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Volumn 358, Issue , 2013, Pages 155-213

Bacterial moonlighting proteins and bacterial virulence

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; ADHESIN; ALDEHYDE DEHYDROGENASE; BACTERIAL PROTEIN; CELL PROTEIN; CHAPERONIN 60; CITRATE SYNTHASE; CPN 10 PROTEIN; CPN60 PROTEIN; CYTOCHROME C; EARLY PREGNANCY FACTOR; ENOLASE; FUMARATE HYDRATASE; GELSOLIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOGEN SYNTHASE KINASE 3BETA; GLYCOLYTIC ENZYME; HEAT SHOCK PROTEIN 70; HEXOKINASE; ISOCITRATE DEHYDROGENASE; LACTATE DEHYDROGENASE; PEPTIDYL PROLYL ISOMERASE; PHOSPHOGLYCERATE KINASE; QUINONE OXIDOREDUCTASE; STAT3 PROTEIN; SUCCINATE DEHYDROGENASE; THIOREDOXIN; THYMIDINE PHOSPHORYLASE; UNCLASSIFIED DRUG; XANTHINE OXIDASE;

EID: 84880153102     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/82_2011_188     Document Type: Article
Times cited : (108)

References (303)
  • 1
    • 0023689742 scopus 로고
    • Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG
    • Abou-Zeid C, Ratliff TL, Wiker HG, Harboe M, Bennedsen J, Rook GA (1988) Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG. Infect Immun 56:3046-3051
    • (1988) Infect Immun , vol.56 , pp. 3046-3051
    • Abou-Zeid, C.1    Ratliff, T.L.2    Wiker, H.G.3    Harboe, M.4    Bennedsen, J.5    Rook, G.A.6
  • 2
    • 0037031133 scopus 로고    scopus 로고
    • Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding
    • Allignet J, England P, Old I El Solh N (2001) Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding. FEMS Microbiol Lett 213:193-197
    • (2001) FEMS Microbiol Lett , vol.213 , pp. 193-197
    • Allignet, J.1    England, P.2    Old, I.3    El Solh, N.4
  • 3
    • 1842301085 scopus 로고    scopus 로고
    • 3-phosphoglycerate kinase: A glycolytic enzyme protein present in the cell wall of Candida albicans
    • Alloush HM, López-Ribot JL, Masten BJ, Chaffin WL (1997) 3-phosphoglycerate kinase: a glycolytic enzyme protein present in the cell wall of Candida albicans. Microbiology 143: 321-330
    • (1997) Microbiology , vol.143 , pp. 321-330
    • Alloush, H.M.1    López-Ribot, J.L.2    Masten, B.J.3    Chaffin, W.L.4
  • 4
    • 0029972134 scopus 로고    scopus 로고
    • Phagocytosed live Listeria monocytogenes influences Rab5-regulated in vitro phagosomeendosome fusion
    • Alvarez-Dominguez C, Barbieri AM, Berón W, Wandinger-Ness A, Stahl PD (1996) Phagocytosed live Listeria monocytogenes influences Rab5-regulated in vitro phagosomeendosome fusion. J Biol Chem 271:13834-13843
    • (1996) J Biol Chem , vol.271 , pp. 13834-13843
    • Alvarez-Dominguez, C.1    Barbieri, A.M.2    Berón, W.3    Wandinger-Ness, A.4    Stahl, P.D.5
  • 7
    • 0037077685 scopus 로고    scopus 로고
    • Species specificity of the cytokine function of phosphoglucose isomerase
    • Amraei M, Nabi IR (2002) Species specificity of the cytokine function of phosphoglucose isomerase. FEBS Lett 525:151-155
    • (2002) FEBS Lett , vol.525 , pp. 151-155
    • Amraei, M.1    Nabi, I.R.2
  • 9
    • 34250333853 scopus 로고    scopus 로고
    • PH-dependent 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) pH-dependent 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
  • 10
    • 78649498398 scopus 로고    scopus 로고
    • Paenibacillus larvae enolase as a virulence factor in honeybee larvae infection
    • Antúnez K, Anido M, Arredondo D, Evans JD, Zunino P (2011) Paenibacillus larvae enolase as a virulence factor in honeybee larvae infection. Vet Microbiol 87:83-89
    • (2011) Vet Microbiol , vol.87 , pp. 83-89
    • Antúnez, K.1    Anido, M.2    Arredondo, D.3    Evans, J.D.4    Zunino, P.5
  • 11
    • 4444254836 scopus 로고    scopus 로고
    • Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition
    • Asquith KL, Baleato RM, McLaughlin EA, Nixon B, Aitken RJ (2004) Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition. J Cell Sci 117:3645-3657
    • (2004) J Cell Sci , vol.117 , pp. 3645-3657
    • Asquith, K.L.1    Baleato, R.M.2    McLaughlin, E.A.3    Nixon, B.4    Aitken, R.J.5
  • 12
    • 0036164147 scopus 로고    scopus 로고
    • Novel antigens of Helicobacter pylori correspond to ulcer-related antibody pattern of sera from infected patients
    • Atanassov C, Pezennec L, d'Alayer J, Grollier G, Picard B, Fauchère JL (2002) Novel antigens of Helicobacter pylori correspond to ulcer-related antibody pattern of sera from infected patients. J Clin Microbiol 40:547-552
    • (2002) J Clin Microbiol , vol.40 , pp. 547-552
    • Atanassov, C.1    Pezennec, L.2    D'Alayer, J.3    Grollier, G.4    Picard, B.5    Fauchère, J.L.6
  • 13
    • 55849124698 scopus 로고    scopus 로고
    • The interaction of Streptococcus pneumoniae with plasmin mediates transmigration across endothelial and epithelial monolayers by intercellular junction cleavage
    • Attali C, Durmort C, Vernet T, Di Guilmi AM (2008) The interaction of Streptococcus pneumoniae with plasmin mediates transmigration across endothelial and epithelial monolayers by intercellular junction cleavage. Infect Immun 76:5350-5356
    • (2008) Infect Immun , vol.76 , pp. 5350-5356
    • Attali, C.1    Durmort, C.2    Vernet, T.3    Di Guilmi, A.M.4
  • 14
    • 33646050050 scopus 로고    scopus 로고
    • 60-kDa heat shock protein of Chlamydia pneumoniae promotes a T helper type 1 immune response through IL-12/IL-23 production in monocyte-derived dendritic cells
    • Ausiello CM, Fedele G, Palazzo R, Spensieri F, Ciervo A, Cassone A (2006) 60-kDa heat shock protein of Chlamydia pneumoniae promotes a T helper type 1 immune response through IL-12/IL-23 production in monocyte-derived dendritic cells. Microbes Infect 8:714-720
    • (2006) Microbes Infect , vol.8 , pp. 714-720
    • Ausiello, C.M.1    Fedele, G.2    Palazzo, R.3    Spensieri, F.4    Ciervo, A.5    Cassone, A.6
  • 15
    • 33947360705 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 infection of human CD4+ T cells by microbial HSP70 and the peptide epitope 407-426
    • Babaahmady K, Oehlmann W, Singh M, Lehner T (2007) Inhibition of human immunodeficiency virus type 1 infection of human CD4+ T cells by microbial HSP70 and the peptide epitope 407-426. J Virol 81:3354-3360
    • (2007) J Virol , vol.81 , pp. 3354-3360
    • Babaahmady, K.1    Oehlmann, W.2    Singh, M.3    Lehner, T.4
  • 16
    • 46449125693 scopus 로고    scopus 로고
    • The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin
    • Balasubramanian S, Kannan TR, Baseman JB (2008) The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin. Infect Immun 76: 3116-3123
    • (2008) Infect Immun , vol.76 , pp. 3116-3123
    • Balasubramanian, S.1    Kannan, T.R.2    Baseman, J.B.3
  • 17
    • 69049083513 scopus 로고    scopus 로고
    • Amino acid changes in elongation factor Tu of Mycoplasma pneumoniae and Mycoplasma genitalium influence fibronectin binding
    • Balasubramanian S, Kannan TR, Hart PJ, Baseman JB (2009) Amino acid changes in elongation factor Tu of Mycoplasma pneumoniae and Mycoplasma genitalium influence fibronectin binding. Infect Immun 77:3533-3541
    • (2009) Infect Immun , vol.77 , pp. 3533-3541
    • Balasubramanian, S.1    Kannan, T.R.2    Hart, P.J.3    Baseman, J.B.4
  • 18
  • 19
    • 17844399575 scopus 로고    scopus 로고
    • The secreted peptidyl prolyl cis, trans-isomerase HP0175 of Helicobacter pylori induces apoptosis of gastric epithelial cells in a TLR4- and apoptosis signal-regulating kinase 1-dependent manner
    • Basak C, Pathak SK, Bhattacharyya A, Pathak S, Basu J, Kundu M (2005) The secreted peptidyl prolyl cis, trans-isomerase HP0175 of Helicobacter pylori induces apoptosis of gastric epithelial cells in a TLR4- and apoptosis signal-regulating kinase 1-dependent manner. J Immunol 174:5672-5680
    • (2005) J Immunol , vol.174 , pp. 5672-5680
    • Basak, C.1    Pathak, S.K.2    Bhattacharyya, A.3    Pathak, S.4    Basu, J.5    Kundu, M.6
  • 20
    • 0037144808 scopus 로고    scopus 로고
    • CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes
    • Becker T, Hartl FU, Wieland F (2002) CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J Cell Biol 158:1277-1285
    • (2002) J Cell Biol , vol.158 , pp. 1277-1285
    • Becker, T.1    Hartl, F.U.2    Wieland, F.3
  • 21
    • 0036266052 scopus 로고    scopus 로고
    • Identification of novel adhesins from Group B Streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding
    • Beckmann C, Waggoner JD, Harris TO, Tamura GS, Rubens CE (2002) Identification of novel adhesins from Group B Streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding. Infect Immun 70:2869-2876
    • (2002) Infect Immun , vol.70 , pp. 2869-2876
    • Beckmann, C.1    Waggoner, J.D.2    Harris, T.O.3    Tamura, G.S.4    Rubens, C.E.5
  • 23
    • 0034931519 scopus 로고    scopus 로고
    • A-enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S (2001) A-enolase 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
  • 24
    • 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, Frank R, Bracht D, Chhatwal GS, Hammerschmidt S (2003) Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol Microbiol 49:411-423
    • (2003) Mol Microbiol , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6    Hammerschmidt, S.7
  • 25
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann S, Rohde M, Hammerschmidt S (2004) Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect Immun 72:2416-2419
    • (2004) Infect Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 26
    • 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, Granato D, Pridmore RD, Marvin-Guy LF, Donnicola D, Corthésy-Theulaz IE (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    Granato, D.2    Pridmore, R.D.3    Marvin-Guy, L.F.4    Donnicola, D.5    Corthésy-Theulaz, I.E.6
  • 28
    • 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
  • 29
    • 77953893605 scopus 로고    scopus 로고
    • Listeria monocytogenes internalin and E-cadherin: From bench to bedside
    • a003087
    • Bonazzi M, Lecuit M, Cossart P (2009) Listeria monocytogenes internalin and E-cadherin: from bench to bedside. Cold Spring Harb Perspect Biol 1:a003087
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Bonazzi, M.1    Lecuit, M.2    Cossart, P.3
  • 30
    • 67650094733 scopus 로고    scopus 로고
    • Chlamydial heat shock protein 60 induces acute pulmonary inflammation in mice via the toll-like receptor 4- and MyD88-dependent pathway
    • Bulut Y, Shimada K, Wong MH, Chen S, Gray P, Alsabeh R, Doherty TM, Crother TR, Arditi M (2009) Chlamydial heat shock protein 60 induces acute pulmonary inflammation in mice via the toll-like receptor 4- and MyD88-dependent pathway. Infect Immun 77:2683-2690
    • (2009) Infect Immun , vol.77 , pp. 2683-2690
    • Bulut, Y.1    Shimada, K.2    Wong, M.H.3    Chen, S.4    Gray, P.5    Alsabeh, R.6    Doherty, T.M.7    Crother, T.R.8    Arditi, M.9
  • 32
    • 78649979695 scopus 로고    scopus 로고
    • Listeria monocytogenes uses Listeria adhesion protein (LAP) to promote bacterial transepithelial translocation and induces expression of LAP receptor Hsp60
    • Burkholder KM, Bhunia AK (2010) Listeria monocytogenes uses Listeria adhesion protein (LAP) to promote bacterial transepithelial translocation and induces expression of LAP receptor Hsp60. Infect Immun 78:5062-5073
    • (2010) Infect Immun , vol.78 , pp. 5062-5073
    • Burkholder, K.M.1    Bhunia, A.K.2
  • 33
    • 19544389507 scopus 로고    scopus 로고
    • Phosphoglycerate kinase inhibits epithelial cell invasion by group B streptococci
    • Burnham C-AD, Shokoples SE, Tyrrell GJ (2005) Phosphoglycerate kinase inhibits epithelial cell invasion by group B streptococci. Microbe Pathog 38:189-200
    • (2005) Microbe Pathog , vol.38 , pp. 189-200
    • Burnham, C.-A.D.1    Shokoples, S.E.2    Tyrrell, G.J.3
  • 34
  • 35
    • 0028865899 scopus 로고
    • Endocrine peptides 'moonlighting' as immune modulators: Roles for somatostatin and GH-releasing factor
