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Volumn 27, Issue 1, 2007, Pages 11-21

Innate and Adaptive Immunity through Autophagy

Author keywords

[No Author keywords available]

Indexed keywords

CELL ANTIGEN; HYDROLASE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PROTEASOME;

EID: 34447629523     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.immuni.2007.07.004     Document Type: Review
Times cited : (383)

References (106)
  • 2
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes F.A., Terlecky S.R., and Dice J.F. An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J. Cell Biol. 137 (1997) 825-834
    • (1997) J. Cell Biol. , vol.137 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 3
    • 34250802980 scopus 로고    scopus 로고
    • Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy
    • Alonso S., Pethe K., Russell D.G., and Purdy G.E. Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy. Proc. Natl. Acad. Sci. USA 104 (2007) 6031-6036
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6031-6036
    • Alonso, S.1    Pethe, K.2    Russell, D.G.3    Purdy, G.E.4
  • 4
    • 3342927582 scopus 로고    scopus 로고
    • Interaction of Chlamydia trachomatis serovar L2 with the host autophagic pathway
    • Al-Younes H.M., Brinkmann V., and Meyer T.F. Interaction of Chlamydia trachomatis serovar L2 with the host autophagic pathway. Infect. Immun. 72 (2004) 4751-4762
    • (2004) Infect. Immun. , vol.72 , pp. 4751-4762
    • Al-Younes, H.M.1    Brinkmann, V.2    Meyer, T.F.3
  • 5
    • 19644388051 scopus 로고    scopus 로고
    • Macrophages rapidly transfer pathogens from lipid raft vacuoles to autophagosomes
    • Amer A.O., Byrne B.G., and Swanson M.S. Macrophages rapidly transfer pathogens from lipid raft vacuoles to autophagosomes. Autophagy 1 (2005) 53-58
    • (2005) Autophagy , vol.1 , pp. 53-58
    • Amer, A.O.1    Byrne, B.G.2    Swanson, M.S.3
  • 6
    • 19644382161 scopus 로고    scopus 로고
    • Autophagy is an immediate macrophage response to Legionella pneumophila
    • Amer A.O., and Swanson M.S. Autophagy is an immediate macrophage response to Legionella pneumophila. Cell. Microbiol. 7 (2005) 765-778
    • (2005) Cell. Microbiol. , vol.7 , pp. 765-778
    • Amer, A.O.1    Swanson, M.S.2
  • 7
    • 33748331335 scopus 로고    scopus 로고
    • CD40 induces macrophage anti-Toxoplasma gondii activity by triggering autophagy-dependent fusion of pathogen-containing vacuoles and lysosomes
    • Andrade R.M., Wessendarp M., Gubbels M.J., Striepen B., and Subauste C.S. CD40 induces macrophage anti-Toxoplasma gondii activity by triggering autophagy-dependent fusion of pathogen-containing vacuoles and lysosomes. J. Clin. Invest. 116 (2006) 2366-2377
    • (2006) J. Clin. Invest. , vol.116 , pp. 2366-2377
    • Andrade, R.M.1    Wessendarp, M.2    Gubbels, M.J.3    Striepen, B.4    Subauste, C.S.5
  • 8
    • 0027280820 scopus 로고
    • Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes
    • Aniento F., Roche E., Cuervo A.M., and Knecht E. Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes. J. Biol. Chem. 268 (1993) 10463-10470
    • (1993) J. Biol. Chem. , vol.268 , pp. 10463-10470
    • Aniento, F.1    Roche, E.2    Cuervo, A.M.3    Knecht, E.4
  • 9
    • 0032555641 scopus 로고    scopus 로고
    • Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes
    • Berg T.O., Fengsrud M., Stromhaug P.E., Berg T., and Seglen P.O. Isolation and characterization of rat liver amphisomes. Evidence for fusion of autophagosomes with both early and late endosomes. J. Biol. Chem. 273 (1998) 21883-21892
    • (1998) J. Biol. Chem. , vol.273 , pp. 21883-21892
