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Volumn 3, Issue 5, 2005, Pages 0861-0871

Subversion of cellular autophagosomal machinery by RNA viruses

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYLADENINE; DANSYLCADAVERINE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; MESSENGER RNA; HYBRID PROTEIN; PRIMER DNA; SMALL INTERFERING RNA;

EID: 21344452171     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0030156     Document Type: Article
Times cited : (745)

References (93)
  • 1
    • 0000115806 scopus 로고
    • Electron microscopic study of the formation of poliovirus
    • Dales S, Eggers HJ, Tamm I, Palade GE (1965) Electron microscopic study of the formation of poliovirus. Virology 26: 379-389.
    • (1965) Virology , vol.26 , pp. 379-389
    • Dales, S.1    Eggers, H.J.2    Tamm, I.3    Palade, G.E.4
  • 2
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel A, Giddings TH Jr, Ladinsky MS, Kirkegaard K (1996) Cellular origin and ultrastructure of membranes induced during poliovirus infection. J Virol 70: 6576-6588.
    • (1996) J Virol , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings Jr., T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 3
    • 0023415083 scopus 로고
    • Association of polioviral proteins of the P2 genomic region with the viral replication complex and virus-induced membrane synthesis as visualized by electron microscopic immunocytochemistry and autoradiography
    • Bienz K, Egger D, Pasamontes L (1987) Association of polioviral proteins of the P2 genomic region with the viral replication complex and virus-induced membrane synthesis as visualized by electron microscopic immunocytochemistry and autoradiography. Virology 60: 220-226.
    • (1987) Virology , vol.60 , pp. 220-226
    • Bienz, K.1    Egger, D.2    Pasamontes, L.3
  • 4
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • Cho MW, Teterina N, Egger D, Bienz K, Ehrenfeld E (1994) Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 202: 129-145.
    • (1994) Virology , vol.202 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 5
    • 0033919961 scopus 로고    scopus 로고
    • Formation of the poliovirus replication complex requires coupled viral translation, vesicle production and viral RNA synthesis
    • Egger D, Teterina N, Ehrenfeld E, Bienz K (2000) Formation of the poliovirus replication complex requires coupled viral translation, vesicle production and viral RNA synthesis. J Virol 74: 6570-6580.
    • (2000) J Virol , vol.74 , pp. 6570-6580
    • Egger, D.1    Teterina, N.2    Ehrenfeld, E.3    Bienz, K.4
  • 6
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle JM, Bullitt E, Bienz K, Kirkegaard K (2002) Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 296: 2218-2222.
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 7
    • 0037320030 scopus 로고    scopus 로고
    • An alternate pathway for recruiting template RNA to the brome mosaic virus RNA replication complex
    • Chen J, Noueiry A, Ahlquist P (2003) An alternate pathway for recruiting template RNA to the brome mosaic virus RNA replication complex. J Virol 77: 2568-2577.
    • (2003) J Virol , vol.77 , pp. 2568-2577
    • Chen, J.1    Noueiry, A.2    Ahlquist, P.3
  • 8
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine B, Klionsky DJ (2004) Development by self-digestion: Molecular mechanisms and biological functions of autophagy. Dev Cell 6: 463-477.
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 9
    • 0034012322 scopus 로고    scopus 로고
    • Autophagic and apoptotic types of programmed cell death exhibit different fates of cytoskeletal filaments
    • Bursch W, Hochegger K, Torok L, Marian B, Ellinger A, et al. (2000) Autophagic and apoptotic types of programmed cell death exhibit different fates of cytoskeletal filaments. J Cell Sci 113: 1189-1198.
    • (2000) J Cell Sci , vol.113 , pp. 1189-1198
    • Bursch, W.1    Hochegger, K.2    Torok, L.3    Marian, B.4    Ellinger, A.5
  • 10
    • 0035725835 scopus 로고    scopus 로고
    • Autophagy and nuclear changes in FM3A breast tumor cells after epirubicin, medroxyprogesterone and tamoxifen treatment in vitro
    • Bilir A, Altinoz MA, Erkan M, Ozmen V, Aydiner A (2001) Autophagy and nuclear changes in FM3A breast tumor cells after epirubicin, medroxyprogesterone and tamoxifen treatment in vitro. Pathobiology 69: 120-126.
