메뉴 건너뛰기




Volumn 18, Issue 1, 2014, Pages 55-65

Autophagy in inflammation, infection, neurodegeneration and cancer

Author keywords

ATG; Autophagy; Beclin 1; Diseases; Neuroinflammation

Indexed keywords

BECLIN 1; BRCA1 PROTEIN; CHLOROQUINE; HEAT SHOCK PROTEIN 90; HYDROXYCHLOROQUINE; INTERLEUKIN 1; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; MAMMALIAN TARGET OF RAPAMYCIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; OPTINEURIN; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PROTEIN SERINE THREONINE KINASE VPS15; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SALINOSPORAMIDE A; TEMOZOLOMIDE; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 9; TUMOR NECROSIS FACTOR ALPHA;

EID: 84888140819     PISSN: 15675769     EISSN: 18781705     Source Type: Journal    
DOI: 10.1016/j.intimp.2013.11.001     Document Type: Review
Times cited : (107)

References (167)
  • 1
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • N. Mizushima, B. Levine, A.M. Cuervo, and D.J. Klionsky Autophagy fights disease through cellular self-digestion Nature 451 2008 1069 1075 (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 2
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • B. Levine, and G. Kroemer Autophagy in the pathogenesis of disease Cell 132 2008 27 42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 3
    • 77955708390 scopus 로고    scopus 로고
    • Overview of macroautophagy regulation in mammalian cells
    • M. Mehrpour, A. Esclatine, I. Beau, and P. Codogno Overview of macroautophagy regulation in mammalian cells Cell Res 20 2010 748 762
    • (2010) Cell Res , vol.20 , pp. 748-762
    • Mehrpour, M.1    Esclatine, A.2    Beau, I.3    Codogno, P.4
  • 4
    • 78649704325 scopus 로고    scopus 로고
    • Autophagy and metabolism
    • J.D. Rabinowitz, and E. White Autophagy and metabolism Science 330 2010 1344 1348
    • (2010) Science , vol.330 , pp. 1344-1348
    • Rabinowitz, J.D.1    White, E.2
  • 6
    • 78651226124 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis eis regulates autophagy, inflammation, and cell death through redox-dependent signaling
    • D.M. Shin, B.Y. Jeon, H.M. Lee, H.S. Jin, J.M. Yuk, and C.H. Song Mycobacterium tuberculosis eis regulates autophagy, inflammation, and cell death through redox-dependent signaling PLoS Pathog 6 2010 e1001230
    • (2010) PLoS Pathog , vol.6 , pp. 1001230
    • Shin, D.M.1    Jeon, B.Y.2    Lee, H.M.3    Jin, H.S.4    Yuk, J.M.5    Song, C.H.6
  • 8
    • 33748506089 scopus 로고    scopus 로고
    • Human IRGM induces autophagy to eliminate intracellular mycobacteria
    • DOI 10.1126/science.1129577
    • S.B. Singh, A.S. Davis, G.A. Taylor, and V. Deretic Human IRGM induces autophagy to eliminate intracellular mycobacteria Science 313 2006 1438 1441 (Pubitemid 44360272)
    • (2006) Science , vol.313 , Issue.5792 , pp. 1438-1441
    • Singh, S.B.1    Davis, A.S.2    Taylor, G.A.3    Deretic, V.4
  • 9
    • 37549043217 scopus 로고    scopus 로고
    • Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis
    • M.A. Sanjuan, C.P. Dillon, S.W. Tait, S. Moshiach, F. Dorsey, and S. Connell Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis Nature 450 2007 1253 1257
    • (2007) Nature , vol.450 , pp. 1253-1257
    • Sanjuan, M.A.1    Dillon, C.P.2    Tait, S.W.3    Moshiach, S.4    Dorsey, F.5    Connell, S.6
  • 10
    • 33947134377 scopus 로고    scopus 로고
    • Autophagy-dependent viral recognition by plasmacytoid dendritic cells
    • DOI 10.1126/science.1136880
    • H.K. Lee, J.M. Lund, B. Ramanathan, N. Mizushima, and A. Iwasaki Autophagy-dependent viral recognition by plasmacytoid dendritic cells Science 315 2007 1398 1401 (Pubitemid 46399546)
    • (2007) Science , vol.315 , Issue.5817 , pp. 1398-1401
    • Lee, H.K.1    Lund, J.M.2    Ramanathan, B.3    Mizushima, N.4    Iwasaki, A.5
  • 11
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: A caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • L. Franchi, T. Eigenbrod, R. Munoz-Planillo, and G. Nunez The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis Nat Immunol 10 2009 241 247
    • (2009) Nat Immunol , vol.10 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Munoz-Planillo, R.3    Nunez, G.4
  • 12
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • K. Nakahira, J.A. Haspel, V.A. Rathinam, S.J. Lee, T. Dolinay, and H.C. Lam Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome Nat Immunol 12 2011 222 230
    • (2011) Nat Immunol , vol.12 , pp. 222-230
    • Nakahira, K.1    Haspel, J.A.2    Rathinam, V.A.3    Lee, S.J.4    Dolinay, T.5    Lam, H.C.6
  • 13
    • 33847404337 scopus 로고    scopus 로고
    • Autophagy Gene-Dependent Clearance of Apoptotic Cells during Embryonic Development
    • DOI 10.1016/j.cell.2006.12.044, PII S009286740700178X
    • X. Qu, Z. Zou, Q. Sun, K. Luby-Phelps, P. Cheng, and R.N. Hogan Autophagy gene-dependent clearance of apoptotic cells during embryonic development Cell 128 2007 931 946 (Pubitemid 46341412)
    • (2007) Cell , vol.128 , Issue.5 , pp. 931-946
    • Qu, X.1    Zou, Z.2    Sun, Q.3    Luby-Phelps, K.4    Cheng, P.5    Hogan, R.N.6    Gilpin, C.7    Levine, B.8
  • 15
    • 84861526009 scopus 로고    scopus 로고
    • Deconvoluting the context-dependent role for autophagy in cancer
    • E. White Deconvoluting the context-dependent role for autophagy in cancer Nat Rev Cancer 12 2012 401 410
    • (2012) Nat Rev Cancer , vol.12 , pp. 401-410
    • White, E.1
  • 16
    • 65249187333 scopus 로고    scopus 로고
    • Enhancing immunity through autophagy
    • C. Munz Enhancing immunity through autophagy Annu Rev Immunol 27 2009 423 449
    • (2009) Annu Rev Immunol , vol.27 , pp. 423-449
    • Munz, C.1
  • 18
    • 65249108735 scopus 로고    scopus 로고
    • Autophagy genes in immunity
    • H.W. Virgin, and B. Levine Autophagy genes in immunity Nat Immunol 10 2009 461 470
    • (2009) Nat Immunol , vol.10 , pp. 461-470
    • Virgin, H.W.1    Levine, B.2
  • 19
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • N. Mizushima The role of the Atg1/ULK1 complex in autophagy regulation Curr Opin Cell Biol 22 2010 132 139
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 20