    • Berg, T.O.1    Fengsrud, M.2    Stromhaug, P.E.3    Berg, T.4    Seglen, P.O.5
  • 10
    • 33744935521 scopus 로고    scopus 로고
    • Rotavirus NSP4 induces a novel vesicular compartment regulated by calcium and associated with viroplasms
    • Berkova Z., Crawford S.E., Trugnan G., Yoshimori T., Morris A.P., and Estes M.K. Rotavirus NSP4 induces a novel vesicular compartment regulated by calcium and associated with viroplasms. J. Virol. 80 (2006) 6061-6071
    • (2006) J. Virol. , vol.80 , pp. 6061-6071
    • Berkova, Z.1    Crawford, S.E.2    Trugnan, G.3    Yoshimori, T.4    Morris, A.P.5    Estes, M.K.6
  • 12
    • 33744958258 scopus 로고    scopus 로고
    • Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole
    • Birmingham C.L., Smith A.C., Bakowski M.A., Yoshimori T., and Brumell J.H. Autophagy controls Salmonella infection in response to damage to the Salmonella-containing vacuole. J. Biol. Chem. 281 (2006) 11374-11383
    • (2006) J. Biol. Chem. , vol.281 , pp. 11374-11383
    • Birmingham, C.L.1    Smith, A.C.2    Bakowski, M.A.3    Yoshimori, T.4    Brumell, J.H.5
  • 13
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., Stenmark H., and Johansen T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171 (2005) 603-614
    • (2005) J. Cell Biol. , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 14
    • 1842407189 scopus 로고    scopus 로고
    • Excessive degradation of intracellular protein in macrophages prevents presentation in the context of major histocompatibility complex class II molecules
    • Brazil M.I., Weiss S., and Stockinger B. Excessive degradation of intracellular protein in macrophages prevents presentation in the context of major histocompatibility complex class II molecules. Eur. J. Immunol. 27 (1997) 1506-1514
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1506-1514
    • Brazil, M.I.1    Weiss, S.2    Stockinger, B.3
  • 15
    • 0041920932 scopus 로고    scopus 로고
    • Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum
    • Celli J., de Chastellier C., Franchini D.M., Pizarro-Cerda J., Moreno E., and Gorvel J.P. Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum. J. Exp. Med. 198 (2003) 545-556
    • (2003) J. Exp. Med. , vol.198 , pp. 545-556
    • Celli, J.1    de Chastellier, C.2    Franchini, D.M.3    Pizarro-Cerda, J.4    Moreno, E.5    Gorvel, J.P.6
  • 16
    • 33749264796 scopus 로고    scopus 로고
    • Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication
    • Checroun C., Wehrly T.D., Fischer E.R., Hayes S.F., and Celli J. Autophagy-mediated reentry of Francisella tularensis into the endocytic compartment after cytoplasmic replication. Proc. Natl. Acad. Sci. USA 103 (2006) 14578-14583
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14578-14583
    • Checroun, C.1    Wehrly, T.D.2    Fischer, E.R.3    Hayes, S.F.4    Celli, J.5
  • 17
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang H.L., Terlecky S.R., Plant C.P., and Dice J.F. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246 (1989) 382-385
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 19
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover A., Finley D., and Varshavsky A. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell 37 (1984) 57-66
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 20
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo A.M., and Dice J.F. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273 (1996) 501-503
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 21
    • 0034510572 scopus 로고    scopus 로고
    • Unique properties of lamp2a compared to other lamp2 isoforms