    • (2001) Pathobiology , vol.69 , pp. 120-126
    • Bilir, A.1    Altinoz, M.A.2    Erkan, M.3    Ozmen, V.4    Aydiner, A.5
  • 11
    • 0028899789 scopus 로고
    • Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes
    • Blommaart EF, Luiken JJ, Blommaart PJ, van Woerkom GM, Meijer AJ (1995) Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J Biol Chem 270: 2320-2326.
    • (1995) J Biol Chem , vol.270 , pp. 2320-2326
    • Blommaart, E.F.1    Luiken, J.J.2    Blommaart, P.J.3    Van Woerkom, G.M.4    Meijer, A.J.5
  • 12
    • 0033534734 scopus 로고    scopus 로고
    • Regulation of translational effectors by amino acid and mammalian target of rapamycin signaling pathways: Possible involvement of autophagy in cultured hepatoma cells
    • Shigemitsu K, Tsujishita Y, Hara K, Nanahoshi M, Avruch J, et al. (1999) Regulation of translational effectors by amino acid and mammalian target of rapamycin signaling pathways: Possible involvement of autophagy in cultured hepatoma cells. J Biol Chem 274: 1058-1065.
    • (1999) J Biol Chem , vol.274 , pp. 1058-1065
    • Shigemitsu, K.1    Tsujishita, Y.2    Hara, K.3    Nanahoshi, M.4    Avruch, J.5
  • 13
    • 0034703021 scopus 로고    scopus 로고
    • Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway
    • Mordier S, Deval C, Bechet D, Tassa A, Ferrara M (2000) Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway. J Biol Chem 275: 29900-29906.
    • (2000) J Biol Chem , vol.275 , pp. 29900-29906
    • Mordier, S.1    Deval, C.2    Bechet, D.3    Tassa, A.4    Ferrara, M.5
  • 14
    • 4344595626 scopus 로고    scopus 로고
    • Regulation and role of autophagy in mammalian cells
    • Meijer AJ (2004) Regulation and role of autophagy in mammalian cells. Int J Biochem Cell Biol 36: 2445-2462.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2445-2462
    • Meijer, A.J.1
  • 15
    • 0038309329 scopus 로고    scopus 로고
    • The molecular mechanism of autophagy
    • Wang CW, Klionsky DJ (2003) The molecular mechanism of autophagy. Mol Med 9: 65-76.
    • (2003) Mol Med , vol.9 , pp. 65-76
    • Wang, C.W.1    Klionsky, D.J.2
  • 16
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, et al. (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19: 5720-5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5
  • 17
    • 0033791650 scopus 로고    scopus 로고
    • Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells
    • Kim J, Klionsky DJ (2000) Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells. Annu Rev Biochem 69: 303-342.
    • (2000) Annu Rev Biochem , vol.69 , pp. 303-342
    • Kim, J.1    Klionsky, D.J.2
  • 18
    • 0037134443 scopus 로고    scopus 로고
    • Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p
    • Tanida I, Tanida-Miyake E, Komatsu M, Ueno T, Kominami E (2002) Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p. J Biol Chem 277: 13739-13744.
    • (2002) J Biol Chem , vol.277 , pp. 13739-13744
    • Tanida, I.1    Tanida-Miyake, E.2    Komatsu, M.3    Ueno, T.4    Kominami, E.5
  • 19
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: Many paths to the same end
    • Cuervo AM (2004) Autophagy: Many paths to the same end. Mol Cell Biochem 263: 55-72.
    • (2004) Mol Cell Biochem , vol.263 , pp. 55-72
    • Cuervo, A.M.1
  • 20
    • 14044277429 scopus 로고    scopus 로고
    • The molecular mechanism of autophagy: Unanswered questions
    • Klionsky DJ (2005) The molecular mechanism of autophagy: Unanswered questions. J Cell Sci 118: 7-18.
    • (2005) J Cell Sci , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 22
    • 0032532323 scopus 로고    scopus 로고
    • Purification and characterization of autophagosomes from rat hepatocytes
    • Stromhaug PE, Berg TO, Fengsrud M, Seglen PO (1998) Purification and characterization of autophagosomes from rat hepatocytes. Biochem J 335: 217-224.
    • (1998) Biochem J , vol.335 , pp. 217-224
    • Stromhaug, P.E.1    Berg, T.O.2    Fengsrud, M.3    Seglen, P.O.4
  • 23
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima N, Yamamoto A, Hatano M, Kobayashi Y, Kabeya Y, et al. (2001) Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol 152: 657-668.