    • 84857058225 scopus 로고    scopus 로고
    • Control of autophagy as a therapy for neurodegenerative disease
    • H. Harris, and D.C. Rubinsztein Control of autophagy as a therapy for neurodegenerative disease Nat Rev Neurol 8 2012 108 117
    • (2012) Nat Rev Neurol , vol.8 , pp. 108-117
    • Harris, H.1    Rubinsztein, D.C.2
  • 21
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • N. Mizushima, T. Yoshimori, and B. Levine Methods in mammalian autophagy research Cell 140 2010 313 326
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 22
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • L. Yu, C.K. McPhee, L. Zheng, G.A. Mardones, Y. Rong, and J. Peng Termination of autophagy and reformation of lysosomes regulated by mTOR Nature 465 2010 942 946
    • (2010) Nature , vol.465 , pp. 942-946
    • Yu, L.1    McPhee, C.K.2    Zheng, L.3    Mardones, G.A.4    Rong, Y.5    Peng, J.6
  • 23
    • 33846224369 scopus 로고    scopus 로고
    • Antigen-Loading Compartments for Major Histocompatibility Complex Class II Molecules Continuously Receive Input from Autophagosomes
    • DOI 10.1016/j.immuni.2006.10.018, PII S1074761306005255
    • D. Schmid, M. Pypaert, and C. Munz Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes Immunity 26 2007 79 92 (Pubitemid 46109341)
    • (2007) Immunity , vol.26 , Issue.1 , pp. 79-92
    • Schmid, D.1    Pypaert, M.2    Munz, C.3
  • 24
    • 77956414236 scopus 로고    scopus 로고
    • The origin of the autophagosomal membrane
    • S.A. Tooze, and T. Yoshimori The origin of the autophagosomal membrane Nat Cell Biol 12 2010 831 835
    • (2010) Nat Cell Biol , vol.12 , pp. 831-835
    • Tooze, S.A.1    Yoshimori, T.2
  • 26
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • E.L. Axe, S.A. Walker, M. Manifava, P. Chandra, H.L. Roderick, and A. Habermann Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum J Cell Biol 182 2008 685 701
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6
  • 27
    • 77955895424 scopus 로고    scopus 로고
    • Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L
    • K. Matsunaga, E. Morita, T. Saitoh, S. Akira, N.T. Ktistakis, and T. Izumi Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L J Cell Biol 190 2010 511 521
    • (2010) J Cell Biol , vol.190 , pp. 511-521
    • Matsunaga, K.1    Morita, E.2    Saitoh, T.3    Akira, S.4    Ktistakis, N.T.5    Izumi, T.6
  • 29
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Y. Kabeya, N. Mizushima, T. Ueno, A. Yamamoto, T. Kirisako, and T. Noda LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing EMBO J 19 2000 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    Noda, T.6
  • 30
  • 31
    • 65649136884 scopus 로고    scopus 로고
    • The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy
    • K. Satoo, N.N. Noda, H. Kumeta, Y. Fujioka, N. Mizushima, and Y. Ohsumi The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy EMBO J 28 2009 1341 1350
    • (2009) EMBO J , vol.28 , pp. 1341-1350
    • Satoo, K.1    Noda, N.N.2    Kumeta, H.3    Fujioka, Y.4    Mizushima, N.5    Ohsumi, Y.6
  • 32
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • C. Behrends, M.E. Sowa, S.P. Gygi, and J.W. Harper Network organization of the human autophagy system Nature 466 2010 68 76
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 33
    • 77955637249 scopus 로고    scopus 로고
    • ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death
    • L. Radoshevich, L. Murrow, N. Chen, E. Fernandez, S. Roy, and C. Fung ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death Cell 142 2010 590 600
    • (2010) Cell , vol.142 , pp. 590-600
    • Radoshevich, L.1    Murrow, L.2    Chen, N.3    Fernandez, E.4    Roy, S.5    Fung, C.6
  • 34
    • 79959415069 scopus 로고    scopus 로고
    • Biogenesis and cargo selectivity of autophagosomes
    • H. Weidberg, E. Shvets, and Z. Elazar Biogenesis and cargo selectivity of autophagosomes Annu Rev Biochem 80 2011 125 156
    • (2011) Annu Rev Biochem , vol.80 , pp. 125-156
    • Weidberg, H.1    Shvets, E.2    Elazar, Z.3
  • 36
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • B. Ravikumar, K. Moreau, L. Jahreiss, C. Puri, and D.C. Rubinsztein Plasma membrane contributes to the formation of pre-autophagosomal structures Nat Cell Biol 12 2010 747 757
    • (2010) Nat Cell Biol , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 38
    • 77949448601 scopus 로고    scopus 로고
    • Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes
    • N. Furuta, N. Fujita, T. Noda, T. Yoshimori, and A. Amano Combinational soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins VAMP8 and Vti1b mediate fusion of antimicrobial and canonical autophagosomes with lysosomes Mol Biol Cell 21 2010 1001 1010
    • (2010) Mol Biol Cell , vol.21 , pp. 1001-1010
    • Furuta, N.1    Fujita, N.2    Noda, T.3    Yoshimori, T.4    Amano, A.5
  • 39
    • 0014148066 scopus 로고
    • Participation of lysosomes in cellular autophagy induced in rat liver by glucagon
    • R.L. Deter, P. Baudhuin, and C. De Duve Participation of lysosomes in cellular autophagy induced in rat liver by glucagon J Cell Biol 35 1967 C11 C16
    • (1967) J Cell Biol , vol.35
    • Deter, R.L.1    Baudhuin, P.2    De Duve, C.3
  • 40
    • 0031417385 scopus 로고    scopus 로고
    • Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome
    • DOI 10.1083/jcb.139.7.1687
    • M. Baba, M. Osumi, S.V. Scott, D.J. Klionsky, and Y. Ohsumi Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome J Cell Biol 139 1997 1687 1695 (Pubitemid 28079234)
    • (1997) Journal of Cell Biology , vol.139 , Issue.7 , pp. 1687-1695
    • Baba, M.1    Osumi, M.2    Scott, S.V.3    Klionsky, D.J.4    Ohsumi, Y.5
  • 42
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • DOI 10.1083/jcb.200507002
    • G. Bjorkoy, T. Lamark, A. Brech, H. Outzen, M. Perander, and A. Overvatn 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 (Pubitemid 41668720)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , 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
  • 44
    • 77953139736 scopus 로고    scopus 로고
    • Fighting disease by selective autophagy of aggregate-prone proteins