    • Cuervo A.M., and Dice J.F. Unique properties of lamp2a compared to other lamp2 isoforms. J. Cell Sci. 113 (2000) 4441-4450
    • (2000) J. Cell Sci. , vol.113 , pp. 4441-4450
    • Cuervo, A.M.1    Dice, J.F.2
  • 22
    • 0000115806 scopus 로고
    • Electron microscopic study of the formation of poliovirus
    • Dales S., Eggers H.J., Tamm I., and Palade G.E. Electron microscopic study of the formation of poliovirus. Virology 26 (1965) 379-389
    • (1965) Virology , vol.26 , pp. 379-389
    • Dales, S.1    Eggers, H.J.2    Tamm, I.3    Palade, G.E.4
  • 25
    • 0016808917 scopus 로고
    • A statistical analysis of the relationship between degradative rates and molecular weights of proteins
    • Dice J.F., and Goldberg A.L. A statistical analysis of the relationship between degradative rates and molecular weights of proteins. Arch. Biochem. Biophys. 170 (1975) 213-219
    • (1975) Arch. Biochem. Biophys. , vol.170 , pp. 213-219
    • Dice, J.F.1    Goldberg, A.L.2
  • 28
    • 17044381835 scopus 로고    scopus 로고
    • Processing and presentation of HLA class I and II epitopes by dendritic cells after transfection with in vitro transcribed MUC1 RNA
    • Dörfel D., Appel S., Grunebach F., Weck M.M., Muller M.R., Heine A., and Brossart P. Processing and presentation of HLA class I and II epitopes by dendritic cells after transfection with in vitro transcribed MUC1 RNA. Blood 105 (2005) 3199-3205
    • (2005) Blood , vol.105 , pp. 3199-3205
    • Dörfel, D.1    Appel, S.2    Grunebach, F.3    Weck, M.M.4    Muller, M.R.5    Heine, A.6    Brossart, P.7
  • 29
    • 0034876410 scopus 로고    scopus 로고
    • Porphyromonas gingivalis traffics to autophagosomes in human coronary artery endothelial cells
    • Dorn B.R., Dunn Jr. W.A., and Progulske-Fox A. Porphyromonas gingivalis traffics to autophagosomes in human coronary artery endothelial cells. Infect. Immun. 69 (2001) 5698-5708
    • (2001) Infect. Immun. , vol.69 , pp. 5698-5708
    • Dorn, B.R.1    Dunn Jr., W.A.2    Progulske-Fox, A.3
  • 31
    • 0034529528 scopus 로고    scopus 로고
    • Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy
    • Fengsrud M., Erichsen E.S., Berg T.O., Raiborg C., and Seglen P.O. Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy. Eur. J. Cell Biol. 79 (2000) 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
  • 33
    • 0029907090 scopus 로고    scopus 로고
    • Presentation of a cytosolic antigen by major histocompatibility complex class II molecules requires a long-lived form of the antigen
    • Gueguen M., and Long E.O. Presentation of a cytosolic antigen by major histocompatibility complex class II molecules requires a long-lived form of the antigen. Proc. Natl. Acad. Sci. USA 93 (1996) 14692-14697
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14692-14697
    • Gueguen, M.1    Long, E.O.2
  • 34
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism Inhibiting BCG and mycobacterium tuberculosis survival in infected macrophages
    • Gutierrez M.G., Master S.S., Singh S.B., Taylor G.A., Colombo M.I., and Deretic V. Autophagy is a defense mechanism Inhibiting BCG and mycobacterium tuberculosis survival in infected macrophages. Cell 119 (2004) 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    Deretic, V.6
  • 39
    • 17044368771 scopus 로고    scopus 로고
    • The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation
    • Heessen S., Masucci M.G., and Dantuma N.P. The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation. Mol. Cell 18 (2005) 225-235
    • (2005) Mol. Cell , vol.18 , pp. 225-235
    • Heessen, S.1    Masucci, M.G.2    Dantuma, N.P.3
