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Volumn 5, Issue 3, 2010, Pages

Mass spectrometric analysis of Ehrlichia chaffeensis tandem repeat proteins reveals evidence of phosphorylation and absence of glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; AMIDE; CARBOXYLIC ACID; GLYCAN DERIVATIVE; PROTEIN; SERINE; TANDEM REPEAT PROTEIN 32; TANDEM REPEAT PROTEIN 47; TYROSINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; PHOSPHOPROTEIN; PHOSPHOTYROSINE; POLYSACCHARIDE;

EID: 77949723101     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009552     Document Type: Article
Times cited : (16)

References (58)
  • 1
    • 0030959591 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis inclusions are early endosomes which selectively accumulate transferrin receptor
    • Barnewall RE, Rikihisa Y, Lee EH (1997) Ehrlichia chaffeensis inclusions are early endosomes which selectively accumulate transferrin receptor. Infect Immun 65: 1455-1461.
    • (1997) Infect Immun , vol.65 , pp. 1455-1461
    • Barnewall, R.E.1    Rikihisa, Y.2    Lee, E.H.3
  • 2
    • 0031867451 scopus 로고    scopus 로고
    • Protein kinase A-mediated inhibition of gamma interferon-induced tyrosine phosphorylation of Janus kinases and latent cytoplasmic transcription factors in human monocytes by Ehrlichia chaffeensis
    • Lee EH, Rikihisa Y (1998) Protein kinase A-mediated inhibition of gamma interferon-induced tyrosine phosphorylation of Janus kinases and latent cytoplasmic transcription factors in human monocytes by Ehrlichia chaffeensis. Infect Immun 66: 2514-2520.
    • (1998) Infect Immun , vol.66 , pp. 2514-2520
    • Lee, E.H.1    Rikihisa, Y.2
  • 3
    • 1642473014 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis downregulates surface Toll-like receptors 2/4, CD14 and transcription factors PU.1 and inhibits lipopolysaccharide activation of NF-kappa B, ERK 1/2 and p38 MAPK in host monocytes
    • Lin M, Rikihisa Y (2004) Ehrlichia chaffeensis downregulates surface Toll-like receptors 2/4, CD14 and transcription factors PU.1 and inhibits lipopolysaccharide activation of NF-kappa B, ERK 1/2 and p38 MAPK in host monocytes. Cell Microbiol 6: 175-186.
    • (2004) Cell Microbiol , vol.6 , pp. 175-186
    • Lin, M.1    Rikihisa, Y.2
  • 4
    • 0030727110 scopus 로고    scopus 로고
    • Western immunoblotting analysis of the antibody responses of patients with human monocytotropic ehrlichiosis to different strains of Ehrlichia chaffeensis and Ehrlichia canis
    • Chen SM, Cullman LC, Walker DH (1997) Western immunoblotting analysis of the antibody responses of patients with human monocytotropic ehrlichiosis to different strains of Ehrlichia chaffeensis and Ehrlichia canis. Clin Diagn Lab Immunol 4: 731-735.
    • (1997) Clin Diagn Lab Immunol , vol.4 , pp. 731-735
    • Chen, S.M.1    Cullman, L.C.2    Walker, D.H.3
  • 5
    • 0028079454 scopus 로고
    • Identification of the antigenic constituents of Ehrlichia chaffeensis
    • Chen SM, Dumler JS, Feng HM, Walker DH (1994) Identification of the antigenic constituents of Ehrlichia chaffeensis. Am J Trop Med Hyg 50: 52-58.
    • (1994) Am J Trop Med Hyg , vol.50 , pp. 52-58
    • Chen, S.M.1    Dumler, J.S.2    Feng, H.M.3    Walker, D.H.4
  • 6
    • 0242500346 scopus 로고    scopus 로고
    • Kinetics of antibody response to Ehrlichia canis immunoreactive proteins
    • McBride JW, Corstvet RE, Gaunt SD, Boudreaux C, Guedry T, et al. (2003) Kinetics of antibody response to Ehrlichia canis immunoreactive proteins. Infect Immun 71: 2516-2524.
