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Volumn 194, Issue 10, 2012, Pages 2509-2519

Glutamine synthetase and glucose-6-phosphate isomerase are adhesive moonlighting proteins of Lactobacillus crispatus released by epithelial cathelicidin LL-37

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; COLLAGEN TYPE 1; ENOLASE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLUTAMATE AMMONIA LIGASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HISTIDINE; HYBRID PROTEIN; LAMININ; MATRIGEL; PLASMINOGEN; PLASMINOGEN RECEPTOR; PROPIDIUM IODIDE; UNCLASSIFIED DRUG;

EID: 84861361412     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06704-11     Document Type: Article
Times cited : (84)

References (63)
  • 1
    • 33745406873 scopus 로고    scopus 로고
    • Beneficial immunomodulatory activity of Lactobacillus casei in malnourished mice pneumonia: effect on inflammation and coagulation
    • Aguero G, Villena J, Racedo S, Haro C, Alvarez S. 2006. Beneficial immunomodulatory activity of Lactobacillus casei in malnourished mice pneumonia: effect on inflammation and coagulation. Nutrition 22:810-819.
    • (2006) Nutrition , vol.22 , pp. 810-819
    • Aguero, G.1    Villena, J.2    Racedo, S.3    Haro, C.4    Alvarez, S.5
  • 2
    • 0025788775 scopus 로고
    • Collagen binding by lactobacilli
    • Aleljung P, et al. 1991. Collagen binding by lactobacilli. Curr. Microbiol. 23:33-38.
    • (1991) Curr. Microbiol. , vol.23 , pp. 33-38
    • Aleljung, P.1
  • 4
    • 34250333853 scopus 로고    scopus 로고
    • pHdependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids
    • Antikainen J, Kuparinen V, Lähteenmäki K, Korhonen TK. 2007. pHdependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids. J. Bacteriol. 189:4539-4543.
    • (2007) J. Bacteriol. , vol.189 , pp. 4539-4543
    • Antikainen, J.1    Kuparinen, V.2    Lähteenmäki, K.3    Korhonen, T.K.4
  • 5
    • 35948951215 scopus 로고    scopus 로고
    • Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits
    • Antikainen J, Kuparinen V, Lähteenmäki K, Korhonen TK. 2007. Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits. FEMS Immunol. Med. Microbiol. 51:526-534.
    • (2007) FEMS Immunol. Med. Microbiol. , vol.51 , pp. 526-534
    • Antikainen, J.1    Kuparinen, V.2    Lähteenmäki, K.3    Korhonen, T.K.4
  • 6
    • 0036430117 scopus 로고    scopus 로고
    • Domains in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence to collagens, laminin and lipoteichoic acids and in self-assembly
    • Antikainen J, Anton L, Sillanpää J, Korhonen TK. 2002. Domains in the S-layer protein CbsA of Lactobacillus crispatus involved in adherence to collagens, laminin and lipoteichoic acids and in self-assembly. Mol. Microbiol. 46:381-394.
    • (2002) Mol. Microbiol. , vol.46 , pp. 381-394
    • Antikainen, J.1    Anton, L.2    Sillanpää, J.3    Korhonen, T.K.4
  • 7
    • 0036284194 scopus 로고    scopus 로고
    • Escherichia coli survival in groundwater and effluent measured using a combination of propidium iodide and the green fluorescent protein
    • Banning N, Toze S, Mee BJ. 2002. Escherichia coli survival in groundwater and effluent measured using a combination of propidium iodide and the green fluorescent protein. J. Appl. Microbiol. 93:69-76.
    • (2002) J. Appl. Microbiol. , vol.93 , pp. 69-76
    • Banning, N.1    Toze, S.2    Mee, B.J.3
  • 8
    • 0347983827 scopus 로고    scopus 로고
    • Use of some pre-, pro- and synbiotics in critically ill patients
    • Bengmark S. 2003. Use of some pre-, pro- and synbiotics in critically ill patients. Best Pract. Res. Clin. Gastroenterol. 17:833-848.
