메뉴 건너뛰기




Volumn 24, Issue 1, 2014, Pages 24-41

The machinery of macroautophagy

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; MAMMALIA;

EID: 84891747382     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2013.168     Document Type: Review
Times cited : (1676)

References (179)
  • 1
    • 80655124407 scopus 로고    scopus 로고
    • A comprehensive glossary of autophagy-related molecules and processes (2nd edition)
    • Klionsky DJ, Baehrecke EH, Brumell JH, et al. A comprehensive glossary of autophagy-related molecules and processes (2nd edition). Autophagy 2011; 7:1273-1294.
    • (2011) Autophagy , vol.7 , pp. 1273-1294
    • Klionsky, D.J.1    Baehrecke, E.H.2    Brumell, J.H.3
  • 2
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: Unanswered questions
    • Klionsky DJ. The molecular machinery of autophagy: unanswered questions. J Cell Sci 2005; 118:7-18.
    • (2005) J Cell Sci , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 3
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • Yorimitsu T, Klionsky DJ. Autophagy: molecular machinery for self-eating. Cell Death Differ 2005; 12:1542-1552.
    • (2005) Cell Death Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 4
    • 0029414780 scopus 로고
    • Analysis of the membrane structures involved in autophagy in yeast by freeze-replica method
    • Baba M, Osumi M, Ohsumi Y. Analysis of the membrane structures involved in autophagy in yeast by freeze-replica method. Cell Struct Funct 1995; 20:465-471.
    • (1995) Cell Struct Funct , vol.20 , pp. 465-471
    • Baba, M.1    Osumi, M.2    Ohsumi, Y.3
  • 5
    • 34347344990 scopus 로고    scopus 로고
    • Ambra1 regulates autophagy and development of the nervous system
    • Fimia GM, Stoykova A, Romagnoli A, et al. Ambra1 regulates autophagy and development of the nervous system. Nature 2007; 447:1121-1125.
    • (2007) Nature , vol.447 , pp. 1121-1125
    • Fimia, G.M.1    Stoykova, A.2    Romagnoli, A.3
  • 6
    • 0025340880 scopus 로고
    • Studies on the mechanisms of autophagy: Maturation of the autophagic vacuole
    • Dunn WA Jr. Studies on the mechanisms of autophagy: maturation of the autophagic vacuole. J Cell Biol 1990; 110:1935-1945.
    • (1990) J Cell Biol , vol.110 , pp. 1935-1945
    • Dunn Jr., W.A.1
  • 7
    • 34248581861 scopus 로고    scopus 로고
    • Atg9 trafficking in autophagy-related pathways
    • He C, Klionsky DJ. Atg9 trafficking in autophagy-related pathways. Autophagy 2007; 3:271-274.
    • (2007) Autophagy , vol.3 , pp. 271-274
    • He, C.1    Klionsky, D.J.2
  • 8
    • 0035503594 scopus 로고    scopus 로고
    • The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
    • Suzuki K, Kirisako T, Kamada Y, et al. The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO J 2001; 20:5971-5981.
    • (2001) EMBO J , vol.20 , pp. 5971-5981
    • Suzuki, K.1    Kirisako, T.2    Kamada, Y.3
  • 9
    • 0037016752 scopus 로고    scopus 로고
    • Convergence of multiple autophagy and cytoplasm to vacuole targeting components to a perivacuolar membrane compartment prior to de novo vesicle formation
    • Kim J, Huang WP, Stromhaug PE, Klionsky DJ. Convergence of multiple autophagy and cytoplasm to vacuole targeting components to a perivacuolar membrane compartment prior to de novo vesicle formation. J Biol Chem 2002; 277:763-773.
    • (2002) J Biol Chem , vol.277 , pp. 763-773
    • Kim, J.1    Huang, W.P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 11
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • de Duve C, Pressman BC, Gianetto R, Wattiaux R, Appelmans F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J 1955; 60:604-617.