    • (2003) Infect Immun , vol.71 , pp. 2516-2524
    • McBride, J.W.1    Corstvet, R.E.2    Gaunt, S.D.3    Boudreaux, C.4    Guedry, T.5
  • 7
    • 0027982519 scopus 로고
    • Western immunoblot analysis of Ehrlichia chaffeensis, E. canis, or E. ewingii infections in dogs and humans
    • Rikihisa Y, Ewing SA, Fox JC (1994) Western immunoblot analysis of Ehrlichia chaffeensis, E. canis, or E. ewingii infections in dogs and humans. J Clin Microbiol 32: 2107-2112.
    • (1994) J Clin Microbiol , vol.32 , pp. 2107-2112
    • Rikihisa, Y.1    Ewing, S.A.2    Fox, J.C.3
  • 8
    • 29644434935 scopus 로고    scopus 로고
    • Differentially expressed and secreted major immunoreactive protein orthologs of Ehrlichia canis and E. chaffeensis elicit early antibody responses to epitopes on glycosylated tandem repeats
    • Doyle CK, Nethery KA, Popov VL, McBride JW (2006) Differentially expressed and secreted major immunoreactive protein orthologs of Ehrlichia canis and E. chaffeensis elicit early antibody responses to epitopes on glycosylated tandem repeats. Infect Immun 74: 711-720.
    • (2006) Infect Immun , vol.74 , pp. 711-720
    • Doyle, C.K.1    Nethery, K.A.2    Popov, V.L.3    McBride, J.W.4
  • 9
    • 42149191556 scopus 로고    scopus 로고
    • A variable-length PCR target protein of Ehrlichia chaffeensis contains major species-specific antibody epitopes in acidic serine-rich tandem repeats
    • Luo T, Zhang X, Wakeel A, Popov VL, McBride JW (2008) A variable-length PCR target protein of Ehrlichia chaffeensis contains major species-specific antibody epitopes in acidic serine-rich tandem repeats. Infect Immun 76: 1572-1580.
    • (2008) Infect Immun , vol.76 , pp. 1572-1580
    • Luo, T.1    Zhang, X.2    Wakeel, A.3    Popov, V.L.4    McBride, J.W.5
  • 10
    • 0029858809 scopus 로고    scopus 로고
    • The recombinant 120-kilodalton protein of Ehrlichia chaffeensis, a potential diagnostic tool
    • Yu XJ, Crocquet-Valdes P, Cullman LC, Walker DH (1996) The recombinant 120-kilodalton protein of Ehrlichia chaffeensis, a potential diagnostic tool. J Clin Microbiol 34: 2853-2855.
    • (1996) J Clin Microbiol , vol.34 , pp. 2853-2855
    • Yu, X.J.1    Crocquet-Valdes, P.2    Cullman, L.C.3    Walker, D.H.4
  • 11
    • 2942706116 scopus 로고    scopus 로고
    • Diversity in coding tandem repeats in related Neisseria spp
    • Jordan P, Snyder LA, Saunders NJ (2003) Diversity in coding tandem repeats in related Neisseria spp. BMC Microbiol 3: 23.
    • (2003) BMC Microbiol , vol.3 , pp. 23
    • Jordan, P.1    Snyder, L.A.2    Saunders, N.J.3
  • 13
    • 21544480823 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the chlamydial effector protein Tarp is species specific and not required for recruitment of actin
    • Clifton DR, Dooley CA, Grieshaber SS, Carabeo RA, Fields KA, et al. (2005) Tyrosine phosphorylation of the chlamydial effector protein Tarp is species specific and not required for recruitment of actin. Infect Immun 73: 3860-3868.
    • (2005) Infect Immun , vol.73 , pp. 3860-3868
    • Clifton, D.R.1    Dooley, C.A.2    Grieshaber, S.S.3    Carabeo, R.A.4    Fields, K.A.5
  • 14
    • 0025739814 scopus 로고
    • Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci
    • Gaillard JL, Berche P, Frehel C, Gouin E, Cossart P (1991) Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci. Cell 65: 1127-1141.
