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Volumn 169, Issue 2, 2010, Pages 108-114

Gel free analysis of the proteome of intracellular Leishmania mexicana

Author keywords

Bone marrow; FACS; Macrophages; Parasite; Secreted proteins

Indexed keywords

PROTEOME;

EID: 71949086629     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2009.10.009     Document Type: Article
Times cited : (57)

References (34)
  • 1
    • 0033517487 scopus 로고    scopus 로고
    • Leishmaniasis
    • Herwaldt B.L. Leishmaniasis. Lancet 354 (1999) 1191-1199
    • (1999) Lancet , vol.354 , pp. 1191-1199
    • Herwaldt, B.L.1
  • 2
    • 0031793544 scopus 로고    scopus 로고
    • The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages
    • Antoine J.C., Prina E., Lang T., and Courret N. The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages. Trends Microbiol 6 (1998) 392-401
    • (1998) Trends Microbiol , vol.6 , pp. 392-401
    • Antoine, J.C.1    Prina, E.2    Lang, T.3    Courret, N.4
  • 3
    • 0034825692 scopus 로고    scopus 로고
    • Life in vacuoles-nutrient acquisition by Leishmania amastigotes
    • Burchmore R.J., and Barrett M.P. Life in vacuoles-nutrient acquisition by Leishmania amastigotes. Int J Parasitol 31 (2001) 1311-1320
    • (2001) Int J Parasitol , vol.31 , pp. 1311-1320
    • Burchmore, R.J.1    Barrett, M.P.2
  • 4
    • 0033953695 scopus 로고    scopus 로고
    • Subunit vaccination of mice against new world cutaneous leishmaniasis: comparison of three proteins expressed in amastigotes and six adjuvants
    • Aebischer T., Wolfram M., Patzer S.I., Ilg T., Wiese M., and Overath P. Subunit vaccination of mice against new world cutaneous leishmaniasis: comparison of three proteins expressed in amastigotes and six adjuvants. Infect Immun 68 (2000) 1328-1336
    • (2000) Infect Immun , vol.68 , pp. 1328-1336
    • Aebischer, T.1    Wolfram, M.2    Patzer, S.I.3    Ilg, T.4    Wiese, M.5    Overath, P.6
  • 5
    • 0033178708 scopus 로고    scopus 로고
    • Antigen presentation by macrophages harboring intravesicular pathogens
    • Overath P., and Aebischer T. Antigen presentation by macrophages harboring intravesicular pathogens. Parasitol Today 15 (1999) 325-332
    • (1999) Parasitol Today , vol.15 , pp. 325-332
    • Overath, P.1    Aebischer, T.2
  • 6
    • 0029840937 scopus 로고    scopus 로고
    • Antigen presentation by Leishmania mexicana-infected macrophages: activation of helper T cells by a model parasite antigen secreted into the parasitophorous vacuole or expressed on the amastigote surface
    • Wolfram M., Fuchs M., Wiese M., Stierhof Y.D., and Overath P. Antigen presentation by Leishmania mexicana-infected macrophages: activation of helper T cells by a model parasite antigen secreted into the parasitophorous vacuole or expressed on the amastigote surface. Eur J Immunol 26 (1996) 3153-3162
    • (1996) Eur J Immunol , vol.26 , pp. 3153-3162
    • Wolfram, M.1    Fuchs, M.2    Wiese, M.3    Stierhof, Y.D.4    Overath, P.5
  • 7
    • 33645797570 scopus 로고    scopus 로고
    • In vivo recognition of ovalbumin expressed by transgenic Leishmania is determined by its subcellular localization
    • Prickett S., Gray P.M., Colpitts S.L., Scott P., Kaye P.M., and Smith D.F. In vivo recognition of ovalbumin expressed by transgenic Leishmania is determined by its subcellular localization. J Immunol 176 (2006) 4826-4833
    • (2006) J Immunol , vol.176 , pp. 4826-4833
    • Prickett, S.1    Gray, P.M.2    Colpitts, S.L.3    Scott, P.4    Kaye, P.M.5    Smith, D.F.6
  • 8
    • 31444443666 scopus 로고    scopus 로고
    • Approaches for the identification of potential excreted/secreted proteins of Leishmania major parasites
    • Chenik M., Lakhal S., Ben Khalef N., Zribi L., Louzir H., and Dellagi K. Approaches for the identification of potential excreted/secreted proteins of Leishmania major parasites. Parasitology 132 (2006) 493-509
    • (2006) Parasitology , vol.132 , pp. 493-509
    • Chenik, M.1    Lakhal, S.2    Ben Khalef, N.3    Zribi, L.4    Louzir, H.5    Dellagi, K.6