    • (1955) Biochem J , vol.60 , pp. 604-617
    • De Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 12
    • 0000730374 scopus 로고
    • Cytoplasmic components in hepatic cell lysosomes
    • Ashford TP, Porter KR. Cytoplasmic components in hepatic cell lysosomes. J Cell Biol 1962; 12:198-202.
    • (1962) J Cell Biol , vol.12 , pp. 198-202
    • Ashford, T.P.1    Porter, K.R.2
  • 13
    • 0000189281 scopus 로고
    • Cellular differentiation in the kidneys of newborn mice studied with the electron microscope
    • Clark SL Jr. Cellular differentiation in the kidneys of newborn mice studied with the electron microscope. J Biophys Biochem Cytol 1957; 3:349-362.
    • (1957) J Biophys Biochem Cytol , vol.3 , pp. 349-362
    • Clark Jr., S.L.1
  • 15
    • 1642559773 scopus 로고
    • The proximal tubule cell in experimental hydronephrosis
    • Novikoff AB. The proximal tubule cell in experimental hydronephrosis. J Biophys Biochem Cytol 1959; 6:136-138.
    • (1959) J Biophys Biochem Cytol , vol.6 , pp. 136-138
    • Novikoff, A.B.1
  • 16
    • 0014148066 scopus 로고
    • Participation of lysosomes in cellular autophagy induced in rat liver by glucagon
    • Deter RL, Baudhuin P, de Duve C. Participation of lysosomes in cellular autophagy induced in rat liver by glucagon. J Cell Biol 1967; 35:C11-C16.
    • (1967) J Cell Biol , vol.35
    • Deter, R.L.1    Baudhuin, P.2    De Duve, C.3
  • 17
    • 0005677775 scopus 로고
    • 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • Seglen PO, Gordon PB. 3-Methyladenine: specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes. Proc Natl Acad Sci USA 1982; 79:1889-1892.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 18
    • 0015592534 scopus 로고
    • A morphometric study of the removal of phenobarbital-induced membranes from hepatocytes after cessation of threatment
    • Bolender RP, Weibel ER. A morphometric study of the removal of phenobarbital-induced membranes from hepatocytes after cessation of threatment. J Cell Biol 1973; 56:746-761.
    • (1973) J Cell Biol , vol.56 , pp. 746-761
    • Bolender, R.P.1    Weibel, E.R.2
  • 19
    • 0017748853 scopus 로고
    • Ultrastructural study of the normal degeneration of the intersegmental muscles of Anthereae polyphemus and Manduca sexta (Insecta, Lepidoptera) with particular reference of cellular autophagy
    • Beaulaton J, Lockshin RA. Ultrastructural study of the normal degeneration of the intersegmental muscles of Anthereae polyphemus and Manduca sexta (Insecta, Lepidoptera) with particular reference of cellular autophagy. J Morphol 1977; 154:39-57.
    • (1977) J Morphol , vol.154 , pp. 39-57
    • Beaulaton, J.1    Lockshin, R.A.2
  • 20
    • 0020772844 scopus 로고
    • Degradation and turnover of peroxisomes in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes
    • Veenhuis M, Douma A, Harder W, Osumi M. Degradation and turnover of peroxisomes in the yeast Hansenula polymorpha induced by selective inactivation of peroxisomal enzymes. Arch Microbiol 1983; 134:193-203.
    • (1983) Arch Microbiol , vol.134 , pp. 193-203
    • Veenhuis, M.1    Douma, A.2    Harder, W.3    Osumi, M.4
  • 21
    • 0027936092 scopus 로고
    • Isolation of autophagocytosis mutants of Saccharomyces cerevisiae
    • Thumm M, Egner R, Koch B, et al. Isolation of autophagocytosis mutants of Saccharomyces cerevisiae. FEBS Lett 1994; 349:275-280.
    • (1994) FEBS Lett , vol.349 , pp. 275-280
    • Thumm, M.1    Egner, R.2    Koch, B.3
  • 22
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada M, Ohsumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 1993; 333:169-174.