    • Campbell RM, Scanes CG (1995) Endocrine peptides 'moonlighting' as immune modulators: roles for somatostatin and GH-releasing factor. J Endocrinol 147:383-396
    • (1995) J Endocrinol , vol.147 , pp. 383-396
    • Campbell, R.M.1    Scanes, C.G.2
  • 37
    • 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, Centanni M, Fiori J, Biagi E, Turroni S, Orrico C, Bergmann S, Hammerschmidt S, Brigidi P (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    Centanni, M.2    Fiori, J.3    Biagi, E.4    Turroni, S.5    Orrico, C.6    Bergmann, S.7    Hammerschmidt, S.8    Brigidi, P.9
  • 38
    • 79952830765 scopus 로고    scopus 로고
    • A-Enolase: A promising therapeutic and diagnostic tumor target
    • Epub ahead of print
    • Capello M, Ferri-Borgogno S, Cappello P, Novelli F (2011) a-Enolase: a promising therapeutic and diagnostic tumor target. FEBS J [Epub ahead of print]
    • (2011) FEBS J
    • Capello, M.1    Ferri-Borgogno, S.2    Cappello, P.3    Novelli, F.4
  • 41
    • 77953952682 scopus 로고    scopus 로고
    • Comparison of the moonlighting actions of the two highly homologous chaperonin 60 proteins of Mycobacterium tuberculosis
    • Cehovin A, Coates AR, Riffo-Vasquez Y, Tormay P, Botanch C, Altare F, Henderson B (2010) Comparison of the moonlighting actions of the two highly homologous chaperonin 60 proteins of Mycobacterium tuberculosis. Infect Immun 78:3196-3206
    • (2010) Infect Immun , vol.78 , pp. 3196-3206
    • Cehovin, A.1    Coates, A.R.2    Riffo-Vasquez, Y.3    Tormay, P.4    Botanch, C.5    Altare, F.6    Henderson, B.7
  • 44
    • 70350461453 scopus 로고    scopus 로고
    • The purified and recombinant Legionella pneumophila chaperonin alters mitochondrial trafficking and microfilament organization
    • Chong A, Lima CA, Allan DS, Nasrallah GK, Garduño RA (2009) The purified and recombinant Legionella pneumophila chaperonin alters mitochondrial trafficking and microfilament organization. Infect Immun 77:4724-4739
    • (2009) Infect Immun , vol.77 , pp. 4724-4739
    • Chong, A.1    Lima, C.A.2    Allan, D.S.3    Nasrallah, G.K.4    Garduño, R.A.5
  • 45
    • 0034756244 scopus 로고    scopus 로고
    • Pathogenicity of Legionella pneumophila
    • Cianciotto NP (2001) Pathogenicity of Legionella pneumophila. Int J Med Microbiol 291331-291343
    • (2001) Int J Med Microbiol , pp. 291331-291343
    • Cianciotto, N.P.1
  • 47
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • Copley SD (2003) Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr Opin Chem Biol 7:265-272
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 49
    • 77951638914 scopus 로고    scopus 로고
    • Basal release of ATP: An autocrine-paracrine mechanism for cell regulation
    • re1
    • Corriden R, Insel PA (2010) Basal release of ATP: an autocrine-paracrine mechanism for cell regulation. Sci Signal 3:re1
    • (2010) Sci Signal , vol.3
    • Corriden, R.1    Insel, P.A.2
  • 51
    • 77955369669 scopus 로고    scopus 로고
    • The structure and function of serum opacity factor: A unique streptococcal virulence determinant that targets high-density lipoproteins
    • Courtney HS, Pownall HJ (2010) The structure and function of serum opacity factor: a unique streptococcal virulence determinant that targets high-density lipoproteins. J Biomed Biotechnol 2010:956071
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 956071
    • Courtney, H.S.1    Pownall, H.J.2
  • 52
    • 67649700878 scopus 로고    scopus 로고
    • Serum opacity factor is a streptococcal receptor for the extracellular matrix protein fibulin-1
    • Courtney HS, Li Y, Twal WO, Argraves WS (2009) Serum opacity factor is a streptococcal receptor for the extracellular matrix protein fibulin-1. J Biol Chem 284:12966-12971
    • (2009) J Biol Chem , vol.284 , pp. 12966-12971
    • Courtney, H.S.1    Li, Y.2    Twal, W.O.3    Argraves, W.S.4
  • 53
    • 0037344772 scopus 로고    scopus 로고
    • Candida albicans binds human plasminogen: Identification of eight plasminogen-binding proteins
    • Crowe JD, Sievwright IK, Auld GC, Moore NR, Gow NA, Booth NA (2003) Candida albicans binds human plasminogen: identification of eight plasminogen-binding proteins. Mol Microbiol 47:1637-1651
    • (2003) Mol Microbiol , vol.47 , pp. 1637-1651
    • Crowe, J.D.1    Sievwright, I.K.2    Auld, G.C.3    Moore, N.R.4    Gow, N.A.5    Booth, N.A.6
  • 54
    • 7244251610 scopus 로고    scopus 로고
    • Heat shock protein 60 from Chlamydia pneumoniae elicits an unusual set of inflammatory responses via toll-like receptor 2 and 4 in vivo
    • Da Costa CU, Wantia N, Kirschning CJ, Busch DH, Rodriguez N, Wagner H, Miethke T (2004) Heat shock protein 60 from Chlamydia pneumoniae elicits an unusual set of inflammatory responses via toll-like receptor 2 and 4 in vivo. Eur J Immunol 34:2874-2884
    • (2004) Eur J Immunol , vol.34 , pp. 2874-2884
    • Da Costa, C.U.1    Wantia, N.2    Kirschning, C.J.3    Busch, D.H.4    Rodriguez, N.5    Wagner, H.6    Miethke, T.7
  • 55
    • 33244462633 scopus 로고    scopus 로고
    • Neuronal surface glycolytic enzymes are autoantigen targets in post-streptococcal autoimmune CNS disease
    • Dale RC, Candler PM, Church AJ, Wait R, Pocock JM, Giovannoni G (2006) Neuronal surface glycolytic enzymes are autoantigen targets in post-streptococcal autoimmune CNS disease. J Neuroimmunol 172:187-197
    • (2006) J Neuroimmunol , vol.172 , pp. 187-197
    • Dale, R.C.1    Candler, P.M.2    Church, A.J.3    Wait, R.4    Pocock, J.M.5    Giovannoni, G.6
  • 56
    • 0036434714 scopus 로고    scopus 로고
    • Elongation factor Tu and E1 b subunit of pyruvate dehydrogenase complex act as fibronectin-binding proteins in Mycoplasma pneumonia
    • Dallo SF, Kannan TR, Blaylock MW, Baseman JB (2002) Elongation factor Tu and E1 b subunit of pyruvate dehydrogenase complex act as fibronectin-binding proteins in Mycoplasma pneumonia. Mol Microbiol 46:1041-1051
    • (2002) Mol Microbiol , vol.46 , pp. 1041-1051
    • Dallo, S.F.1    Kannan, T.R.2    Blaylock, M.W.3    Baseman, J.B.4
  • 59
    • 77953102683 scopus 로고    scopus 로고
    • Pathogenesis of genital tract disease due to Chlamydia trachomatis
    • Darville T, Hiltke TJ (2010) Pathogenesis of genital tract disease due to Chlamydia trachomatis. J Infect Dis 201(2):S114-S125
    • (2010) J Infect Dis , vol.201 , Issue.2
    • Darville, T.1    Hiltke, T.J.2
  • 60
    • 25844438419 scopus 로고    scopus 로고
    • Acid and bile-salt stress of enteropathogenic Escherichia coli enhances adhesion to epithelial cells and alters glycolipid receptor binding specificity
    • de Jesus MC, Urban AA, Marasigan ME, Barnett Foster DE (2005) Acid and bile-salt stress of enteropathogenic Escherichia coli enhances adhesion to epithelial cells and alters glycolipid receptor binding specificity. J Infect Dis 192:1430-1440
    • (2005) J Infect Dis , vol.192 , pp. 1430-1440
    • De Jesus, M.C.1    Urban, A.A.2    Marasigan, M.E.3    Barnett Foster, D.E.4
  • 61
    • 77749264327 scopus 로고    scopus 로고
    • Xanthomonas oryzae pv. oryzae XKK.12 contains an AroQgamma chorismate mutase that is involved in rice virulence
    • Degrassi G, Devescovi G, Bigirimana J, Venturi V (2010) Xanthomonas oryzae pv. oryzae XKK.12 contains an AroQgamma chorismate mutase that is involved in rice virulence. Phytopathology 100:262-270
    • (2010) Phytopathology , vol.100 , pp. 262-270
    • Degrassi, G.1    Devescovi, G.2    Bigirimana, J.3    Venturi, V.4
  • 62
    • 0346881417 scopus 로고    scopus 로고
    • Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci
    • Derbise A, Song YP, Parikh S, Fischetti VA, Pancholi V (2004) Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci. Infect Immun 72:94-105
    • (2004) Infect Immun , vol.72 , pp. 94-105
    • Derbise, A.1    Song, Y.P.2    Parikh, S.3    Fischetti, V.A.4    Pancholi, V.5
  • 63
    • 0034807818 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is negatively regulated by ADP-ribosylation in the fungus Phycomyces blakesleeanus
    • Deveze-Alvarez M, García-Soto J, Martínez-Cadena G (2001) Glyceraldehyde-3-phosphate dehydrogenase is negatively regulated by ADP-ribosylation in the fungus Phycomyces blakesleeanus. Microbiology 147:2579-2584
    • (2001) Microbiology , vol.147 , pp. 2579-2584
    • Deveze-Alvarez, M.1    García-Soto, J.2    Martínez-Cadena, G.3
  • 64
    • 0026795982 scopus 로고
    • Nitric oxide causes ADP-ribosylation and inhibition of glyceraldehyde-3-phosphate dehydrogenase
    • Dimmeler S, Lottspeich F, Brüne B (1992) Nitric oxide causes ADP-ribosylation and inhibition of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 267:16771-16774
    • (1992) J Biol Chem , vol.267 , pp. 16771-16774
    • Dimmeler, S.1    Lottspeich, F.2    Brüne, B.3
  • 66
    • 62149142455 scopus 로고    scopus 로고
    • Chaperonin 10 as an endothelial-derived differentiation factor: Role of glycogen synthase kinase-3
    • Dobocan MC, Sadvakassova G, Congote LF (2009) Chaperonin 10 as an endothelial-derived differentiation factor: role of glycogen synthase kinase-3. J Cell Physiol 219:470-476
    • (2009) J Cell Physiol , vol.219 , pp. 470-476
    • Dobocan, M.C.1    Sadvakassova, G.2    Congote, L.F.3
  • 67
    • 0042337199 scopus 로고    scopus 로고
    • Surface localized heat shock protein 20 (HslV) of Helicobacter pylori
    • Du RJ, Ho B (2003) Surface localized heat shock protein 20 (HslV) of Helicobacter pylori. Helicobacter 8:257-267
    • (2003) Helicobacter , vol.8 , pp. 257-267
    • Du, R.J.1    Ho, B.2
  • 68
    • 31544449974 scopus 로고    scopus 로고
    • Identification of the major outer membrane proteins of Aeromonas salmonicida
    • Ebanks RO, Goguen M, McKinnon S, Pinto DM, Ross NW (2005) Identification of the major outer membrane proteins of Aeromonas salmonicida. Dis Aquat Organ 68:29-38
    • (2005) Dis Aquat Organ , vol.68 , pp. 29-38
    • Ebanks, R.O.1    Goguen, M.2    McKinnon, S.3    Pinto, D.M.4    Ross, N.W.5
  • 69
    • 0033103020 scopus 로고    scopus 로고
    • Surface bound plasmin promotes migration of Streptococcus pneumoniae through reconstituted basement membranes
    • Eberhard T, Kronvall G, Ullberg M (1999) Surface bound plasmin promotes migration of Streptococcus pneumoniae through reconstituted basement membranes. Microb Pathog 26: 175-181
    • (1999) Microb Pathog , vol.26 , pp. 175-181
    • Eberhard, T.1    Kronvall, G.2    Ullberg, M.3
  • 70
    • 34249332380 scopus 로고    scopus 로고
    • Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: Interaction of the extracellular enzyme with human plasminogen and fibrinogen
    • Egea L, Aguilera L, Giménez R, Sorolla MA, Aguilar J, Badía J, Baldoma L (2007) Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human plasminogen and fibrinogen. Int J Biochem Cell Biol 39:1190-1203
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1190-1203
    • Egea, L.1    Aguilera, L.2    Giménez, R.3    Sorolla, M.A.4    Aguilar, J.5    Badía, J.6    Baldoma, L.7
  • 71
    • 33746099650 scopus 로고    scopus 로고
    • Protein aggregation in crowded environments
    • Ellis RJ, Minton AP (2006) Protein aggregation in crowded environments. Biol Chem 387:485-497
    • (2006) Biol Chem , vol.387 , pp. 485-497
    • Ellis, R.J.1    Minton, A.P.2
  • 72
    • 3042533736 scopus 로고    scopus 로고
    • A 29.5 kDa heat-modifiable major outer membrane protein of Rickettsia prowazekii, putative virulence factor, is a peptidyl-prolyl cis/trans isomerase
    • Emelyanov VV, Loukianov EV (2004) A 29.5 kDa heat-modifiable major outer membrane protein of Rickettsia prowazekii, putative virulence factor, is a peptidyl-prolyl cis/trans isomerase. IUBMB Life 56:215-219
    • (2004) IUBMB Life , vol.56 , pp. 215-219
    • Emelyanov, V.V.1    Loukianov, E.V.2
  • 73
    • 0026642506 scopus 로고
    • A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus
    • Ensgraber M, Loos M (1992) A 66-kilodalton heat shock protein of Salmonella typhimurium is responsible for binding of the bacterium to intestinal mucus. Infect Immun 60:3072-3078
    • (1992) Infect Immun , vol.60 , pp. 3072-3078