    • (2001) J Cell Biol , vol.152 , pp. 657-668
    • Mizushima, N.1    Yamamoto, A.2    Hatano, M.3    Kobayashi, Y.4    Kabeya, Y.5
  • 24
    • 0025363276 scopus 로고
    • Studies on the mechanisms of autophagy: Formation of the autophagic vacuole
    • Dunn WA Jr (1990) Studies on the mechanisms of autophagy: Formation of the autophagic vacuole. J Cell Biol 110: 1923-1933.
    • (1990) J Cell Biol , vol.110 , pp. 1923-1933
    • Dunn Jr., W.A.1
  • 25
    • 0025340880 scopus 로고
    • Studies on the mechanisms of autophagy: Maturation of the autophagic vacuole
    • Dunn WA Jr (1990) Studies on the mechanisms of autophagy: Maturation of the autophagic vacuole. J Cell Biol 110: 1935-1945.
    • (1990) J Cell Biol , vol.110 , pp. 1935-1945
    • Dunn Jr., W.A.1
  • 26
    • 0034529528 scopus 로고    scopus 로고
    • Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy
    • Fengsrud M, Erichsen ES, Berg T O, Raiborg C, Seglen PO (2000) Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy. Eur J Cell Biol 79: 871-882.
    • (2000) Eur J Cell Biol , vol.79 , pp. 871-882
    • Fengsrud, M.1    Erichsen, E.S.2    Berg, T.O.3    Raiborg, C.4    Seglen, P.O.5
  • 27
    • 19244384656 scopus 로고    scopus 로고
    • Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice
    • Tanaka Y, Guhde G, Suter A, Eskelinen EL, Hartmann D, et al (2000) Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice. Nature 406: 902-906.
    • (2000) Nature , vol.406 , pp. 902-906
    • Tanaka, Y.1    Guhde, G.2    Suter, A.3    Eskelinen, E.L.4    Hartmann, D.5
  • 29
    • 0032414333 scopus 로고    scopus 로고
    • Identification of autolysosomes directly associated with proteolysis on the density gradients in isolated rat hepatocytes
    • Niioka S, Goto M, Ishibashi T, Kadowaki M (1998) Identification of autolysosomes directly associated with proteolysis on the density gradients in isolated rat hepatocytes. J Biochem 124: 1086-1093.
    • (1998) J Biochem , vol.124 , pp. 1086-1093
    • Niioka, S.1    Goto, M.2    Ishibashi, T.3    Kadowaki, M.4
  • 30
    • 0021720256 scopus 로고
    • Association of poliovirus proteins with the endoplasmic reticulum
    • Tershak DR (1984) Association of poliovirus proteins with the endoplasmic reticulum. J Virol 52: 777-783.
    • (1984) J Virol , vol.52 , pp. 777-783
    • Tershak, D.R.1
  • 31
    • 0034802046 scopus 로고    scopus 로고
    • Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex
    • Rust RC, Landmann L, Gosert R, Tang BL, Hong W, et al. (2001) Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex. J Virol 75: 9808-9818.
    • (2001) J Virol , vol.75 , pp. 9808-9818
    • Rust, R.C.1    Landmann, L.2    Gosert, R.3    Tang, B.L.4    Hong, W.5
  • 32
    • 0036838235 scopus 로고    scopus 로고
    • Differential requirements for COPI coats in formation of replication complexes among three genera of Picornaviridae
    • Gazina EV, Mackenzie JM, Gorrell RJ, Anderson DA (2002) Differential requirements for COPI coats in formation of replication complexes among three genera of Picornaviridae. J Virol 76: 11113-11122.
    • (2002) J Virol , vol.76 , pp. 11113-11122
    • Gazina, E.V.1    Mackenzie, J.M.2    Gorrell, R.J.3    Anderson, D.A.4
  • 33
    • 0026794415 scopus 로고
    • Involvement of membrane traffic in the replication of poliovirus genomes: Effects of brefeldin A
    • Irurzun A, Perez L, Carrasco L (1992) Involvement of membrane traffic in the replication of poliovirus genomes: Effects of brefeldin A. Virology 191: 166-175.