    • (1993) FEBS Lett , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 23
    • 10744225487 scopus 로고    scopus 로고
    • A unified nomenclature for yeast autophagy-related genes
    • Klionsky DJ, Cregg JM, Dunn WA Jr, et al. A unified nomenclature for yeast autophagy-related genes. Dev Cell 2003; 5:539-545.
    • (2003) Dev Cell , vol.5 , pp. 539-545
    • Klionsky, D.J.1    Cregg, J.M.2    Dunn Jr., W.A.3
  • 24
    • 0030983504 scopus 로고    scopus 로고
    • Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae
    • Matsuura A, Tsukada M, Wada Y, Ohsumi Y. Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae. Gene 1997; 192:245-250.
    • (1997) Gene , vol.192 , pp. 245-250
    • Matsuura, A.1    Tsukada, M.2    Wada, Y.3    Ohsumi, Y.4
  • 25
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • Liang XH, Jackson S, Seaman M, et al. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 1999; 402:672-676.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3
  • 26
    • 0021322401 scopus 로고
    • Glycogen autophagosomes in polymorphonuclear leukocytes induced by rickettsiae
    • Rikihisa Y. Glycogen autophagosomes in polymorphonuclear leukocytes induced by rickettsiae. Anat Rec 1984; 208:319-327.
    • (1984) Anat Rec , vol.208 , pp. 319-327
    • Rikihisa, Y.1
  • 27
    • 0001488499 scopus 로고    scopus 로고
    • Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein
    • Liang XH, Kleeman LK, Jiang HH, et al. Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein. J Virol 1998; 72:8586-8596.
    • (1998) J Virol , vol.72 , pp. 8586-8596
    • Liang, X.H.1    Kleeman, L.K.2    Jiang, H.H.3
  • 28
    • 33947715151 scopus 로고    scopus 로고
    • HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein
    • Orvedahl A, Alexander D, Tallczy Z, et al. HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein. Cell Host Microbe 2007; 1:23-35.
    • (2007) Cell Host Microbe , vol.1 , pp. 23-35
    • Orvedahl, A.1    Alexander, D.2    Tallczy, Z.3
  • 29
    • 33644609471 scopus 로고    scopus 로고
    • PKR-dependent autophagic degradation of herpes simplex virus type 1
    • Tallczy Z, Virgin HW IV, Levine B. PKR-dependent autophagic degradation of herpes simplex virus type 1. Autophagy 2006; 2:24-29.
    • (2006) Autophagy , vol.2 , pp. 24-29
    • Tallczy, Z.1    Virgin, H.W.I.V.2    Levine, B.3
  • 30
    • 26444515364 scopus 로고    scopus 로고
    • Autophagy and its possible roles in nervous system diseases, damage and repair
    • Rubinsztein DC, DiFiglia M, Heintz N, et al. Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy 2005; 1:11-22.
    • (2005) Autophagy , vol.1 , pp. 11-22
    • Rubinsztein, D.C.1    Difiglia, M.2    Heintz, N.3
  • 31
    • 19944434059 scopus 로고    scopus 로고
    • Inhibition of macroautophagy triggers apoptosis
    • Boya P, Gonzalez-Polo RA, Casares N, et al. Inhibition of macroautophagy triggers apoptosis. Mol Cell Biol 2005; 25:1025-1040.
    • (2005) Mol Cell Biol , vol.25 , pp. 1025-1040
    • Boya, P.1    Gonzalez-Polo, R.A.2    Casares, N.3
  • 32
    • 2642553881 scopus 로고    scopus 로고
    • Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8
    • Yu L, Alva A, Su H, et al. Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science 2004; 304:1500-1502.
