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Volumn 198, Issue 1, 2003, Pages 1-4

Dangerous liaisons between a microbe and the prion protein

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 60; PRION PROTEIN;

EID: 0038491424     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.20030732     Document Type: Note
Times cited : (21)

References (48)
  • 2
    • 0037146657 scopus 로고    scopus 로고
    • Brucella intracellular life: From invasion to intracellular replication
    • Gorvel, J.P., and E. Moreno. 2002. Brucella intracellular life: from invasion to intracellular replication. Vet. Microbiol. 90:281-297.
    • (2002) Vet. Microbiol. , vol.90 , pp. 281-297
    • Gorvel, J.P.1    Moreno, E.2
  • 3
    • 0035171953 scopus 로고    scopus 로고
    • Brucella suis-impaired specific recognition of phagosomes by lysosomes due to phagosomal membrane modifications
    • Naroeni, A., N. Jouy, S. Ouahrani-Bettache, J.P. Liautard, and F. Porte. 2001. Brucella suis-impaired specific recognition of phagosomes by lysosomes due to phagosomal membrane modifications. Infect. Immun. 69:486-493.
    • (2001) Infect. Immun. , vol.69 , pp. 486-493
    • Naroeni, A.1    Jouy, N.2    Ouahrani-Bettache, S.3    Liautard, J.P.4    Porte, F.5
  • 4
    • 0035079679 scopus 로고    scopus 로고
    • Essential role of the VirB machinery in the maturation of the Brucella abortus-containing vacuole
    • Comerci, D.J., M.J. Martinez-Lorenzo, R. Sieira, J.P. Gorvel, and R.A. Ugalde. 2001. Essential role of the VirB machinery in the maturation of the Brucella abortus-containing vacuole. Cell. Microbiol. 3:159-168.
    • (2001) Cell. Microbiol. , vol.3 , pp. 159-168
    • Comerci, D.J.1    Martinez-Lorenzo, M.J.2    Sieira, R.3    Gorvel, J.P.4    Ugalde, R.A.5
  • 5
    • 0033872757 scopus 로고    scopus 로고
    • A homologue of an operon required for DNA transfer in Agrobacterium is required in Brucella abortus for virulence and intracellular multiplication
    • Sieira, R., D.J. Comerci, D.O. Sanchez, and R.A. Ugalde. 2000. A homologue of an operon required for DNA transfer in Agrobacterium is required in Brucella abortus for virulence and intracellular multiplication. J. Bacteriol. 182:4849-4855.
    • (2000) J. Bacteriol. , vol.182 , pp. 4849-4855
    • Sieira, R.1    Comerci, D.J.2    Sanchez, D.O.3    Ugalde, R.A.4
  • 6
    • 0032868454 scopus 로고    scopus 로고
    • A homologue of the Agrobacterium tumefaciens VirB and Bordetella pertussis Ptl type IV secretion systems is essential for intracellular survival of Brucella suis
    • O'Callaghan, D., C. Cazevieille, A. Allardet-Servent, M.L. Boschiroli, G. Bourg, V. Foulongne, P, Frutos, Y. Kulakov, and M. Ramuz. 1999. A homologue of the Agrobacterium tumefaciens VirB and Bordetella pertussis Ptl type IV secretion systems is essential for intracellular survival of Brucella suis. Mol. Microbiol. 33:1210-1220.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1210-1220
    • O'Callaghan, D.1    Cazevieille, C.2    Allardet-Servent, A.3    Boschiroli, M.L.4    Bourg, G.5    Foulongne, V.6    Frutos, P.7    Kulakov, Y.8    Ramuz, M.9
  • 7
    • 0033961615 scopus 로고    scopus 로고
    • Identification of Brucella suis genes affecting intracellular survival in an in vitro human macrophage infection model by signature-tagged transposon mutagenesis
    • Foulongne, V., G. Bourg, C. Cazevieille, S. Michaux-Charachon, and D. O'Callaghan. 2000. Identification of Brucella suis genes affecting intracellular survival in an in vitro human macrophage infection model by signature-tagged transposon mutagenesis. Infect. Immun. 68:1297-1303.
    • (2000) Infect. Immun. , vol.68 , pp. 1297-1303
    • Foulongne, V.1    Bourg, G.2    Cazevieille, C.3    Michaux-Charachon, S.4    O'Callaghan, D.5
  • 8
    • 0036716769 scopus 로고    scopus 로고
    • virB-mediated survival of Brucella abortus in mice and macrophages is independent of a functional inducible nitric oxide synthase or NADPH oxidase in macrophages
    • Sun, Y.H., A.B. den Hartigh, R.L. Santos, L.G. Adams, and R.M. Tsolis. 2002. virB-mediated survival of Brucella abortus in mice and macrophages is independent of a functional inducible nitric oxide synthase or NADPH oxidase in macrophages. Infect. Immun. 70:4826-4832.