    • H. Knaevelsrud, and A. Simonsen Fighting disease by selective autophagy of aggregate-prone proteins FEBS Lett 584 2010 2635 2645
    • (2010) FEBS Lett , vol.584 , pp. 2635-2645
    • Knaevelsrud, H.1    Simonsen, A.2
  • 47
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • T.L. Thurston, G. Ryzhakov, S. Bloor, N. von Muhlinen, and F. Randow The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria Nat Immunol 10 2009 1215 1221
    • (2009) Nat Immunol , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 49
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • S. Bernales, K.L. McDonald, and P. Walter Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response PLoS Biol 4 2006 e423
    • (2006) PLoS Biol , vol.4 , pp. 423
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 50
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • DOI 10.1038/ncb1723, PII NCB1723
    • C. Kraft, A. Deplazes, M. Sohrmann, and M. Peter Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease Nat Cell Biol 10 2008 602 610 (Pubitemid 351627380)
    • (2008) Nature Cell Biology , vol.10 , Issue.5 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 51
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • T. Johansen, and T. Lamark Selective autophagy mediated by autophagic adapter proteins Autophagy 7 2011 279 296
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 52
    • 84886797274 scopus 로고    scopus 로고
    • Autophagy in infection, inflammation and immunity
    • V. Deretic, T. Saitoh, and S. Akira Autophagy in infection, inflammation and immunity Nat Rev Immunol 13 2013 722 737
    • (2013) Nat Rev Immunol , vol.13 , pp. 722-737
    • Deretic, V.1    Saitoh, T.2    Akira, S.3
  • 53
    • 70349443224 scopus 로고    scopus 로고
    • Transcriptional control of the inflammatory response
    • R. Medzhitov, and T. Horng Transcriptional control of the inflammatory response Nat Rev Immunol 9 2009 692 703
    • (2009) Nat Rev Immunol , vol.9 , pp. 692-703
    • Medzhitov, R.1    Horng, T.2
  • 54
    • 78649526394 scopus 로고    scopus 로고
    • Sterile inflammation: Sensing and reacting to damage
    • G.Y. Chen, and G. Nunez Sterile inflammation: sensing and reacting to damage Nat Rev Immunol 10 2010 826 837
    • (2010) Nat Rev Immunol , vol.10 , pp. 826-837
    • Chen, G.Y.1    Nunez, G.2
  • 55
    • 40049108218 scopus 로고    scopus 로고
    • COPs and POPs: Modulators of inflammasome activity
    • C. Stehlik, and A. Dorfleutner COPs and POPs: modulators of inflammasome activity J Immunol 179 2007 7993 7998
    • (2007) J Immunol , vol.179 , pp. 7993-7998
    • Stehlik, C.1    Dorfleutner, A.2
  • 56
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • B. Levine, N. Mizushima, and H.W. Virgin Autophagy in immunity and inflammation Nature 469 2011 323 335
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 57
    • 77953858790 scopus 로고    scopus 로고
    • TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy
    • C.S. Shi, and J.H. Kehrl TRAF6 and A20 regulate lysine 63-linked ubiquitination of Beclin-1 to control TLR4-induced autophagy Sci Signal 3 2010 ra42
    • (2010) Sci Signal , vol.3 , pp. 42
    • Shi, C.S.1    Kehrl, J.H.2
  • 58
    • 84870861513 scopus 로고    scopus 로고
    • Noncanonical autophagy is required for type i interferon secretion in response to DNA-immune complexes
    • J. Henault, J. Martinez, J.M. Riggs, J. Tian, P. Mehta, and L. Clarke Noncanonical autophagy is required for type I interferon secretion in response to DNA-immune complexes Immunity 37 2012 986 997
    • (2012) Immunity , vol.37 , pp. 986-997
    • Henault, J.1    Martinez, J.2    Riggs, J.M.3    Tian, J.4    Mehta, P.5    Clarke, L.6
  • 59
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • T. Saitoh, N. Fujita, M.H. Jang, S. Uematsu, B.G. Yang, and T. Satoh Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production Nature 456 2008 264 268
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3    Uematsu, S.4    Yang, B.G.5    Satoh, T.6
  • 60
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • K. Schroder, and J. Tschopp The inflammasomes Cell 140 2010 821 832
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 61
    • 70350575440 scopus 로고    scopus 로고
    • Modulation of intracellular ROS levels by TIGAR controls autophagy
    • K. Bensaad, E.C. Cheung, and K.H. Vousden Modulation of intracellular ROS levels by TIGAR controls autophagy EMBO J 28 2009 3015 3026
    • (2009) EMBO J , vol.28 , pp. 3015-3026
    • Bensaad, K.1    Cheung, E.C.2    Vousden, K.H.3
  • 62
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • R. Zhou, A.S. Yazdi, P. Menu, and J. Tschopp A role for mitochondria in NLRP3 inflammasome activation Nature 469 2011 221 225
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 63
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction
    • C.S. Shi, K. Shenderov, N.N. Huang, J. Kabat, M. Abu-Asab, and K.A. Fitzgerald Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction Nat Immunol 13 2012 255 263
    • (2012) Nat Immunol , vol.13 , pp. 255-263
    • Shi, C.S.1    Shenderov, K.2    Huang, N.N.3    Kabat, J.4    Abu-Asab, M.5    Fitzgerald, K.A.6
  • 64
    • 0028201732 scopus 로고
    • Tolerance, danger, and the extended family
    • P. Matzinger Tolerance, danger, and the extended family Annu Rev Immunol 12 1994 991 1045 (Pubitemid 24140436)
    • (1994) Annual Review of Immunology , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 67
    • 84877328234 scopus 로고    scopus 로고
    • DAMPs and autophagy: Cellular adaptation to injury and unscheduled cell death
    • Q. Zhang, R. Kang, H.J. Zeh III, M.T. Lotze, and D. Tang DAMPs and autophagy: cellular adaptation to injury and unscheduled cell death Autophagy 9 2013 451 458
    • (2013) Autophagy , vol.9 , pp. 451-458
    • Zhang, Q.1    Kang, R.2    Zeh III, H.J.3    Lotze, M.T.4    Tang, D.5
  • 68
    • 80052589806 scopus 로고    scopus 로고
    • High mobility group box 1 (HMGB1) activates an autophagic response to oxidative stress
    • D. Tang, R. Kang, K.M. Livesey, H.J. Zeh III, and M.T. Lotze High mobility group box 1 (HMGB1) activates an autophagic response to oxidative stress Antioxid Redox Signal 15 2011 2185 2195