    • (1991) Cell , vol.65 , pp. 1127-1141
    • Gaillard, J.L.1    Berche, P.2    Frehel, C.3    Gouin, E.4    Cossart, P.5
  • 15
    • 34547962985 scopus 로고    scopus 로고
    • Gene conversion is a convergent strategy for pathogen antigenic variation
    • Palmer GH, Brayton KA (2007) Gene conversion is a convergent strategy for pathogen antigenic variation. Trends Parasitol 23: 408-413.
    • (2007) Trends Parasitol , vol.23 , pp. 408-413
    • Palmer, G.H.1    Brayton, K.A.2
  • 16
    • 0025896984 scopus 로고
    • A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences
    • Wren BW (1991) A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol Microbiol 5: 797-803.
    • (1991) Mol Microbiol , vol.5 , pp. 797-803
    • Wren, B.W.1
  • 17
    • 65049091364 scopus 로고    scopus 로고
    • A chlamydial type III-secreted effector protein (Tarp) is predominantly recognized by antibodies from humans infected with Chlamydia trachomatis and induces protective immunity against upper genital tract pathologies in mice
    • Wang J, Chen L, Chen F, Zhang X, Zhang Y, et al. (2009) A chlamydial type III-secreted effector protein (Tarp) is predominantly recognized by antibodies from humans infected with Chlamydia trachomatis and induces protective immunity against upper genital tract pathologies in mice. Vaccine 27: 2967-2980.
    • (2009) Vaccine , vol.27 , pp. 2967-2980
    • Wang, J.1    Chen, L.2    Chen, F.3    Zhang, X.4    Zhang, Y.5
  • 18
    • 0030909642 scopus 로고    scopus 로고
    • Characterization of two distinct opsonic and protective epitopes within the alpha C protein of the group B Streptococcus
    • Kling DE, Gravekamp C, Madoff LC, Michel JL (1997) Characterization of two distinct opsonic and protective epitopes within the alpha C protein of the group B Streptococcus. Infect Immun 65: 1462-1467.
    • (1997) Infect Immun , vol.65 , pp. 1462-1467
    • Kling, D.E.1    Gravekamp, C.2    Madoff, L.C.3    Michel, J.L.4
  • 19
  • 20
    • 2142714511 scopus 로고    scopus 로고
    • Glycosylation of Anaplasma marginale major surface protein 1a and its putative role in adhesion to tick cells
    • Garcia-Garcia JC, de la Fuente J, Bell-Eunice G, Blouin EF, Kocan KM (2004) Glycosylation of Anaplasma marginale major surface protein 1a and its putative role in adhesion to tick cells. Infect Immun 72: 3022-3030.
    • (2004) Infect Immun , vol.72 , pp. 3022-3030
    • Garcia-Garcia, J.C.1    de la Fuente, J.2    Bell-Eunice, G.3    Blouin, E.F.4    Kocan, K.M.5
  • 21
    • 0033823329 scopus 로고    scopus 로고
    • The 120 kDa outer membrane protein of Ehrlichia chaffeensis: Preferential expression on dense-core cells and gene expression in Escherichia coli associated with attachment and entry
    • Popov VL, Yu X, Walker DH (2000) The 120 kDa outer membrane protein of Ehrlichia chaffeensis: preferential expression on dense-core cells and gene expression in Escherichia coli associated with attachment and entry. Microb Pathog 28: 71-80.
    • (2000) Microb Pathog , vol.28 , pp. 71-80
    • Popov, V.L.1    Yu, X.2    Walker, D.H.3
  • 22
    • 0035753611 scopus 로고    scopus 로고
    • Evolution and function of tandem repeats in the major surface protein 1a of the ehrlichial pathogen Anaplasma marginale
    • de la Fuente J, Garcia-Garcia JC, Blouin EF, Rodriguez SD, Garcia MA, et al. (2001) Evolution and function of tandem repeats in the major surface protein 1a of the ehrlichial pathogen Anaplasma marginale. Anim Health Res Rev 2: 163-173.
