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Volumn 7, Issue 12, 2012, Pages

Analysis of the Secretomes of Paracoccidioides Mycelia and Yeast Cells

Author keywords

[No Author keywords available]

Indexed keywords

BREFELDIN A; CELL PROTEIN; FUNGAL PROTEIN; ISOPROTEIN; PROTEOME;

EID: 84871341396     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052470     Document Type: Article
Times cited : (46)

References (76)
  • 1
    • 33646730017 scopus 로고    scopus 로고
    • Paracoccdidioides brasiliensis
    • Mandell GL, Bennet JE, Dollin R, editors, Philadelphia
    • Restrepo A, Tobon A (2005) Paracoccdidioides brasiliensis. In: Mandell GL, Bennet JE, Dollin R, editors. Principles and Practice of infectious diseases. Philadelphia. 3062-3068.
    • (2005) Principles and Practice of infectious diseases , pp. 3062-3068
    • Restrepo, A.1    Tobon, A.2
  • 2
    • 28944448746 scopus 로고    scopus 로고
    • Cryptic speciation and recombination in the fungus Paracoccidioides brasiliensis as revealed by gene genealogies
    • Matute DR, McEwen JG, Puccia R, Montes BA, San-Blas G, et al. (2006) Cryptic speciation and recombination in the fungus Paracoccidioides brasiliensis as revealed by gene genealogies. Mol Biol Evol 23: 65-73.
    • (2006) Mol Biol Evol , vol.23 , pp. 65-73
    • Matute, D.R.1    McEwen, J.G.2    Puccia, R.3    Montes, B.A.4    San-Blas, G.5
  • 3
    • 41649095870 scopus 로고    scopus 로고
    • New Paracoccidioides brasiliensis isolate reveals unexpected genomic variability in this human pathogen
    • Carrero LL, Nino-Vega G, Teixeira MM, Carvalho MJ, Soares CMA, et al. (2008) New Paracoccidioides brasiliensis isolate reveals unexpected genomic variability in this human pathogen. Fungal Genet Biol 45: 605-612.
    • (2008) Fungal Genet Biol , vol.45 , pp. 605-612
    • Carrero, L.L.1    Nino-Vega, G.2    Teixeira, M.M.3    Carvalho, M.J.4    Soares, C.M.A.5
  • 6
    • 0002059569 scopus 로고
    • Historical evolution of the knowledge on paracoccidioidomycosis and its etiological agent, Paracoccidioides brasiliensis
    • Franco M, Lacaz CS, Restrepo-Moreno A, del Negro GB, editors, London: CRC Press
    • Lacaz CS (1994) Historical evolution of the knowledge on paracoccidioidomycosis and its etiological agent, Paracoccidioides brasiliensis. In: Franco M, Lacaz CS, Restrepo-Moreno A, del Negro GB, editors. Paracoccidioidomycosis. London: CRC Press. 1-7.
    • (1994) Paracoccidioidomycosis , pp. 1-7
    • Lacaz, C.S.1
  • 7
    • 0036301549 scopus 로고    scopus 로고
    • Paracoccidioides brasiliensis and paracoccidioidomycosis: molecular approaches to morphogenesis, diagnosis, epidemiology, taxonomy and genetics
    • San-Blas G, Nino-Vega G, Iturriaga T, (2002) Paracoccidioides brasiliensis and paracoccidioidomycosis: molecular approaches to morphogenesis, diagnosis, epidemiology, taxonomy and genetics. Med Mycol 40: 225-242.
    • (2002) Med Mycol , vol.40 , pp. 225-242
    • San-Blas, G.1    Nino-Vega, G.2    Iturriaga, T.3
  • 8
    • 78650296757 scopus 로고    scopus 로고
    • Secretome: clues into pathogen infection and clinical applications
    • Ranganathan S, Garg G, (2009) Secretome: clues into pathogen infection and clinical applications. Genome Med 1: 113.111-113.117.
    • (2009) Genome Med , vol.1 , pp. 111-117
    • Ranganathan, S.1    Garg, G.2
  • 9
    • 30344443077 scopus 로고    scopus 로고
    • Non-conventional protein secretion in yeast
    • Nombela C, Gil C, Chaffin WL, (2006) Non-conventional protein secretion in yeast. Trends Microbiol 14: 15-21.
    • (2006) Trends Microbiol , vol.14 , pp. 15-21
    • Nombela, C.1    Gil, C.2    Chaffin, W.L.3
  • 10
    • 79953675108 scopus 로고    scopus 로고
    • Definition of the extracellular proteome of pathogenic-phase Histoplasma capsulatum
    • Holbrook ED, Edwards JA, Youseff BH, Rappleye CA, (2011) Definition of the extracellular proteome of pathogenic-phase Histoplasma capsulatum. J Proteome Res 10: 1929-1943.