    • (2011) Antioxid Redox Signal , vol.15 , pp. 2185-2195
    • Tang, D.1    Kang, R.2    Livesey, K.M.3    Zeh III, H.J.4    Lotze, M.T.5
  • 70
    • 79953685881 scopus 로고    scopus 로고
    • EGCG stimulates autophagy and reduces cytoplasmic HMGB1 levels in endotoxin-stimulated macrophages
    • W. Li, S. Zhu, J. Li, A. Assa, A. Jundoria, and J. Xu EGCG stimulates autophagy and reduces cytoplasmic HMGB1 levels in endotoxin-stimulated macrophages Biochem Pharmacol 81 2011 1152 1163
    • (2011) Biochem Pharmacol , vol.81 , pp. 1152-1163
    • Li, W.1    Zhu, S.2    Li, J.3    Assa, A.4    Jundoria, A.5    Xu, J.6
  • 71
    • 83755181759 scopus 로고    scopus 로고
    • Autophagy-dependent anticancer immune responses induced by chemotherapeutic agents in mice
    • M. Michaud, I. Martins, A.Q. Sukkurwala, S. Adjemian, Y. Ma, and P. Pellegatti Autophagy-dependent anticancer immune responses induced by chemotherapeutic agents in mice Science 334 2011 1573 1577
    • (2011) Science , vol.334 , pp. 1573-1577
    • Michaud, M.1    Martins, I.2    Sukkurwala, A.Q.3    Adjemian, S.4    Ma, Y.5    Pellegatti, P.6
  • 72
    • 84865299726 scopus 로고    scopus 로고
    • PAMPs and DAMPs: Signal 0s that spur autophagy and immunity
    • D. Tang, R. Kang, C.B. Coyne, H.J. Zeh, and M.T. Lotze PAMPs and DAMPs: signal 0s that spur autophagy and immunity Immunol Rev 249 2012 158 175
    • (2012) Immunol Rev , vol.249 , pp. 158-175
    • Tang, D.1    Kang, R.2    Coyne, C.B.3    Zeh, H.J.4    Lotze, M.T.5
  • 73
    • 48449094878 scopus 로고    scopus 로고
    • ATP-induced autophagy is associated with rapid killing of intracellular mycobacteria within human monocytes/macrophages
    • D. Biswas, O.S. Qureshi, W.Y. Lee, J.E. Croudace, M. Mura, and D.A. Lammas ATP-induced autophagy is associated with rapid killing of intracellular mycobacteria within human monocytes/macrophages BMC Immunol 9 2008 35
    • (2008) BMC Immunol , vol.9 , pp. 35
    • Biswas, D.1    Qureshi, O.S.2    Lee, W.Y.3    Croudace, J.E.4    Mura, M.5    Lammas, D.A.6
  • 74
    • 61449162046 scopus 로고    scopus 로고
    • The activation of P2X7 receptor impairs lysosomal functions and stimulates the release of autophagolysosomes in microglial cells
    • T. Takenouchi, M. Nakai, Y. Iwamaru, S. Sugama, M. Tsukimoto, and M. Fujita The activation of P2X7 receptor impairs lysosomal functions and stimulates the release of autophagolysosomes in microglial cells J Immunol 182 2009 2051 2062
    • (2009) J Immunol , vol.182 , pp. 2051-2062
    • Takenouchi, T.1    Nakai, M.2    Iwamaru, Y.3    Sugama, S.4    Tsukimoto, M.5    Fujita, M.6
  • 76
    • 84855406005 scopus 로고    scopus 로고
    • HMGB1 promotes drug resistance in osteosarcoma
    • J. Huang, J. Ni, K. Liu, Y. Yu, M. Xie, and R. Kang HMGB1 promotes drug resistance in osteosarcoma Cancer Res 72 2012 230 238
    • (2012) Cancer Res , vol.72 , pp. 230-238
    • Huang, J.1    Ni, J.2    Liu, K.3    Yu, Y.4    Xie, M.5    Kang, R.6
  • 77
    • 73849151394 scopus 로고    scopus 로고
    • NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation
    • R. Cooney, J. Baker, O. Brain, B. Danis, T. Pichulik, and P. Allan NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation Nat Med 16 2010 90 97
    • (2010) Nat Med , vol.16 , pp. 90-97
    • Cooney, R.1    Baker, J.2    Brain, O.3    Danis, B.4    Pichulik, T.5    Allan, P.6
  • 78
    • 78649489009 scopus 로고    scopus 로고
    • Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci
    • A. Franke, D.P. McGovern, J.C. Barrett, K. Wang, G.L. Radford-Smith, and T. Ahmad Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci Nat Genet 42 2010 1118 1125
    • (2010) Nat Genet , vol.42 , pp. 1118-1125
    • Franke, A.1    McGovern, D.P.2    Barrett, J.C.3    Wang, K.4    Radford-Smith, G.L.5    Ahmad, T.6
  • 79
    • 48349136889 scopus 로고    scopus 로고
    • Genome-wide association defines more than 30 distinct susceptibility loci for Crohn's disease
    • J.C. Barrett, S. Hansoul, D.L. Nicolae, J.H. Cho, R.H. Duerr, and J.D. Rioux Genome-wide association defines more than 30 distinct susceptibility loci for Crohn's disease Nat Genet 40 2008 955 962
    • (2008) Nat Genet , vol.40 , pp. 955-962
    • Barrett, J.C.1    Hansoul, S.2    Nicolae, D.L.3    Cho, J.H.4    Duerr, R.H.5    Rioux, J.D.6
  • 80
    • 54549089752 scopus 로고    scopus 로고
    • The immunity-related GTPase Irgm1 promotes the expansion of activated CD4 + T cell populations by preventing interferon-gamma-induced cell death
    • C.G. Feng, L. Zheng, D. Jankovic, A. Bafica, J.L. Cannons, and W.T. Watford The immunity-related GTPase Irgm1 promotes the expansion of activated CD4 + T cell populations by preventing interferon-gamma-induced cell death Nat Immunol 9 2008 1279 1287
    • (2008) Nat Immunol , vol.9 , pp. 1279-1287
    • Feng, C.G.1    Zheng, L.2    Jankovic, D.3    Bafica, A.4    Cannons, J.L.5    Watford, W.T.6
  • 81
    • 73849121209 scopus 로고    scopus 로고
    • Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry
    • L.H. Travassos, L.A. Carneiro, M. Ramjeet, S. Hussey, Y.G. Kim, and J.G. Magalhaes Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry Nat Immunol 11 2010 55 62
    • (2010) Nat Immunol , vol.11 , pp. 55-62
    • Travassos, L.H.1    Carneiro, L.A.2    Ramjeet, M.3    Hussey, S.4    Kim, Y.G.5    Magalhaes, J.G.6
  • 82
    • 77953785765 scopus 로고    scopus 로고
    • NOD2-mediated autophagy and Crohn disease
    • O. Brain, P. Allan, and A. Simmons NOD2-mediated autophagy and Crohn disease Autophagy 6 2010 412 414
    • (2010) Autophagy , vol.6 , pp. 412-414
    • Brain, O.1    Allan, P.2    Simmons, A.3
  • 83
    • 77953904042 scopus 로고    scopus 로고
    • Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine
    • K. Cadwell, K.K. Patel, N.S. Maloney, T.C. Liu, A.C. Ng, and C.E. Storer Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine Cell 141 2010 1135 1145
    • (2010) Cell , vol.141 , pp. 1135-1145
    • Cadwell, K.1    Patel, K.K.2    Maloney, N.S.3    Liu, T.C.4    Ng, A.C.5    Storer, C.E.6
  • 84
    • 84875892111 scopus 로고    scopus 로고
    • Autophagy as a stress-response and quality-control mechanism: Implications for cell injury and human disease