  • 41
    • 0023097064 scopus 로고
    • Degradation of short- and long-lived proteins in perfused liver and in isolated autophagic vacuoles-lysosomes
    • Henell F., Berkenstam A., Ahlberg J., and Glaumann H. Degradation of short- and long-lived proteins in perfused liver and in isolated autophagic vacuoles-lysosomes. Exp. Mol. Pathol. 46 (1987) 1-14
    • (1987) Exp. Mol. Pathol. , vol.46 , pp. 1-14
    • Henell, F.1    Berkenstam, A.2    Ahlberg, J.3    Glaumann, H.4
  • 42
    • 0346849709 scopus 로고    scopus 로고
    • A Salmonella protein causes macrophage cell death by inducing autophagy
    • Hernandez L.D., Pypaert M., Flavell R.A., and Galan J.E. A Salmonella protein causes macrophage cell death by inducing autophagy. J. Cell Biol. 163 (2003) 1123-1131
    • (2003) J. Cell Biol. , vol.163 , pp. 1123-1131
    • Hernandez, L.D.1    Pypaert, M.2    Flavell, R.A.3    Galan, J.E.4
  • 43
    • 33646152750 scopus 로고    scopus 로고
    • Glycine-alanine repeats impair proper substrate unfolding by the proteasome
    • Hoyt M.A., Zich J., Takeuchi J., Zhang M., Govaerts C., and Coffino P. Glycine-alanine repeats impair proper substrate unfolding by the proteasome. EMBO J. 25 (2006) 1720-1729
    • (2006) EMBO J. , vol.25 , pp. 1720-1729
    • Hoyt, M.A.1    Zich, J.2    Takeuchi, J.3    Zhang, M.4    Govaerts, C.5    Coffino, P.6
  • 45
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • Inbal B., Bialik S., Sabanay I., Shani G., and Kimchi A. DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death. J. Cell Biol. 157 (2002) 455-468
    • (2002) J. Cell Biol. , vol.157 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 47
    • 0025035510 scopus 로고
    • An endogenous processing pathway in vaccinia virus-infected cells for presentation of cytoplasmic antigens to class II-restricted T cells
    • Jaraquemada D., Marti M., and Long E.O. An endogenous processing pathway in vaccinia virus-infected cells for presentation of cytoplasmic antigens to class II-restricted T cells. J. Exp. Med. 172 (1990) 947-954
    • (1990) J. Exp. Med. , vol.172 , pp. 947-954
    • Jaraquemada, D.1    Marti, M.2    Long, E.O.3
  • 48
    • 33244481532 scopus 로고    scopus 로고
    • Autophagy: A forty-year search for a missing membrane source
    • Juhasz G., and Neufeld T.P. Autophagy: A forty-year search for a missing membrane source. PLoS Biol. 4 (2006) e36
    • (2006) PLoS Biol. , vol.4
    • Juhasz, G.1    Neufeld, T.P.2
  • 50
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara A., Kabeya Y., Ohsumi Y., and Yoshimori T. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2 (2001) 330-335
    • (2001) EMBO Rep. , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 52
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G., and Jaattela M. Lysosomes and autophagy in cell death control. Nat. Rev. Cancer 5 (2005) 886-897
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 53
    • 33947134377 scopus 로고    scopus 로고
    • Autophagy-dependent viral recognition by plasmacytoid dendritic cells
    • Lee H.K., Lund J.M., Ramanathan B., Mizushima N., and Iwasaki A. Autophagy-dependent viral recognition by plasmacytoid dendritic cells. Science 315 (2007) 1398-1401
    • (2007) Science , vol.315 , pp. 1398-1401
    • Lee, H.K.1    Lund, J.M.2    Ramanathan, B.3    Mizushima, N.4    Iwasaki, A.5
  • 56
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya J., Sharipo A., Leonchiks A., Ciechanover A., and Masucci M.G. Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl. Acad. Sci. USA 94 (1997) 12616-12621
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Sharipo, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 59