    • (2011) J Proteome Res , vol.10 , pp. 1929-1943
    • Holbrook, E.D.1    Edwards, J.A.2    Youseff, B.H.3    Rappleye, C.A.4
  • 12
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G, Dobberstein B, (1996) Common principles of protein translocation across membranes. Science 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 13
    • 70349998172 scopus 로고    scopus 로고
    • A two-dimensional electrophoretic profile of the proteins secreted by Herbaspirillum seropedicae strain Z78
    • Chaves DF, de Souza EM, Monteiro RA, de Oliveira Pedrosa F, (2009) A two-dimensional electrophoretic profile of the proteins secreted by Herbaspirillum seropedicae strain Z78. J Proteomics 73: 50-56.
    • (2009) J Proteomics , vol.73 , pp. 50-56
    • Chaves, D.F.1    de Souza, E.M.2    Monteiro, R.A.3    de Oliveira Pedrosa, F.4
  • 14
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • 2009/01/06 ed
    • Nickel W, Rabouille C (2009) Mechanisms of regulated unconventional protein secretion. Nat Rev Mol Cell Biol. 2009/01/06 ed. 148-155.
    • (2009) Nat Rev Mol Cell Biol , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 15
    • 33751199883 scopus 로고    scopus 로고
    • Exosomes: from biogenesis and secretion to biological function
    • Keller S, Sanderson MP, Stoeck A, Altevogt P, (2006) Exosomes: from biogenesis and secretion to biological function. Immunol Lett 107: 102-108.
    • (2006) Immunol Lett , vol.107 , pp. 102-108
    • Keller, S.1    Sanderson, M.P.2    Stoeck, A.3    Altevogt, P.4
  • 16
    • 77956216059 scopus 로고    scopus 로고
    • Characterization of yeast extracellular vesicles: evidence for the participation of different pathways of cellular traffic in vesicle biogenesis
    • Oliveira DL, Nakayasu ES, Joffe LS, Guimaraes AJ, Sobreira TJ, et al. (2010) Characterization of yeast extracellular vesicles: evidence for the participation of different pathways of cellular traffic in vesicle biogenesis. PLoS One 5: e11113.
    • (2010) PLoS One , vol.5
    • Oliveira, D.L.1    Nakayasu, E.S.2    Joffe, L.S.3    Guimaraes, A.J.4    Sobreira, T.J.5
  • 17
    • 69949169040 scopus 로고    scopus 로고
    • A role for vesicular transport of macromolecules across cell walls in fungal pathogenesis
    • Nosanchuk JD, Nimrichter L, Casadevall A, Rodrigues ML, (2008) A role for vesicular transport of macromolecules across cell walls in fungal pathogenesis. Commun Integr Biol 1: 37-39.
    • (2008) Commun Integr Biol , vol.1 , pp. 37-39
    • Nosanchuk, J.D.1    Nimrichter, L.2    Casadevall, A.3    Rodrigues, M.L.4
  • 18
    • 47549119474 scopus 로고    scopus 로고
    • Vesicular transport in Histoplasma capsulatum: an effective mechanism for trans-cell wall transfer of proteins and lipids in ascomycetes
    • Albuquerque PC, Nakayasu ES, Rodrigues ML, Frases S, Casadevall A, et al. (2008) Vesicular transport in Histoplasma capsulatum: an effective mechanism for trans-cell wall transfer of proteins and lipids in ascomycetes. Cell Microbiol 10: 1695-1710.
    • (2008) Cell Microbiol , vol.10 , pp. 1695-1710
    • Albuquerque, P.C.1    Nakayasu, E.S.2    Rodrigues, M.L.3    Frases, S.4    Casadevall, A.5
  • 19
    • 40649121336 scopus 로고    scopus 로고
    • Extracellular vesicles produced by Cryptococcus neoformans contain protein components associated with virulence
    • Rodrigues ML, Nakayasu ES, Oliveira DL, Nimrichter L, Nosanchuk JD, et al. (2008) Extracellular vesicles produced by Cryptococcus neoformans contain protein components associated with virulence. Eukaryot Cell 7: 58-67.
    • (2008) Eukaryot Cell , vol.7 , pp. 58-67
    • Rodrigues, M.L.1    Nakayasu, E.S.2    Oliveira, D.L.3    Nimrichter, L.4    Nosanchuk, J.D.5
  • 20
    • 79952300000 scopus 로고    scopus 로고
    • The pathogenic fungus Paracoccidioides brasiliensis exports extracellular vesicles containing highly immunogenic alpha-Galactosyl epitopes
    • Vallejo MC, Matsuo AL, Ganiko L, Medeiros LC, Miranda K, et al. (2011) The pathogenic fungus Paracoccidioides brasiliensis exports extracellular vesicles containing highly immunogenic alpha-Galactosyl epitopes. Eukaryot Cell 10: 343-351.