    • (2003) Best Pract. Res. Clin. Gastroenterol. , vol.17 , pp. 833-848
    • Bengmark, S.1
  • 9
    • 34548667697 scopus 로고    scopus 로고
    • Fibrinolysis and host response in bacterial infections
    • Bergmann S, Hammerschmidt S. 2007. Fibrinolysis and host response in bacterial infections. Thromb. Haemost. 98:512-520.
    • (2007) Thromb. Haemost. , vol.98 , pp. 512-520
    • Bergmann, S.1    Hammerschmidt, S.2
  • 10
    • 0034931519 scopus 로고    scopus 로고
    • Alphaenolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S. 2001. Alphaenolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol. Microbiol. 40:1273-1287.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 11
    • 29644437923 scopus 로고    scopus 로고
    • GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: potential role in interactions with the host and the gastric pathogen Helicobacter pylori
    • Bergonzelli GE, et al. 2006. GroEL of Lactobacillus johnsonii La1 (NCC 533) is cell surface associated: potential role in interactions with the host and the gastric pathogen Helicobacter pylori. Infect. Immun. 74:425-434.
    • (2006) Infect. Immun. , vol.74 , pp. 425-434
    • Bergonzelli, G.E.1
  • 12
    • 25444529704 scopus 로고    scopus 로고
    • Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties
    • Boël G, Jin H, Pancholi V. 2005. Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties. Infect. Immun. 73:6237-6248.
    • (2005) Infect. Immun. , vol.73 , pp. 6237-6248
    • Boël, G.1    Jin, H.2    Pancholi, V.3
  • 14
    • 34547816626 scopus 로고    scopus 로고
    • Binding of human plasminogen to Bifidobacterium
    • Candela M, et al. 2007. Binding of human plasminogen to Bifidobacterium. J. Bacteriol. 189:5929-5936.
    • (2007) J. Bacteriol. , vol.189 , pp. 5929-5936
    • Candela, M.1
  • 15
    • 77953221206 scopus 로고    scopus 로고
    • DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts
    • Candela M, et al. 2010. DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts. Microbiology 156:1609-1618.
    • (2010) Microbiology , vol.156 , pp. 1609-1618
    • Candela, M.1
  • 16
    • 62749196670 scopus 로고    scopus 로고
    • Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein
    • Castaldo C, et al. 2009. Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein. Microb. Cell Fact. 8:14.
    • (2009) Microb. Cell Fact. , vol.8 , pp. 14
    • Castaldo, C.1
  • 17
    • 0942297972 scopus 로고    scopus 로고
    • Environmental stress responses in Lactobacillus: a review
    • De Angelis M, Gobbetti M. 2004. Environmental stress responses in Lactobacillus: a review. Proteomics 4:106-122.
    • (2004) Proteomics , vol.4 , pp. 106-122
    • De Angelis, M.1    Gobbetti, M.2
  • 18
    • 0036794846 scopus 로고    scopus 로고
    • In vitro adhesion specificity of indigenous lactobacilli within the avian intestinal tract
    • Edelman S, et al. 2002. In vitro adhesion specificity of indigenous lactobacilli within the avian intestinal tract. Appl. Environ. Microbiol. 68: 5155-5159.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5155-5159
    • Edelman, S.1
  • 19
    • 0029967327 scopus 로고    scopus 로고
    • Iron starvation causes release from the group A Streptococcus of the ADP-ribosylating protein called plasmin receptor or surface glyceraldehyde-3-phosphate-dehydrogenase
    • Eichenbaum Z, Green BD, Scott JR. 1996. Iron starvation causes release from the group A Streptococcus of the ADP-ribosylating protein called plasmin receptor or surface glyceraldehyde-3-phosphate-dehydrogenase. Infect. Immun. 64:1956-1960.
    • (1996) Infect. Immun. , vol.64 , pp. 1956-1960
    • Eichenbaum, Z.1    Green, B.D.2    Scott, J.R.3
  • 20
    • 0029824356 scopus 로고    scopus 로고
    • Identification of plasminogen in Matrigel and its activation by reconstitution of this basement membrane extract
    • Farina AR, et al. 1996. Identification of plasminogen in Matrigel and its activation by reconstitution of this basement membrane extract. Biotechniques 21:904-909.