  • 9
    • 1642601386 scopus 로고    scopus 로고
    • Proteophosphoglycans of Leishmania mexicana. Molecular cloning and characterization of the Leishmania mexicana ppg2 gene encoding the proteophosphoglycans aPPG and pPPG2 that are secreted by amastigotes and promastigotes
    • Gopfert U., Goehring N., Klein C., and Ilg T. Proteophosphoglycans of Leishmania mexicana. Molecular cloning and characterization of the Leishmania mexicana ppg2 gene encoding the proteophosphoglycans aPPG and pPPG2 that are secreted by amastigotes and promastigotes. Biochem J 344 (1999) 787-795
    • (1999) Biochem J , vol.344 , pp. 787-795
    • Gopfert, U.1    Goehring, N.2    Klein, C.3    Ilg, T.4
  • 10
    • 52649088373 scopus 로고    scopus 로고
    • Transgenic, fluorescent Leishmania mexicana allow direct analysis of the proteome of intracellular amastigotes
    • Paape D., Lippuner C., Schmid M., et al. Transgenic, fluorescent Leishmania mexicana allow direct analysis of the proteome of intracellular amastigotes. Mol Cell Proteomics 7 9 (2008) 1688-1701
    • (2008) Mol Cell Proteomics , vol.7 , Issue.9 , pp. 1688-1701
    • Paape, D.1    Lippuner, C.2    Schmid, M.3
  • 11
    • 46749097225 scopus 로고    scopus 로고
    • Proteomic analysis of the secretome of Leishmania donovani
    • Silverman J.M., Chan S.K., Robinson D.P., et al. Proteomic analysis of the secretome of Leishmania donovani. Genome Biol 9 (2008) R35
    • (2008) Genome Biol , vol.9
    • Silverman, J.M.1    Chan, S.K.2    Robinson, D.P.3
  • 12
    • 14644399785 scopus 로고    scopus 로고
    • Direct transport across the plasma membrane of mammalian cells of Leishmania HASPB as revealed by a CHO export mutant
    • Stegmayer C., Kehlenbach A., Tournaviti S., et al. Direct transport across the plasma membrane of mammalian cells of Leishmania HASPB as revealed by a CHO export mutant. J Cell Sci 118 (2005) 517-527
    • (2005) J Cell Sci , vol.118 , pp. 517-527
    • Stegmayer, C.1    Kehlenbach, A.2    Tournaviti, S.3
  • 14
    • 0141537895 scopus 로고    scopus 로고
    • Rapidly maturing red fluorescent protein variants with strongly enhanced brightness in bacteria
    • Sorensen M., Lippuner C., Kaiser T., Misslitz A., Aebischer T., and Bumann D. Rapidly maturing red fluorescent protein variants with strongly enhanced brightness in bacteria. FEBS Lett 552 (2003) 110-114
    • (2003) FEBS Lett , vol.552 , pp. 110-114
    • Sorensen, M.1    Lippuner, C.2    Kaiser, T.3    Misslitz, A.4    Aebischer, T.5    Bumann, D.6
  • 15
    • 0242693036 scopus 로고    scopus 로고
    • Targeted integration into a rRNA locus results in uniform and high level expression of transgenes in Leishmania amastigotes
    • Misslitz A., Mottram J.C., Overath P., and Aebischer T. Targeted integration into a rRNA locus results in uniform and high level expression of transgenes in Leishmania amastigotes. Mol Biochem Parasitol 107 (2000) 251-261
    • (2000) Mol Biochem Parasitol , vol.107 , pp. 251-261
    • Misslitz, A.1    Mottram, J.C.2    Overath, P.3    Aebischer, T.4
  • 16
    • 0028156734 scopus 로고
    • Complete developmental cycle of Leishmania mexicana in axenic culture
    • Bates P.A. Complete developmental cycle of Leishmania mexicana in axenic culture. Parasitology 108 Pt. 1 (1994) 1-9
    • (1994) Parasitology , vol.108 , Issue.PART 1 , pp. 1-9
    • Bates, P.A.1
  • 17
    • 0031903139 scopus 로고    scopus 로고
    • Phagocytosis of Leishmania mexicana amastigotes by macrophages leads to a sustained suppression of IL-12 production
    • Weinheber N., Wolfram M., Harbecke D., and Aebischer T. Phagocytosis of Leishmania mexicana amastigotes by macrophages leads to a sustained suppression of IL-12 production. Eur J Immunol 28 (1998) 2467-2477
    • (1998) Eur J Immunol , vol.28 , pp. 2467-2477
    • Weinheber, N.1    Wolfram, M.2    Harbecke, D.3    Aebischer, T.4
  • 18
    • 0345868786 scopus 로고    scopus 로고
    • Simple and reliable method to precipitate proteins from bacterial culture supernatant