    • (2004) Science , vol.304 , pp. 1500-1502
    • Yu, L.1    Alva, A.2    Su, H.3
  • 33
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • Shintani T, Klionsky DJ. Autophagy in health and disease: a double-edged sword. Science 2004; 306:990-995.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 34
    • 1642329712 scopus 로고    scopus 로고
    • Determination of four sequential stages during microautophagy in vitro
    • Kunz JB, Schwarz H, Mayer A. Determination of four sequential stages during microautophagy in vitro. J Biol Chem 2004; 279:9987-9996.
    • (2004) J Biol Chem , vol.279 , pp. 9987-9996
    • Kunz, J.B.1    Schwarz, H.2    Mayer, A.3
  • 35
    • 67649363854 scopus 로고    scopus 로고
    • Glutathione participates in the regulation of mitophagy in yeast
    • Deffieu M, Bhatia-Kissova I, Salin B, et al. Glutathione participates in the regulation of mitophagy in yeast. J Biol Chem 2009; 284:14828-14837.
    • (2009) J Biol Chem , vol.284 , pp. 14828-14837
    • Deffieu, M.1    Bhatia-Kissova, I.2    Salin, B.3
  • 36
    • 33644586142 scopus 로고    scopus 로고
    • Pexophagy: The selective autophagy of peroxisomes
    • Dunn WA Jr, Cregg JM, Kiel JAKW, et al. Pexophagy: the selective autophagy of peroxisomes. Autophagy 2005; 1:75-83.
    • (2005) Autophagy , vol.1 , pp. 75-83
    • Dunn Jr., W.A.1    Cregg, J.M.2    Jakw, K.3
  • 37
    • 0034050457 scopus 로고    scopus 로고
    • The itinerary of a vesicle component, Aut7p/Cvt5p, terminates in the yeast vacuole via the autophagy/Cvt pathways
    • Huang W-P, Scott SV, Kim J, Klionsky DJ. The itinerary of a vesicle component, Aut7p/Cvt5p, terminates in the yeast vacuole via the autophagy/Cvt pathways. J Biol Chem 2000; 275:5845-5851.
    • (2000) J Biol Chem , vol.275 , pp. 5845-5851
    • Huang, W.-P.1    Scott, S.V.2    Kim, J.3    Klionsky, D.J.4
  • 38
    • 0032701984 scopus 로고    scopus 로고
    • Formation process of autophagosome is traced with Apg8/Aut7p in yeast
    • Kirisako T, Baba M, Ishihara N, et al. Formation process of autophagosome is traced with Apg8/Aut7p in yeast. J Cell Biol 1999; 147:435-446.
    • (1999) J Cell Biol , vol.147 , pp. 435-446
    • Kirisako, T.1    Baba, M.2    Ishihara, N.3
  • 39
    • 33846514235 scopus 로고    scopus 로고
    • Hierarchy of Atg proteins in pre-autophagosomal structure organization
    • Suzuki K, Kubota Y, Sekito T, Ohsumi Y. Hierarchy of Atg proteins in pre-autophagosomal structure organization. Genes Cells 2007; 12:209-218.
    • (2007) Genes Cells , vol.12 , pp. 209-218
    • Suzuki, K.1    Kubota, Y.2    Sekito, T.3    Ohsumi, Y.4
  • 40
    • 48249129649 scopus 로고    scopus 로고
    • Dual role of Atg1 in regulation of autophagy-specific PAS assembly in Saccharomyces cerevisiae
    • Cheong H, Klionsky DJ. Dual role of Atg1 in regulation of autophagy-specific PAS assembly in Saccharomyces cerevisiae. Autophagy 2008; 4:724-726.
    • (2008) Autophagy , vol.4 , pp. 724-726
    • Cheong, H.1    Klionsky, D.J.2
  • 41
    • 84881091197 scopus 로고    scopus 로고
    • Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation
    • Mao K, Chew LH, Inoue-Aono Y, et al. Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation. Proc Natl Acad Sci USA 2013; 110:E2875-E2884.