    • (2001) Anim Health Res Rev , vol.2 , pp. 163-173
    • de la Fuente, J.1    Garcia-Garcia, J.C.2    Blouin, E.F.3    Rodriguez, S.D.4    Garcia, M.A.5
  • 23
    • 1242298610 scopus 로고    scopus 로고
    • Adhesion of outer membrane proteins containing tandem repeats of Anaplasma and Ehrlichia species (Rickettsiales: Anaplasmataceae) to tick cells
    • de la Fuente J, Garcia-Garcia JC, Barbet AF, Blouin EF, Kocan KM (2004) Adhesion of outer membrane proteins containing tandem repeats of Anaplasma and Ehrlichia species (Rickettsiales: Anaplasmataceae) to tick cells. Vet Microbiol 98: 313-322.
    • (2004) Vet Microbiol , vol.98 , pp. 313-322
    • de la Fuente, J.1    Garcia-Garcia, J.C.2    Barbet, A.F.3    Blouin, E.F.4    Kocan, K.M.5
  • 24
    • 0032038633 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of three granulocytic Ehrlichia genes encoding high-molecular-weight immunoreactive proteins
    • Storey JR, Doros-Richert LA, Gingrich-Baker C, Munroe K, Mather TN, et al. (1998) Molecular cloning and sequencing of three granulocytic Ehrlichia genes encoding high-molecular-weight immunoreactive proteins. Infect Immun 66: 1356-1363.
    • (1998) Infect Immun , vol.66 , pp. 1356-1363
    • Storey, J.R.1    Doros-Richert, L.A.2    Gingrich-Baker, C.3    Munroe, K.4    Mather, T.N.5
  • 25
    • 65449163095 scopus 로고    scopus 로고
    • An Ehrlichia chaffeensis tandem repeat protein interacts with multiple host targets involved in cell signaling, transcriptional regulation, and vesicle trafficking
    • Wakeel A, Kuriakose JA, McBride JW (2009) An Ehrlichia chaffeensis tandem repeat protein interacts with multiple host targets involved in cell signaling, transcriptional regulation, and vesicle trafficking. Infect Immun 77: 1734-1745.
    • (2009) Infect Immun , vol.77 , pp. 1734-1745
    • Wakeel, A.1    Kuriakose, J.A.2    McBride, J.W.3
  • 26
    • 0036067107 scopus 로고    scopus 로고
    • Never say never again: Protein glycosylation in pathogenic bacteria
    • Benz I, Schmidt MA (2002) Never say never again: protein glycosylation in pathogenic bacteria. Mol Microbiol 45: 267-276.
    • (2002) Mol Microbiol , vol.45 , pp. 267-276
    • Benz, I.1    Schmidt, M.A.2
  • 27
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski CM, Wren BW (2005) Protein glycosylation in bacterial mucosal pathogens. Nat Rev Microbiol 3: 225-237.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 28
    • 65449156907 scopus 로고    scopus 로고
    • Differential expression and glycosylation of Anaplasma phagocytophilum major surface protein 2 paralogs during cultivation in sialyl Lewis x-deficient host cells
    • Troese MJ, Sarkar M, Galloway NL, Thomas RJ, Kearns SA, et al. (2009) Differential expression and glycosylation of Anaplasma phagocytophilum major surface protein 2 paralogs during cultivation in sialyl Lewis x-deficient host cells. Infect Immun 77: 1746-1756.
    • (2009) Infect Immun , vol.77 , pp. 1746-1756
    • Troese, M.J.1    Sarkar, M.2    Galloway, N.L.3    Thomas, R.J.4    Kearns, S.A.5
  • 29
    • 0037387036 scopus 로고    scopus 로고
    • Bacterial glycoproteins: Functions, biosynthesis and applications
    • Upreti RK, Kumar M, Shankar V (2003) Bacterial glycoproteins: functions, biosynthesis and applications. Proteomics 3: 363-379.
    • (2003) Proteomics , vol.3 , pp. 363-379
    • Upreti, R.K.1    Kumar, M.2    Shankar, V.3
  • 30
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt MA, Riley LW, Benz I (2003) Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol 11: 554-561.