    • (1996) Biotechniques , vol.21 , pp. 904-909
    • Farina, A.R.1
  • 21
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato D, et al. 2004. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect. Immun. 72:2160-2169.
    • (2004) Infect. Immun. , vol.72 , pp. 2160-2169
    • Granato, D.1
  • 22
    • 70450265562 scopus 로고    scopus 로고
    • Lactobacillus casei modulates the inflammation-coagulation interaction in a pneumococcal pneumonia experimental model
    • Haro C, Villena J, Zelaya H, Alvarez S, Aguero G. 2009. Lactobacillus casei modulates the inflammation-coagulation interaction in a pneumococcal pneumonia experimental model. J. Inflamm. (Lond.) 6:28.
    • (2009) J. Inflamm. (Lond.) , vol.6 , pp. 28
    • Haro, C.1    Villena, J.2    Zelaya, H.3    Alvarez, S.4    Aguero, G.5
  • 24
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious diseases
    • Henderson B, Martin A. 2011. Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious diseases. Infect. Immun. 79:3476-3491.
    • (2011) Infect. Immun. , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 25
    • 80054001998 scopus 로고    scopus 로고
    • Synthesis of capsular polysaccharide at the division septum of Streptococcus pneumoniae is dependent on a bacterial tyrosine kinase
    • Henriques MX, Rodrigues T, Carido M, Ferreira L, Filipe SR. 2011. Synthesis of capsular polysaccharide at the division septum of Streptococcus pneumoniae is dependent on a bacterial tyrosine kinase. Mol. Microbiol. 82:515-534.
    • (2011) Mol. Microbiol. , vol.82 , pp. 515-534
    • Henriques, M.X.1    Rodrigues, T.2    Carido, M.3    Ferreira, L.4    Filipe, S.R.5
  • 26
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: an intriguing mode of multitasking
    • Huberts DH, van der Klei IJ. 2010. Moonlighting proteins: an intriguing mode of multitasking. Biochim. Biophys. Acta 1803:520-525.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 520-525
    • Huberts, D.H.1    van der Klei, I.J.2
  • 27
    • 34247215679 scopus 로고    scopus 로고
    • Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen
    • Hurmalainen V, et al. 2007. Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen. Microbiology 153:1112-1122.
    • (2007) Microbiology , vol.153 , pp. 1112-1122
    • Hurmalainen, V.1
  • 28
    • 57449097178 scopus 로고    scopus 로고
    • Population heterogeneity of Lactobacillus plantarum WCFS1 microcolonies in response to and recovery from acid stress
    • Ingham CJ, Beerthuyzen M, van Hylckama Vlieg J. 2008. Population heterogeneity of Lactobacillus plantarum WCFS1 microcolonies in response to and recovery from acid stress. Appl. Environ. Microbiol. 74: 7750-7758.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 7750-7758
    • Ingham, C.J.1    Beerthuyzen, M.2    van Hylckama Vlieg, J.3
  • 29
    • 9944225262 scopus 로고    scopus 로고
    • Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins
    • Jeffery CJ. 2004. Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins. Curr. Opin. Struct. Biol. 14:663-668.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 663-668
    • Jeffery, C.J.1
  • 30
    • 70350134948 scopus 로고    scopus 로고
    • Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human-mucus binding protein
    • Kankainen M, et al. 2009. Comparative genomic analysis of Lactobacillus rhamnosus GG reveals pili containing a human-mucus binding protein. Proc. Natl. Acad. Sci. U. S. A. 106:17193-17198.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 17193-17198
    • Kankainen, M.1
  • 31
    • 77149147111 scopus 로고    scopus 로고
    • Lactic acid bacteria display on the cell surface cytosolic proteins that recognize yeast mannan
    • Katakura Y, Sano R, Hashimoto T, Ninomiya K, Shioya S. 2010. Lactic acid bacteria display on the cell surface cytosolic proteins that recognize yeast mannan. Appl. Microbiol. Biotechnol. 86:319-326.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 319-326
    • Katakura, Y.1    Sano, R.2    Hashimoto, T.3    Ninomiya, K.4    Shioya, S.5
  • 32
    • 44249099682 scopus 로고    scopus 로고
    • Cell surface Lactobacillus plantarum LA 318 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) adheres to human colonic mucin
    • Kinoshita H, et al. 2008. Cell surface Lactobacillus plantarum LA 318 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) adheres to human colonic mucin. J. Appl. Microbiol. 104:1667-1674.