    • (2002) Infect. Immun. , vol.70 , pp. 4826-4832
    • Sun, Y.H.1    Den Hartigh, A.B.2    Santos, R.L.3    Adams, L.G.4    Tsolis, R.M.5
  • 9
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U., and M. Hayer-Hartl. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 10
    • 0036307071 scopus 로고    scopus 로고
    • Modulation of Brucella-induced macropinocytosis by lipid rafts mediates intracellular replication
    • Watarai, M., S. Makino, Y. Fujii, K. Okamoto, and T. Shirahata. 2002. Modulation of Brucella-induced macropinocytosis by lipid rafts mediates intracellular replication. Cell. Microbiol. 4:341-355.
    • (2002) Cell. Microbiol. , vol.4 , pp. 341-355
    • Watarai, M.1    Makino, S.2    Fujii, Y.3    Okamoto, K.4    Shirahata, T.5
  • 11
    • 0036175876 scopus 로고    scopus 로고
    • Role of cholesterol and the ganglioside GM(1) in entry and short-term survival of Brucella suis in murine macrophages
    • Naroeni, A., and F. Porte. 2002. Role of cholesterol and the ganglioside GM(1) in entry and short-term survival of Brucella suis in murine macrophages. Infect. Immun. 70:1640-1644.
    • (2002) Infect. Immun. , vol.70 , pp. 1640-1644
    • Naroeni, A.1    Porte, F.2
  • 12
  • 13
    • 0033933751 scopus 로고    scopus 로고
    • Identification of genes required for chronic persistence of Brucella abortus in mice
    • Hong, P.C., R.M. Tsolis, and T.A. Ficht. 2000. Identification of genes required for chronic persistence of Brucella abortus in mice. Infect. Immun. 68:4102-4107.
    • (2000) Infect. Immun. , vol.68 , pp. 4102-4107
    • Hong, P.C.1    Tsolis, R.M.2    Ficht, T.A.3
  • 14
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S.B. 1982. Novel proteinaceous infectious particles cause scrapie. Science. 216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 19
    • 0030890097 scopus 로고    scopus 로고
    • Mossy fibre reorganization in the hippocampus of prion protein null mice
    • Colling, S.B., M. Khana, J. Collinge, and J.G. Jefferys. 1997. Mossy fibre reorganization in the hippocampus of prion protein null mice. Brain Res. 755:28-35.
    • (1997) Brain Res. , vol.755 , pp. 28-35
    • Colling, S.B.1    Khana, M.2    Collinge, J.3    Jefferys, J.G.4
  • 23
    • 0029916617 scopus 로고    scopus 로고
    • Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus
    • Lledo, P.M., P. Tremblay, S.J. Dearmond, S.B. Prusiner, and R.A. Nicoll. 1996. Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc. Natl. Acad. Sci. USA. 93:2403-2407.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2403-2407
    • Lledo, P.M.1    Tremblay, P.2    Dearmond, S.J.3    Prusiner, S.B.4    Nicoll, R.A.5
  • 29
    • 0035914410 scopus 로고    scopus 로고
    • Prion protein protects human neurons against Bax-mediated apoptosis
    • Bounhar, Y., Y. Zhang, C.G. Goodyer, and A. LeBlanc. 2001. Prion protein protects human neurons against Bax-mediated apoptosis. J. Biol. Chem. 276:39145-39149.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39145-39149
    • Bounhar, Y.1    Zhang, Y.2    Goodyer, C.G.3    LeBlanc, A.4
  • 30
    • 0037855771 scopus 로고    scopus 로고
    • Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53-dependent caspase 3-like activation
    • Paitel, E., R. Fahraeus, and F. Checler. 2003. Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53-dependent caspase 3-like activation. J. Biol. Chem. 278:10061-10066.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10061-10066
    • Paitel, E.1    Fahraeus, R.2    Checler, F.3
  • 31
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host protein in neurotoxicity of a prion protein fragment
    • Brown, D.R., B. Schmidt, and H.A. Kretzschmar. 1996. Role of microglia and host protein in neurotoxicity of a prion protein fragment. Nature. 380:345-347.
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 32
    • 0032859326 scopus 로고    scopus 로고
    • Neurotoxicity of prion peptide 106-126 not confirmed
    • Kunz, B., E. Sandmeier, and P. Christen. 1999. Neurotoxicity of prion peptide 106-126 not confirmed. FEBS Lett. 458:65-68.