    • Ensgraber, M.1    Loos, M.2
  • 74
    • 20444478000 scopus 로고    scopus 로고
    • Cloning, characterization and DNA immunization of an Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH)
    • Erttmann KD, Kleensang A, Schneider E, Hammerschmidt S, Büttner DW, Gallin M (2005) Cloning, characterization and DNA immunization of an Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH). Biochim Biophys Acta 1741:85-94
    • (2005) Biochim Biophys Acta , vol.1741 , pp. 85-94
    • Erttmann, K.D.1    Kleensang, A.2    Schneider, E.3    Hammerschmidt, S.4    Büttner, D.W.5    Gallin, M.6
  • 75
    • 0030637548 scopus 로고    scopus 로고
    • Subcellular localization of the 65-kDa heat shock protein in mycobacteria by immunoblotting and immunogold ultracytochemistry
    • Esaguy N, Aguas AP (1997) Subcellular localization of the 65-kDa heat shock protein in mycobacteria by immunoblotting and immunogold ultracytochemistry. J Submicrosc Cytol Pathol 29:85-90
    • (1997) J Submicrosc Cytol Pathol , vol.29 , pp. 85-90
    • Esaguy, N.1    Aguas, A.P.2
  • 76
    • 53449101619 scopus 로고    scopus 로고
    • Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis
    • Esgleas M, Li Y, Hancock MA, Harel J, Dubreuil JD, Gottschalk M (2008) Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis. Microbiology 154:2668-2679
    • (2008) Microbiology , vol.154 , pp. 2668-2679
    • Esgleas, M.1    Li, Y.2    Hancock, M.A.3    Harel, J.4    Dubreuil, J.D.5    Gottschalk, M.6
  • 77
    • 70349328536 scopus 로고    scopus 로고
    • The complex biology of autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and its receptor, the gp78/AMFR E3 ubiquitin ligase
    • Fairbank M, St-Pierre P, Nabi IR (2009) The complex biology of autocrine motility factor/phosphoglucose isomerase (AMF/PGI) and its receptor, the gp78/AMFR E3 ubiquitin ligase. Mol Biosyst 5:793-801
    • (2009) Mol Biosyst , vol.5 , pp. 793-801
    • Fairbank, M.1    St-Pierre, P.2    Nabi, I.R.3
  • 79
    • 75749099328 scopus 로고    scopus 로고
    • Discovery and characterization of cadherin domains in Saccharophagus degradans 2-40
    • Fraiberg M, Borovok I, Weiner RM, Lamed R (2010) Discovery and characterization of cadherin domains in Saccharophagus degradans 2-40. J Bacteriol 192:1066-1074
    • (2010) J Bacteriol , vol.192 , pp. 1066-1074
    • Fraiberg, M.1    Borovok, I.2    Weiner, R.M.3    Lamed, R.4
  • 80
    • 84892934043 scopus 로고
    • Moonlighting molecules
    • Freedman R (1978) Moonlighting molecules. New Sci 79:560-562
    • (1978) New Sci , vol.79 , pp. 560-562
    • Freedman, R.1
  • 81
    • 0027472869 scopus 로고
    • Mycobacterial 65-kD heat shock protein induces release of proinflammatory cytokines from human monocytic cells
    • Friedland JS, Shattock R, Remick DG, Griffin GE (1993) Mycobacterial 65-kD heat shock protein induces release of proinflammatory cytokines from human monocytic cells. Clin Exp Immunol 91:58-62
    • (1993) Clin Exp Immunol , vol.91 , pp. 58-62
    • Friedland, J.S.1    Shattock, R.2    Remick, D.G.3    Griffin, G.E.4
  • 82
    • 0031888740 scopus 로고    scopus 로고
    • GroEL heat shock protein of Haemophilus ducreyi: Association with cell surface and capacity to bind to eukaryotic cells
    • Frisk A, Ison CA, Lagergård T (1998) GroEL heat shock protein of Haemophilus ducreyi: association with cell surface and capacity to bind to eukaryotic cells. Infect Immun 66: 1252-1257
    • (1998) Infect Immun , vol.66 , pp. 1252-1257
    • Frisk, A.1    Ison, C.A.2    Lagergård, T.3
  • 83
    • 79955839745 scopus 로고    scopus 로고
    • Autocrine motility factor/phosphoglucose isomerase regulates ER stress and cell death through control of ER calcium release
    • Epub ahead of print
    • Fu M, Li L, Albrecht T, Johnson JD, Kojic LD, Nabi IR (2011) Autocrine motility factor/phosphoglucose isomerase regulates ER stress and cell death through control of ER calcium release. Cell Death Differ [Epub ahead of print]
    • (2011) Cell Death Differ
    • Fu, M.1    Li, L.2    Albrecht, T.3    Johnson, J.D.4    Kojic, L.D.5    Nabi, I.R.6
  • 84
    • 67650463104 scopus 로고    scopus 로고
    • Phosphoglucose isomerase/autocrine motility factor mediates epithelial and mesenchymal phenotype conversions in breast cancer
    • Funasaka T, Hogan V, Raz A (2009) Phosphoglucose isomerase/autocrine motility factor mediates epithelial and mesenchymal phenotype conversions in breast cancer. Cancer Res 69:5349-5356
    • (2009) Cancer Res , vol.69 , pp. 5349-5356
    • Funasaka, T.1    Hogan, V.2    Raz, A.3
  • 85
    • 69949148010 scopus 로고    scopus 로고
    • Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and alpha-(1->3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans
    • Furuya H, Ikeda R (2009) Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and alpha-(1>3)- mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans. Microbiology 155:2707-2713
    • (2009) Microbiology , vol.155 , pp. 2707-2713
    • Furuya, H.1    Ikeda, R.2
  • 87
    • 0031692318 scopus 로고    scopus 로고
    • Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model
    • Garduño RA, Garduño E, Hoffman PS (1998b) Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model. Infect Immun 66:4602-4610
    • (1998) Infect Immun , vol.66 , pp. 4602-4610
    • Garduño, R.A.1    Garduño, E.2    Hoffman, P.S.3
  • 88
    • 0029995819 scopus 로고    scopus 로고
    • Cloning, sequencing and functional overexpression of the Streptococcus equisimilis H46A gapC gene encoding a glyceraldehyde-3-phosphate dehydrogenase that also functions as a plasmin(ogen)-binding protein. Purification and biochemical characterization of the protein
    • Gase K, Gase A, Schirmer H, Malke H (1996) Cloning, sequencing and functional overexpression of the Streptococcus equisimilis H46A gapC gene encoding a glyceraldehyde-3-phosphate dehydrogenase that also functions as a plasmin(ogen)-binding protein. Purification and biochemical characterization of the protein. Eur J Biochem 239:42-51
    • (1996) Eur J Biochem , vol.239 , pp. 42-51
    • Gase, K.1    Gase, A.2    Schirmer, H.3    Malke, H.4
  • 90
    • 0345791527 scopus 로고    scopus 로고
    • Helicobacter pylori heat shock protein 60 mediates interleukin-6 production by macrophages via a toll-like receptor (TLR)-2-, TLR-4-, and myeloid differentiation factor 88-independent mechanism
    • Gobert AP, Bambou JC, Werts C, Balloy V, Chignard M, Moran AP, Ferrero RL (2004) Helicobacter pylori heat shock protein 60 mediates interleukin-6 production by macrophages via a toll-like receptor (TLR)-2-, TLR-4-, and myeloid differentiation factor 88-independent mechanism. J Biol Chem 279:245-250
    • (2004) J Biol Chem , vol.279 , pp. 245-250
    • Gobert, A.P.1    Bambou, J.C.2    Werts, C.3    Balloy, V.4    Chignard, M.5    Moran, A.P.6    Ferrero, R.L.7
  • 91
    • 58149182885 scopus 로고    scopus 로고
    • Histoplasma capsulatum cyclophilin A mediates attachment to dendritic cell VLA-5
    • Gomez FJ, Pilcher-Roberts R, Alborzi A, Newman SL (2008) Histoplasma capsulatum cyclophilin A mediates attachment to dendritic cell VLA-5. J Immunol 181:7106-7114
    • (2008) J Immunol , vol.181 , pp. 7106-7114
    • Gomez, F.J.1    Pilcher-Roberts, R.2    Alborzi, A.3    Newman, S.L.4
  • 92
    • 0032438164 scopus 로고    scopus 로고
    • Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans
    • Goulhen F, Hafezi A, Uitto VJ, Hinode D, Nakamura R, Grenier D, Mayrand D (1998) Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans. Infect Immun 66:5307-5313
    • (1998) Infect Immun , vol.66 , pp. 5307-5313
    • Goulhen, F.1    Hafezi, A.2    Uitto, V.J.3    Hinode, D.4    Nakamura, R.5    Grenier, D.6    Mayrand, D.7
  • 93
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray MW, Burger G, Lang BF (1999) Mitochondrial evolution. Science 283:1476-1481
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 94
    • 79952036205 scopus 로고    scopus 로고
    • Protein misfolding and cellular stress: An overview
    • Gregersen N, Bross P (2010) Protein misfolding and cellular stress: an overview. Methods Mol Biol 648:3-23
    • (2010) Methods Mol Biol , vol.648 , pp. 3-23
    • Gregersen, N.1    Bross, P.2
  • 96
    • 77954383542 scopus 로고    scopus 로고
    • Functional dissection of a trigger enzyme: Mutations of the Bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties
    • Gunka K, Newman JA, Commichau FM, Herzberg C, Rodrigues C, Hewitt L, Lewis RJ, Stülke J (2010) Functional dissection of a trigger enzyme: mutations of the Bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties. J Mol Biol 400:815-827
    • (2010) J Mol Biol , vol.400 , pp. 815-827
    • Gunka, K.1    Newman, J.A.2    Commichau, F.M.3    Herzberg, C.4    Rodrigues, C.5    Hewitt, L.6    Lewis, R.J.7    Stülke, J.8
  • 97
    • 1842612577 scopus 로고    scopus 로고
    • Bacterial biofilms: From the natural environment to infectious diseases
    • Hall-Stoodley L, Costerton JW, Stoodley P (2004) Bacterial biofilms: from the natural environment to infectious diseases. Nat Rev Microbiol 2:95-108
    • (2004) Nat Rev Microbiol , vol.2 , pp. 95-108
    • Hall-Stoodley, L.1    Costerton, J.W.2    Stoodley, P.3
  • 98
    • 0030944503 scopus 로고    scopus 로고
    • Brief heat shock treatment induces a long-lasting alteration in the glycolipid receptor binding specificity and growth rate of Haemophilus influenzae
    • Hartmann E, Lingwood C (1997) Brief heat shock treatment induces a long-lasting alteration in the glycolipid receptor binding specificity and growth rate of Haemophilus influenzae. Infect Immun 65:1729-1733
    • (1997) Infect Immun , vol.65 , pp. 1729-1733
    • Hartmann, E.1    Lingwood, C.2
  • 99
    • 0035055499 scopus 로고    scopus 로고
    • Heat-inducible surface stress protein (Hsp70) mediates sulfatide recognition of the respiratory pathogen Haemophilus influenzae
    • Hartmann E, Lingwood CA, Reidl J (2001) Heat-inducible surface stress protein (Hsp70) mediates sulfatide recognition of the respiratory pathogen Haemophilus influenzae. Infect Immun 69:3438-3441
    • (2001) Infect Immun , vol.69 , pp. 3438-3441
    • Hartmann, E.1    Lingwood, C.A.2    Reidl, J.3
  • 100
    • 76849115257 scopus 로고    scopus 로고
    • Characterization of a virulence-associated and cell-wall-located DNase of Streptococcus pyogenes
    • Hasegawa T, Minami M, Okamoto A, Tatsuno I, Isaka M, Ohta M (2010) Characterization of a virulence-associated and cell-wall-located DNase of Streptococcus pyogenes. Microbiology 156:184-190
    • (2010) Microbiology , vol.156 , pp. 184-190
    • Hasegawa, T.1    Minami, M.2    Okamoto, A.3    Tatsuno, I.4    Isaka, M.5    Ohta, M.6
  • 101
    • 0030938622 scopus 로고    scopus 로고
    • Binding of the 68-kilodalton protein of Mycobacterium avium to alpha(v)beta3 on human monocyte-derived macrophages enhances complement receptor type 3 expression
    • Hayashi T, Rao SP, Catanzaro A (1997) Binding of the 68-kilodalton protein of Mycobacterium avium to alpha(v)beta3 on human monocyte-derived macrophages enhances complement receptor type 3 expression. Infect Immun 65:1211-1216
    • (1997) Infect Immun , vol.65 , pp. 1211-1216
    • Hayashi, T.1    Rao, S.P.2    Catanzaro, A.3
  • 102
    • 0142042875 scopus 로고    scopus 로고
    • Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis
    • Heilmann C, Thumm G, Chhatwal GS, Hartleib J, Uekötter A, Peters G (2003) Identification and characterization of a novel autolysin (Aae) with adhesive properties from Staphylococcus epidermidis. Microbiology 149:2769-2778
    • (2003) Microbiology , vol.149 , pp. 2769-2778
    • Heilmann, C.1    Thumm, G.2    Chhatwal, G.S.3    Hartleib, J.4    Uekötter, A.5    Peters, G.6
  • 103
    • 21344433812 scopus 로고    scopus 로고
    • The multifunctional Staphylococcus aureus autolysin aaa mediates adherence to immobilized fibrinogen and fibronectin
    • Heilmann C, Hartleib J, Hussain MS, Peters G (2005) The multifunctional Staphylococcus aureus autolysin aaa mediates adherence to immobilized fibrinogen and fibronectin. Infect Immun 73:4793-4802