    • (2003) Trends Microbiol , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 31
    • 0033985107 scopus 로고    scopus 로고
    • Glycosylation of homologous immunodominant proteins of Ehrlichia chaffeensis and Ehrlichia canis
    • McBride JW, Yu XJ, Walker DH (2000) Glycosylation of homologous immunodominant proteins of Ehrlichia chaffeensis and Ehrlichia canis. Infect Immun 68: 13-18.
    • (2000) Infect Immun , vol.68 , pp. 13-18
    • McBride, J.W.1    Yu, X.J.2    Walker, D.H.3
  • 32
    • 33845968519 scopus 로고    scopus 로고
    • Identification of a glycosylated Ehrlichia canis 19-kilodalton major immunoreactive protein with a species-specific serine-rich glycopeptide epitope
    • McBride JW, Doyle CK, Zhang X, Cardenas AM, Popov VL, et al. (2007) Identification of a glycosylated Ehrlichia canis 19-kilodalton major immunoreactive protein with a species-specific serine-rich glycopeptide epitope. Infect Immun 75: 74-82.
    • (2007) Infect Immun , vol.75 , pp. 74-82
    • McBride, J.W.1    Doyle, C.K.2    Zhang, X.3    Cardenas, A.M.4    Popov, V.L.5
  • 33
    • 11044231152 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis expresses macrophage- and tick cell-specific 28-kilodalton outer membrane proteins
    • Singu V, Liu H, Cheng C, Ganta RR (2005) Ehrlichia chaffeensis expresses macrophage- and tick cell-specific 28-kilodalton outer membrane proteins. Infect Immun 73: 79-87.
    • (2005) Infect Immun , vol.73 , pp. 79-87
    • Singu, V.1    Liu, H.2    Cheng, C.3    Ganta, R.R.4
  • 34
    • 33747009964 scopus 로고    scopus 로고
    • Unique macrophage and tick cell-specific protein expression from the p28/p30-outer membrane protein multigene locus in Ehrlichia chaffeensis and Ehrlichia canis
    • Singu V, Peddireddi L, Sirigireddy KR, Cheng C, Munderloh U, et al. (2006) Unique macrophage and tick cell-specific protein expression from the p28/p30-outer membrane protein multigene locus in Ehrlichia chaffeensis and Ehrlichia canis. Cell Microbiol 8: 1475-1487.
    • (2006) Cell Microbiol , vol.8 , pp. 1475-1487
    • Singu, V.1    Peddireddi, L.2    Sirigireddy, K.R.3    Cheng, C.4    Munderloh, U.5
  • 35
    • 42949116993 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum MSP2(P44)-18 predominates and is modified into multiple isoforms in human myeloid cells
    • Sarkar M, Troese MJ, Kearns SA, Yang T, Reneer DV, et al. (2008) Anaplasma phagocytophilum MSP2(P44)-18 predominates and is modified into multiple isoforms in human myeloid cells. Infect Immun 76: 2090-2098.
    • (2008) Infect Immun , vol.76 , pp. 2090-2098
    • Sarkar, M.1    Troese, M.J.2    Kearns, S.A.3    Yang, T.4    Reneer, D.V.5
  • 37
    • 33744820791 scopus 로고    scopus 로고
    • The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies
    • Mavromatis K, Doyle CK, Lykidis A, Ivanova N, Francino MP, et al. (2006) The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies. J Bacteriol 188: 4015-4023.
    • (2006) J Bacteriol , vol.188 , pp. 4015-4023
    • Mavromatis, K.1    Doyle, C.K.2    Lykidis, A.3    Ivanova, N.4    Francino, M.P.5
  • 39
    • 0028840449 scopus 로고
    • Meningococcal pilin: A glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose
    • Stimson E, Virji M, Makepeace K, Dell A, Morris HR, et al. (1995) Meningococcal pilin: a glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose. Mol Microbiol 17: 1201-1214.