    • (2008) J. Appl. Microbiol. , vol.104 , pp. 1667-1674
    • Kinoshita, H.1
  • 33
    • 12944325306 scopus 로고    scopus 로고
    • Bacterial metastasis: the host plasminogen system in bacterial invasion
    • Lähteenmäki K, Edelman S, Korhonen TK. 2005. Bacterial metastasis: the host plasminogen system in bacterial invasion. Trends Microbiol. 13: 79-85.
    • (2005) Trends Microbiol , vol.13 , pp. 79-85
    • Lähteenmäki, K.1    Edelman, S.2    Korhonen, T.K.3
  • 35
    • 79955436621 scopus 로고    scopus 로고
    • Exopolysaccharides of Lactobacillus rhamnosus GG form a protective shield against innate immune factors in the intestine
    • Lebeer S, Claes IJ, Verhoeven TL, Vanderleyden J, De Keersmaecker SC. 2011. Exopolysaccharides of Lactobacillus rhamnosus GG form a protective shield against innate immune factors in the intestine. Microb. Biotechnol. 4:368-374.
    • (2011) Microb. Biotechnol. , vol.4 , pp. 368-374
    • Lebeer, S.1    Claes, I.J.2    Verhoeven, T.L.3    Vanderleyden, J.4    De Keersmaecker, S.C.5
  • 37
    • 79955546828 scopus 로고    scopus 로고
    • Proteomic analysis of protein expression in Lactobacillus plantarum in response to alkaline stress
    • Lee K, Rho BS, Pi K, Kim HJ, Choi YJ. 2011. Proteomic analysis of protein expression in Lactobacillus plantarum in response to alkaline stress. J. Biotechnol. 153:1-7.
    • (2011) J. Biotechnol. , vol.153 , pp. 1-7
    • Lee, K.1    Rho, B.S.2    Pi, K.3    Kim, H.J.4    Choi, Y.J.5
  • 38
    • 0142091351 scopus 로고    scopus 로고
    • SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis
    • Lenz LL, Mohammadi S, Geissler A, Portnoy DA. 2003. SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 100:12432-12437.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12432-12437
    • Lenz, L.L.1    Mohammadi, S.2    Geissler, A.3    Portnoy, D.A.4
  • 39
    • 77951224520 scopus 로고    scopus 로고
    • Fluorescence microscopy demonstrates enhanced targeting of telavancin to the division septum of Staphylococcus aureus
    • Lunde CS, Rexer CH, Hartouni SR, Axt S, Benton BM. 2010. Fluorescence microscopy demonstrates enhanced targeting of telavancin to the division septum of Staphylococcus aureus. Antimicrob. Agents Chemother. 54:2198-2200.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2198-2200
    • Lunde, C.S.1    Rexer, C.H.2    Hartouni, S.R.3    Axt, S.4    Benton, B.M.5
  • 40
    • 33846410245 scopus 로고    scopus 로고
    • Functional phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv: rapid purification with high yield and purity
    • Mathur D, Garg LC. 2007. Functional phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv: rapid purification with high yield and purity. Protein Expr. Purif. 52:373-378.
    • (2007) Protein Expr. Purif. , vol.52 , pp. 373-378
    • Mathur, D.1    Garg, L.C.2
  • 41
    • 0029249889 scopus 로고
    • Specific and charge interactions mediate collagen recognition by oral lactobacilli
    • McGrady JA, Butcher WG, Beighton D, Switalski LM. 1995. Specific and charge interactions mediate collagen recognition by oral lactobacilli. J. Dent. Res. 74:649-657.