    • L. Murrow, and J. Debnath Autophagy as a stress-response and quality-control mechanism: implications for cell injury and human disease Annu Rev Pathol 8 2013 105 137
    • (2013) Annu Rev Pathol , vol.8 , pp. 105-137
    • Murrow, L.1    Debnath, J.2
  • 85
    • 34447629523 scopus 로고    scopus 로고
    • Innate and Adaptive Immunity through Autophagy
    • DOI 10.1016/j.immuni.2007.07.004, PII S1074761307003408
    • D. Schmid, and C. Munz Innate and adaptive immunity through autophagy Immunity 27 2007 11 21 (Pubitemid 47089030)
    • (2007) Immunity , vol.27 , Issue.1 , pp. 11-21
    • Schmid, D.1    Munz, C.2
  • 86
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • D.C. Rubinsztein, P. Codogno, and B. Levine Autophagy modulation as a potential therapeutic target for diverse diseases Nat Rev Drug Discov 11 2012 709 730
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 87
    • 77954590749 scopus 로고    scopus 로고
    • Specific behavior of intracellular Streptococcus pyogenes that has undergone autophagic degradation is associated with bacterial streptolysin O and host small G proteins Rab5 and Rab7
    • A. Sakurai, F. Maruyama, J. Funao, T. Nozawa, C. Aikawa, and N. Okahashi Specific behavior of intracellular Streptococcus pyogenes that has undergone autophagic degradation is associated with bacterial streptolysin O and host small G proteins Rab5 and Rab7 J Biol Chem 285 2010 22666 22675
    • (2010) J Biol Chem , vol.285 , pp. 22666-22675
    • Sakurai, A.1    Maruyama, F.2    Funao, J.3    Nozawa, T.4    Aikawa, C.5    Okahashi, N.6
  • 88
    • 73549102459 scopus 로고    scopus 로고
    • An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7
    • H. Yamaguchi, I. Nakagawa, A. Yamamoto, A. Amano, T. Noda, and T. Yoshimori An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7 PLoS Pathog 5 2009 e1000670
    • (2009) PLoS Pathog , vol.5 , pp. 1000670
    • Yamaguchi, H.1    Nakagawa, I.2    Yamamoto, A.3    Amano, A.4    Noda, T.5    Yoshimori, T.6
  • 89
    • 84864009466 scopus 로고    scopus 로고
    • The small GTPases Rab9A and Rab23 function at distinct steps in autophagy during Group A Streptococcus infection
    • T. Nozawa, C. Aikawa, A. Goda, F. Maruyama, S. Hamada, and I. Nakagawa The small GTPases Rab9A and Rab23 function at distinct steps in autophagy during Group A Streptococcus infection Cell Microbiol 14 2012 1149 1165
    • (2012) Cell Microbiol , vol.14 , pp. 1149-1165
    • Nozawa, T.1    Aikawa, C.2    Goda, A.3    Maruyama, F.4    Hamada, S.5    Nakagawa, I.6
  • 91
    • 77953496542 scopus 로고    scopus 로고
    • NDP52, a novel autophagy receptor for ubiquitin-decorated cytosolic bacteria
    • N. von Muhlinen, T. Thurston, G. Ryzhakov, S. Bloor, and F. Randow NDP52, a novel autophagy receptor for ubiquitin-decorated cytosolic bacteria Autophagy 6 2010 288 289
    • (2010) Autophagy , vol.6 , pp. 288-289
    • Von Muhlinen, N.1    Thurston, T.2    Ryzhakov, G.3    Bloor, S.4    Randow, F.5
  • 92
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • V. Kirkin, T. Lamark, Y.S. Sou, G. Bjorkoy, J.L. Nunn, and J.A. Bruun A role for NBR1 in autophagosomal degradation of ubiquitinated substrates Mol Cell 33 2009 505 516
    • (2009) Mol Cell , vol.33 , pp. 505-516
    • Kirkin, V.1    Lamark, T.2    Sou, Y.S.3    Bjorkoy, G.4    Nunn, J.L.5    Bruun, J.A.6
  • 93
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • P. Wild, H. Farhan, D.G. McEwan, S. Wagner, V.V. Rogov, and N.R. Brady Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth Science 333 2011 228 233
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1    Farhan, H.2    McEwan, D.G.3    Wagner, S.4    Rogov, V.V.5    Brady, N.R.6
  • 94
  • 95
    • 68349143052 scopus 로고    scopus 로고
    • Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy
    • N. Dupont, S. Lacas-Gervais, J. Bertout, I. Paz, B. Freche, and G.T. Van Nhieu Shigella phagocytic vacuolar membrane remnants participate in the cellular response to pathogen invasion and are regulated by autophagy Cell Host Microbe 6 2009 137 149
    • (2009) Cell Host Microbe , vol.6 , pp. 137-149
    • Dupont, N.1    Lacas-Gervais, S.2    Bertout, J.3    Paz, I.4    Freche, B.5    Van Nhieu, G.T.6
  • 96
    • 77956310643 scopus 로고    scopus 로고
    • A diacylglycerol-dependent signaling pathway contributes to regulation of antibacterial autophagy
    • S. Shahnazari, W.L. Yen, C.L. Birmingham, J. Shiu, A. Namolovan, and Y.T. Zheng A diacylglycerol-dependent signaling pathway contributes to regulation of antibacterial autophagy Cell Host Microbe 8 2010 137 146
    • (2010) Cell Host Microbe , vol.8 , pp. 137-146
    • Shahnazari, S.1    Yen, W.L.2    Birmingham, C.L.3    Shiu, J.4    Namolovan, A.5    Zheng, Y.T.6
  • 97
    • 77649112187 scopus 로고    scopus 로고
    • Genome-wide analysis of the host intracellular network that regulates survival of Mycobacterium tuberculosis
    • D. Kumar, L. Nath, M.A. Kamal, A. Varshney, A. Jain, and S. Singh Genome-wide analysis of the host intracellular network that regulates survival of Mycobacterium tuberculosis Cell 140 2010 731 743
    • (2010) Cell , vol.140 , pp. 731-743
    • Kumar, D.1    Nath, L.2    Kamal, M.A.3    Varshney, A.4    Jain, A.5    Singh, S.6
  • 98
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • DOI 10.1016/j.cell.2004.11.038, PII S0092867404011067
    • M.G. Gutierrez, S.S. Master, S.B. Singh, G.A. Taylor, M.I. Colombo, and V. Deretic Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages Cell 119 2004 753 766 (Pubitemid 40017683)
    • (2004) Cell , vol.119 , Issue.6 , 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
  • 99
    • 80051810145 scopus 로고    scopus 로고
    • Critical role for NLRP3 in necrotic death triggered by Mycobacterium tuberculosis
    • K.W. Wong, and W.R. Jacobs Jr. Critical role for NLRP3 in necrotic death triggered by Mycobacterium tuberculosis Cell Microbiol 13 2011 1371 1384
    • (2011) Cell Microbiol , vol.13 , pp. 1371-1384
    • Wong, K.W.1    Jacobs, Jr.W.R.2
  • 100
    • 84865220380 scopus 로고    scopus 로고
    • Extracellular M. Tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway
    • R.O. Watson, P.S. Manzanillo, and J.S. Cox Extracellular M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway Cell 150 2012 803 815
    • (2012) Cell , vol.150 , pp. 803-815
    • Watson, R.O.1    Manzanillo, P.S.2    Cox, J.S.3
  • 101
    • 77949997805 scopus 로고    scopus 로고
    • Delivery of cytosolic components by autophagic adaptor protein p62 endows autophagosomes with unique antimicrobial properties
    • M. Ponpuak, A.S. Davis, E.A. Roberts, M.A. Delgado, C. Dinkins, and Z. Zhao Delivery of cytosolic components by autophagic adaptor protein p62 endows autophagosomes with unique antimicrobial properties Immunity 32 2010 329 341
    • (2010) Immunity , vol.32 , pp. 329-341
    • Ponpuak, M.1    Davis, A.S.2    Roberts, E.A.3    Delgado, M.A.4    Dinkins, C.5    Zhao, Z.6
  • 103
    • 79955777383 scopus 로고    scopus 로고
    • A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection
    • B.H. Kim, A.R. Shenoy, P. Kumar, R. Das, S. Tiwari, and J.D. MacMicking A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection Science 332 2011 717 721
    • (2011) Science , vol.332 , pp. 717-721
    • Kim, B.H.1    Shenoy, A.R.2    Kumar, P.3    Das, R.4    Tiwari, S.5    Macmicking, J.D.6
  • 104
    • 55249109400 scopus 로고    scopus 로고
    • Autophagosome-independent essential function for the autophagy protein Atg5 in cellular immunity to intracellular pathogens
    • Z. Zhao, B. Fux, M. Goodwin, I.R. Dunay, D. Strong, and B.C. Miller Autophagosome-independent essential function for the autophagy protein Atg5 in cellular immunity to intracellular pathogens Cell Host Microbe 4 2008 458 469
    • (2008) Cell Host Microbe , vol.4 , pp. 458-469
    • Zhao, Z.1    Fux, B.2    Goodwin, M.3    Dunay, I.R.4    Strong, D.5    Miller, B.C.6
  • 105
    • 79959228478 scopus 로고    scopus 로고
    • The IFN-gamma-inducible GTPase, Irga6, protects mice against Toxoplasma gondii but not against Plasmodium berghei and some other intracellular pathogens
    • O. Liesenfeld, I. Parvanova, J. Zerrahn, S.J. Han, F. Heinrich, and M. Munoz The IFN-gamma-inducible GTPase, Irga6, protects mice against Toxoplasma gondii but not against Plasmodium berghei and some other intracellular pathogens PLoS One 6 2011 e20568
    • (2011) PLoS One , vol.6 , pp. 20568
    • Liesenfeld, O.1    Parvanova, I.2    Zerrahn, J.3    Han, S.J.4    Heinrich, F.5    Munoz, M.6
  • 106
    • 79251517741 scopus 로고    scopus 로고
    • The CD40-autophagy pathway is needed for host protection despite IFN-Gamma-dependent immunity and CD40 induces autophagy via control of P21 levels
    • J.A. Portillo, G. Okenka, E. Reed, A. Subauste, J. Van Grol, and K. Gentil The CD40-autophagy pathway is needed for host protection despite IFN-Gamma-dependent immunity and CD40 induces autophagy via control of P21 levels PLoS One 5 2010 e14472
    • (2010) PLoS One , vol.5 , pp. 14472
    • Portillo, J.A.1    Okenka, G.2    Reed, E.3    Subauste, A.4    Van Grol, J.5    Gentil, K.6
  • 108
    • 41449098293 scopus 로고    scopus 로고
    • Downregulation of autophagy by herpesvirus Bcl-2 homologs
    • C. Liang, X. E, and J.U. Jung Downregulation of autophagy by herpesvirus Bcl-2 homologs Autophagy 4 2008 268 272 (Pubitemid 351458084)
    • (2008) Autophagy , vol.4 , Issue.3 , pp. 268-272
    • Liang, C.1    Xiaofei, E.2    Jung, J.U.3
  • 109
    • 79960112123 scopus 로고    scopus 로고
    • ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2alpha (eIF2alpha) and protein phosphatase 1
    • Y. Li, C. Zhang, X. Chen, J. Yu, Y. Wang, and Y. Yang ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2alpha (eIF2alpha) and protein phosphatase 1 J Biol Chem 286 2011 24785 24792
    • (2011) J Biol Chem , vol.286 , pp. 24785-24792
    • Li, Y.1    Zhang, C.2    Chen, X.3    Yu, J.4    Wang, Y.5    Yang, Y.6
  • 110
    • 73649092138 scopus 로고    scopus 로고
    • Viral Bcl-2-mediated evasion of autophagy aids chronic infection of gammaherpesvirus 68
    • X. E, S. Hwang, S. Oh, J.S. Lee, J.H. Jeong, and Y. Gwack Viral Bcl-2-mediated evasion of autophagy aids chronic infection of gammaherpesvirus 68 PLoS Pathog 5 2009 e1000609
    • (2009) PLoS Pathog , vol.5 , pp. 1000609
    • Hwang, S.1    Oh, S.2    Lee, J.S.3    Jeong, J.H.4    Gwack, Y.5
  • 111
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • G.B. Kyei, C. Dinkins, A.S. Davis, E. Roberts, S.B. Singh, and C. Dong Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages J Cell Biol 186 2009 255 268
    • (2009) J Cell Biol , vol.186 , pp. 255-268
    • Kyei, G.B.1    Dinkins, C.2    Davis, A.S.3    Roberts, E.4    Singh, S.B.5    Dong, C.6
  • 113
    • 77953272740 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 inhibition of immunoamphisomes in dendritic cells impairs early innate and adaptive immune responses
    • F.P. Blanchet, A. Moris, D.S. Nikolic, M. Lehmann, S. Cardinaud, and R. Stalder Human immunodeficiency virus-1 inhibition of immunoamphisomes in dendritic cells impairs early innate and adaptive immune responses Immunity 32 2010 654 669
    • (2010) Immunity , vol.32 , pp. 654-669
    • Blanchet, F.P.1    Moris, A.2    Nikolic, D.S.3    Lehmann, M.4    Cardinaud, S.5    Stalder, R.6
  • 114
    • 67651065500 scopus 로고    scopus 로고
    • HIV-1-infected dendritic cells show 2 phases of gene expression changes, with lysosomal enzyme activity decreased during the second phase
    • A.N. Harman, M. Kraus, C.R. Bye, K. Byth, S.G. Turville, and O. Tang HIV-1-infected dendritic cells show 2 phases of gene expression changes, with lysosomal enzyme activity decreased during the second phase Blood 114 2009 85 94
    • (2009) Blood , vol.114 , pp. 85-94
    • Harman, A.N.1    Kraus, M.2    Bye, C.R.3    Byth, K.4    Turville, S.G.5    Tang, O.6
  • 115
    • 41349095737 scopus 로고    scopus 로고
    • Human immunodeficiency virus type-1 infection inhibits autophagy
    • DOI 10.1097/QAD.0b013e3282f4a836, PII 0000203020080330000003
    • D. Zhou, and S.A. Spector Human immunodeficiency virus type-1 infection inhibits autophagy AIDS 22 2008 695 699 (Pubitemid 351450637)
    • (2008) AIDS , vol.22 , Issue.6 , pp. 695-699
    • Zhou, D.1    Spector, S.A.2
  • 117
    • 33845628839 scopus 로고    scopus 로고
    • What is immune privilege (not)?