    • Caldwell R.B., and Lattemann C.T. Simple and reliable method to precipitate proteins from bacterial culture supernatant. Appl Environ Microbiol 70 (2004) 610-612
    • (2004) Appl Environ Microbiol , vol.70 , pp. 610-612
    • Caldwell, R.B.1    Lattemann, C.T.2
  • 19
    • 0030949844 scopus 로고    scopus 로고
    • A simple assay for quantification of protein in tissue sections, cell cultures, and cell homogenates, and of protein immobilized on solid surfaces
    • Dieckmann-Schuppert A., and Schnittler H.J. A simple assay for quantification of protein in tissue sections, cell cultures, and cell homogenates, and of protein immobilized on solid surfaces. Cell Tissue Res 288 (1997) 119-126
    • (1997) Cell Tissue Res , vol.288 , pp. 119-126
    • Dieckmann-Schuppert, A.1    Schnittler, H.J.2
  • 20
    • 0037224514 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • Rappsilber J., Ryder U., Lamond A.I., and Mann M. Large-scale proteomic analysis of the human spliceosome. Genome Res 12 (2002) 1231-1245
    • (2002) Genome Res , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 21
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y., Oda Y., and Tabata T.E.-A. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4 (2005) 1265-1272
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.E.-A.3
  • 22
    • 3042662113 scopus 로고    scopus 로고
    • In silico proteome analysis to facilitate proteomics experiments using mass spectrometry
    • Cagney G., Amiri S., Premawaradena T., Lindo M., and Emili A. In silico proteome analysis to facilitate proteomics experiments using mass spectrometry. Proteome Sci 1 (2003) 5
    • (2003) Proteome Sci , vol.1 , pp. 5
    • Cagney, G.1    Amiri, S.2    Premawaradena, T.3    Lindo, M.4    Emili, A.5
  • 23
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., and Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2 (2007) 953-971
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 24
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O., Nielsen H., Brunak S., and von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 300 (2000) 1005-1016
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 25
  • 26
    • 0031603460 scopus 로고    scopus 로고
    • Prediction of signal peptides and signal anchors by a hidden Markov model
    • Nielsen H., and Krogh A. Prediction of signal peptides and signal anchors by a hidden Markov model. Proc Int Conf Intell Syst Mol Biol 6 (1998) 122-130
    • (1998) Proc Int Conf Intell Syst Mol Biol , vol.6 , pp. 122-130
    • Nielsen, H.1    Krogh, A.2
  • 27
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., and Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305 (2001) 567-580
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 30
    • 34347376906 scopus 로고    scopus 로고
    • The relationships between the isoelectric point and: length of proteins, taxonomy and ecology of organisms
    • Kiraga J., Mackiewicz P., Mackiewicz D., et al. The relationships between the isoelectric point and: length of proteins, taxonomy and ecology of organisms. BMC Genomics 8 (2007) 163
    • (2007) BMC Genomics , vol.8 , pp. 163
    • Kiraga, J.1    Mackiewicz, P.2    Mackiewicz, D.3
  • 31
    • 33947221526 scopus 로고    scopus 로고
    • Metabolism of Leishmania: proven and predicted
    • Opperdoes F.R., and Coombs G.H. Metabolism of Leishmania: proven and predicted. Trends Parasitol 23 (2007) 149-158
    • (2007) Trends Parasitol , vol.23 , pp. 149-158
    • Opperdoes, F.R.1    Coombs, G.H.2
  • 33
    • 33645788058 scopus 로고    scopus 로고
    • Virulence of Leishmania major in macrophages and mice requires the gluconeogenic enzyme fructose-1,6-bisphosphatase
    • Naderer T., Ellis M.A., Sernee M.F., et al. Virulence of Leishmania major in macrophages and mice requires the gluconeogenic enzyme fructose-1,6-bisphosphatase. Proc Natl Acad Sci U S A 103 (2006) 5502-5507
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5502-5507
    • Naderer, T.1    Ellis, M.A.2    Sernee, M.F.3


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