    • 0034194155 scopus 로고    scopus 로고
    • Cytoplasmic processing is a prerequisite for presentation of an endogenous antigen by major histocompatibility complex class II proteins
    • Lich J.D., Elliott J.F., and Blum J.S. Cytoplasmic processing is a prerequisite for presentation of an endogenous antigen by major histocompatibility complex class II proteins. J. Exp. Med. 191 (2000) 1513-1524
    • (2000) J. Exp. Med. , vol.191 , pp. 1513-1524
    • Lich, J.D.1    Elliott, J.F.2    Blum, J.S.3
  • 60
    • 33748444233 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages
    • Ling Y.M., Shaw M.H., Ayala C., Coppens I., Taylor G.A., Ferguson D.J., and Yap G.S. Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages. J. Exp. Med. 203 (2006) 2063-2071
    • (2006) J. Exp. Med. , vol.203 , pp. 2063-2071
    • Ling, Y.M.1    Shaw, M.H.2    Ayala, C.3    Coppens, I.4    Taylor, G.A.5    Ferguson, D.J.6    Yap, G.S.7
  • 61
    • 0031031041 scopus 로고    scopus 로고
    • The autophagic and endocytic pathways converge at the nascent autophagic vacuoles
    • Liou W., Geuze H.J., Geelen M.J., and Slot J.W. The autophagic and endocytic pathways converge at the nascent autophagic vacuoles. J. Cell Biol. 136 (1997) 61-70
    • (1997) J. Cell Biol. , vol.136 , pp. 61-70
    • Liou, W.1    Geuze, H.J.2    Geelen, M.J.3    Slot, J.W.4
  • 62
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Liu Y., Schiff M., Czymmek K., Talloczy Z., Levine B., and Dinesh-Kumar S.P. Autophagy regulates programmed cell death during the plant innate immune response. Cell 121 (2005) 567-577
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1    Schiff, M.2    Czymmek, K.3    Talloczy, Z.4    Levine, B.5    Dinesh-Kumar, S.P.6
  • 64
    • 0031958596 scopus 로고    scopus 로고
    • Insertion of a sequence encoding light chain 3 of microtubule-associated proteins 1A and 1B in a pestivirus genome: Connection with virus cytopathogenicity and induction of lethal disease in cattle
    • Meyers G., Stoll D., and Gunn M. Insertion of a sequence encoding light chain 3 of microtubule-associated proteins 1A and 1B in a pestivirus genome: Connection with virus cytopathogenicity and induction of lethal disease in cattle. J. Virol. 72 (1998) 4139-4148
    • (1998) J. Virol. , vol.72 , pp. 4139-4148
    • Meyers, G.1    Stoll, D.2    Gunn, M.3
  • 65
    • 1542513774 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is required for induction of autophagy during lumen formation in vitro
    • Mills K.R., Reginato M., Debnath J., Queenan B., and Brugge J.S. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is required for induction of autophagy during lumen formation in vitro. Proc. Natl. Acad. Sci. USA 101 (2004) 3438-3443
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3438-3443
    • Mills, K.R.1    Reginato, M.2    Debnath, J.3    Queenan, B.4    Brugge, J.S.5
  • 66
    • 4344712684 scopus 로고    scopus 로고
    • Methods for monitoring autophagy
    • Mizushima N. Methods for monitoring autophagy. Int. J. Biochem. Cell Biol. 36 (2004) 2491-2502
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2491-2502
    • Mizushima, N.1
  • 67
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: Implications for metabolism
    • 10.1146/annurev.nutr.27.061406.093749 in press. Published online February 20, 2007
    • Mizushima N., and Klionsky D.J. Protein turnover via autophagy: Implications for metabolism. Annu. Rev. Nutr. (2007) 10.1146/annurev.nutr.27.061406.093749 in press. Published online February 20, 2007
    • (2007) Annu. Rev. Nutr.