    • (1992) Virology , vol.191 , pp. 166-175
    • Irurzun, A.1    Perez, L.2    Carrasco, L.3
  • 34
    • 0026533754 scopus 로고
    • Inhibition of poliovirus RNA synthesis by brefeldin A
    • Maynell LA, Kirkegaard K, Klymkowsky MW (1992) Inhibition of poliovirus RNA synthesis by brefeldin A. J Virol 66: 1985-1994.
    • (1992) J Virol , vol.66 , pp. 1985-1994
    • Maynell, L.A.1    Kirkegaard, K.2    Klymkowsky, M.W.3
  • 35
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: An autophagy-like origin for virus-induced vesicles
    • Suhy DA, Giddings TH Jr, Kirkegaard K (2000) Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: An autophagy-like origin for virus-induced vesicles. J Virol 74: 8953-8965.
    • (2000) J Virol , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings Jr., T.H.2    Kirkegaard, K.3
  • 36
    • 0030728931 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: Genetic and ultrastructural analysis
    • Doedens JR, Giddings TH Jr, Kirkegaard K (1997) Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: Genetic and ultrastructural analysis. J Virol 71: 9054-9064.
    • (1997) J Virol , vol.71 , pp. 9054-9064
    • Doedens, J.R.1    Giddings Jr., T.H.2    Kirkegaard, K.3
  • 37
    • 0035192612 scopus 로고    scopus 로고
    • Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion
    • Ishihara N, Hamasaki M, Yokota S, Suzuki K, Kamada Y, et al. (2001) Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell 12: 3690-3702.
    • (2001) Mol Biol Cell , vol.12 , pp. 3690-3702
    • Ishihara, N.1    Hamasaki, M.2    Yokota, S.3    Suzuki, K.4    Kamada, Y.5
  • 38
    • 0036463736 scopus 로고    scopus 로고
    • Autophagy in the eukaryotic cell
    • Reggiori F, Klionsky, DJ (2002) Autophagy in the eukaryotic cell. Eukaryot Cell 1: 11-21.
    • (2002) Eukaryot Cell , vol.1 , pp. 11-21
    • Reggiori, F.1    Klionsky, D.J.2
  • 39
    • 0037308987 scopus 로고    scopus 로고
    • The early secretory pathway contributes to autophagy in yeast
    • Hamasaki M, Noda T, Ohsumi Y (2003) The early secretory pathway contributes to autophagy in yeast. Cell Struct Funct 28: 49-54.
    • (2003) Cell Struct Funct , vol.28 , pp. 49-54
    • Hamasaki, M.1    Noda, T.2    Ohsumi, Y.3
  • 40
    • 0029836930 scopus 로고    scopus 로고
    • COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI
    • Rowe T, Aridor M, McCaffery JM, Plutner H, Nuoffer C, et al. (1996) COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI. J Cell Biol 135: 895-911.
    • (1996) J Cell Biol , vol.135 , pp. 895-911
    • Rowe, T.1    Aridor, M.2    McCaffery, J.M.3    Plutner, H.4    Nuoffer, C.5
  • 41
    • 0033548165 scopus 로고    scopus 로고
    • Cargo can modulate COPII vesicle formation from the endoplasmic reticulum
    • Aridor M, Bannykh SI, Rowe T, Balch WE (1999) Cargo can modulate COPII vesicle formation from the endoplasmic reticulum. J Biol Chem 274: 4389-4399.
    • (1999) J Biol Chem , vol.274 , pp. 4389-4399
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 43
    • 2142752480 scopus 로고    scopus 로고
    • Cellular autophagy: Surrender, avoidance and subversion by microorganisms
    • Kirkegaard K, Taylor MP, Jackson WT (2004) Cellular autophagy: Surrender, avoidance and subversion by microorganisms. Nat Rev Microbiol 2: 301-314.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 301-314
    • Kirkegaard, K.1    Taylor, M.P.2    Jackson, W.T.3
  • 44
    • 0037039442 scopus 로고    scopus 로고
    • Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway
    • Talloczy Z, Jiang W, Virgin HWT, Leib DA, Scheuner D, et al. (2002) Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway. Proc Natl Acad Sci U S A 99: 190-195.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 190-195
    • Talloczy, Z.1    Jiang, W.2    Virgin, H.W.T.3    Leib, D.A.4    Scheuner, D.5
  • 45
    • 8344247016 scopus 로고    scopus 로고
    • Autophagy defends cells against invading group A Streptococcus
    • Nakagawa I, Amano A, Mizushima N, Yamamoto A, Yamaguchi H, et al. (2004) Autophagy defends cells against invading group A Streptococcus. Science 306: 1037-1040.