    • (2011) Eukaryot Cell , vol.10 , pp. 343-351
    • Vallejo, M.C.1    Matsuo, A.L.2    Ganiko, L.3    Medeiros, L.C.4    Miranda, K.5
  • 22
    • 77956640401 scopus 로고    scopus 로고
    • Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cells
    • Nogueira SV, Fonseca FL, Rodrigues ML, Mundodi V, Abi-Chacra EA, et al. (2010) Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cells. Infect Immun 78: 4040-4050.
    • (2010) Infect Immun , vol.78 , pp. 4040-4050
    • Nogueira, S.V.1    Fonseca, F.L.2    Rodrigues, M.L.3    Mundodi, V.4    Abi-Chacra, E.A.5
  • 23
    • 74549142895 scopus 로고    scopus 로고
    • Detection of a homotetrameric structure and protein-protein interactions of Paracoccidioides brasiliensis formamidase lead to new functional insights
    • Borges CL, Parente JA, Barbosa MS, Santana JM, Bao SN, et al. (2010) Detection of a homotetrameric structure and protein-protein interactions of Paracoccidioides brasiliensis formamidase lead to new functional insights. FEMS Yeast Res 10: 104-113.
    • (2010) FEMS Yeast Res , vol.10 , pp. 104-113
    • Borges, C.L.1    Parente, J.A.2    Barbosa, M.S.3    Santana, J.M.4    Bao, S.N.5
  • 24
    • 73649107910 scopus 로고    scopus 로고
    • Characterization of a secreted aspartyl protease of the fungal pathogen Paracoccidioides brasiliensis
    • Tacco BA, Parente JA, Barbosa MS, Bao SN, Goes Tde S, et al. (2009) Characterization of a secreted aspartyl protease of the fungal pathogen Paracoccidioides brasiliensis. Med Mycol 47: 845-854.
    • (2009) Med Mycol , vol.47 , pp. 845-854
    • Tacco, B.A.1    Parente, J.A.2    Barbosa, M.S.3    Bao, S.N.4    Goes, T.S.5
  • 25
    • 78149493291 scopus 로고    scopus 로고
    • A secreted serine protease of Paracoccidioides brasiliensis and its interactions with fungal proteins
    • Parente JA, Salem-Izacc SM, Santana JM, Pereira M, Borges CL, et al. (2010) A secreted serine protease of Paracoccidioides brasiliensis and its interactions with fungal proteins. BMC Microbiol 10: 292.
    • (2010) BMC Microbiol , vol.10 , pp. 292
    • Parente, J.A.1    Salem-Izacc, S.M.2    Santana, J.M.3    Pereira, M.4    Borges, C.L.5
  • 26
    • 34548594209 scopus 로고    scopus 로고
    • The transcriptional profile of Paracoccidioides brasiliensis yeast cells is influenced by human plasma
    • Bailão AM, Shrank A, Borges CL, Parente JA, Dutra V, et al. (2007) The transcriptional profile of Paracoccidioides brasiliensis yeast cells is influenced by human plasma. FEMS Immunol Med Microbiol 51: 43-57.
    • (2007) FEMS Immunol Med Microbiol , vol.51 , pp. 43-57
    • Bailão, A.M.1    Shrank, A.2    Borges, C.L.3    Parente, J.A.4    Dutra, V.5
  • 27
    • 84857823526 scopus 로고    scopus 로고
    • Vesicle and vesicle-free extracellular proteome of Paracoccidioides brasiliensis: comparative analysis with other pathogenic fungi
    • Vallejo MC, Nakayasu ES, Matsuo AL, Sobreira TJ, Longo LV, et al. (2012) Vesicle and vesicle-free extracellular proteome of Paracoccidioides brasiliensis: comparative analysis with other pathogenic fungi. J Proteome Res 11: 1676-1685.
    • (2012) J Proteome Res , vol.11 , pp. 1676-1685
    • Vallejo, M.C.1    Nakayasu, E.S.2    Matsuo, A.L.3    Sobreira, T.J.4    Longo, L.V.5
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0004262043 scopus 로고    scopus 로고
    • A Laboratory Manual. New York: Cold Spring Harbor Laboratory Press
    • Sambrook J, Russel DW (2001) Molecular Cloning. A Laboratory Manual. New York: Cold Spring Harbor Laboratory Press.