    • Mizushima, N.1    Klionsky, D.J.2
  • 69
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N., Yamamoto A., Matsui M., Yoshimori T., and Ohsumi Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol. Biol. Cell 15 (2004) 1101-1111
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 75
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi Y. Molecular dissection of autophagy: Two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2 (2001) 211-216
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 79
    • 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 K.W., van der Meer Y., Roos N., and Snijder E.J. 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 (1999) 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
  • 80
    • 0031899678 scopus 로고    scopus 로고
    • Virulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments
    • Pizarro-Cerda J., Moreno E., Sanguedolce V., Mege J.L., and Gorvel J.P. Virulent Brucella abortus prevents lysosome fusion and is distributed within autophagosome-like compartments. Infect. Immun. 66 (1998) 2387-2392
    • (1998) Infect. Immun. , vol.66 , pp. 2387-2392
    • Pizarro-Cerda, J.1    Moreno, E.2    Sanguedolce, V.3    Mege, J.L.4    Gorvel, J.P.5
  • 81
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice E., Jerome W.G., Yoshimori T., Mizushima N., and Denison M.R. Coronavirus replication complex formation utilizes components of cellular autophagy. J. Biol. Chem. 279 (2004) 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
  • 82
    • 4444246734 scopus 로고    scopus 로고
    • Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins
    • Prentice E., McAuliffe J., Lu X., Subbarao K., and Denison M.R. Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins. J. Virol. 78 (2004) 9977-9986
    • (2004) J. Virol. , vol.78 , pp. 9977-9986
    • Prentice, E.1    McAuliffe, J.2    Lu, X.3    Subbarao, K.4    Denison, M.R.5
  • 83
    • 33846461678 scopus 로고    scopus 로고
    • A critical role for the autophagy gene Atg5 in T cell survival and proliferation
    • Pua H.H., Dzhagalov I., Chuck M., Mizushima N., and He Y.W. A critical role for the autophagy gene Atg5 in T cell survival and proliferation. J. Exp. Med. 204 (2007) 25-31
    • (2007) J. Exp. Med. , vol.204 , pp. 25-31
    • Pua, H.H.1    Dzhagalov, I.2    Chuck, M.3    Mizushima, N.4    He, Y.W.5
  • 84
    • 20144381544 scopus 로고    scopus 로고
    • Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death
    • Pyo J.O., Jang M.H., Kwon Y.K., Lee H.J., Jun J.I., Woo H.N., Cho D.H., Choi B., Lee H., Kim J.H., et al. Essential roles of Atg5 and FADD in autophagic cell death: Dissection of autophagic cell death into vacuole formation and cell death. J. Biol. Chem. 280 (2005) 20722-20729
    • (2005) J. Biol. Chem. , vol.280 , pp. 20722-20729
    • Pyo, J.O.1    Jang, M.H.2    Kwon, Y.K.3    Lee, H.J.4    Jun, J.I.5    Woo, H.N.6    Cho, D.H.7    Choi, B.8    Lee, H.9    Kim, J.H.10
  • 86
    • 0035064073 scopus 로고    scopus 로고
    • The bare lymphocyte syndrome and the regulation of MHC expression
    • Reith W., and Mach B. The bare lymphocyte syndrome and the regulation of MHC expression. Annu. Rev. Immunol. 19 (2001) 331-373
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 331-373
    • Reith, W.1    Mach, B.2
  • 87
    • 0037711625 scopus 로고    scopus 로고
    • Cytoplasmic bacteria can be targets for autophagy
    • Rich K.A., Burkett C., and Webster P. Cytoplasmic bacteria can be targets for autophagy. Cell. Microbiol. 5 (2003) 455-468
    • (2003) Cell. Microbiol. , vol.5 , pp. 455-468
    • Rich, K.A.1    Burkett, C.2    Webster, P.3
  • 89
    • 0032996570 scopus 로고    scopus 로고
    • Parasitophorous vacuoles of Leishmania mexicana acquire macromolecules from the host cell cytosol via two independent routes
    • Schaible U.E., Schlesinger P.H., Steinberg T.H., Mangel W.F., Kobayashi T., and Russell D.G. Parasitophorous vacuoles of Leishmania mexicana acquire macromolecules from the host cell cytosol via two independent routes. J. Cell Sci. 112 (1999) 681-693