    • (2004) Science , vol.306 , pp. 1037-1040
    • Nakagawa, I.1    Amano, A.2    Mizushima, N.3    Yamamoto, A.4    Yamaguchi, H.5
  • 46
    • 4344712684 scopus 로고    scopus 로고
    • Methods for monitoring autophagy
    • Mizushima N (2004) Methods for monitoring autophagy. Int J Biochem Cell Biol 36: 2491-2502.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2491-2502
    • Mizushima, N.1
  • 47
    • 0028289946 scopus 로고
    • Molecular characterization of light chain 3: A microtubule binding subunit of MAP1A and MAP1B
    • Mann SS, Hammarback JA (1994) Molecular characterization of light chain 3: A microtubule binding subunit of MAP1A and MAP1B. J Biol Chem 269: 11492-11497.
    • (1994) J Biol Chem , vol.269 , pp. 11492-11497
    • Mann, S.S.1    Hammarback, J.A.2
  • 48
    • 0034757896 scopus 로고    scopus 로고
    • A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation
    • Munafo DB, Colombo MI (2001) A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation. J Cell Sci 114: 3619-3629.
    • (2001) J Cell Sci , vol.114 , pp. 3619-3629
    • Munafo, D.B.1    Colombo, M.I.2
  • 49
    • 0036017758 scopus 로고    scopus 로고
    • Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24
    • Munafo DB, Colombo MI (2002) Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24. Traffic 3: 472-482.
    • (2002) Traffic , vol.3 , pp. 472-482
    • Munafo, D.B.1    Colombo, M.I.2
  • 50
    • 0013921592 scopus 로고
    • Aspects of the synthesis of poliovirus RNA and the formation of virus particles
    • Baltimore D, Girard M, Darnell JE (1966) Aspects of the synthesis of poliovirus RNA and the formation of virus particles. J Virol 29: 179-189.
    • (1966) J Virol , vol.29 , pp. 179-189
    • Baltimore, D.1    Girard, M.2    Darnell, J.E.3
  • 51
    • 0028812170 scopus 로고
    • Induction of membrane proliferation by poliovirus proteins 2C and 2BC
    • Aldabe R, Carrasco L (1995) Induction of membrane proliferation by poliovirus proteins 2C and 2BC. Biochem Biophys Res Commun 206: 64-76.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 64-76
    • Aldabe, R.1    Carrasco, L.2
  • 52
    • 0030807887 scopus 로고    scopus 로고
    • Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells
    • Teterina NL, Gorbalenya AE, Egger D, Bienz K, Ehrenfeld E (1997) Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells. J Virol 71: 8962-8972.
    • (1997) J Virol , vol.71 , pp. 8962-8972
    • Teterina, N.L.1    Gorbalenya, A.E.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 53
    • 0028918959 scopus 로고
    • Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A
    • Doedens JR, Kirkegaard K (1995) Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A. EMBO J 14: 894-907.
    • (1995) EMBO J , vol.14 , pp. 894-907
    • Doedens, J.R.1    Kirkegaard, K.2
  • 54
    • 0028836002 scopus 로고
    • Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles
    • Biederbick A, Kern HF, Elsasser HP (1995) Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles. Eur J Cell Biol 66: 3-14.
    • (1995) Eur J Cell Biol , vol.66 , pp. 3-14
    • Biederbick, A.1    Kern, H.F.2    Elsasser, H.P.3
  • 55
    • 0033997045 scopus 로고    scopus 로고
    • The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe
    • Niemann A, Takatsuki A, Elsasser HP (2000) The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe. J Histochem Cytochem 48: 251-258.
    • (2000) J Histochem Cytochem , vol.48 , pp. 251-258
    • Niemann, A.1    Takatsuki, A.2    Elsasser, H.P.3
  • 56
    • 0005677775 scopus 로고
    • 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen PO, Gordon PB (1982) 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc Natl Acad Sci U S A 79: 1889-1892.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 57
    • 0041411115 scopus 로고    scopus 로고
    • Autophagic programmed cell death in Drosophila
    • Baehrecke EH (2003) Autophagic programmed cell death in Drosophila. Cell Death Differ 10: 940-945.