    • (1995) J. Dent. Res. , vol.74 , pp. 649-657
    • McGrady, J.A.1    Butcher, W.G.2    Beighton, D.3    Switalski, L.M.4
  • 42
    • 0027457724 scopus 로고
    • Binding of bacterial adhesins to rat glomerular mesangium in vivo
    • Miettinen A, et al. 1993. Binding of bacterial adhesins to rat glomerular mesangium in vivo. Kidney Int. 43:592-600.
    • (1993) Kidney Int , vol.43 , pp. 592-600
    • Miettinen, A.1
  • 43
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti P, Rifkin DB. 1993. Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev. 73:161-195.
    • (1993) Physiol. Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 44
    • 0034986066 scopus 로고    scopus 로고
    • pH- regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: purification, characterization, and cloning of the gene encoding this enzyme
    • Nelson D, et al. 2001. pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: purification, characterization, and cloning of the gene encoding this enzyme. J. Dent. Res. 80:371-377.
    • (2001) J. Dent. Res. , vol.80 , pp. 371-377
    • Nelson, D.1
  • 45
    • 77954374362 scopus 로고    scopus 로고
    • Genome sequence of Lactobacillus crispatus ST1
    • Ojala T, et al. 2010. Genome sequence of Lactobacillus crispatus ST1. J. Bacteriol. 192:3547-3548.
    • (2010) J. Bacteriol. , vol.192 , pp. 3547-3548
    • Ojala, T.1
  • 46
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • Pancholi V, Chhatwal GS. 2003. Housekeeping enzymes as virulence factors for pathogens. Int. J. Med. Microbiol. 293:391-401.
    • (2003) Int. J. Med. Microbiol. , vol.293 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 47
    • 0017660779 scopus 로고
    • Studies on the metabolism of the renal glomerular basement membrane Turnover measurements in the rat with the use of radiolabeled amino acids
    • Price RG, Spiro RG. 1977. Studies on the metabolism of the renal glomerular basement membrane. Turnover measurements in the rat with the use of radiolabeled amino acids. J. Biol. Chem. 252:8597-8602.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8597-8602
    • Price, R.G.1    Spiro, R.G.2
  • 48
    • 49549110708 scopus 로고    scopus 로고
    • Surface-bound proteins of Lactobacillus plantarum 423 that contribute to adhesion of Caco-2 cells and their role in competitive exclusion and displacement of Clostridium sporogenes and Enterococcus faecalis
    • Ramiah K, van Reenen CA, Dicks LM. 2008. Surface-bound proteins of Lactobacillus plantarum 423 that contribute to adhesion of Caco-2 cells and their role in competitive exclusion and displacement of Clostridium sporogenes and Enterococcus faecalis. Res. Microbiol. 159:470-475.
    • (2008) Res. Microbiol. , vol.159 , pp. 470-475
    • Ramiah, K.1    van Reenen, C.A.2    Dicks, L.M.3
  • 49
    • 0029011971 scopus 로고
    • Receptors for plasminogen and t-PA: an update
    • Redlitz A, Plow EF. 1995. Receptors for plasminogen and t-PA: an update. Baillieres Clin. Haematol. 8:313-327.
    • (1995) Baillieres Clin. Haematol. , vol.8 , pp. 313-327
    • Redlitz, A.1    Plow, E.F.2
  • 50
    • 57749189817 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of the fibrinolytic system
    • Rijken DC, Lijnen HR. 2009. New insights into the molecular mechanisms of the fibrinolytic system. J. Thromb. Haemost. 7:4-13.
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 4-13
    • Rijken, D.C.1    Lijnen, H.R.2
  • 51
    • 74749109630 scopus 로고    scopus 로고
    • Lactobacillus plantarum 299v surface-bound GAPDH: a new insight into enzyme cell walls location
    • Saad N, et al. 2009. Lactobacillus plantarum 299v surface-bound GAPDH: a new insight into enzyme cell walls location. J. Microbiol. Biotechnol. 19:1635-1643.