    • (2001) Molecular Cloning
    • Sambrook, J.1    Russel, D.W.2
  • 30
    • 0041358797 scopus 로고    scopus 로고
    • Sample preparation for two-dimensional gel electrophoresis
    • Shaw MM, Riederer BM, (2003) Sample preparation for two-dimensional gel electrophoresis. Proteomics 3: 1408-1417.
    • (2003) Proteomics , vol.3 , pp. 1408-1417
    • Shaw, M.M.1    Riederer, B.M.2
  • 31
    • 0034940957 scopus 로고    scopus 로고
    • Reduction and alkylation of proteins in preparation of two-dimensional map analysis: why, when, and how?
    • Herbert B, Galvani M, Hamdan M, Olivieri E, MacCarthy J, et al. (2001) Reduction and alkylation of proteins in preparation of two-dimensional map analysis: why, when, and how? Electrophoresis 22: 2046-2057.
    • (2001) Electrophoresis , vol.22 , pp. 2046-2057
    • Herbert, B.1    Galvani, M.2    Hamdan, M.3    Olivieri, E.4    MacCarthy, J.5
  • 32
    • 79960852690 scopus 로고    scopus 로고
    • Proteomic analysis reveals that iron availability alters the metabolic status of the pathogenic fungus Paracoccidioides brasiliensis
    • Parente AF, Borges CL, Bailao AM, Sousa MV, Ricart CA, et al. (2011) Proteomic analysis reveals that iron availability alters the metabolic status of the pathogenic fungus Paracoccidioides brasiliensis. PLoS One 6: e22810.
    • (2011) PLoS One , vol.6
    • Parente, A.F.1    Borges, C.L.2    Bailao, A.M.3    Sousa, M.V.4    Ricart, C.A.5
  • 33
    • 82355192281 scopus 로고    scopus 로고
    • A quantitative view of the morphological phases of Paracoccidioides brasiliensis using proteomics
    • Rezende TC, Borges CL, Magalhaes AD, de Sousa MV, Ricart CA, et al. (2011) A quantitative view of the morphological phases of Paracoccidioides brasiliensis using proteomics. J Proteomics 75: 572-587.
    • (2011) J Proteomics , vol.75 , pp. 572-587
    • Rezende, T.C.1    Borges, C.L.2    Magalhaes, A.D.3    de Sousa, M.V.4    Ricart, C.A.5
  • 34
    • 79959943460 scopus 로고    scopus 로고
    • Fungal secretome database: integrated platform for annotation of fungal secretomes
    • Choi J, Park J, Kim D, Jung K, Kang S, et al. (2010) Fungal secretome database: integrated platform for annotation of fungal secretomes. BMC Genomics 11: 105.
    • (2010) BMC Genomics , vol.11 , pp. 105
    • Choi, J.1    Park, J.2    Kim, D.3    Jung, K.4    Kang, S.5
  • 35
    • 79951963663 scopus 로고    scopus 로고
    • FaaPred: a SVM-based prediction method for fungal adhesins and adhesin-like proteins
    • Ramana J, Gupta D, (2010) FaaPred: a SVM-based prediction method for fungal adhesins and adhesin-like proteins. PLoS One 5: e9695.
    • (2010) PLoS One , vol.5
    • Ramana, J.1    Gupta, D.2
  • 36
    • 1442348239 scopus 로고    scopus 로고
    • A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe
    • Eisenhaber B, Schneider G, Wildpaner M, Eisenhaber F, (2004) A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe. J Mol Biol 337: 243-253.
    • (2004) J Mol Biol , vol.337 , pp. 243-253
    • Eisenhaber, B.1    Schneider, G.2    Wildpaner, M.3    Eisenhaber, F.4
  • 37
    • 80052761783 scopus 로고    scopus 로고
    • Secretome analysis of Aspergillus fumigatus reveals Asp-hemolysin as a major secreted protein
    • Wartenberg D, Lapp K, Jacobsen ID, Dahse HM, Kniemeyer O, et al. (2011) Secretome analysis of Aspergillus fumigatus reveals Asp-hemolysin as a major secreted protein. Int J Med Microbiol 301: 602-611.
    • (2011) Int J Med Microbiol , vol.301 , pp. 602-611
    • Wartenberg, D.1    Lapp, K.2    Jacobsen, I.D.3    Dahse, H.M.4    Kniemeyer, O.5
  • 38
    • 0000427106 scopus 로고    scopus 로고
    • Isolation of Murine Macrophages
    • Coligan JE, Bierer BE, Margulies DH, Shevach EM, Strober W, et al., editors, Hoboken, NJ: John Wiley and Sons
    • Fortier AH, Falk LA (2006) Isolation of Murine Macrophages. In: Coligan JE, Bierer BE, Margulies DH, Shevach EM, Strober W, et al., editors. Current protocols in immunology. Hoboken, NJ: John Wiley and Sons. 14.11.11-14.11.19.