    • (2003) Cell Death Differ , vol.10 , pp. 940-945
    • Baehrecke, E.H.1
  • 58
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: Apoptosis, necrosis and autophagy
    • Edinger AL, Thompson CB (2004) Death by design: Apoptosis, necrosis and autophagy. Curr Opin Cell Biol 16: 663-669.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 59
    • 0028795216 scopus 로고
    • Poliovirus subviral particles associated with progeny RNA in the replication complex
    • Pfister T, Egger D, Bienz K (1995) Poliovirus subviral particles associated with progeny RNA in the replication complex. J Gen Virol 76: 63-71.
    • (1995) J Gen Virol , vol.76 , pp. 63-71
    • Pfister, T.1    Egger, D.2    Bienz, K.3
  • 60
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of poliovirus replicon RNA
    • Nugent CI, Johnson KL, Sarnow P, Kirkegaard K (1999) Functional coupling between replication and packaging of poliovirus replicon RNA. J Virol 73: 427-435.
    • (1999) J Virol , vol.73 , pp. 427-435
    • Nugent, C.I.1    Johnson, K.L.2    Sarnow, P.3    Kirkegaard, K.4
  • 61
    • 0033017866 scopus 로고    scopus 로고
    • Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex
    • Pedersen KW, van der Meer Y, Roos N, Snijder EJ (1999) Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex. J Virol 73: 2016-2026.
    • (1999) J Virol , vol.73 , pp. 2016-2026
    • Pedersen, K.W.1    Van Der Meer, Y.2    Roos, N.3    Snijder, E.J.4
  • 62
    • 0036196634 scopus 로고    scopus 로고
    • RNA replication of mouse hepatitis virus takes place at double-membrane vesicles
    • Gosert R, Kanjanahaluethai A, Egger D, Bienz K, Baker SC (2002) RNA replication of mouse hepatitis virus takes place at double-membrane vesicles. J Virol 76: 3697-3708.
    • (2002) J Virol , vol.76 , pp. 3697-3708
    • Gosert, R.1    Kanjanahaluethai, A.2    Egger, D.3    Bienz, K.4    Baker, S.C.5
  • 64
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice E, Jerome WG, Yoshimori T, Mizushima N, Denison MR (2004) Coronavirus replication complex formation utilizes components of cellular autophagy. J Biol Chem 279: 10136-10141.
    • (2004) J Biol Chem , vol.279 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 65
    • 0035008260 scopus 로고    scopus 로고
    • Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex
    • Snijder EJ, van Tol H, Roos N, Pedersen KW (2001) Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex. J Gen Virol 82: 985-994.
    • (2001) J Gen Virol , vol.82 , pp. 985-994
    • Snijder, E.J.1    Van Tol, H.2    Roos, N.3    Pedersen, K.W.4
  • 66
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophage
    • Gutierrez MG, Master SS, Singh SB, Taylor GA, Colombo MI, et al. (2004) Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophage. Cell 119: 753-766.
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5
  • 68
    • 0037405929 scopus 로고    scopus 로고
    • Caspase cleavage of the nonstructural protein NS1 mediates replication of Aleutian mink disease virus
    • Best SM, Shelton JF, Pompey JM, Wolfinbarger JB, Bloom ME (2003) Caspase cleavage of the nonstructural protein NS1 mediates replication of Aleutian mink disease virus. J Virol 77: 5305-5312.
    • (2003) J Virol , vol.77 , pp. 5305-5312
    • Best, S.M.1    Shelton, J.F.2    Pompey, J.M.3    Wolfinbarger, J.B.4    Bloom, M.E.5
  • 69
    • 0034806363 scopus 로고    scopus 로고
    • Murine cytomegalovirus CC chemokine homolog MCK-2 (m131-129) is a determinant of dissemination that increases inflammation at initial sites of infection
    • Saederup N, Mocarski ES Jr (2002) Murine cytomegalovirus CC chemokine homolog MCK-2 (m131-129) is a determinant of dissemination that increases inflammation at initial sites of infection. J Virol 75: 9966-9976.
    • (2002) J Virol , vol.75 , pp. 9966-9976
    • Saederup, N.1    Mocarski Jr., E.S.2
  • 70
    • 0029155737 scopus 로고
    • Association of Legionella pneumophila with the macrophage endoplasmic reticulum
    • Swanson MS, Isberg RR (1995) Association of Legionella pneumophila with the macrophage endoplasmic reticulum. Infect Immun 63: 3609-3620.