    • (1995) Mol Microbiol , vol.17 , pp. 1201-1214
    • Stimson, E.1    Virji, M.2    Makepeace, K.3    Dell, A.4    Morris, H.R.5
  • 40
    • 3242663192 scopus 로고    scopus 로고
    • Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili
    • Hegge FT, Hitchen PG, Aas FE, Kristiansen H, Lovold C, et al. (2004) Unique modifications with phosphocholine and phosphoethanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili. Proc Natl Acad Sci U S A 101: 10798-10803.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10798-10803
    • Hegge, F.T.1    Hitchen, P.G.2    Aas, F.E.3    Kristiansen, H.4    Lovold, C.5
  • 41
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • Schirm M, Soo EC, Aubry AJ, Austin J, Thibault P, et al. (2003) Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori. Mol Microbiol 48: 1579-1592.
    • (2003) Mol Microbiol , vol.48 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5
  • 42
    • 34347231618 scopus 로고    scopus 로고
    • Targeted metabolomics analysis of Campylobacter coli VC167 reveals legionaminic acid derivatives as novel flagellar glycans
    • McNally DJ, Aubry AJ, Hui JP, Khieu NH, Whitfield D, et al. (2007) Targeted metabolomics analysis of Campylobacter coli VC167 reveals legionaminic acid derivatives as novel flagellar glycans. J Biol Chem 282: 14463-14475.
    • (2007) J Biol Chem , vol.282 , pp. 14463-14475
    • McNally, D.J.1    Aubry, A.J.2    Hui, J.P.3    Khieu, N.H.4    Whitfield, D.5
  • 43
    • 33845940986 scopus 로고    scopus 로고
    • Glycosylation of Pseudomonas aeruginosa strain Pa5196 type IV pilins with mycobacterium-like alpha-1,5-linked d-Araf oligosaccharides
    • Voisin S, Kus JV, Houliston S, St-Michael F, Watson D, et al. (2007) Glycosylation of Pseudomonas aeruginosa strain Pa5196 type IV pilins with mycobacterium-like alpha-1,5-linked d-Araf oligosaccharides. J Bacteriol 189: 151-159.
    • (2007) J Bacteriol , vol.189 , pp. 151-159
    • Voisin, S.1    Kus, J.V.2    Houliston, S.3    St-Michael, F.4    Watson, D.5
  • 44
    • 67650410438 scopus 로고    scopus 로고
    • Major species-specific antibody epitopes of the Ehrlichia chaffeensis p120 and E. canis p140 orthologs in surface-exposed tandem repeat regions
    • Luo T, Zhang X, McBride JW (2009) Major species-specific antibody epitopes of the Ehrlichia chaffeensis p120 and E. canis p140 orthologs in surface-exposed tandem repeat regions. Clin Vaccine Immunol 16: 982-990.
    • (2009) Clin Vaccine Immunol , vol.16 , pp. 982-990
    • Luo, T.1    Zhang, X.2    McBride, J.W.3
  • 45
    • 24944519321 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated bacterial effector proteins: The enemies within
    • Backert S, Selbach M (2005) Tyrosine-phosphorylated bacterial effector proteins: the enemies within. Trends Microbiol 13: 476-484.
    • (2005) Trends Microbiol , vol.13 , pp. 476-484
    • Backert, S.1    Selbach, M.2
  • 46
    • 34848862803 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection
    • Lin M, den Dulk-Ras A, Hooykaas PJ, Rikihisa Y (2007) Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection. Cell Microbiol 9: 2644-2657.
    • (2007) Cell Microbiol , vol.9 , pp. 2644-2657
    • Lin, M.1    den Dulk-Ras, A.2    Hooykaas, P.J.3    Rikihisa, Y.4
  • 47
    • 56649083314 scopus 로고    scopus 로고
    • Complex kinase requirements for Chlamydia trachomatis Tarp phosphorylation
    • Mehlitz A, Banhart S, Hess S, Selbach M, Meyer TF (2008) Complex kinase requirements for Chlamydia trachomatis Tarp phosphorylation. FEMS Microbiol Lett 289: 233-240.