    • (2009) J. Microbiol. Biotechnol. , vol.19 , pp. 1635-1643
    • Saad, N.1
  • 52
    • 3342988044 scopus 로고    scopus 로고
    • Interaction of Dr adhesin with collagen type IV is a critical step in Escherichia coli renal persistence
    • Selvarangan R, et al. 2004. Interaction of Dr adhesin with collagen type IV is a critical step in Escherichia coli renal persistence. Infect. Immun. 72: 4827-4835.
    • (2004) Infect. Immun. , vol.72 , pp. 4827-4835
    • Selvarangan, R.1
  • 54
    • 77953923581 scopus 로고    scopus 로고
    • Lactobacillus jensenii surfaceassociated proteins inhibit Neisseria gonorrhoeae adherence to epithelial cells
    • Spurbeck RR, Arvidson CG. 2010. Lactobacillus jensenii surfaceassociated proteins inhibit Neisseria gonorrhoeae adherence to epithelial cells. Infect. Immun. 78:3103-3111.
    • (2010) Infect. Immun. , vol.78 , pp. 3103-3111
    • Spurbeck, R.R.1    Arvidson, C.G.2
  • 55
    • 0032829727 scopus 로고    scopus 로고
    • Cellular lysis in Bacillus subtilis; the affect of multiple extracellular protease deficiencies
    • Stephenson K, Bron S, Harwood CR. 1999. Cellular lysis in Bacillus subtilis; the affect of multiple extracellular protease deficiencies. Lett. Appl. Microbiol. 29:141-145.
    • (1999) Lett. Appl. Microbiol. , vol.29 , pp. 141-145
    • Stephenson, K.1    Bron, S.2    Harwood, C.R.3
  • 56
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa GS, et al. 2003. The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J. Immunol. 171:6690-6696.
    • (2003) J. Immunol. , vol.171 , pp. 6690-6696
    • Tjabringa, G.S.1
  • 57
    • 0025332745 scopus 로고
    • Epithelial basement membrane of mouse jejunum Evidence for laminin turnover along the entire crypt-villus axis
    • Trier JS, Allan CH, Abrahamson DR, Hagen SJ. 1990. Epithelial basement membrane of mouse jejunum. Evidence for laminin turnover along the entire crypt-villus axis. J. Clin. Invest. 86:87-95.
    • (1990) J. Clin. Invest. , vol.86 , pp. 87-95
    • Trier, J.S.1    Allan, C.H.2    Abrahamson, D.R.3    Hagen, S.J.4
  • 58
    • 0021954364 scopus 로고
    • Clinical application of inhibitors of fibrinolysis
    • Verstraete M. 1985. Clinical application of inhibitors of fibrinolysis. Drugs 29:236-261.
    • (1985) Drugs , vol.29 , pp. 236-261
    • Verstraete, M.1
  • 60
    • 0030003263 scopus 로고    scopus 로고
    • Interaction of Haemophilus influenzae with the mammalian extracellular matrix
    • Virkola R, et al. 1996. Interaction of Haemophilus influenzae with the mammalian extracellular matrix. J. Infect. Dis. 173:1137-1147.
    • (1996) J. Infect. Dis. , vol.173 , pp. 1137-1147
    • Virkola, R.1
  • 61
    • 34948857581 scopus 로고    scopus 로고
    • Identification of novel bacterial plasminogenbinding proteins in the human pathogen Mycobacterium tuberculosis
    • Xolalpa W, et al. 2007. Identification of novel bacterial plasminogenbinding proteins in the human pathogen Mycobacterium tuberculosis. Proteomics 7:3332-3341.
    • (2007) Proteomics , vol.7 , pp. 3332-3341
    • Xolalpa, W.1
  • 62
    • 80053578297 scopus 로고    scopus 로고
    • Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis
    • Yang CK, et al. 2011. Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis. J. Bacteriol. 193:5607-5615.
    • (2011) J. Bacteriol. , vol.193 , pp. 5607-5615
    • Yang, C.K.1
  • 63
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti M. 2005. The role of cathelicidins in the innate host defenses of mammals. Curr. Issues Mol. Biol. 7:179-196.
    • (2005) Curr. Issues Mol. Biol. , vol.7 , pp. 179-196
    • Zanetti, M.1


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