    • (1995) Infect Immun , vol.63 , pp. 3609-3620
    • Swanson, M.S.1    Isberg, R.R.2
  • 71
    • 0030450505 scopus 로고    scopus 로고
    • Analysis of the intracellular fate of Legionella pneumophila mutants
    • Swanson MS, Isberg RR (1996) Analysis of the intracellular fate of Legionella pneumophila mutants. Ann N Y Acad Sci 797: 8-18.
    • (1996) Ann N Y Acad Sci , vol.797 , pp. 8-18
    • Swanson, M.S.1    Isberg, R.R.2
  • 72
    • 0035133794 scopus 로고    scopus 로고
    • Evidence that Dot-dependent and -independent factors isolate the Legionella pneumophila phagosome from the endocytic network in mouse macrophages
    • Joshi AD, Sturgill-Koszycki S, Swanson MS (2001) Evidence that Dot-dependent and -independent factors isolate the Legionella pneumophila phagosome from the endocytic network in mouse macrophages. Cell Microbiol 3: 99-114.
    • (2001) Cell Microbiol , vol.3 , pp. 99-114
    • Joshi, A.D.1    Sturgill-Koszycki, S.2    Swanson, M.S.3
  • 73
    • 0242300174 scopus 로고    scopus 로고
    • Engineered retargeting of viral RNA replication complexes to an alternative intracellular membrane
    • Miller DJ, Schwartz MD, Dye BT, Ahlquist P (2003) Engineered retargeting of viral RNA replication complexes to an alternative intracellular membrane. J Virol 77: 12193-12202.
    • (2003) J Virol , vol.77 , pp. 12193-12202
    • Miller, D.J.1    Schwartz, M.D.2    Dye, B.T.3    Ahlquist, P.4
  • 75
    • 0027185479 scopus 로고
    • Persistent infection of human erythroblastoid cells by poliovirus
    • Lloyd RE, Bovee M (1993) Persistent infection of human erythroblastoid cells by poliovirus. Virol 194: 200-209.
    • (1993) Virol , vol.194 , pp. 200-209
    • Lloyd, R.E.1    Bovee, M.2
  • 76
    • 0030772723 scopus 로고    scopus 로고
    • Persistent echovirus infection of mouse cells expressing the viral receptor VLA-2
    • Zhang S, Racaniello VR (1997) Persistent echovirus infection of mouse cells expressing the viral receptor VLA-2. Virol 235: 293-301.
    • (1997) Virol , vol.235 , pp. 293-301
    • Zhang, S.1    Racaniello, V.R.2
  • 77
    • 0034284909 scopus 로고    scopus 로고
    • Expression of mutated poliovirus receptors in human neuroblastoma cells persistently infected with poliovirus
    • Pavio N, Couderc T, Girard S, Sgro J-Y, Blondel B, et al. (2000) Expression of mutated poliovirus receptors in human neuroblastoma cells persistently infected with poliovirus. Virology 274: 331-342.
    • (2000) Virology , vol.274 , pp. 331-342
    • Pavio, N.1    Couderc, T.2    Girard, S.3    Sgro, J.-Y.4    Blondel, B.5
  • 78
    • 0027246363 scopus 로고
    • Vectorial release of poliovirus from polarized human intestinal epithelial cells
    • Tucker SP, Thronton CL, Wimmer E, Compans RW (1993) Vectorial release of poliovirus from polarized human intestinal epithelial cells. J Virol 67: 4274-4282.
    • (1993) J Virol , vol.67 , pp. 4274-4282
    • Tucker, S.P.1    Thronton, C.L.2    Wimmer, E.3    Compans, R.W.4
  • 79
    • 0015579629 scopus 로고
    • A physico-chemical subgrouping of the mammalian picornaviruses
    • Newman JFE, Rowlands DF, Brown F (1973) A physico-chemical subgrouping of the mammalian picornaviruses. J Gen Virol 18: 171-180.
    • (1973) J Gen Virol , vol.18 , pp. 171-180
    • Newman, J.F.E.1    Rowlands, D.F.2    Brown, F.3
  • 80
    • 0031756803 scopus 로고    scopus 로고
    • Variability in the integrity of human enteroviruses exposed to various simulated in vivo environments
    • Piirainen L, Hovi T, Roivainen M (1998) Variability in the integrity of human enteroviruses exposed to various simulated in vivo environments. Microb Pathog 25: 131-137.