    • (2008) FEMS Microbiol Lett , vol.289 , pp. 233-240
    • Mehlitz, A.1    Banhart, S.2    Hess, S.3    Selbach, M.4    Meyer, T.F.5
  • 49
    • 64649100982 scopus 로고    scopus 로고
    • Host cell interactome of tyrosine-phosphorylated bacterial proteins
    • Selbach M, Paul FE, Brandt S, Guye P, Daumke O, et al. (2009) Host cell interactome of tyrosine-phosphorylated bacterial proteins. Cell Host Microbe 5: 397-403.
    • (2009) Cell Host Microbe , vol.5 , pp. 397-403
    • Selbach, M.1    Paul, F.E.2    Brandt, S.3    Guye, P.4    Daumke, O.5
  • 50
    • 33846683630 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: An emerging regulatory device of bacterial physiology
    • Grangeasse C, Cozzone AJ, Deutscher J, Mijakovic I (2007) Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. Trends Biochem Sci 32: 86-94.
    • (2007) Trends Biochem Sci , vol.32 , pp. 86-94
    • Grangeasse, C.1    Cozzone, A.J.2    Deutscher, J.3    Mijakovic, I.4
  • 51
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R, Goodlett DR (2001) Mass spectrometry in proteomics. Chem Rev 101: 269-295.
    • (2001) Chem Rev , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 52
    • 0026657722 scopus 로고
    • Modification of acidic residues normalizes sodium dodecyl sulfate-polyacrylamide gel electrophoresis of caldesmon and other proteins that migrate anomalously
    • Graceffa P, Jancso A, Mabuchi K (1992) Modification of acidic residues normalizes sodium dodecyl sulfate-polyacrylamide gel electrophoresis of caldesmon and other proteins that migrate anomalously. Arch Biochem Biophys 297: 46-51.
    • (1992) Arch Biochem Biophys , vol.297 , pp. 46-51
    • Graceffa, P.1    Jancso, A.2    Mabuchi, K.3
  • 53
    • 0027184837 scopus 로고
    • The anomalous electrophoretic behavior of the human papillomavirus type 16 E7 protein is due to the high content of acidic amino acid residues
    • Armstrong DJ, Roman A (1993) The anomalous electrophoretic behavior of the human papillomavirus type 16 E7 protein is due to the high content of acidic amino acid residues. Biochem Biophys Res Commun 192: 1380-1387.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 1380-1387
    • Armstrong, D.J.1    Roman, A.2
  • 55
    • 0346095160 scopus 로고    scopus 로고
    • Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior
    • Alves VS, Pimenta DC, Sattlegger E, Castilho BA (2004) Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior. Biochem Biophys Res Commun 314: 229-234.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 229-234
    • Alves, V.S.1    Pimenta, D.C.2    Sattlegger, E.3    Castilho, B.A.4
  • 56
    • 19444386382 scopus 로고    scopus 로고
    • Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms
    • Alves VS, Castilho BA (2005) Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms. Biochem Biophys Res Commun 332: 450-455.
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 450-455
    • Alves, V.S.1    Castilho, B.A.2
  • 57
    • 41549138353 scopus 로고    scopus 로고
    • Flagellin and outer surface proteins from Borrelia burgdorferi are not glycosylated
    • Sterba J, Vancova M, Rudenko N, Golovchenko M, Tremblay TL, et al. (2008) Flagellin and outer surface proteins from Borrelia burgdorferi are not glycosylated. J Bacteriol 190: 2619-2623.
    • (2008) J Bacteriol , vol.190 , pp. 2619-2623
    • Sterba, J.1    Vancova, M.2    Rudenko, N.3    Golovchenko, M.4    Tremblay, T.L.5
  • 58
    • 33748310540 scopus 로고    scopus 로고
    • Proteomic analysis of hypoxia/ischemia-induced alteration of cortical development and dopamine neurotransmission in neonatal rat
    • Hu X, Rea HC, Wiktorowicz JE, Perez-Polo JR (2006) Proteomic analysis of hypoxia/ischemia-induced alteration of cortical development and dopamine neurotransmission in neonatal rat. J Proteome Res 5: 2396-2404.
    • (2006) J Proteome Res , vol.5 , pp. 2396-2404
    • Hu, X.1    Rea, H.C.2    Wiktorowicz, J.E.3    Perez-Polo, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.