    • (2005) Infect Immun , vol.73 , pp. 4793-4802
    • Heilmann, C.1    Hartleib, J.2    Hussain, M.S.3    Peters, G.4
  • 104
    • 0035135102 scopus 로고    scopus 로고
    • Immunolocalization of the Mip protein of intracellularly and extracellularly grown Legionella pneumophila
    • Helbig JH, Lück PC, Steinert M, Jacobs E, Witt M (2001) Immunolocalization of the Mip protein of intracellularly and extracellularly grown Legionella pneumophila. Lett Appl Microbiol 32:83-88
    • (2001) Lett Appl Microbiol , vol.32 , pp. 83-88
    • Helbig, J.H.1    Lück, P.C.2    Steinert, M.3    Jacobs, E.4    Witt, M.5
  • 106
    • 0031904826 scopus 로고    scopus 로고
    • Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties
    • Hell W, Meyer HG, Gatermann SG (1998) Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties. Mol Microbiol 29: 871-881
    • (1998) Mol Microbiol , vol.29 , pp. 871-881
    • Hell, W.1    Meyer, H.G.2    Gatermann, S.G.3
  • 107
    • 33745589526 scopus 로고    scopus 로고
    • Stress wars: The direct role of host and bacterial molecular chaperones in bacterial Infection
    • Henderson B, Allan E, Coates ARM (2006) Stress wars: the direct role of host and bacterial molecular chaperones in bacterial Infection. Infect Immun 74:3693-3706
    • (2006) Infect Immun , vol.74 , pp. 3693-3706
    • Henderson, B.1    Allan, E.2    Arm, C.3
  • 108
    • 70350488843 scopus 로고    scopus 로고
    • Unfolding the relationship between secreted molecular chaperones and macrophage activation states
    • Henderson B, Henderson S (2009) Unfolding the relationship between secreted molecular chaperones and macrophage activation states. Cell Stress Chaperones 14:329-341
    • (2009) Cell Stress Chaperones , vol.14 , pp. 329-341
    • Henderson, B.1    Henderson, S.2
  • 109
    • 77957153127 scopus 로고    scopus 로고
    • Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation
    • Henderson B, Pockley AG (2010) Molecular chaperones and protein-folding catalysts as intercellular signaling regulators in immunity and inflammation. J Leukoc Biol 88:445-462
    • (2010) J Leukoc Biol , vol.88 , pp. 445-462
    • Henderson, B.1    Pockley, A.G.2
  • 111
    • 77950593732 scopus 로고    scopus 로고
    • Multiple moonlighting functions of mycobacterial molecular chaperones
    • Henderson B, Lund PA, Coates ARM (2010) Multiple moonlighting functions of mycobacterial molecular chaperones. Tuberculosis 90:119-124
    • (2010) Tuberculosis , vol.90 , pp. 119-124
    • Henderson, B.1    Lund, P.A.2    Coates, A.R.M.3
  • 112
    • 78650028835 scopus 로고    scopus 로고
    • Fibronectin: A multidomain host adhesin targeted by bacterial fibronectin-binding proteins
    • Henderson B, Nair S, Pallas J, Williams MA (2011) Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins. FEMS Microbiol Rev 35:147-200
    • (2011) FEMS Microbiol Rev , vol.35 , pp. 147-200
    • Henderson, B.1    Nair, S.2    Pallas, J.3    Williams, M.A.4
  • 115
    • 34447536729 scopus 로고    scopus 로고
    • Friend and foe: The two faces of Xenorhabdus nematophila
    • Herbert EE, Goodrich-Blair H (2007) Friend and foe: the two faces of Xenorhabdus nematophila. Nat Rev Microbiol 5:634-646
    • (2007) Nat Rev Microbiol , vol.5 , pp. 634-646
    • Herbert, E.E.1    Goodrich-Blair, H.2
  • 117
    • 67651215965 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages
    • Hickey TB, Thorson LM, Speert DP, Daffé M, Stokes RW (2009) Mycobacterium tuberculosis Cpn60.2 and DnaK are located on the bacterial surface, where Cpn60.2 facilitates efficient bacterial association with macrophages. Infect Immun 77:3389-3401
    • (2009) Infect Immun , vol.77 , pp. 3389-3401
    • Hickey, T.B.1    Thorson, L.M.2    Speert, D.P.3    Daffé, M.4    Stokes, R.W.5
  • 118
    • 79953719657 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis employs Cpn60.2 as an adhesin that binds CD43 on the macrophage surface
    • Hickey TB, Ziltener HJ, Speert DP, Stokes RW (2010) Mycobacterium tuberculosis employs Cpn60.2 as an adhesin that binds CD43 on the macrophage surface. Cell Microbiol 12: 1634-1647
    • (2010) Cell Microbiol , vol.12 , pp. 1634-1647
    • Hickey, T.B.1    Ziltener, H.J.2    Speert, D.P.3    Stokes, R.W.4
  • 120
    • 0032909564 scopus 로고    scopus 로고
    • Surface-associated heat shock proteins of Legionella pneumophila and Helicobacter pylori: Roles in pathogenesis and immunity
    • Hoffman PS, Garduno RA (1999) Surface-associated heat shock proteins of Legionella pneumophila and Helicobacter pylori: roles in pathogenesis and immunity. Infect Dis Obstet Gynecol 7:58-63
    • (1999) Infect Dis Obstet Gynecol , vol.7 , pp. 58-63
    • Hoffman, P.S.1    Garduno, R.A.2
  • 121
    • 68649123756 scopus 로고    scopus 로고
    • The GroEL/GroES cis cavity as a passive antiaggregation device
    • Horwich AL, Apetri AC, Fenton WA (2009) The GroEL/GroES cis cavity as a passive antiaggregation device. FEBS Lett 583:2654-2662
    • (2009) FEBS Lett , vol.583 , pp. 2654-2662
    • Horwich, A.L.1    Apetri, A.C.2    Fenton, W.A.3
  • 124
    • 42149117075 scopus 로고    scopus 로고
    • A mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection
    • Hu Y, Henderson B, Lund PA, Tormay P, Ahmed MT, Gurcha SS, Besra GS, Coates AR (2008) A mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection. Infect Immun 76:1535-1546
    • (2008) Infect Immun , vol.76 , pp. 1535-1546
    • Hu, Y.1    Henderson, B.2    Lund, P.A.3    Tormay, P.4    Ahmed, M.T.5    Gurcha, S.S.6    Besra, G.S.7    Coates, A.R.8
  • 125
    • 0031714167 scopus 로고    scopus 로고
    • Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori
    • Huesca M, Goodwin A, Bhagwansingh A, Hoffman P, Lingwood CA (1998) Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori. Infect Immun 66:4061-4067
    • (1998) Infect Immun , vol.66 , pp. 4061-4067
    • Huesca, M.1    Goodwin, A.2    Bhagwansingh, A.3    Hoffman, P.4    Lingwood, C.A.5
  • 128
    • 34347385440 scopus 로고    scopus 로고
    • Contribution of the mannan backbone of cryptococcal glucuronoxylomannan and a glycolytic enzyme of Staphylococcus aureus to contact-mediated killing of Cryptococcus neoformans
    • Ikeda R, Saito F, Matsuo M, Kurokawa K, Sekimizu K, Yamaguchi M, Kawamoto S (2007) Contribution of the mannan backbone of cryptococcal glucuronoxylomannan and a glycolytic enzyme of Staphylococcus aureus to contact-mediated killing of Cryptococcus neoformans. J Bacteriol 189:4815-4826
    • (2007) J Bacteriol , vol.189 , pp. 4815-4826
    • Ikeda, R.1    Saito, F.2    Matsuo, M.3    Kurokawa, K.4    Sekimizu, K.5    Yamaguchi, M.6    Kawamoto, S.7
  • 129
    • 77956359469 scopus 로고    scopus 로고
    • LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species
    • Jagadeesan B, Koo OK, Kim KP, Burkholder KM, Mishra KK, Aroonnual A, Bhunia AK (2010) LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeria, promotes bacterial adhesion to enterocyte-like Caco-2 cells only in pathogenic species. Microbiology 156:2782-2795
    • (2010) Microbiology , vol.156 , pp. 2782-2795
    • Jagadeesan, B.1    Koo, O.K.2    Kim, K.P.3    Burkholder, K.M.4    Mishra, K.K.5    Aroonnual, A.6    Bhunia, A.K.7
  • 130
  • 131
    • 27844471239 scopus 로고    scopus 로고
    • Mass spectrometry and the search for moonlighting proteins
    • Jeffery CJ (2005) Mass spectrometry and the search for moonlighting proteins. Mass Spec Revs 24:772-782
    • (2005) Mass Spec Revs , vol.24 , pp. 772-782
    • Jeffery, C.J.1
  • 132
    • 20444425311 scopus 로고    scopus 로고
    • Group A streptococcal surface GAPDF, SDH recognises uPAR/CD87 as its receptor on the human pharyngeal cell and mediates bacterial adherence to host cells
    • Jin H, Youngmia P, Boel G, Kochar J, Pancholi V (2005) Group A streptococcal surface GAPDF, SDH recognises uPAR/CD87 as its receptor on the human pharyngeal cell and mediates bacterial adherence to host cells. J Mol Biol 350:27-41
    • (2005) J Mol Biol , vol.350 , pp. 27-41
    • Jin, H.1    Youngmia, P.2    Boel, G.3    Kochar, J.4    Pancholi, V.5
  • 133
    • 0348141889 scopus 로고    scopus 로고
    • Acquisition of host plasmin activity by the swine pathogen Streptococcus suis serotype 2
    • Jobin MC, Brassard J, Quessy S, Gottschalk M, Grenier D (2004) Acquisition of host plasmin activity by the swine pathogen Streptococcus suis serotype 2. Infect Immun 72:606-610
    • (2004) Infect Immun , vol.72 , pp. 606-610
    • Jobin, M.C.1    Brassard, J.2    Quessy, S.3    Gottschalk, M.4    Grenier, D.5
  • 137
    • 70449564515 scopus 로고    scopus 로고
    • Streptococcus mutans autolysin AtlA is a fibronectin-binding protein and contributes to bacterial survival in the bloodstream and virulence for infective endocarditis
    • Jung CJ, Zheng QH, Shieh YH, Lin CS, Chia JS (2009) Streptococcus mutans autolysin AtlA is a fibronectin-binding protein and contributes to bacterial survival in the bloodstream and virulence for infective endocarditis. Mol Microbiol 74:888-902
    • (2009) Mol Microbiol , vol.74 , pp. 888-902
    • Jung, C.J.1    Zheng, Q.H.2    Shieh, Y.H.3    Lin, C.S.4    Chia, J.S.5
  • 138
    • 0034049837 scopus 로고    scopus 로고
    • Chlamydial virulence determinants in atherogenesis: The role of chlamydial lipopolysaccharide and heat shock protein 60 in macrophage- lipoprotein interactions
    • Kalayoglu MV, Indrawati, Morrison RP, Morrison SG, Yuan Y, Byrne GI (2000) Chlamydial virulence determinants in atherogenesis: the role of chlamydial lipopolysaccharide and heat shock protein 60 in macrophage- lipoprotein interactions. J Infect Dis 181(3):S483-489
    • (2000) J Infect Dis , vol.181 , Issue.3
    • Kalayoglu, M.V.1    Indrawati2    Morrison, R.P.3    Morrison, S.G.4    Yuan, Y.5    Byrne, G.I.6
  • 141
    • 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
  • 142
  • 143
    • 47649118596 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis heat shock protein 60 modulates immune response to PPD by manipulating the surface expression of TLR2 on macrophages
    • Khan N, Alam K, Mande SC, Valluri VL, Hasnain SE, Mukhopadhyay S (2008) Mycobacterium tuberculosis heat shock protein 60 modulates immune response to PPD by manipulating the surface expression of TLR2 on macrophages. Cell Microbiol 10:1711-1722
    • (2008) Cell Microbiol , vol.10 , pp. 1711-1722
    • Khan, N.1    Alam, K.2    Mande, S.C.3    Valluri, V.L.4    Hasnain, S.E.5    Mukhopadhyay, S.6
  • 144
    • 33644824393 scopus 로고    scopus 로고
    • Adhesion characteristics of Listeria adhesion protein (LAP)-expressing Escherichia coli to Caco-2 cells and of recombinant LAP to eukaryotic receptor Hsp60 as examined in a surface plasmon resonance sensor
    • Kim KP, Jagadeesan B, Burkholder KM, Jaradat ZW, Wampler JL, Lathrop AA, Morgan MT, Bhunia AK (2006) Adhesion characteristics of Listeria adhesion protein (LAP)-expressing Escherichia coli to Caco-2 cells and of recombinant LAP to eukaryotic receptor Hsp60 as examined in a surface plasmon resonance sensor. FEMS Microbiol Lett 256:324-332
    • (2006) FEMS Microbiol Lett , vol.256 , pp. 324-332
    • Kim, K.P.1    Jagadeesan, B.2    Burkholder, K.M.3    Jaradat, Z.W.4    Wampler, J.L.5    Lathrop, A.A.6    Morgan, M.T.7    Bhunia, A.K.8
  • 146
    • 42949153528 scopus 로고    scopus 로고
    • Plasminogen binding by oral streptococci from dental plaque and inflammatory lesions
    • Kinnby B, Booth NA, Svensater G (2008) Plasminogen binding by oral streptococci from dental plaque and inflammatory lesions. Microbiology 154:924-931
    • (2008) Microbiology , vol.154 , pp. 924-931
    • Kinnby, B.1    Booth, N.A.2    Svensater, G.3
  • 148
    • 34247854961 scopus 로고    scopus 로고
    • Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis
    • Knaust A, Weber MV, Hammerschmidt S, Bergmann S, Frosch M, Kurzai O (2007) Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis. J Bacteriol 189:3246-3255