    • (1998) Microb Pathog , vol.25 , pp. 131-137
    • Piirainen, L.1    Hovi, T.2    Roivainen, M.3
  • 81
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophage
    • Pelchin-Matthews A, Kramer B, Marsh M (2003) Infectious HIV-1 assembles in late endosomes in primary macrophage. J Cell Biol 162: 443-455.
    • (2003) J Cell Biol , vol.162 , pp. 443-455
    • Pelchin-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 83
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body
    • Ono A, Freed EO (2004) Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body. J Virol 78: 1552-1563.
    • (2004) J Virol , vol.78 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 84
    • 0041888375 scopus 로고    scopus 로고
    • Tsg101 control of human immunodeficiency virus type 1 gag trafficking and release
    • Goff A, Ehrlich LS, Cohen SN, Carter CA (2003) Tsg101 control of human immunodeficiency virus type 1 gag trafficking and release. J Virol 77: 9173-9182.
    • (2003) J Virol , vol.77 , pp. 9173-9182
    • Goff, A.1    Ehrlich, L.S.2    Cohen, S.N.3    Carter, C.A.4
  • 86
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • Katzmann DJ, Stefan CJ, Babst M, Emr SD (2003) Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J Cell Biol 160: 413-423.
    • (2003) J Cell Biol , vol.160 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 87
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • Bache KG, Brech A, Mehlum A, Stenmark H (2003) Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J Cell Biol 162: 435-442.
    • (2003) J Cell Biol , vol.162 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 88
    • 4143061605 scopus 로고    scopus 로고
    • The human endosomal sorting complex required for transprot (ESCRT-I) and its role in HIV-1 budding
    • Stuchell MD, Garrus JE, Müller B, Stray KM, Ghaffarian S, et al. (2004) The human endosomal sorting complex required for transprot (ESCRT-I) and its role in HIV-1 budding. J Biol Chem 279: 36059-36071.
    • (2004) J Biol Chem , vol.279 , pp. 36059-36071
    • Stuchell, M.D.1    Garrus, J.E.2    Müller, B.3    Stray, K.M.4    Ghaffarian, S.5
  • 89
    • 0019808773 scopus 로고
    • Cloned poliovirus complementary DNA is infectious in mammalian cells
    • Racaniello VR, Baltimore D (1981) Cloned poliovirus complementary DNA is infectious in mammalian cells. Science 214: 916-919.
    • (1981) Science , vol.214 , pp. 916-919
    • Racaniello, V.R.1    Baltimore, D.2
  • 90
    • 0029159796 scopus 로고
    • Infection of a human respiratory epithelial cell line with rhinovirus. Induction of cytokine release and modulation of susceptibility to infection by cytokine exposure
    • Subauste MC, Jacoby DB, Richards SM, Proud D (1995) Infection of a human respiratory epithelial cell line with rhinovirus. Induction of cytokine release and modulation of susceptibility to infection by cytokine exposure. J Clin Invest 96: 549-557.
    • (1995) J Clin Invest , vol.96 , pp. 549-557
    • Subauste, M.C.1    Jacoby, D.B.2    Richards, S.M.3    Proud, D.4
  • 91
    • 0027174945 scopus 로고
    • Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone
    • Takizawa PA, Yucel JK, Veit B, Faulkner DJ, Deerinck T, et al. (1993) Complete vesiculation of Golgi membranes and inhibition of protein transport by a novel sea sponge metabolite, ilimaquinone. Cell 73: 1079-1090.
    • (1993) Cell , vol.73 , pp. 1079-1090
    • Takizawa, P.A.1    Yucel, J.K.2    Veit, B.3    Faulkner, D.J.4    Deerinck, T.5
  • 92
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole NB, Sciaky N, Marotta A, Song J, Lippincott-Schwartz J (1996) Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol Biol Cell 7: 631-650.
    • (1996) Mol Biol Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 93
    • 0042206454 scopus 로고    scopus 로고
    • Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B
    • He H, Dang Y, Dai F, Guo Z, Wu J, et al. (2003) Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B. J Biol Chem 278: 29278-29287.
    • (2003) J Biol Chem , vol.278 , pp. 29278-29287
    • He, H.1    Dang, Y.2    Dai, F.3    Guo, Z.4    Wu, J.5


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