    • DOI 10.1016/j.it.2006.11.004, PII S1471490606003267
    • I. Galea, I. Bechmann, and V.H. Perry What is immune privilege (not)? Trends Immunol 28 2007 12 18 (Pubitemid 44960159)
    • (2007) Trends in Immunology , vol.28 , Issue.1 , pp. 12-18
    • Galea, I.1    Bechmann, I.2    Perry, V.H.3
  • 119
    • 66449130960 scopus 로고    scopus 로고
    • Regulation of innate immune responses in the brain
    • S. Rivest Regulation of innate immune responses in the brain Nat Rev Immunol 9 2009 429 439
    • (2009) Nat Rev Immunol , vol.9 , pp. 429-439
    • Rivest, S.1
  • 120
    • 43949114888 scopus 로고    scopus 로고
    • Can the immune system be harnessed to repair the CNS?
    • DOI 10.1038/nrn2398, PII NRN2398
    • P.G. Popovich, and E.E. Longbrake Can the immune system be harnessed to repair the CNS? Nat Rev Neurosci 9 2008 481 493 (Pubitemid 351704948)
    • (2008) Nature Reviews Neuroscience , vol.9 , Issue.6 , pp. 481-493
    • Popovich, P.G.1    Longbrake, E.E.2
  • 121
    • 0036847816 scopus 로고    scopus 로고
    • Microglia as neuroprotective, immunocompetent cells of the CNS
    • DOI 10.1002/glia.10154
    • W.J. Streit Microglia as neuroprotective, immunocompetent cells of the CNS Glia 40 2002 133 139 (Pubitemid 35337371)
    • (2002) GLIA , vol.40 , Issue.2 , pp. 133-139
    • Streit, W.J.1
  • 122
    • 77950363010 scopus 로고    scopus 로고
    • Mechanisms underlying inflammation in neurodegeneration
    • C.K. Glass, K. Saijo, B. Winner, M.C. Marchetto, and F.H. Gage Mechanisms underlying inflammation in neurodegeneration Cell 140 2010 918 934
    • (2010) Cell , vol.140 , pp. 918-934
    • Glass, C.K.1    Saijo, K.2    Winner, B.3    Marchetto, M.C.4    Gage, F.H.5
  • 123
    • 0036849018 scopus 로고    scopus 로고
    • Microglia as a source and target of cytokines
    • U.K. Hanisch Microglia as a source and target of cytokines Glia 40 2002 140 155
    • (2002) Glia , vol.40 , pp. 140-155
    • Hanisch, U.K.1
  • 124
    • 84857700077 scopus 로고    scopus 로고
    • Cell death pathways and autophagy in the central nervous system and its involvement in neurodegeneration, immunity and central nervous system infection: To die or not to die - That is the question
    • A. Rosello, G. Warnes, and U.C. Meier Cell death pathways and autophagy in the central nervous system and its involvement in neurodegeneration, immunity and central nervous system infection: to die or not to die - that is the question Clin Exp Immunol 168 2012 52 57
    • (2012) Clin Exp Immunol , vol.168 , pp. 52-57
    • Rosello, A.1    Warnes, G.2    Meier, U.C.3
  • 125
    • 56449083411 scopus 로고    scopus 로고
    • Autophagy in neurodegeneration and development
    • A.R. Winslow, and D.C. Rubinsztein Autophagy in neurodegeneration and development Biochim Biophys Acta 1782 2008 723 729
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 723-729
    • Winslow, A.R.1    Rubinsztein, D.C.2
  • 126
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: A continuum from development to late age
    • R.A. Nixon, D.S. Yang, and J.H. Lee Neurodegenerative lysosomal disorders: a continuum from development to late age Autophagy 4 2008 590 599
    • (2008) Autophagy , vol.4 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 129
    • 84872609730 scopus 로고    scopus 로고
    • MTOR kinase, a key player in the regulation of glial functions: Relevance for the therapy of multiple sclerosis
    • C. Dello Russo, L. Lisi, D.L. Feinstein, and P. Navarra mTOR kinase, a key player in the regulation of glial functions: relevance for the therapy of multiple sclerosis Glia 61 2013 301 311
    • (2013) Glia , vol.61 , pp. 301-311
    • Dello Russo, C.1    Lisi, L.2    Feinstein, D.L.3    Navarra, P.4
  • 130
    • 70349807619 scopus 로고    scopus 로고
    • Immune activation in brain aging and neurodegeneration: Too much or too little?
    • K.M. Lucin, and T. Wyss-Coray Immune activation in brain aging and neurodegeneration: too much or too little? Neuron 64 2009 110 122
    • (2009) Neuron , vol.64 , pp. 110-122
    • Lucin, K.M.1    Wyss-Coray, T.2
  • 131
    • 84884185631 scopus 로고    scopus 로고
    • Microglial beclin 1 regulates retromer trafficking and phagocytosis and is impaired in Alzheimer's disease
    • K.M. Lucin, C.E. O'Brien, G. Bieri, E. Czirr, K.I. Mosher, and R.J. Abbey Microglial beclin 1 regulates retromer trafficking and phagocytosis and is impaired in Alzheimer's disease Neuron 79 2013 873 886
    • (2013) Neuron , vol.79 , pp. 873-886
    • Lucin, K.M.1    O'Brien, C.E.2    Bieri, G.3    Czirr, E.4    Mosher, K.I.5    Abbey, R.J.6
  • 132
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • E. Wong, and A.M. Cuervo Autophagy gone awry in neurodegenerative diseases Nat Neurosci 13 2010 805 811
    • (2010) Nat Neurosci , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 133
    • 79960635284 scopus 로고    scopus 로고
    • Fighting neurodegeneration with rapamycin: Mechanistic insights
    • J. Bove, M. Martinez-Vicente, and M. Vila Fighting neurodegeneration with rapamycin: mechanistic insights Nat Rev Neurosci 12 2011 437 452
    • (2011) Nat Rev Neurosci , vol.12 , pp. 437-452
    • Bove, J.1    Martinez-Vicente, M.2    Vila, M.3
  • 136
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations
    • J.H. Lee, W.H. Yu, A. Kumar, S. Lee, P.S. Mohan, and C.M. Peterhoff Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations Cell 141 2010 1146 1158
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1    Yu, W.H.2    Kumar, A.3    Lee, S.4    Mohan, P.S.5    Peterhoff, C.M.6
  • 138
    • 0032413192 scopus 로고    scopus 로고
    • Alzheimer's disease: Genetic studies and transgenic models
    • DOI 10.1146/annurev.genet.32.1.461
    • D.L. Price, R.E. Tanzi, D.R. Borchelt, and S.S. Sisodia Alzheimer's disease: genetic studies and transgenic models Annu Rev Genet 32 1998 461 493 (Pubitemid 29045321)
    • (1998) Annual Review of Genetics , vol.32 , pp. 461-493
    • Price, D.L.1    Tanzi, R.E.2    Borchelt, D.R.3    Sisodia, S.S.4
  • 139