    • (2007) J Bacteriol , vol.189 , pp. 3246-3255
    • Knaust, A.1    Weber, M.V.2    Hammerschmidt, S.3    Bergmann, S.4    Frosch, M.5    Kurzai, O.6
  • 149
    • 0032575305 scopus 로고    scopus 로고
    • Chlamydial heat shock protein 60 localizes in human atheroma and regulates macrophage tumor necrosis factor-alpha and matrix metalloproteinase expression
    • Kol A, Sukhova GK, Lichtman AH, Libby P (1998) Chlamydial heat shock protein 60 localizes in human atheroma and regulates macrophage tumor necrosis factor-alpha and matrix metalloproteinase expression. Circulation 98:300-307
    • (1998) Circulation , vol.98 , pp. 300-307
    • Kol, A.1    Sukhova, G.K.2    Lichtman, A.H.3    Libby, P.4
  • 154
    • 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
  • 155
    • 67650032436 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a surface-associated, fibronectin-binding protein of Trichomonas vaginalis
    • Lama A, Kucknoor A, Mundodi V, Alderete JF (2009) Glyceraldehyde-3- phosphate dehydrogenase is a surface-associated, fibronectin-binding protein of Trichomonas vaginalis. Infect Immun 77:2703-2711
    • (2009) Infect Immun , vol.77 , pp. 2703-2711
    • Lama, A.1    Kucknoor, A.2    Mundodi, V.3    Alderete, J.F.4
  • 156
    • 34248389725 scopus 로고    scopus 로고
    • Chlamydial Hsp60-2 is iron responsive in Chlamydia trachomatis serovar E-infected human endometrial epithelial cells in vitro
    • LeaRue RW, Dill BD, Giles DK, Whittimore JD, Raulston JE (2007) Chlamydial Hsp60-2 is iron responsive in Chlamydia trachomatis serovar E-infected human endometrial epithelial cells in vitro. Infect Immun 75:2374-2380
    • (2007) Infect Immun , vol.75 , pp. 2374-2380
    • Learue, R.W.1    Dill, B.D.2    Giles, D.K.3    Whittimore, J.D.4    Raulston, J.E.5
  • 157
    • 0028861520 scopus 로고
    • Fibronectin-binding antigen 85 and the 10-kilodalton GroES-related heat shock protein are the predominant TH-1 response inducers in leprosy contacts
    • Launois P, N'Diaye MN, Cartel JL, Mane I, Drowart A, Van Vooren JP, Sarthou JL, Huygen K (1995) Fibronectin-binding antigen 85 and the 10-kilodalton GroES-related heat shock protein are the predominant TH-1 response inducers in leprosy contacts. Infect Immun 63:88-93
    • (1995) Infect Immun , vol.63 , pp. 88-93
    • Launois, P.1    N'Diaye, M.N.2    Cartel, J.L.3    Mane, I.4    Drowart, A.5    Van Vooren, J.P.6    Sarthou, J.L.7    Huygen, K.8
  • 159
    • 0033976502 scopus 로고    scopus 로고
    • Heat shock proteins generate beta-chemokines which function as innate adjuvants enhancing adaptive immunity
    • Lehner T, Bergmeier LA, Wang Y, Tao L, Sing M, Spallek R, van der Zee R (2000) Heat shock proteins generate beta-chemokines which function as innate adjuvants enhancing adaptive immunity. Eur J Immunol 30:594-603
    • (2000) Eur J Immunol , vol.30 , pp. 594-603
    • Lehner, T.1    Bergmeier, L.A.2    Wang, Y.3    Tao, L.4    Sing, M.5    Spallek, R.6    Van Der Zee, R.7
  • 160
    • 27444447753 scopus 로고    scopus 로고
    • Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages
    • Leuzzi R, Serino L, Scarselli M, Savino S, Fontana MR, Monaci E, Taddei A, Fischer G, Rappuoli R, Pizza M (2005) Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages. Mol Microbiol 58:669-681
    • (2005) Mol Microbiol , vol.58 , pp. 669-681
    • Leuzzi, R.1    Serino, L.2    Scarselli, M.3    Savino, S.4    Fontana, M.R.5    Monaci, E.6    Taddei, A.7    Fischer, G.8    Rappuoli, R.9    Pizza, M.10
  • 161
    • 0035183063 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (hsp 65) and contains a CD14-binding domain
    • Lewthwaite JC, Coates AR, Tormay P, Singh M, Mascagni P, Poole S, Roberts M, Sharp L, Henderson B (2001) Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (hsp 65) and contains a CD14-binding domain. Infect Immun 69:7349-7355
    • (2001) Infect Immun , vol.69 , pp. 7349-7355
    • Lewthwaite, J.C.1    Coates, A.R.2    Tormay, P.3    Singh, M.4    Mascagni, P.5    Poole, S.6    Roberts, M.7    Sharp, L.8    Henderson, B.9
  • 162
    • 0036556704 scopus 로고    scopus 로고
    • Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: Activity is dependent on interaction with cell surface CD14
    • Lewthwaite J, George R, Lund PA, Poole S, Tormay P, Sharp L, Coates AR, Henderson B (2002) Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is dependent on interaction with cell surface CD14. Cell Stress Chaperones 7:130-136
    • (2002) Cell Stress Chaperones , vol.7 , pp. 130-136
    • Lewthwaite, J.1    George, R.2    Lund, P.A.3    Poole, S.4    Tormay, P.5    Sharp, L.6    Coates, A.R.7    Henderson, B.8
  • 163
    • 19644368499 scopus 로고    scopus 로고
    • The Listeria protein internalin B mimics hepatocyte growth factor-induced receptor trafficking
    • Li N, Xiang GS, Dokainish H, Ireton K, Elferink LA (2005) The Listeria protein internalin B mimics hepatocyte growth factor-induced receptor trafficking. Traffic 6:459-473
    • (2005) Traffic , vol.6 , pp. 459-473
    • Li, N.1    Xiang, G.S.2    Dokainish, H.3    Ireton, K.4    Elferink, L.A.5
  • 167
    • 8144221393 scopus 로고    scopus 로고
    • Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse
    • Ling E, Feldman G, Portnoi M, Dagan R, Overweg K, Mulholland F, Chalifa-Caspi V, Wells J, Mizrachi-Nebenzahl Y (2004) Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse. Clin Exp Immunol 138:290-298
    • (2004) Clin Exp Immunol , vol.138 , pp. 290-298
    • Ling, E.1    Feldman, G.2    Portnoi, M.3    Dagan, R.4    Overweg, K.5    Mulholland, F.6    Chalifa-Caspi, V.7    Wells, J.8    Mizrachi-Nebenzahl, Y.9
  • 168
    • 0037223264 scopus 로고    scopus 로고
    • Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages
    • Long KH, Gomez FJ, Morris RE, Newman SL (2003) Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages. J Immunol 170:487-494
    • (2003) J Immunol , vol.170 , pp. 487-494
    • Long, K.H.1    Gomez, F.J.2    Morris, R.E.3    Newman, S.L.4
  • 169
    • 0026673916 scopus 로고
    • Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor
    • Lottenberg R, Broder CC, Boyle MD, Kain SJ, Schroeder BL, Curtiss R (1992) Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor. J Bacteriol 174:5204-5210
    • (1992) J Bacteriol , vol.174 , pp. 5204-5210
    • Lottenberg, R.1    Broder, C.C.2    Boyle, M.D.3    Kain, S.J.4    Schroeder, B.L.5    Curtiss, R.6
  • 170
    • 66749187185 scopus 로고    scopus 로고
    • Multiple chaperonins in bacteria - Why so many?
    • Lund PA (2009) Multiple chaperonins in bacteria - why so many? FEMS Microbiol Revs 3:785-800
    • (2009) FEMS Microbiol Revs , vol.3 , pp. 785-800
    • Lund, P.A.1
  • 171
    • 0027483193 scopus 로고
    • Chlamydia trachomatis Mip-like protein has peptidylprolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection
    • Lundemose AG, Kay JE, Pearce JH (1993) Chlamydia trachomatis Mip-like protein has peptidylprolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection. Mol Microbiol 7:777-783
    • (1993) Mol Microbiol , vol.7 , pp. 777-783
    • Lundemose, A.G.1    Kay, J.E.2    Pearce, J.H.3
  • 172
    • 0027218871 scopus 로고
    • The Hsp60 protein of Helicobacter pylori: Structure and immune response in patients with gastroduodenal diseases
    • Macchia G, Massone A, Burroni D, Covacci A, Censini S, Rappuoli R (1993) The Hsp60 protein of Helicobacter pylori: structure and immune response in patients with gastroduodenal diseases. Mol Microbiol 9:645-652
    • (1993) Mol Microbiol , vol.9 , pp. 645-652
    • Macchia, G.1    Massone, A.2    Burroni, D.3    Covacci, A.4    Censini, S.5    Rappuoli, R.6
  • 173
    • 0031769504 scopus 로고    scopus 로고
    • Identification of a 71-kilodalton surface-associated Hsp70 homologue in Coxiella burneti
    • Macellaro A, Tujulin E, Hjalmarsson K, Norlander L (1998) Identification of a 71-kilodalton surface-associated Hsp70 homologue in Coxiella burneti. Infect Immun 66:5882-5888
    • (1998) Infect Immun , vol.66 , pp. 5882-5888
    • Macellaro, A.1    Tujulin, E.2    Hjalmarsson, K.3    Norlander, L.4
  • 175
    • 35148826082 scopus 로고    scopus 로고
    • Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model
    • Magalhães V, Veiga-Malta I, Almeida MR, Baptista M, Ribeiro A, Trieu-Cuot P, Ferreira P (2007) Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model. Microbes Infect 9:1276-1284
    • (2007) Microbes Infect , vol.9 , pp. 1276-1284
    • Magalhães, V.1    Veiga-Malta, I.2    Almeida, M.R.3    Baptista, M.4    Ribeiro, A.5    Trieu-Cuot, P.6    Ferreira, P.7
  • 177
    • 0035957230 scopus 로고    scopus 로고
    • Hsp70s contain a specific sulfogalactolipid binding site. Differential aglycone influence on sulfogalactosyl ceramide binding by recombinant prokaryotic and eukaryotic hsp70 family members
    • Mamelak D, Mylvaganam M, Whetstone H, Hartmann E, Lennarz W, Wyrick PB, Raulston J, Han H, Hoffman P, Lingwood CA (2001) Hsp70s contain a specific sulfogalactolipid binding site. Differential aglycone influence on sulfogalactosyl ceramide binding by recombinant prokaryotic and eukaryotic hsp70 family members. Biochemistry 40:3572-3582
    • (2001) Biochemistry , vol.40 , pp. 3572-3582
    • Mamelak, D.1    Mylvaganam, M.2    Whetstone, H.3    Hartmann, E.4    Lennarz, W.5    Wyrick, P.B.6    Raulston, J.7    Han, H.8    Hoffman, P.9    Lingwood, C.A.10
  • 178
    • 67650485985 scopus 로고    scopus 로고
    • Alternative activation of macrophages: An immunologic functional perspective
    • Martinez FO, Helming L, Gordon S (2009) Alternative activation of macrophages: an immunologic functional perspective. Annu Rev Immunol 27:451-483
    • (2009) Annu Rev Immunol , vol.27 , pp. 451-483
    • Martinez, F.O.1    Helming, L.2    Gordon, S.3
  • 179
    • 77956649845 scopus 로고    scopus 로고
    • Surface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding protein
    • Matta SK, Agarwal S, Bhatnagar R (2010) Surface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding protein. Biochim Biophys Acta 1804:2111-2120
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 2111-2120
    • Matta, S.K.1    Agarwal, S.2    Bhatnagar, R.3
  • 180
    • 64849108649 scopus 로고    scopus 로고
    • Psoriasis and streptococci: The natural selection of psoriasis revisited
    • McFadden JP, Baker BS, Powles AV, Fry L (2009) Psoriasis and streptococci: the natural selection of psoriasis revisited. Br J Dermatol 160:929-937
    • (2009) Br J Dermatol , vol.160 , pp. 929-937
    • McFadden, J.P.1    Baker, B.S.2    Powles, A.V.3    Fry, L.4
  • 182
    • 55949120073 scopus 로고    scopus 로고
    • Expression and regulation of chemokines in mycobacterial infection
    • Méndez-Samperio P (2008) Expression and regulation of chemokines in mycobacterial infection. J Infect 57:374-384
    • (2008) J Infect , vol.57 , pp. 374-384
    • Méndez-Samperio, P.1
  • 183
    • 34548398028 scopus 로고    scopus 로고
    • Analysis of chaperone proteins associated with human spermatozoa during capacitation
    • Mitchell LA, Nixon B, Aitken RJ (2007) Analysis of chaperone proteins associated with human spermatozoa during capacitation. Mol Hum Reprod 13:605-613
    • (2007) Mol Hum Reprod , vol.13 , pp. 605-613
    • Mitchell, L.A.1    Nixon, B.2    Aitken, R.J.3
  • 184
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
    • Modun B, Williams P (1999) The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect Immun 67:1086-1092
    • (1999) Infect Immun , vol.67 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 185
    • 2442430450 scopus 로고    scopus 로고
    • Bifunctional and moonlighting enzymes: Lighting the way to regulatory control
    • Moore BD (2004) Bifunctional and moonlighting enzymes: lighting the way to regulatory control. Trends Plant Sci 9:221-228
    • (2004) Trends Plant Sci , vol.9 , pp. 221-228
    • Moore, B.D.1
  • 187
    • 77953680605 scopus 로고    scopus 로고
    • Spotlight on mycobacteria and dendritic cells: Will novel targets to fight tuberculosis emerge?