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Mao, K.1    Chew, L.H.2    Inoue-Aono, Y.3
  • 42
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima N, Yamamoto A, Hatano M, et al. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol 2001; 152:657-668.
    • (2001) J Cell Biol , vol.152 , pp. 657-668
    • Mizushima, N.1    Yamamoto, A.2    Hatano, M.3
  • 43
    • 24044513985 scopus 로고    scopus 로고
    • Endothelial nitricoxide synthase antisense (NOS3AS) gene encodes an autophagy- related protein (APG9-like2) highly expressed in trophoblast
    • Yamada T, Carson AR, Caniggia I, et al. Endothelial nitricoxide synthase antisense (NOS3AS) gene encodes an autophagy- related protein (APG9-like2) highly expressed in trophoblast. J Biol Chem 2005; 280:18283-18290.
    • (2005) J Biol Chem , vol.280 , pp. 18283-18290
    • Yamada, T.1    Carson, A.R.2    Caniggia, I.3
  • 44
    • 33750366092 scopus 로고    scopus 로고
    • Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
    • Young ARJ, Chan EYW, Hu XW, et al. Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci 2006; 119:3888-3900.
    • (2006) J Cell Sci , vol.119 , pp. 3888-3900
    • Arj, Y.1    Eyw, C.2    Hu, X.W.3
  • 45
    • 0036569331 scopus 로고    scopus 로고
    • Yeast autophagosomes: De novo formation of a membrane structure
    • Noda T, Suzuki K, Ohsumi Y. Yeast autophagosomes: de novo formation of a membrane structure. Trends Cell Biol 2002; 12:231-235.
    • (2002) Trends Cell Biol , vol.12 , pp. 231-235
    • Noda, T.1    Suzuki, K.2    Ohsumi, Y.3
  • 46
    • 35948971795 scopus 로고    scopus 로고
    • Sequestration revisited: Integrating traditional electron microscopy, de novo assembly and new results
    • Kovcs AL, Palfia Z, Rez G, Vellai T, Kovcs J. Sequestration revisited: integrating traditional electron microscopy, de novo assembly and new results. Autophagy 2007; 3:655-662.
    • (2007) Autophagy , vol.3 , pp. 655-662
    • Kovcs, A.L.1    Palfia, Z.2    Rez, G.3    Vellai, T.4    Kovcs, J.5
  • 47
    • 0024299286 scopus 로고
    • Prelysosomal convergence of autophagic and endocytic pathways
    • Gordon PB, Seglen PO. Prelysosomal convergence of autophagic and endocytic pathways. Biochem Biophys Res Commun 1988; 151:40-47.
    • (1988) Biochem Biophys Res Commun , vol.151 , pp. 40-47
    • Gordon, P.B.1    Seglen, P.O.2
  • 48
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy
    • Geng J, Klionsky DJ. The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. EMBO Rep 2008; 9:859-864.
    • (2008) EMBO Rep , vol.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 49
    • 77957198526 scopus 로고    scopus 로고
    • An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
    • Mari M, Griffith J, Rieter E, et al. An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis. J Cell Biol 2010; 190:1005-1022.
    • (2010) J Cell Biol , vol.190 , pp. 1005-1022
    • Mari, M.1    Griffith, J.2    Rieter, E.3
  • 50
    • 77954197767 scopus 로고    scopus 로고
    • Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae
    • van der Vaart A, Griffith J, Reggiori F. Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae. Mol Biol Cell 2010; 21:2270-2284.
    • (2010) Mol Biol Cell , vol.21 , pp. 2270-2284
    • Van Der Vaart, A.1    Griffith, J.2    Reggiori, F.3
  • 51
    • 75749135725 scopus 로고    scopus 로고
    • The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy
    • Yen W-L, Shintani T, Nair U, et al. The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy. J Cell Biol 2010; 188:101-114.