    • (1999) FEBS Lett. , vol.458 , pp. 65-68
    • Kunz, B.1    Sandmeier, E.2    Christen, P.3
  • 33
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma, J., R. Wollmann, and S. Lindquist. 2002. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science. 298:1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 34
    • 0038159514 scopus 로고    scopus 로고
    • Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation
    • Drisaldi, B., R.S. Stewart, C. Adles, L.R. Stewart, E. Quaglio, E. Biasini, L. Fioriti, R. Chiesa, and D.A. Harris. 2003. Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation. J. Biol. Chem. 278:21732-21743.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21732-21743
    • Drisaldi, B.1    Stewart, R.S.2    Adles, C.3    Stewart, L.R.4    Quaglio, E.5    Biasini, E.6    Fioriti, L.7    Chiesa, R.8    Harris, D.A.9
  • 36
    • 0033615415 scopus 로고    scopus 로고
    • Perspectives: Neurobiology. PrP's double causes trouble
    • Weissmann, C., and A. Aguzzi. 1999. Perspectives: neurobiology. PrP's double causes trouble. Science. 286:914-915.
    • (1999) Science , vol.286 , pp. 914-915
    • Weissmann, C.1    Aguzzi, A.2
  • 37
    • 0036498430 scopus 로고    scopus 로고
    • Small is not beautiful: Antagonizing functions for the prion protein PrP(C) and its homologue Dpl
    • Behrens, A., and A. Aguzzi. 2002. Small is not beautiful: antagonizing functions for the prion protein PrP(C) and its homologue Dpl. Trends Neurosci. 25:150-154.
    • (2002) Trends Neurosci. , vol.25 , pp. 150-154
    • Behrens, A.1    Aguzzi, A.2
  • 39
    • 0031436335 scopus 로고    scopus 로고
    • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • Rieger, R., F. Edenhofer, C.I. Lasmezas, and S. Weiss. 1997. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med. 3:1383-1388.
    • (1997) Nat. Med. , vol.3 , pp. 1383-1388
    • Rieger, R.1    Edenhofer, F.2    Lasmezas, C.I.3    Weiss, S.4
  • 40
    • 0028256222 scopus 로고
    • Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red
    • erratum published 68:4107
    • Caughey, B., K. Brown, G.J. Raymond, G.E. Katzenstein, and W. Thresher. 1994. Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red. J. Virol. 68:2135-2141. (erratum published 68:4107).
    • (1994) J. Virol. , vol.68 , pp. 2135-2141
    • Caughey, B.1    Brown, K.2    Raymond, G.J.3    Katzenstein, G.E.4    Thresher, W.5
  • 43
    • 0027472869 scopus 로고
    • Mycobacterial 65-kD heat shock protein induces release of proinflammatory cytokines from human monocytic cells
    • Friedland, J.S., R. Shattock, D.G. Remick, and G.E. Griffin. 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
  • 44
    • 0035139983 scopus 로고    scopus 로고
    • Danger signals: SOS to the immune system
    • Gallucci, S., and P. Matzinger. 2001. Danger signals: SOS to the immune system. Curr. Opin. Immunol. 13:114-119.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 114-119
    • Gallucci, S.1    Matzinger, P.2
  • 45
    • 0034595877 scopus 로고    scopus 로고
    • Essential role for cholesterol in entry of mycobacteria into macrophages
    • Gatfield, J., and J. Pieters. 2000. Essential role for cholesterol in entry of mycobacteria into macrophages. Science. 288:1647-1650.
    • (2000) Science , vol.288 , pp. 1647-1650
    • Gatfield, J.1    Pieters, J.2
  • 46
    • 0034949325 scopus 로고    scopus 로고
    • Association of caveolin with Chlamydia trachomatis inclusions at early and late stages of infection
    • Norkin, L.C., S.A. Wolfrom, and E.S. Stuart. 2001. Association of caveolin with Chlamydia trachomatis inclusions at early and late stages of infection. Exp. Cell Res. 266:229-238.
    • (2001) Exp. Cell Res. , vol.266 , pp. 229-238
    • Norkin, L.C.1    Wolfrom, S.A.2    Stuart, E.S.3
  • 47
    • 0034604515 scopus 로고    scopus 로고
    • Involvement of cellular caveolae in bacterial entry into mast cells
    • Shin, J.S., Z. Gao, and S.N. Abraham. 2000. Involvement of cellular caveolae in bacterial entry into mast cells. Science. 289:785-788.
    • (2000) Science , vol.289 , pp. 785-788
    • Shin, J.S.1    Gao, Z.2    Abraham, S.N.3
  • 48
    • 18744387685 scopus 로고    scopus 로고
    • Microbial entry through caveolae: Variations on a theme
    • Duncan, M.J., J.S. Shin, and S.N. Abraham. 2002. Microbial entry through caveolae: variations on a theme. Cell. Microbiol. 4:783-791.
    • (2002) Cell. Microbiol. , vol.4 , pp. 783-791
    • Duncan, M.J.1    Shin, J.S.2    Abraham, S.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.