    • Mortellaro A, Robinson L, Ricciardi-Castagnoli P (2009) Spotlight on mycobacteria and dendritic cells: will novel targets to fight tuberculosis emerge? EMBO Mol Med 1:19-29
    • (2009) EMBO Mol Med , vol.1 , pp. 19-29
    • Mortellaro, A.1    Robinson, L.2    Ricciardi-Castagnoli, P.3
  • 188
    • 70349182303 scopus 로고    scopus 로고
    • Sequential reactions of surface-tethered glycolytic enzymes
    • Mukai C, Bergkvist M, Nelson JL, Travis AJ (2009) Sequential reactions of surface-tethered glycolytic enzymes. Chem Biol 16:1013-1020
    • (2009) Chem Biol , vol.16 , pp. 1013-1020
    • Mukai, C.1    Bergkvist, M.2    Nelson, J.L.3    Travis, A.J.4
  • 189
    • 0032579246 scopus 로고    scopus 로고
    • The novel fibronectin-binding motif and key residues of mycobacteria
    • Naito M, Ohara N, Matsumoto S, Yamada T (1998) The novel fibronectin-binding motif and key residues of mycobacteria. J Biol Chem 273:2905-2909
    • (1998) J Biol Chem , vol.273 , pp. 2905-2909
    • Naito, M.1    Ohara, N.2    Matsumoto, S.3    Yamada, T.4
  • 190
    • 0034194278 scopus 로고    scopus 로고
    • The domains of human fibronectin mediating the binding of alpha antigen, the most immunopotent antigen of mycobacteria that induces protective immunity against mycobacterial infection
    • Naito M, Fukuda T, Sekiguchi K, Yamada T, Naito M (2000) The domains of human fibronectin mediating the binding of alpha antigen, the most immunopotent antigen of mycobacteria that induces protective immunity against mycobacterial infection. Biochem J 347:725-731
    • (2000) Biochem J , vol.347 , pp. 725-731
    • Naito, M.1    Fukuda, T.2    Sekiguchi, K.3    Yamada, T.4    Naito, M.5
  • 192
    • 77950223610 scopus 로고    scopus 로고
    • GroEL and lipopolysaccharide from Francisella tularensis live vaccine strain synergistically activate human macrophages
    • Noah CE, Malik M, Bublitz DC, Camenares D, Sellati TJ, Benach JL, Furie MB (2010) GroEL and lipopolysaccharide from Francisella tularensis live vaccine strain synergistically activate human macrophages. Infect Immun 78:1797-1806
    • (2010) Infect Immun , vol.78 , pp. 1797-1806
    • Noah, C.E.1    Malik, M.2    Bublitz, D.C.3    Camenares, D.4    Sellati, T.J.5    Benach, J.L.6    Furie, M.B.7
  • 194
    • 33645697959 scopus 로고    scopus 로고
    • Comparative proteome analysis of subcellular fractions from Borrelia burgdorferi by NEPHGE and IPG
    • Nowalk AJ, Nolder C, Clifton DR, Carroll JA (2006) Comparative proteome analysis of subcellular fractions from Borrelia burgdorferi by NEPHGE and IPG. Proteomics 6: 2121-2134
    • (2006) Proteomics , vol.6 , pp. 2121-2134
    • Nowalk, A.J.1    Nolder, C.2    Clifton, D.R.3    Carroll, J.A.4
  • 197
    • 28344453690 scopus 로고    scopus 로고
    • GroEL1: A dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria
    • Ojha A, Anand M, Bhatt A, Kremer L, Jacobs WR Jr, Hatfull GF (2005) GroEL1: a dedicated chaperone involved in mycolic acid biosynthesis during biofilm formation in mycobacteria. Cell 123:861-873
    • (2005) Cell , vol.123 , pp. 861-873
    • Ojha, A.1    Anand, M.2    Bhatt, A.3    Kremer, L.4    Jacobs Jr., W.R.5    Hatfull, G.F.6
  • 198
  • 199
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: Its role in diseases
    • Pancholi V (2001) Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 58:902-920
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 200
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3- phosphate-dehydrogenase with multiple binding activity
    • Pancholi V, Fischetti VA (1992) A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J Exp Med 176: 415-426
    • (1992) J Exp Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 201
    • 0027249488 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme
    • Pancholi V, Fischetti VA (1993) Glyceraldehyde-3-phosphate dehydrogenase on the surface of group A streptococci is also an ADP-ribosylating enzyme. Proc Natl Acad Sci U S A 90:8154-8158
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8154-8158
    • Pancholi, V.1    Fischetti, V.A.2
  • 202
    • 0030661706 scopus 로고    scopus 로고
    • Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptoccal surface dehydrogenase: Signal transduction between streptococci and pharyngeal cells
    • Pancholi V, Fischetti VA (1997) Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptoccal surface dehydrogenase: signal transduction between streptococci and pharyngeal cells. J Exp Med 186:1633-1643
    • (1997) J Exp Med , vol.186 , pp. 1633-1643
    • Pancholi, V.1    Fischetti, V.A.2
  • 203
    • 0032486286 scopus 로고    scopus 로고
    • Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi V, Fischetti VA (1998) Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273:14503-14515
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 204
    • 33749361574 scopus 로고    scopus 로고
    • Binding of Haemophilus ducreyi to carbohydrate receptors is mediated by the 58.5-kDa GroEL heat shock protein
    • Pantzar M, Teneberg S, Lagergård T (2006) Binding of Haemophilus ducreyi to carbohydrate receptors is mediated by the 58.5-kDa GroEL heat shock protein. Microbes Infect 8: 2452-2458
    • (2006) Microbes Infect , vol.8 , pp. 2452-2458
    • Pantzar, M.1    Teneberg, S.2    Lagergård, T.3
  • 205
    • 33751578866 scopus 로고    scopus 로고
    • TLR4-dependent NF-kappaB activation and mitogen- and stress-activated protein kinase 1-triggered phosphorylation events are central to Helicobacter pylori peptidyl prolyl cis-, trans-isomerase (HP0175)-mediated induction of IL-6 release from macrophages
    • Pathak SK, Basu S, Bhattacharyya A, Pathak S, Banerjee A, Basu J, Kundu M (2006) TLR4-dependent NF-kappaB activation and mitogen- and stress-activated protein kinase 1-triggered phosphorylation events are central to Helicobacter pylori peptidyl prolyl cis-, trans-isomerase (HP0175)-mediated induction of IL-6 release from macrophages. J Immunol 177:7950-7958
    • (2006) J Immunol , vol.177 , pp. 7950-7958
    • Pathak, S.K.1    Basu, S.2    Bhattacharyya, A.3    Pathak, S.4    Banerjee, A.5    Basu, J.6    Kundu, M.7
  • 206
    • 0027451948 scopus 로고
    • Mechanism of interaction of the 85B secreted protein of Mycobacterium bovis with fibronectin
    • Peake P, Gooley A, Britton WJ (1993) Mechanism of interaction of the 85B secreted protein of Mycobacterium bovis with fibronectin. Infect Immun 61:4828-4832
    • (1993) Infect Immun , vol.61 , pp. 4828-4832
    • Peake, P.1    Gooley, A.2    Britton, W.J.3
  • 207
    • 0028364251 scopus 로고
    • Mycobacterial heat-shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes
    • Peetermans WE, Raats CJ, Langermans JA, van Furth R (1994) Mycobacterial heat-shock protein 65 induces proinflammatory cytokines but does not activate human mononuclear phagocytes. Scand J Immunol 39:613-617
    • (1994) Scand J Immunol , vol.39 , pp. 613-617
    • Peetermans, W.E.1    Raats, C.J.2    Langermans, J.A.3    Van Furth, R.4
  • 208
    • 0019334977 scopus 로고
    • Study of the interaction of glyceraldehyde-3-phosphate dehydrogenase with DNA
    • Perucho M, Salas J, Salas ML (1980) Study of the interaction of glyceraldehyde-3-phosphate dehydrogenase with DNA. Biochim Biophys Acta 606:181-195
    • (1980) Biochim Biophys Acta , vol.606 , pp. 181-195
    • Perucho, M.1    Salas, J.2    Salas, M.L.3
  • 209
    • 0031970686 scopus 로고    scopus 로고
    • Multifunctional lens crystallins and corneal enzymes. More than meets the eye
    • Piatigorsky J (1998) Multifunctional lens crystallins and corneal enzymes. More than meets the eye. Ann N Y Acad Sci 842:7-15
    • (1998) Ann N y Acad Sci , vol.842 , pp. 7-15
    • Piatigorsky, J.1
  • 214
    • 38049134765 scopus 로고    scopus 로고
    • Gpm1p is a factor H-, FHL-1-, and plasminogen-binding surface protein of Candida albicans
    • Poltermann S, Kunert A, von der Heide M, Eck R, Hartmann A, Zipfel PF (2007) Gpm1p is a factor H-, FHL-1-, and plasminogen-binding surface protein of Candida albicans. J Biol Chem 282:37537-37544
    • (2007) J Biol Chem , vol.282 , pp. 37537-37544
    • Poltermann, S.1    Kunert, A.2    Von Der Heide, M.3    Eck, R.4    Hartmann, A.5    Zipfel, P.F.6
  • 215
    • 0036090968 scopus 로고    scopus 로고
    • Evidence for a partial redundancy of the fibronectin-binding proteins for the transfer of mycoloyl residues onto the cell wall arabinogalactan termini of Mycobacterium tuberculosis
    • Puech V, Guilhot C, Perez E, Tropis M, Armitige LY, Gicquel B, Daffé M (2002) Evidence for a partial redundancy of the fibronectin-binding proteins for the transfer of mycoloyl residues onto the cell wall arabinogalactan termini of Mycobacterium tuberculosis. Mol Microbiol 44:1109-1122
    • (2002) Mol Microbiol , vol.44 , pp. 1109-1122
    • Puech, V.1    Guilhot, C.2    Perez, E.3    Tropis, M.4    Armitige, L.Y.5    Gicquel, B.6    Daffé, M.7
  • 216
    • 9244227956 scopus 로고    scopus 로고
    • Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis
    • Qamra R, Mande SC (2004) Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis. J Bacteriol 186:8105-8113
    • (2004) J Bacteriol , vol.186 , pp. 8105-8113
    • Qamra, R.1    Mande, S.C.2
  • 217
    • 4344587654 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins
    • Qamra R, Srinivas V, Mande SC (2004) Mycobacterium tuberculosis GroEL homologues unusually exist as lower oligomers and retain the ability to suppress aggregation of substrate proteins. J Mol Biol 342:605-617
    • (2004) J Mol Biol , vol.342 , pp. 605-617
    • Qamra, R.1    Srinivas, V.2    Mande, S.C.3
  • 220
    • 34047254111 scopus 로고    scopus 로고
    • The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor
    • Raje CI, Kumar S, Harle A, Nanda JS, Raje M (2007) The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor. J Biol Chem 282: 3252-3261
    • (2007) J Biol Chem , vol.282 , pp. 3252-3261
    • Raje, C.I.1    Kumar, S.2    Harle, A.3    Nanda, J.S.4    Raje, M.5
  • 221
    • 33751190062 scopus 로고    scopus 로고
    • Schistosoma bovis: Plasminogen binding in adults and the identification of plasminogen-binding proteins from the worm tegument
    • Ramajo-Hernández A, Pérez-Sánchez R, Ramajo-Martín V, Oleaga A (2007) Schistosoma bovis: plasminogen binding in adults and the identification of plasminogen-binding proteins from the worm tegument. Exp Parasitol 115:83-91
    • (2007) Exp Parasitol , vol.115 , pp. 83-91
    • Ramajo-Hernández, A.1    Pérez-Sánchez, R.2    Ramajo-Martín, V.3    Oleaga, A.4
  • 222
    • 51449119201 scopus 로고    scopus 로고
    • CD43 controls the intracellular growth of Mycobacterium tuberculosis through the induction of TNF-alpha-mediated apoptosis
    • Randhawa AK, Ziltener HJ, Stokes RW (2008) CD43 controls the intracellular growth of Mycobacterium tuberculosis through the induction of TNF-alpha-mediated apoptosis. Cell Microbiol 10:2105-2117
    • (2008) Cell Microbiol , vol.10 , pp. 2105-2117
    • Randhawa, A.K.1    Ziltener, H.J.2    Stokes, R.W.3
  • 223
    • 77955261029 scopus 로고    scopus 로고
    • Differential expression of the multiple chaperonins of Mycobacterium smegmatis
    • Rao T, Lund PA (2010) Differential expression of the multiple chaperonins of Mycobacterium smegmatis. FEMS Microbiol Lett 310:24-31
    • (2010) FEMS Microbiol Lett , vol.310 , pp. 24-31
    • Rao, T.1    Lund, P.A.2
  • 224
    • 0030550356 scopus 로고    scopus 로고
    • Isolation and characterization of a 70 kDa protein from Mycobacterium avium
    • Ratnakar P, Rao SP, Catanzaro A (1996) Isolation and characterization of a 70 kDa protein from Mycobacterium avium. Microb Pathog 21:471-486
    • (1996) Microb Pathog , vol.21 , pp. 471-486
    • Ratnakar, P.1    Rao, S.P.2    Catanzaro, A.3
  • 226
    • 0347479351 scopus 로고    scopus 로고
    • Mycobacterium avium-superoxide dismutase binds to epithelial cell aldolase, glyceraldehyde-3-phosphate dehydrogenase and cyclophilin A
    • Reddy VM, Suleman FG (2004) Mycobacterium avium-superoxide dismutase binds to epithelial cell aldolase, glyceraldehyde-3-phosphate dehydrogenase and cyclophilin A.Microb Pathog 36:67-74
    • (2004) Microb Pathog , vol.36 , pp. 67-74
    • Reddy, V.M.1    Suleman, F.G.2
  • 227
    • 0028839088 scopus 로고
    • The role of an enolase-related molecule in plasminogen binding to cells
    • Redlitz A, Fowler BJ, Plow EF, Miles LA (1995) The role of an enolase-related molecule in plasminogen binding to cells. Eur J Biochem 227:407-415
    • (1995) Eur J Biochem , vol.227 , pp. 407-415
    • Redlitz, A.1    Fowler, B.J.2    Plow, E.F.3    Miles, L.A.4
  • 229
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • Richter K, Haslbeck M, Buchner J (2010) The heat shock response: life on the verge of death. Mol Cell 40:253-266
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 230
    • 2942519856 scopus 로고    scopus 로고
    • Differential effects of Mycobacterium tuberculosis chaperonins on bronchial eosinophilia and hyperresponsiveness in a murine model of allergic inflammation
    • Riffo-Vasquez Y, Spina D, Page C, Desel C, Whelan M, Tormay P, Singh M, Henderson B, Coates ARM (2004) Differential effects of Mycobacterium tuberculosis chaperonins on bronchial eosinophilia and hyperresponsiveness in a murine model of allergic inflammation. Clin Exp Allergy 34:712-719
    • (2004) Clin Exp Allergy , vol.34 , pp. 712-719
    • Riffo-Vasquez, Y.1    Spina, D.2    Page, C.3    Desel, C.4    Whelan, M.5    Tormay, P.6    Singh, M.7    Henderson, B.8    Arm, C.9