    • (1999) J. Cell Sci. , vol.112 , pp. 681-693
    • Schaible, U.E.1    Schlesinger, P.H.2    Steinberg, T.H.3    Mangel, W.F.4    Kobayashi, T.5    Russell, D.G.6
  • 90
    • 33846224369 scopus 로고    scopus 로고
    • MHC class II antigen loading compartments continuously receive input from autophagosomes
    • Schmid D., Pypaert M., and Münz C. MHC class II antigen loading compartments continuously receive input from autophagosomes. Immunity 26 (2007) 79-92
    • (2007) Immunity , vol.26 , pp. 79-92
    • Schmid, D.1    Pypaert, M.2    Münz, C.3
  • 91
    • 0005677775 scopus 로고
    • 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen P.O., and Gordon P.B. 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc. Natl. Acad. Sci. USA 79 (1982) 1889-1892
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 93
    • 33748506089 scopus 로고    scopus 로고
    • Human IRGM induces autophagy to eliminate intracellular mycobacteria
    • Singh S.B., Davis A.S., Taylor G.A., and Deretic V. Human IRGM induces autophagy to eliminate intracellular mycobacteria. Science 313 (2006) 1438-1441
    • (2006) Science , vol.313 , pp. 1438-1441
    • Singh, S.B.1    Davis, A.S.2    Taylor, G.A.3    Deretic, V.4
  • 96
    • 0032532323 scopus 로고    scopus 로고
    • Purification and characterization of autophagosomes from rat hepatocytes
    • Stromhaug P.E., Berg T.O., Fengsrud M., and Seglen P.O. Purification and characterization of autophagosomes from rat hepatocytes. Biochem. J. 335 (1998) 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
  • 99
    • 14844310233 scopus 로고    scopus 로고
    • Selective inactivation of a Fas-associated death domain protein (FADD)-dependent apoptosis and autophagy pathway in immortal epithelial cells
    • Thorburn J., Moore F., Rao A., Barclay W.W., Thomas L.R., Grant K.W., Cramer S.D., and Thorburn A. Selective inactivation of a Fas-associated death domain protein (FADD)-dependent apoptosis and autophagy pathway in immortal epithelial cells. Mol. Biol. Cell 16 (2005) 1189-1199
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1189-1199
    • Thorburn, J.1    Moore, F.2    Rao, A.3    Barclay, W.W.4    Thomas, L.R.5    Grant, K.W.6    Cramer, S.D.7    Thorburn, A.8
  • 101
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • Trombetta E.S., and Mellman I. Cell biology of antigen processing in vitro and in vivo. Annu. Rev. Immunol. 23 (2005) 975-1028
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 102
    • 0031035350 scopus 로고    scopus 로고
    • Cytokine-induced, nitric oxide-dependent, intracellular antirickettsial activity of mouse endothelial cells
    • Walker D.H., Popov V.L., Crocquet-Valdes P.A., Welsh C.J., and Feng H.M. Cytokine-induced, nitric oxide-dependent, intracellular antirickettsial activity of mouse endothelial cells. Lab. Invest. 76 (1997) 129-138
    • (1997) Lab. Invest. , vol.76 , pp. 129-138
    • Walker, D.H.1    Popov, V.L.2    Crocquet-Valdes, P.A.3    Welsh, C.J.4    Feng, H.M.5
  • 103
    • 34447643958 scopus 로고    scopus 로고
    • Toll-like receptor 4 is a sensor for autophagy associated with innate immunity
    • this issue
    • Xu Y., Jagannath C., Liu X.D., Sharafkhaneh A., Kolodziejska K.E., and Eissa N.T. Toll-like receptor 4 is a sensor for autophagy associated with innate immunity. Immunity 27 (2007) 135-144 this issue
    • (2007) Immunity , vol.27 , pp. 135-144
    • Xu, Y.1    Jagannath, C.2    Liu, X.D.3    Sharafkhaneh, A.4    Kolodziejska, K.E.5    Eissa, N.T.6
  • 104
    • 32244442749 scopus 로고    scopus 로고
    • Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking
    • Zeng X., Overmeyer J.H., and Maltese W.A. Functional specificity of the mammalian Beclin-Vps34 PI 3-kinase complex in macroautophagy versus endocytosis and lysosomal enzyme trafficking. J. Cell Sci. 119 (2006) 259-270
    • (2006) J. Cell Sci. , vol.119 , pp. 259-270
    • Zeng, X.1    Overmeyer, J.H.2    Maltese, W.A.3


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