginines 32 and 34 are essential for fibrin affinity of the kringle 1 domain. J Biol Chem 1984; 259: 13690-13694.
    • (1984) J Biol Chem , vol.259 , pp. 13690-13694
    • Vali, Z.1    Patthy, L.2
  • 51
    • 79952125743 scopus 로고    scopus 로고
    • SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration
    • Fulde M, Rohde M, Hitzmann A, et al. SCM, a novel M-like protein from Streptococcus canis, binds (mini)-plasminogen with high affinity and facilitates bacterial transmigration. Biochem J 2011; 434: 523-535.
    • (2011) Biochem J , vol.434 , pp. 523-535
    • Fulde, M.1    Rohde, M.2    Hitzmann, A.3
  • 52
    • 84880050774 scopus 로고    scopus 로고
    • Cooperative plasminogen recruitment to the surface of Streptococcus canis via M protein and enolase enhances bacterial survival
    • e00629-12
    • Fulde M, Rohde M, Polok A, et al. Cooperative plasminogen recruitment to the surface of Streptococcus canis via M protein and enolase enhances bacterial survival. mBio 2013; 12: e00629-12.
    • (2013) mBio , vol.12
    • Fulde, M.1    Rohde, M.2    Polok, A.3
  • 53
    • 33748744172 scopus 로고    scopus 로고
    • The Maintenance of High Affinity Plasminogen Binding by Group A Streptococcal Plasminogen-binding M-like Protein Is Mediated by Arginine and Histidine Residues within the a1 and a2 Repeat Domains
    • Sanderson-Smith M, Walker MJ, Ranson M. The Maintenance of High Affinity Plasminogen Binding by Group A Streptococcal Plasminogen-binding M-like Protein Is Mediated by Arginine and Histidine Residues within the a1 and a2 Repeat Domains. J Biol Chem 2006; 281: 25965-25971.
    • (2006) J Biol Chem , vol.281 , pp. 25965-25971
    • Sanderson-Smith, M.1    Walker, M.J.2    Ranson, M.3
  • 54
    • 0025729292 scopus 로고
    • Enhancement of tissue plasminogen activator-catalysed plasminogen activation by Escherichia coli S fimbriae associated with neonatal septicaemia and meningitis
    • Parkkinen J, Hacker J, Korhonen TK. Enhancement of tissue plasminogen activator-catalysed plasminogen activation by Escherichia coli S fimbriae associated with neonatal septicaemia and meningitis. Thromb Haemost 1991; 65: 483-486.
    • (1991) Thromb Haemost , vol.65 , pp. 483-486
    • Parkkinen, J.1    Hacker, J.2    Korhonen, T.K.3
  • 55
    • 0024411509 scopus 로고
    • Group A streptococci bind human plasmin but not other structurally related proteins
    • DesJardin LE, Boyle MD, Lottenberg R. Group A streptococci bind human plasmin but not other structurally related proteins. Thromb Res 1989; 55: 187-193.
    • (1989) Thromb Res , vol.55 , pp. 187-193
    • DesJardin, L.E.1    Boyle, M.D.2    Lottenberg, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.