  • 231
    • 0033960935 scopus 로고    scopus 로고
    • Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines
    • Ronning DR, Klabunde T, Besra GS, Vissa VD, Belisle JT, Sacchettini JC (2000) Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Nature Struct Biol 7:141-146
    • (2000) Nature Struct Biol , vol.7 , pp. 141-146
    • Ronning, D.R.1    Klabunde, T.2    Besra, G.S.3    Vissa, V.D.4    Belisle, J.T.5    Sacchettini, J.C.6
  • 232
    • 79953766008 scopus 로고    scopus 로고
    • Molecular model of hexokinase binding to the outer mitochondrial membrane porin (VDAC1): Implication for the design of new cancer therapies
    • Epub ahead of print
    • Rosano C (2011) Molecular model of hexokinase binding to the outer mitochondrial membrane porin (VDAC1): implication for the design of new cancer therapies. Mitochondrion [Epub ahead of print]
    • (2011) Mitochondrion
    • Rosano, C.1
  • 234
    • 30644476416 scopus 로고    scopus 로고
    • Killing of cryptococcus neoformans by Staphylococcus aureus: The role of cryptococcal capsular polysaccharide in the fungal-bacteria interaction
    • Saito F, Ikeda R (2005) Killing of cryptococcus neoformans by Staphylococcus aureus: the role of cryptococcal capsular polysaccharide in the fungal-bacteria interaction. Med Mycol 43: 603-612
    • (2005) Med Mycol , vol.43 , pp. 603-612
    • Saito, F.1    Ikeda, R.2
  • 235
    • 0033050139 scopus 로고    scopus 로고
    • Influence of temperature and growth phase on expression of a 104-kilodalton Listeria adhesion protein in Listeria monocytogenes
    • Santiago NI, Zipf A, Bhunia AK (2006) Influence of temperature and growth phase on expression of a 104-kilodalton Listeria adhesion protein in Listeria monocytogenes. Appl Environ Microbiol 65:2765-2769
    • (2006) Appl Environ Microbiol , vol.65 , pp. 2765-2769
    • Santiago, N.I.1    Zipf, A.2    Bhunia, A.K.3
  • 236
    • 0035800883 scopus 로고    scopus 로고
    • Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation
    • Sasu S, LaVerda D, Qureshi N, Golenbock DT, Beasley D (2001) Chlamydia pneumoniae and chlamydial heat shock protein 60 stimulate proliferation of human vascular smooth muscle cells via toll-like receptor 4 and p44/p42 mitogen-activated protein kinase activation. Circ Res 89:244-250
    • (2001) Circ Res , vol.89 , pp. 244-250
    • Sasu, S.1    Laverda, D.2    Qureshi, N.3    Golenbock, D.T.4    Beasley, D.5
  • 237
    • 77749279755 scopus 로고    scopus 로고
    • The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension
    • Schauer K, Muller C, Carrière M, Labigne A, Cavazza C, De Reuse H (2010) The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension. J Bacteriol 192:1231-1237
    • (2010) J Bacteriol , vol.192 , pp. 1231-1237
    • Schauer, K.1    Muller, C.2    Carrière, M.3    Labigne, A.4    Cavazza, C.5    De Reuse, H.6
  • 238
    • 0037815283 scopus 로고    scopus 로고
    • Glucose-6-phosphate isomerase is necessary for embryo implantation in the domestic ferret
    • Schulz LC, Bahr JM (2003) Glucose-6-phosphate isomerase is necessary for embryo implantation in the domestic ferret. Proc Natl Acad Sci U S A 100:8561-8566
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8561-8566
    • Schulz, L.C.1    Bahr, J.M.2
  • 240
    • 0141834741 scopus 로고    scopus 로고
    • Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: Surface localization, enzymatic activity, and protein-protein interactions
    • Seifert KN, McArthur WP, Bleiweis AS, Brady LJ (2003) Characterization of group B streptococcal glyceraldehyde-3-phosphate dehydrogenase: surface localization, enzymatic activity, and protein-protein interactions. Can J Microbiol 49:350-356
    • (2003) Can J Microbiol , vol.49 , pp. 350-356
    • Seifert, K.N.1    McArthur, W.P.2    Bleiweis, A.S.3    Brady, L.J.4
  • 241
    • 53449086920 scopus 로고    scopus 로고
    • Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: Racemization and DNA gyrase inhibition are two independent activities of the enzyme
    • Sengupta S, Ghosh S, Nagaraja V (2008) Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzyme. Microbiology 154:2796-2803
    • (2008) Microbiology , vol.154 , pp. 2796-2803
    • Sengupta, S.1    Ghosh, S.2    Nagaraja, V.3
  • 242
    • 65549164868 scopus 로고    scopus 로고
    • Surfaceexpressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila
    • Sha J, Erova TE, Alyea RA, Wang S, Olano JP, Pancholi V, Chopra AK (2009) Surfaceexpressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila. J Bacteriol 191:3095-3107
    • (2009) J Bacteriol , vol.191 , pp. 3095-3107
    • Sha, J.1    Erova, T.E.2    Alyea, R.A.3    Wang, S.4    Olano, J.P.5    Pancholi, V.6    Chopra, A.K.7
  • 243
    • 23844452781 scopus 로고    scopus 로고
    • New nuclear functions of the glycolytic protein, glyceraldehyde-3- phosphate dehydrogenase, in mammalian cells
    • Sirover MA (2005) New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. J Cell Biochem 95:45-52
    • (2005) J Cell Biochem , vol.95 , pp. 45-52
    • Sirover, M.A.1
  • 245
    • 33745727551 scopus 로고    scopus 로고
    • Bartonella bacilliformis GroEL: Effect on growth of human vascular endothelial cells in infected cocultures
    • Smitherman LS, Minnick MF (2005) Bartonella bacilliformis GroEL: effect on growth of human vascular endothelial cells in infected cocultures. Ann N Y Acad Sci 1063:286-298
    • (2005) Ann N y Acad Sci , vol.1063 , pp. 286-298
    • Smitherman, L.S.1    Minnick, M.F.2
  • 246
    • 77953923581 scopus 로고    scopus 로고
    • Lactobacillus jensenii surface associated proteins inhibit Neisseria gonorrhoeae adherence to epithelial cells
    • Spurbeck RR, Arvidson CG (2010) Lactobacillus jensenii surface associated 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
  • 248
    • 77953232857 scopus 로고    scopus 로고
    • Moonlighting function of glycerol kinase causes systems-level changes in rat hepatoma cells
    • Sriram G, Parr LS, Rahib L, Liao JC, Dipple KM (2010) Moonlighting function of glycerol kinase causes systems-level changes in rat hepatoma cells. Metab Eng 12:332-340
    • (2010) Metab Eng , vol.12 , pp. 332-340
    • Sriram, G.1    Parr, L.S.2    Rahib, L.3    Liao, J.C.4    Dipple, K.M.5
  • 249
    • 64649106434 scopus 로고    scopus 로고
    • Aldolase is essential for energy production and bridging adhesin-actin cytoskeletal interactions during parasite invasion of host cells
    • Starnes GL, Coincon M, Sygusch J, Sibley LD (2009) Aldolase is essential for energy production and bridging adhesin-actin cytoskeletal interactions during parasite invasion of host cells. Cell Host Microbe 5:353-364
    • (2009) Cell Host Microbe , vol.5 , pp. 353-364
    • Starnes, G.L.1    Coincon, M.2    Sygusch, J.3    Sibley, L.D.4
  • 250
    • 0026762988 scopus 로고
    • Interleukin 4 potently enhances murine macrophage mannose receptor activity: A marker of alternative immunologic macrophage activation
    • Stein M, Keshav S, Harris N, Gordon S (1992) Interleukin 4 potently enhances murine macrophage mannose receptor activity: a marker of alternative immunologic macrophage activation. J Exp Med 176:287-292
    • (1992) J Exp Med , vol.176 , pp. 287-292
    • Stein, M.1    Keshav, S.2    Harris, N.3    Gordon, S.4
  • 252
    • 0033545874 scopus 로고    scopus 로고
    • The crystal structure of a multifunctional protein: Phosphoglucose isomerase/autocrine motility factor/neuroleukin
    • Sun YJ, Chou CC, Chen WS, Wu RT, Meng M, Hsiao CD (1999) The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin. Proc Natl Acad Sci U S A 96:5412-5417
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 5412-5417
    • Sun, Y.J.1    Chou, C.C.2    Chen, W.S.3    Wu, R.T.4    Meng, M.5    Hsiao, C.D.6
  • 253
    • 75049085147 scopus 로고    scopus 로고
    • Osteoimmunology and the effects of the immune system on bone
    • Takayanagi H (2009) Osteoimmunology and the effects of the immune system on bone. Nat Rev Rheumatol 5:667-676
    • (2009) Nat Rev Rheumatol , vol.5 , pp. 667-676
    • Takayanagi, H.1
  • 254
    • 19944424434 scopus 로고    scopus 로고
    • Helicobacter pylori heat-shock protein 60 induces inflammatory responses through the toll-like receptor-triggered pathway in cultured human gastric epithelial cells
    • Takenaka R, Yokota K, Ayada K, Mizuno M, Zhao Y, Fujinami Y, Lin SN, Toyokawa T, Okada H, Shiratori Y, Oguma Y (2004) Helicobacter pylori heat-shock protein 60 induces inflammatory responses through the toll-like receptor-triggered pathway in cultured human gastric epithelial cells. Microbiology 150:3913-3922
    • (2004) Microbiology , vol.150 , pp. 3913-3922
    • Takenaka, R.1    Yokota, K.2    Ayada, K.3    Mizuno, M.4    Zhao, Y.5    Fujinami, Y.6    Lin, S.N.7    Toyokawa, T.8    Okada, H.9    Shiratori, Y.10    Oguma, Y.11
  • 255
    • 67149093411 scopus 로고    scopus 로고
    • Vaccination with Streptococcus suis serotype 2 recombinant 6PGD protein provides protection against S. suis infection in swine
    • Tan C, Liu M, Liu J, Yuan F, Fu S, Liu Y, Jin M, Bei W, Chen H (2009) Vaccination with Streptococcus suis serotype 2 recombinant 6PGD protein provides protection against S. suis infection in swine. FEMS Microbiol Lett 296:78-83
    • (2009) FEMS Microbiol Lett , vol.296 , pp. 78-83
    • Tan, C.1    Liu, M.2    Liu, J.3    Yuan, F.4    Fu, S.5    Liu, Y.6    Jin, M.7    Bei, W.8    Chen, H.9
  • 257
    • 0036275173 scopus 로고    scopus 로고
    • Transferrin binding in Staphylococcus aureus: Involvement of a cell wall-anchored protein
    • Taylor JM, Heinrichs DE (2002) Transferrin binding in Staphylococcus aureus: involvement of a cell wall-anchored protein. Mol Microbiol 43:1603-1614
    • (2002) Mol Microbiol , vol.43 , pp. 1603-1614
    • Taylor, J.M.1    Heinrichs, D.E.2
  • 259
    • 33744901493 scopus 로고    scopus 로고
    • Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils
    • Terao Y, Yamaguchi M, Hamada S, Kawabata S (2006) Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils. J Biol Chem 281:14215-14223
    • (2006) J Biol Chem , vol.281 , pp. 14215-14223
    • Terao, Y.1    Yamaguchi, M.2    Hamada, S.3    Kawabata, S.4
  • 260
    • 17144408301 scopus 로고    scopus 로고
    • The intercellular signaling activity of the Mycobacterium tuberculosis chaperonin 60.1 protein resides in the equatorial domain
    • Tormay P, Coates AR, Henderson B (2005) The intercellular signaling activity of the Mycobacterium tuberculosis chaperonin 60.1 protein resides in the equatorial domain. J Biol Chem 280:14272-14277
    • (2005) J Biol Chem , vol.280 , pp. 14272-14277
    • Tormay, P.1    Coates, A.R.2    Henderson, B.3
  • 261
    • 33845928009 scopus 로고    scopus 로고
    • Cell adherence-promoted activity of Plesiomonas shigelloides groEL
    • Tsugawa H, Ito H, Ohshima M, Okawa Y (2007) Cell adherence-promoted activity of Plesiomonas shigelloides groEL. J Med Microbiol 56:23-29
    • (2007) J Med Microbiol , vol.56 , pp. 23-29
    • Tsugawa, H.1    Ito, H.2    Ohshima, M.3    Okawa, Y.4
  • 262
    • 77951586997 scopus 로고    scopus 로고
    • The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion
    • Tunio SA, Oldfield NJ, Berry A, Ala'Aldeen DA, Wooldridge KG, Turner DP (2010a) The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: surface localization and role in host cell adhesion. Mol Microbiol 76:605-615
    • (2010) Mol Microbiol , vol.76 , pp. 605-615
    • Tunio, S.A.1    Oldfield, N.J.2    Berry, A.3    Ala'Aldeen, D.A.4    Wooldridge, K.G.5    Turner, D.P.6
  • 263
    • 78049510509 scopus 로고    scopus 로고
    • The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells
    • Tunio SA, Oldfield NJ, Ala'Aldeen DA, Wooldridge KG, Turner DP (2010b) The role of glyceraldehyde 3-phosphate dehydrogenase (GapA-1) in Neisseria meningitidis adherence to human cells. BMC Microbiol 10:280
    • (2010) BMC Microbiol , vol.10 , pp. 280
    • Tunio, S.A.1    Oldfield, N.J.2    Ala'Aldeen, D.A.3    Wooldridge, K.G.4    Turner, D.P.5
  • 264
    • 17144417382 scopus 로고    scopus 로고
    • Heat-shock proteins induce T-cell regulation of chronic inflammation
    • Van Eden W, van der Zee R, Prakken B (2005) Heat-shock proteins induce T-cell regulation of chronic inflammation. Nature Revs Immunol 5:318-330
    • (2005) Nature Revs Immunol , vol.5 , pp. 318-330
    • Van Eden, W.1    Van Der Zee, R.2    Prakken, B.3
  • 265
    • 33747881274 scopus 로고    scopus 로고
    • Therapeutic efficacy and safety of chaperonin 10 in patients with rheumatoid arthritis: A double-blind randomised trial
    • Vanags D, Williams B, Johnson B, Hall S, Nash P, Taylor A, Weiss J, Feeney D (2006) Therapeutic efficacy and safety of chaperonin 10 in patients with rheumatoid arthritis: a double-blind randomised trial. Lancet 368:855-863
    • (2006) Lancet , vol.368 , pp. 855-863
    • Vanags, D.1    Williams, B.2    Johnson, B.3    Hall, S.4    Nash, P.5    Taylor, A.6    Weiss, J.7    Feeney, D.8
  • 270
    • 33846230030 scopus 로고    scopus 로고
    • Collagen binding protein Mip enables Legionella pneumophila to transmigrate through a barrier of NCI-H292 lung epithelial cells and extracellular matrix
    • Wagner C, Khan AS, Kamphausen T, Schmausser B, Unal C, Lorenz U, Fischer G, Hacker J, Steinert M (2007) Collagen binding protein Mip enables Legionella pneumophila to transmigrate through a barrier of NCI-H292 lung epithelial cells and extracellular matrix. Cell Microbiol 9:450-462
    • (2007) Cell Microbiol , vol.9 , pp. 450-462