    • (2006) Current protocols in immunology , pp. 11-19
    • Fortier, A.H.1    Falk, L.A.2
  • 39
    • 0036924617 scopus 로고    scopus 로고
    • GP43 from Paracoccidioides brasiliensis inhibits macrophage functions. An evasion mechanism of the fungus
    • Flavia Popi AF, Lopes JD, Mariano M, (2002) GP43 from Paracoccidioides brasiliensis inhibits macrophage functions. An evasion mechanism of the fungus. Cell Immunol 218: 87-94.
    • (2002) Cell Immunol , vol.218 , pp. 87-94
    • Flavia, P.A.F.1    Lopes, J.D.2    Mariano, M.3
  • 40
    • 80053209141 scopus 로고    scopus 로고
    • Detection and expression analysis of recombinant proteins in plant-derived complex mixtures using nanoUPLC-MS(E)
    • Murad AM, Souza GH, Garcia JS, Rech EL, (2011) Detection and expression analysis of recombinant proteins in plant-derived complex mixtures using nanoUPLC-MS(E). J Sep Sci 34: 2618-2630.
    • (2011) J Sep Sci , vol.34 , pp. 2618-2630
    • Murad, A.M.1    Souza, G.H.2    Garcia, J.S.3    Rech, E.L.4
  • 41
    • 35448994847 scopus 로고    scopus 로고
    • Analysis of the Paracoccidioides brasiliensis triosephosphate isomerase suggests the potential for adhesin function
    • Pereira LA, Bao SN, Barbosa MS, da Silva JL, Felipe MS, et al. (2007) Analysis of the Paracoccidioides brasiliensis triosephosphate isomerase suggests the potential for adhesin function. FEMS Yeast Res 7: 1381-1388.
    • (2007) FEMS Yeast Res , vol.7 , pp. 1381-1388
    • Pereira, L.A.1    Bao, S.N.2    Barbosa, M.S.3    da Silva, J.L.4    Felipe, M.S.5
  • 42
    • 77954354972 scopus 로고    scopus 로고
    • Proteome profiling and functional classification of intracellular proteins from conidia of the human-pathogenic mold Aspergillus fumigatus
    • Teutschbein J, Albrecht D, Potsch M, Guthke R, Aimanianda V, et al. (2010) Proteome profiling and functional classification of intracellular proteins from conidia of the human-pathogenic mold Aspergillus fumigatus. J Proteome Res 9: 3427-3442.
    • (2010) J Proteome Res , vol.9 , pp. 3427-3442
    • Teutschbein, J.1    Albrecht, D.2    Potsch, M.3    Guthke, R.4    Aimanianda, V.5
  • 43
    • 1642528831 scopus 로고    scopus 로고
    • Post-translational modifications and their biological functions: proteomic analysis and systematic approaches
    • Seo J, Lee KJ, (2004) Post-translational modifications and their biological functions: proteomic analysis and systematic approaches. J Biochem Mol Biol 37: 35-44.
    • (2004) J Biochem Mol Biol , vol.37 , pp. 35-44
    • Seo, J.1    Lee, K.J.2
  • 44
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • Cleves AE, Cooper DN, Barondes SH, Kelly RB, (1996) A new pathway for protein export in Saccharomyces cerevisiae. J Cell Biol 133: 1017-1026.
    • (1996) J Cell Biol , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.2    Barondes, S.H.3    Kelly, R.B.4
  • 45
    • 0025255629 scopus 로고
    • A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence
    • Rubartelli A, Cozzolino F, Talio M, Sitia R, (1990) A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence. Embo J 9: 1503-1510.
    • (1990) Embo J , vol.9 , pp. 1503-1510
    • Rubartelli, A.1    Cozzolino, F.2    Talio, M.3    Sitia, R.4
  • 46
    • 0026442272 scopus 로고
    • Heat shock induces the release of fibroblast growth factor 1 from NIH 3T3 cells
    • Jackson A, Friedman S, Zhan X, Engleka KA, Forough R, et al. (1992) Heat shock induces the release of fibroblast growth factor 1 from NIH 3T3 cells. Proc Natl Acad Sci U S A 89: 10691-10695.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10691-10695
    • Jackson, A.1    Friedman, S.2    Zhan, X.3    Engleka, K.A.4    Forough, R.5
  • 47
    • 84863821810 scopus 로고    scopus 로고
    • Overexpression of serine hydroxymethyltransferase from halotolerant cyanobacterium in Escherichia coli results in increased accumulation of choline precursors and enhanced salinity tolerance
    • Waditee-Sirisattha R, Sittipol D, Tanaka Y, Takabe T (2012) Overexpression of serine hydroxymethyltransferase from halotolerant cyanobacterium in Escherichia coli results in increased accumulation of choline precursors and enhanced salinity tolerance. FEMS Microbiol Lett.