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
    • R. Sherrington, E.I. Rogaev, Y. Liang, E.A. Rogaeva, G. Levesque, and M. Ikeda Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease Nature 375 1995 754 760
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3    Rogaeva, E.A.4    Levesque, G.5    Ikeda, M.6
  • 141
    • 77957335213 scopus 로고    scopus 로고
    • Amyloid-beta1-42 induces reactive oxygen species-mediated autophagic cell death in U87 and SH-SY5Y cells
    • H. Wang, J. Ma, Y. Tan, Z. Wang, C. Sheng, and S. Chen Amyloid-beta1-42 induces reactive oxygen species-mediated autophagic cell death in U87 and SH-SY5Y cells J Alzheimers Dis 21 2010 597 610
    • (2010) J Alzheimers Dis , vol.21 , pp. 597-610
    • Wang, H.1    Ma, J.2    Tan, Y.3    Wang, Z.4    Sheng, C.5    Chen, S.6
  • 142
    • 79960308079 scopus 로고    scopus 로고
    • Autophagy deregulation in neurodegenerative diseases - Recent advances and future perspectives
    • Z.H. Cheung, and N.Y. Ip Autophagy deregulation in neurodegenerative diseases - recent advances and future perspectives J Neurochem 118 2011 317 325
    • (2011) J Neurochem , vol.118 , pp. 317-325
    • Cheung, Z.H.1    Ip, N.Y.2
  • 143
    • 63149090431 scopus 로고    scopus 로고
    • Parkinson's disease: From monogenic forms to genetic susceptibility factors
    • S. Lesage, and A. Brice Parkinson's disease: from monogenic forms to genetic susceptibility factors Hum Mol Genet 18 2009 R48 R59
    • (2009) Hum Mol Genet , vol.18
    • Lesage, S.1    Brice, A.2
  • 145
    • 79953202481 scopus 로고    scopus 로고
    • Mutant A53T alpha-synuclein induces neuronal death by increasing mitochondrial autophagy
    • V. Choubey, D. Safiulina, A. Vaarmann, M. Cagalinec, P. Wareski, and M. Kuum Mutant A53T alpha-synuclein induces neuronal death by increasing mitochondrial autophagy J Biol Chem 286 2011 10814 10824
    • (2011) J Biol Chem , vol.286 , pp. 10814-10824
    • Choubey, V.1    Safiulina, D.2    Vaarmann, A.3    Cagalinec, M.4    Wareski, P.5    Kuum, M.6
  • 150
    • 33745751085 scopus 로고    scopus 로고
    • Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
    • C. Liang, P. Feng, B. Ku, I. Dotan, D. Canaani, and B.H. Oh Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG Nat Cell Biol 8 2006 688 699
    • (2006) Nat Cell Biol , vol.8 , pp. 688-699
    • Liang, C.1    Feng, P.2    Ku, B.3    Dotan, I.4    Canaani, D.5    Oh, B.H.6
  • 151
    • 34547132328 scopus 로고    scopus 로고
    • Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3
    • DOI 10.1074/jbc.M701194200
    • G. Marino, N. Salvador-Montoliu, A. Fueyo, E. Knecht, N. Mizushima, and C. Lopez-Otin Tissue-specific autophagy alterations and increased tumorigenesis in mice deficient in Atg4C/autophagin-3 J Biol Chem 282 2007 18573 18583 (Pubitemid 47100226)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18573-18583
    • Marino, G.1    Salvador-Montoliu, N.2    Fueyo, A.3    Knecht, E.4    Mizushima, N.5    Lopez-Otin, C.6
  • 152
    • 80053634368 scopus 로고    scopus 로고
    • The dynamic nature of autophagy in cancer
    • A.C. Kimmelman The dynamic nature of autophagy in cancer Genes Dev 25 2011 1999 2010
    • (2011) Genes Dev , vol.25 , pp. 1999-2010
    • Kimmelman, A.C.1
  • 153
    • 33745713171 scopus 로고    scopus 로고
    • Autophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis
    • K. Degenhardt, R. Mathew, B. Beaudoin, K. Bray, D. Anderson, and G. Chen Autophagy promotes tumor cell survival and restricts necrosis, inflammation, and tumorigenesis Cancer Cell 10 2006 51 64
    • (2006) Cancer Cell , vol.10 , pp. 51-64
    • Degenhardt, K.1    Mathew, R.2    Beaudoin, B.3    Bray, K.4    Anderson, D.5    Chen, G.6
  • 154
    • 33644513730 scopus 로고    scopus 로고
    • Beyond PTEN mutations: The PI3K pathway as an integrator of multiple inputs during tumorigenesis
    • DOI 10.1038/nrc1819, PII N1819
    • M. Cully, H. You, A.J. Levine, and T.W. Mak Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis Nat Rev Cancer 6 2006 184 192 (Pubitemid 43292562)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.3 , pp. 184-192
    • Cully, M.1    You, H.2    Levine, A.J.3    Mak, T.W.4
  • 156
    • 84869147050 scopus 로고    scopus 로고
    • Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation
    • R.C. Wang, Y. Wei, Z. An, Z. Zou, G. Xiao, and G. Bhagat Akt-mediated regulation of autophagy and tumorigenesis through Beclin 1 phosphorylation Science 338 2012 956 959
    • (2012) Science , vol.338 , pp. 956-959
    • Wang, R.C.1    Wei, Y.2    An, Z.3    Zou, Z.4    Xiao, G.5    Bhagat, G.6
  • 161
  • 163
    • 84859562694 scopus 로고    scopus 로고
    • Targeting autophagy addiction in cancer
    • J.D. Mancias, and A.C. Kimmelman Targeting autophagy addiction in cancer Oncotarget 2 2011 1302 1306
    • (2011) Oncotarget , vol.2 , pp. 1302-1306
    • Mancias, J.D.1    Kimmelman, A.C.2
  • 164
    • 80052697287 scopus 로고    scopus 로고
    • The role of autophagy in cancer: Therapeutic implications
    • Z.J. Yang, C.E. Chee, S. Huang, and F.A. Sinicrope The role of autophagy in cancer: therapeutic implications Mol Cancer Ther 10 2011 1533 1541
    • (2011) Mol Cancer Ther , vol.10 , pp. 1533-1541
    • Yang, Z.J.1    Chee, C.E.2    Huang, S.3    Sinicrope, F.A.4
  • 166
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • DOI 10.1182/blood-2005-08-3531
    • E.A. Obeng, L.M. Carlson, D.M. Gutman, W.J. Harrington Jr., K.P. Lee, and L.H. Boise Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells Blood 107 2006 4907 4916 (Pubitemid 43882644)
    • (2006) Blood , vol.107 , Issue.12 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, L.H.6
  • 167
    • 75149175502 scopus 로고    scopus 로고
    • Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells
    • K. Zhu, K. Dunner Jr., and D.J. McConkey Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells Oncogene 29 2010 451 462
    • (2010) Oncogene , vol.29 , pp. 451-462
    • Zhu, K.1    Dunner, Jr.K.2    McConkey, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.