    • Wagner, C.1    Khan, A.S.2    Kamphausen, T.3    Schmausser, B.4    Unal, C.5    Lorenz, U.6    Fischer, G.7    Hacker, J.8    Steinert, M.9
  • 271
    • 44349152970 scopus 로고    scopus 로고
    • Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse
    • Walsh A, Whelan D, Bielanowicz A, Skinner B, Aitken RJ, O'Bryan MK, Nixon B (2008) Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse. Biol Reprod 78: 983-993
    • (2008) Biol Reprod , vol.78 , pp. 983-993
    • Walsh, A.1    Whelan, D.2    Bielanowicz, A.3    Skinner, B.4    Aitken, R.J.5    O'Bryan, M.K.6    Nixon, B.7
  • 272
    • 0842283062 scopus 로고    scopus 로고
    • Heat shock protein 60 acts as a receptor for the Listeria adhesion protein in Caco-2 cells
    • Wampler JL, Kim KP, Jaradat Z, Bhunia AK (2004) Heat shock protein 60 acts as a receptor for the Listeria adhesion protein in Caco-2 cells. Infect Immun 72:931-936
    • (2004) Infect Immun , vol.72 , pp. 931-936
    • Wampler, J.L.1    Kim, K.P.2    Jaradat, Z.3    Bhunia, A.K.4
  • 273
    • 51149092565 scopus 로고    scopus 로고
    • A novel cell wall-anchored peptidoglycan hydrolase (autolysin), IspC, essential for Listeria monocytogenes virulence: Genetic and proteomic analysis
    • Wang L, Lin M (2008) A novel cell wall-anchored peptidoglycan hydrolase (autolysin), IspC, essential for Listeria monocytogenes virulence: genetic and proteomic analysis. Microbiology 154:1900-1913
    • (2008) Microbiology , vol.154 , pp. 1900-1913
    • Wang, L.1    Lin, M.2
  • 275
    • 0036721692 scopus 로고    scopus 로고
    • Stimulation of Th1-polarizing cytokines, C-C chemokines, maturation of dendritic cells, and adjuvant function by the peptide binding fragment of heat shock protein 70
    • Wang Y, Kelly CG, Singh M, McGowan EG, Carrara AS, Bergmeier LA, Lehner T (2002) Stimulation of Th1-polarizing cytokines, C-C chemokines, maturation of dendritic cells, and adjuvant function by the peptide binding fragment of heat shock protein 70. J Immunol 169:2422-2429
    • (2002) J Immunol , vol.169 , pp. 2422-2429
    • Wang, Y.1    Kelly, C.G.2    Singh, M.3    McGowan, E.G.4    Carrara, A.S.5    Bergmeier, L.A.6    Lehner, T.7
  • 276
    • 14844355875 scopus 로고    scopus 로고
    • Identification of stimulating and inhibitory epitopes within the heat shock protein 70 molecule that modulate cytokine production and maturation of dendritic cells
    • Wang Y, Whittall T, McGowan E, Younson J, Kelly C, Bergmeier LA, Singh M, Lehner T (2005) Identification of stimulating and inhibitory epitopes within the heat shock protein 70 molecule that modulate cytokine production and maturation of dendritic cells. J Immunol 174: 3306-3316
    • (2005) J Immunol , vol.174 , pp. 3306-3316
    • Wang, Y.1    Whittall, T.2    McGowan, E.3    Younson, J.4    Kelly, C.5    Bergmeier, L.A.6    Singh, M.7    Lehner, T.8
  • 277
    • 0030012538 scopus 로고    scopus 로고
    • Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide
    • Watanabe H, Takehana K, Date M, Shinozaki T, Raz A (1996) Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide. Cancer Res 56:2960-2963
    • (1996) Cancer Res , vol.56 , pp. 2960-2963
    • Watanabe, H.1    Takehana, K.2    Date, M.3    Shinozaki, T.4    Raz, A.5
  • 279
    • 41949084224 scopus 로고    scopus 로고
    • Role of Chlamydia pneumoniae in atherosclerosis
    • Watson C, Alp NJ (2008) Role of Chlamydia pneumoniae in atherosclerosis. Clin Sci (Lond) 114:509-531
    • (2008) Clin Sci (Lond) , vol.114 , pp. 509-531
    • Watson, C.1    Alp, N.J.2
  • 280
    • 0032474895 scopus 로고    scopus 로고
    • Telomeres: Moonlighting by DNA repair proteins
    • Weaver DT (1998) Telomeres: moonlighting by DNA repair proteins. Curr Biol 8:R492-R494
    • (1998) Curr Biol , vol.8
    • Weaver, D.T.1
  • 283
    • 0026465216 scopus 로고
    • The antigen 85 complex: A major secretion product of Mycobacterium tuberculosis
    • Wicker HG, Harboe M (1992) The antigen 85 complex: a major secretion product of Mycobacterium tuberculosis. Microbiol Rev 56:648-661
    • (1992) Microbiol Rev , vol.56 , pp. 648-661
    • Wicker, H.G.1    Harboe, M.2
  • 284
    • 0141593638 scopus 로고    scopus 로고
    • Effect of acidic pH on expression of surfaceassociated proteins of Streptococcus oralis
    • Wilkins JC, Beighton D, Homer KA (2003) Effect of acidic pH on expression of surfaceassociated proteins of Streptococcus oralis. Appl Environ Microbiol 69:5290-5296
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5290-5296
    • Wilkins, J.C.1    Beighton, D.2    Homer, K.A.3
  • 285
    • 44249087380 scopus 로고    scopus 로고
    • Efficacy and safety of chaperonin 10 in patients with moderate to severe plaque psoriasis: Evidence of utility beyond a single indication
    • Williams B, Vanags D, Hall S, McCormack C, Foley P, Weiss J, Johnson B, Latz E, Feeney D (2008) Efficacy and safety of chaperonin 10 in patients with moderate to severe plaque psoriasis: evidence of utility beyond a single indication. Arch Dermatol 144:683-685
    • (2008) Arch Dermatol , vol.144 , pp. 683-685
    • Williams, B.1    Vanags, D.2    Hall, S.3    McCormack, C.4    Foley, P.5    Weiss, J.6    Johnson, B.7    Latz, E.8    Feeney, D.9
  • 286
    • 0031661935 scopus 로고    scopus 로고
    • Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of the plr gene does not reduce plasmin binding to group A streptococci
    • Winram SB, Lottenberg R (1998) Site-directed mutagenesis of streptococcal plasmin receptor protein (Plr) identifies the C-terminal Lys334 as essential for plasmin binding, but mutation of the plr gene does not reduce plasmin binding to group A streptococci. Microbiology 144: 2025-2035
    • (1998) Microbiology , vol.144 , pp. 2025-2035
    • Winram, S.B.1    Lottenberg, R.2
  • 287
    • 51449110112 scopus 로고    scopus 로고
    • The two homologous chaperonin 60 proteins of Mycobacterium tuberculosis have distinct effects on monocyte differentiation into osteoclasts
    • Winrow VR, Mesher J, Meghji S, Morris CJ, Fox S, Coates AR, Tormay P, Blake D, Henderson B (2008) The two homologous chaperonin 60 proteins of Mycobacterium tuberculosis have distinct effects on monocyte differentiation into osteoclasts. Cell Microbiol 10:2091-2104
    • (2008) Cell Microbiol , vol.10 , pp. 2091-2104
    • Winrow, V.R.1    Mesher, J.2    Meghji, S.3    Morris, C.J.4    Fox, S.5    Coates, A.R.6    Tormay, P.7    Blake, D.8    Henderson, B.9
  • 288
    • 48749096247 scopus 로고    scopus 로고
    • Comparative proteome analysis of secreted proteins of Streptococcus suis serotype 9 isolates from diseased and healthy pigs
    • Wu Z, Zhang W, Lu C (2008) Comparative proteome analysis of secreted proteins of Streptococcus suis serotype 9 isolates from diseased and healthy pigs. Microb Pathog 45: 159-166
    • (2008) Microb Pathog , vol.45 , pp. 159-166
    • Wu, Z.1    Zhang, W.2    Lu, C.3
  • 289
    • 47049107204 scopus 로고    scopus 로고
    • Chlamydia pneumoniae GroEL1 protein is cell surface associated and required for infection of HEp-2 cells
    • Wuppermann FN, Mölleken K, Julien M, Jantos CA, Hegemann JH (2008) Chlamydia pneumoniae GroEL1 protein is cell surface associated and required for infection of HEp-2 cells. J Bacteriol 190:3757-3767
    • (2008) J Bacteriol , vol.190 , pp. 3757-3767
    • Wuppermann, F.N.1    Mölleken, K.2    Julien, M.3    Jantos, C.A.4    Hegemann, J.H.5
  • 290
    • 0029898821 scopus 로고    scopus 로고
    • The differentiation and maturation mediator for human myeloid leukemia cells shares homology with neuroleukin or phosphoglucose isomerase
    • Xu W, Seiter K, Feldman E, Ahmed T, Chiao JW (1996) The differentiation and maturation mediator for human myeloid leukemia cells shares homology with neuroleukin or phosphoglucose isomerase. Blood 87:4502-4506
    • (1996) Blood , vol.87 , pp. 4502-4506
    • Xu, W.1    Seiter, K.2    Feldman, E.3    Ahmed, T.4    Chiao, J.W.5
  • 292
    • 0029742511 scopus 로고    scopus 로고
    • Flow cytometric analysis of the heat shock protein 60 expressed on the cell surface of Helicobacter pylori
    • Yamaguchi H, Osaki T, Taguchi H, Hanawa T, Yamamoto T, Kamiya S (1996) Flow cytometric analysis of the heat shock protein 60 expressed on the cell surface of Helicobacter pylori. J Med Microbiol 45:270-277
    • (1996) J Med Microbiol , vol.45 , pp. 270-277
    • Yamaguchi, H.1    Osaki, T.2    Taguchi, H.3    Hanawa, T.4    Yamamoto, T.5    Kamiya, S.6
  • 294
    • 0030882160 scopus 로고    scopus 로고
    • Heat-shock protein 60 homologue of Helicobacter pylori is associated with adhesion of H. pylori to human gastric epithelial cells
    • Yamaguchi H, Osaki T, Kurihara N, Taguchi H, Hanawa T, Yamamoto T, Kamiya S (1997b) Heat-shock protein 60 homologue of Helicobacter pylori is associated with adhesion of H. pylori to human gastric epithelial cells. J Med Microbiol 46:825-831
    • (1997) J Med Microbiol , vol.46 , pp. 825-831
    • Yamaguchi, H.1    Osaki, T.2    Kurihara, N.3    Taguchi, H.4    Hanawa, T.5    Yamamoto, T.6    Kamiya, S.7
  • 295
    • 0032724070 scopus 로고    scopus 로고
    • Induction of secretion of interleukin-8 from human gastric epithelial cells by heatshock protein 60 homologue of Helicobacter pylori
    • Yamaguchi H, Osaki T, Kurihara N, Kitajima M, Kai M, Takahashi M, Taguchi H, Kamiya S (1999) Induction of secretion of interleukin-8 from human gastric epithelial cells by heatshock protein 60 homologue of Helicobacter pylori. J Med Microbiol 48:927-933
    • (1999) J Med Microbiol , vol.48 , pp. 927-933
    • Yamaguchi, H.1    Osaki, T.2    Kurihara, N.3    Kitajima, M.4    Kai, M.5    Takahashi, M.6    Taguchi, H.7    Kamiya, S.8
  • 296
    • 77953548538 scopus 로고    scopus 로고
    • Localization by scanning immunoelectron microscopy of triosephosphate isomerase, the molecules responsible for contact-mediated killing of Cryptococcus, on the surface of Staphylococcus
    • Yamaguchi M, Ikeda R, Nishimura M, Kawamoto S (2010) Localization by scanning immunoelectron microscopy of triosephosphate isomerase, the molecules responsible for contact-mediated killing of Cryptococcus, on the surface of Staphylococcus. Microbiol Immunol 54:368-370
    • (2010) Microbiol Immunol , vol.54 , pp. 368-370
    • Yamaguchi, M.1    Ikeda, R.2    Nishimura, M.3    Kawamoto, S.4
  • 299
    • 0033021431 scopus 로고    scopus 로고
    • Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: Sequestration of ATP from macrophage P2Z receptors?
    • Zaborina O, Li X, Cheng G, Kapatral V, Chakrabarty AM (1999) Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: sequestration of ATP from macrophage P2Z receptors? Mol Microbiol 31:1333-1343
    • (1999) Mol Microbiol , vol.31 , pp. 1333-1343
    • Zaborina, O.1    Li, X.2    Cheng, G.3    Kapatral, V.4    Chakrabarty, A.M.5
  • 300
    • 0037603062 scopus 로고    scopus 로고
    • Early pregnancy factor treatment suppresses the inflammatory response and adhesion molecule expression in the spinal cord of SJL/J mice with experimental autoimmune encephalomyelitis and the delayed-type hypersensitivity reaction to trinitrochlorobenzene in normal BALB/c mice
    • Zhang B, Walsh MD, Nguyen KB, Hillyard NC, Cavanagh AC, McCombe PA, Morton H (2003) Early pregnancy factor treatment suppresses the inflammatory response and adhesion molecule expression in the spinal cord of SJL/J mice with experimental autoimmune encephalomyelitis and the delayed-type hypersensitivity reaction to trinitrochlorobenzene in normal BALB/c mice. J Neurol Sci 212:37-46
    • (2003) J Neurol Sci , vol.212 , pp. 37-46
    • Zhang, B.1    Walsh, M.D.2    Nguyen, K.B.3    Hillyard, N.C.4    Cavanagh, A.C.5    McCombe, P.A.6    Morton, H.7
  • 301
    • 0347511932 scopus 로고    scopus 로고
    • Long-term effect of heat shock protein 60 from Actinobacillus actinomycetemcomitans on epithelial cell viability and mitogen-activated protein kinases
    • Zhang L, Pelech S, Uitto VJ (2004a) Long-term effect of heat shock protein 60 from Actinobacillus actinomycetemcomitans on epithelial cell viability and mitogen-activated protein kinases. Infect Immun 72:38-45
    • (2004) Infect Immun , vol.72 , pp. 38-45
    • Zhang, L.1    Pelech, S.2    Uitto, V.J.3
  • 302
    • 2942611392 scopus 로고    scopus 로고
    • Bacterial heat shock protein 60 may increase epithelial cell migration through activation of MAP kinases and inhibition of alpha6beta4 integrin expression
    • Zhang L, Koivisto L, Heino J, Uitto VJ (2004b) Bacterial heat shock protein 60 may increase epithelial cell migration through activation of MAP kinases and inhibition of alpha6beta4 integrin expression. Biochem Biophys Res Commun 319:1088-1095
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1088-1095
    • Zhang, L.1    Koivisto, L.2    Heino, J.3    Uitto, V.J.4
  • 303
    • 33847226673 scopus 로고    scopus 로고
    • Helicobacter pylori heat-shock protein 60 induces interleukin-8 via a toll-like receptor (TLR)2 and mitogen-activated protein (MAP) kinase pathway in human monocytes
    • Zhao Y, Yokota K, Ayada K, Yamamoto Y, Okada T, Shen L, Oguma K (2007) Helicobacter pylori heat-shock protein 60 induces interleukin-8 via a toll-like receptor (TLR)2 and mitogen-activated protein (MAP) kinase pathway in human monocytes. J Med Microbiol 56: 154-164
    • (2007) J Med Microbiol , vol.56 , pp. 154-164
    • Zhao, Y.1    Yokota, K.2    Ayada, K.3    Yamamoto, Y.4    Okada, T.5    Shen, L.6    Oguma, K.7


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