    • (2012) FEMS Microbiol Lett
    • Waditee-Sirisattha, R.1    Sittipol, D.2    Tanaka, Y.3    Takabe, T.4
  • 49
    • 85027918121 scopus 로고    scopus 로고
    • Screening of bacterial isolates from polluted soils exhibiting catalase and peroxidase activity and diversity of their responses to oxidative stress
    • Bucková M, Godocikova J, Zamocky M, Polek B, (2010) Screening of bacterial isolates from polluted soils exhibiting catalase and peroxidase activity and diversity of their responses to oxidative stress. Curr Microbiol 61: 241-247.
    • (2010) Curr Microbiol , vol.61 , pp. 241-247
    • Bucková, M.1    Godocikova, J.2    Zamocky, M.3    Polek, B.4
  • 50
    • 16244384614 scopus 로고    scopus 로고
    • Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP
    • Liu H, Peng HW, Cheng YS, Yuan HS, Yang-Yen HF, (2005) Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP. Mol Cell Biol 25: 3117-3126.
    • (2005) Mol Cell Biol , vol.25 , pp. 3117-3126
    • Liu, H.1    Peng, H.W.2    Cheng, Y.S.3    Yuan, H.S.4    Yang-Yen, H.F.5
  • 51
    • 33845267470 scopus 로고    scopus 로고
    • The role of cytochrome P450 enzymes in endogenous signalling pathways and environmental carcinogenesis
    • Nebert DW, Dalton TP, (2006) The role of cytochrome P450 enzymes in endogenous signalling pathways and environmental carcinogenesis. Nat Rev Cancer 6: 947-960.
    • (2006) Nat Rev Cancer , vol.6 , pp. 947-960
    • Nebert, D.W.1    Dalton, T.P.2
  • 52
    • 0029266564 scopus 로고
    • Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress
    • Hayes JD, Strange RC, (1995) Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress. Free Radic Res 22: 193-207.
    • (1995) Free Radic Res , vol.22 , pp. 193-207
    • Hayes, J.D.1    Strange, R.C.2
  • 53
    • 84863692804 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase protects histoplasma yeast cells from host-derived oxidative stress
    • Youseff BH, Holbrook ED, Smolnycki KA, Rappleye CA, (2012) Extracellular superoxide dismutase protects histoplasma yeast cells from host-derived oxidative stress. PLoS Pathog 8: e1002713.
    • (2012) PLoS Pathog , vol.8
    • Youseff, B.H.1    Holbrook, E.D.2    Smolnycki, K.A.3    Rappleye, C.A.4
  • 54
    • 33645506912 scopus 로고    scopus 로고
    • Negative cell cycle regulator 14-3-3sigma stabilizes p27 Kip1 by inhibiting the activity of PKB/Akt
    • Yang H, Zhang Y, Zhao R, Wen YY, Fournier K, et al. (2006) Negative cell cycle regulator 14-3-3sigma stabilizes p27 Kip1 by inhibiting the activity of PKB/Akt. Oncogene 25: 4585-4594.
    • (2006) Oncogene , vol.25 , pp. 4585-4594
    • Yang, H.1    Zhang, Y.2    Zhao, R.3    Wen, Y.Y.4    Fournier, K.5
  • 55
    • 0026726423 scopus 로고
    • Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells
    • Morgan A, Burgoyne RD, (1992) Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells. Biochem J 286 (Pt 3): 807-811.
    • (1992) Biochem J 286 (Pt , vol.3 , pp. 807-811
    • Morgan, A.1    Burgoyne, R.D.2
  • 56
    • 0032752399 scopus 로고    scopus 로고
    • Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae
    • Roth D, Birkenfeld J, Betz H, (1999) Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. FEBS Lett 460: 411-416.
    • (1999) FEBS Lett , vol.460 , pp. 411-416
    • Roth, D.1    Birkenfeld, J.2    Betz, H.3
  • 57
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay JA, (2003) Pathways of oxidative damage. Annu Rev Microbiol 57: 395-418.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 58
    • 65249115871 scopus 로고    scopus 로고
    • Comparative proteomic analysis of Botrytis cinerea secretome
    • Shah P, Atwood JA, Orlando R, El Mubarek H, Podila GK, et al. (2009) Comparative proteomic analysis of Botrytis cinerea secretome. J Proteome Res 8: 1123-1130.
    • (2009) J Proteome Res , vol.8 , pp. 1123-1130
    • Shah, P.1    Atwood, J.A.2    Orlando, R.3    El, M.H.4    Podila, G.K.5
  • 59
    • 18144420373 scopus 로고    scopus 로고
    • Protein pI shifts due to posttranslational modifications in the separation and characterization of proteins
    • Zhu K, Zhao J, Lubman DM, Miller FR, Barder TJ, (2005) Protein pI shifts due to posttranslational modifications in the separation and characterization of proteins. Anal Chem 77: 2745-2755.
    • (2005) Anal Chem , vol.77 , pp. 2745-2755
    • Zhu, K.1    Zhao, J.2    Lubman, D.M.3    Miller, F.R.4    Barder, T.J.5
  • 60
    • 58249105084 scopus 로고    scopus 로고
    • Peptides from Paracoccidioides brasiliensis GP43 inhibit macrophage functions and inflammatory response
    • Konno AY, Maricato JT, Konno FT, Mariano M, Lopes JD, (2009) Peptides from Paracoccidioides brasiliensis GP43 inhibit macrophage functions and inflammatory response. Microbes Infect 11: 92-99.
    • (2009) Microbes Infect , vol.11 , pp. 92-99
    • Konno, A.Y.1    Maricato, J.T.2    Konno, F.T.3    Mariano, M.4    Lopes, J.D.5
  • 61
    • 33746387830 scopus 로고    scopus 로고
    • Involvement of the major glycoprotein (gp43) of Paracoccidioides brasiliensis in attachment to macrophages
    • Almeida SR, Unterkircher CS, Camargo ZP, (1998) Involvement of the major glycoprotein (gp43) of Paracoccidioides brasiliensis in attachment to macrophages. Med Mycol 36: 405-411.
    • (1998) Med Mycol , vol.36 , pp. 405-411
    • Almeida, S.R.1    Unterkircher, C.S.2    Camargo, Z.P.3
  • 62
    • 78149480920 scopus 로고    scopus 로고
    • Leishmania exosomes modulate innate and adaptive immune responses through effects on monocytes and dendritic cells
    • Silverman JM, Clos J, Horakova E, Wang AY, Wiesgigl M, et al. (2010) Leishmania exosomes modulate innate and adaptive immune responses through effects on monocytes and dendritic cells. J Immunol 185: 5011-5022.
    • (2010) J Immunol , vol.185 , pp. 5011-5022
    • Silverman, J.M.1    Clos, J.2    Horakova, E.3    Wang, A.Y.4    Wiesgigl, M.5
  • 63
    • 84875154520 scopus 로고    scopus 로고
    • Leishmania exosomes deliver preemptive strikes to create an environment permissive for early infection
    • Silverman JM, Reiner NE, (2012) Leishmania exosomes deliver preemptive strikes to create an environment permissive for early infection. Front Cell Infect Microbiol 1: 26.
    • (2012) Front Cell Infect Microbiol , vol.1 , pp. 26
    • Silverman, J.M.1    Reiner, N.E.2
  • 64
    • 77951152406 scopus 로고    scopus 로고
    • An exosome-based secretion pathway is responsible for protein export from Leishmania and communication with macrophages
    • Silverman JM, Clos J, de'Oliveira CC, Shirvani O, Fang Y, et al. (2010) An exosome-based secretion pathway is responsible for protein export from Leishmania and communication with macrophages. J Cell Sci 123: 842-852.
    • (2010) J Cell Sci , vol.123 , pp. 842-852
    • Silverman, J.M.1    Clos, J.2    de'Oliveira, C.C.3    Shirvani, O.4    Fang, Y.5
  • 65
    • 80053077071 scopus 로고    scopus 로고
    • The facultative intracellular pathogen Candida glabrata subverts macrophage cytokine production and phagolysosome maturation
    • Seider K, Brunke S, Schild L, Jablonowski N, Wilson D, et al. (2011) The facultative intracellular pathogen Candida glabrata subverts macrophage cytokine production and phagolysosome maturation. J Immunol 187: 3072-3086.
    • (2011) J Immunol , vol.187 , pp. 3072-3086
    • Seider, K.1    Brunke, S.2    Schild, L.3    Jablonowski, N.4    Wilson, D.5
  • 66
    • 34250617570 scopus 로고    scopus 로고
    • A family of glycosylphosphatidylinositol-linked aspartyl proteases is required for virulence of Candida glabrata
    • Kaur R, Ma B, Cormack BP, (2007) A family of glycosylphosphatidylinositol-linked aspartyl proteases is required for virulence of Candida glabrata. Proc Natl Acad Sci U S A 104: 7628-7633.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7628-7633
    • Kaur, R.1    Ma, B.2    Cormack, B.P.3
  • 67
    • 79955752210 scopus 로고    scopus 로고
    • Temperature-induced protein secretion by Leishmania mexicana modulates macrophage signalling and function
    • Hassani K, Antoniak E, Jardim A, Olivier M, (2011) Temperature-induced protein secretion by Leishmania mexicana modulates macrophage signalling and function. PLoS One 6: e18724.
    • (2011) PLoS One , vol.6
    • Hassani, K.1    Antoniak, E.2    Jardim, A.3    Olivier, M.4
  • 68
    • 2942561968 scopus 로고    scopus 로고
    • Proteomics of protein secretion by Bacillus subtilis: separating the "secrets" of the secretome
    • Tjalsma H, Antelmann H, Jongbloed JD, Braun PG, Darmon E, et al. (2004) Proteomics of protein secretion by Bacillus subtilis: separating the "secrets" of the secretome. Microbiol Mol Biol Rev 68: 207-233.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 207-233
    • Tjalsma, H.1    Antelmann, H.2    Jongbloed, J.D.3    Braun, P.G.4    Darmon, E.5
  • 69
    • 38049129044 scopus 로고    scopus 로고
    • The Leishmania-macrophage interaction: a metabolic perspective
    • Naderer T, McConville MJ, (2008) The Leishmania-macrophage interaction: a metabolic perspective. Cell Microbiol 10: 301-308.
    • (2008) Cell Microbiol , vol.10 , pp. 301-308
    • Naderer, T.1    McConville, M.J.2
  • 70
    • 0027243781 scopus 로고
    • Histoplasma capsulatum modulates the acidification of phagolysosomes
    • Eissenberg LG, Goldman WE, Schlesinger PH, (1993) Histoplasma capsulatum modulates the acidification of phagolysosomes. J Exp Med 177: 1605-1611.
    • (1993) J Exp Med , vol.177 , pp. 1605-1611
    • Eissenberg, L.G.1    Goldman, W.E.2    Schlesinger, P.H.3
  • 71
    • 64149088754 scopus 로고    scopus 로고
    • NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B
    • Beck MR, Dekoster GT, Cistola DP, Goldman WE, (2009) NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. Mol Microbiol. 72: 344-353.
    • (2009) Mol Microbiol , vol.72 , pp. 344-353
    • Beck, M.R.1    Dekoster, G.T.2    Cistola, D.P.3    Goldman, W.E.4
  • 72
    • 0037022671 scopus 로고    scopus 로고
    • Replication of Cryptococcus neoformans in macrophages is accompanied by phagosomal permeabilization and accumulation of vesicles containing polysaccharide in the cytoplasm
    • Tucker SC, Casadevall A, (2002) Replication of Cryptococcus neoformans in macrophages is accompanied by phagosomal permeabilization and accumulation of vesicles containing polysaccharide in the cytoplasm. Proc Natl Acad Sci U S A 99: 3165-3170.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3165-3170
    • Tucker, S.C.1    Casadevall, A.2
  • 73
    • 62249165087 scopus 로고    scopus 로고
    • Candida albicans actively modulates intracellular membrane trafficking in mouse macrophage phagosomes
    • Fernandez-Arenas E, Bleck CK, Nombela C, Gil C, Griffiths G, et al. (2009) Candida albicans actively modulates intracellular membrane trafficking in mouse macrophage phagosomes. Cell Microbiol 11: 560-589.
    • (2009) Cell Microbiol , vol.11 , pp. 560-589
    • Fernandez-Arenas, E.1    Bleck, C.K.2    Nombela, C.3    Gil, C.4    Griffiths, G.5
  • 74
    • 29644437769 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells
    • Barbosa MS, Bao SN, Andreotti PF, de Faria FP, Felipe MS, et al. (2006) Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells. Infect Immun 74: 382-389.
    • (2006) Infect Immun , vol.74 , pp. 382-389
    • Barbosa, M.S.1    Bao, S.N.2    Andreotti, P.F.3    de Faria, F.P.4    Felipe, M.S.5
  • 75
    • 62949096122 scopus 로고    scopus 로고
    • Moonlighting proteins-an update
    • Jeffery CJ, (2009) Moonlighting proteins-an update. Mol Biosyst 5: 345-350.
    • (2009) Mol Biosyst , vol.5 , pp. 345-350
    • Jeffery, C.J.1
  • 76
    • 48749117456 scopus 로고    scopus 로고
    • Histoplasma capsulatum pathogenesis: making a lifestyle switch
    • Holbrook ED, Rappleye CA, (2008) Histoplasma capsulatum pathogenesis: making a lifestyle switch. Curr Opin Microbiol 11: 318-324.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 318-324
    • Holbrook, E.D.1    Rappleye, C.A.2


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