    • (2010) J Cell Biol , vol.188 , pp. 101-114
    • Yen, W.-L.1    Shintani, T.2    Nair, U.3
  • 52
    • 84866527297 scopus 로고    scopus 로고
    • KCS1 deletion in Saccharomyces cerevisiae leads to a defect in translocation of autophagic proteins and reduces autophagosome formation
    • Taylor R Jr, Chen PH, Chou CC, Patel J, Jin SV. KCS1 deletion in Saccharomyces cerevisiae leads to a defect in translocation of autophagic proteins and reduces autophagosome formation. Autophagy 2012; 8:1300-1311.
    • (2012) Autophagy , vol.8 , pp. 1300-1311
    • Taylor Jr., R.1    Chen, P.H.2    Chou, C.C.3    Patel, J.4    Jin, S.V.5
  • 53
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe EL, Walker SA, Manifava M, et al. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 2008; 182:685-701.
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3
  • 54
    • 0028800171 scopus 로고
    • Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
    • Harding TM, Morano KA, Scott SV, Klionsky DJ. Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J Cell Biol 1995; 131:591-602.
    • (1995) J Cell Biol , vol.131 , pp. 591-602
    • Harding, T.M.1    Morano, K.A.2    Scott, S.V.3    Klionsky, D.J.4
  • 55
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • Mizushima N. Autophagy: process and function. Genes Dev 2007; 21:2861-2873.
    • (2007) Genes Dev , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 57
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • Xie Z, Klionsky DJ. Autophagosome formation: core machinery and adaptations. Nat Cell Biol 2007; 9:1102-1109.
    • (2007) Nat Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 58
    • 21844470747 scopus 로고    scopus 로고
    • Atg17 regulates the magnitude of the autophagic response
    • Cheong H, Yorimitsu T, Reggiori F, et al. Atg17 regulates the magnitude of the autophagic response. Mol Biol Cell 2005; 16:3438-3453.
    • (2005) Mol Biol Cell , vol.16 , pp. 3438-3453
    • Cheong, H.1    Yorimitsu, T.2    Reggiori, F.3
  • 59
    • 18244394277 scopus 로고    scopus 로고
    • Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy
    • Kabeya Y, Kamada Y, Baba M, et al. Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy. Mol Biol Cell 2005; 16:2544-2553.
    • (2005) Mol Biol Cell , vol.16 , pp. 2544-2553
    • Kabeya, Y.1    Kamada, Y.2    Baba, M.3
  • 60
    • 33947378818 scopus 로고    scopus 로고
    • Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae
    • Kabeya Y, Kawamata T, Suzuki K, Ohsumi Y. Cis1/Atg31 is required for autophagosome formation in Saccharomyces cerevisiae. Biochem Biophys Res Commun 2007; 356:405-410.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 405-410
    • Kabeya, Y.1    Kawamata, T.2    Suzuki, K.3    Ohsumi, Y.4
  • 61
    • 0034683568 scopus 로고    scopus 로고
    • Tor-mediated induction of autophagy via an Apg1 protein kinase complex
    • Kamada Y, Funakoshi T, Shintani T, et al. Tor-mediated induction of autophagy via an Apg1 protein kinase complex. J Cell Biol 2000; 150:1507-1513.
    • (2000) J Cell Biol , vol.150 , pp. 1507-1513
    • Kamada, Y.1    Funakoshi, T.2    Shintani, T.3
  • 62
    • 27844461994 scopus 로고    scopus 로고
    • Characterization of a novel autophagy-specific gene, ATG29
    • Kawamata T, Kamada Y, Suzuki K, et al. Characterization of a novel autophagy-specific gene, ATG29. Biochem Biophys Res Commun 2005; 338:1884-1889.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 1884-1889
    • Kawamata, T.1    Kamada, Y.2    Suzuki, K.3
  • 63
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure
    • Reggiori F, Tucker KA, Stromhaug PE, Klionsky DJ. The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure. Dev Cell 2004; 6:79-90.
    • (2004) Dev Cell , vol.6 , pp. 79-90
    • Reggiori, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 64
    • 0037329201 scopus 로고    scopus 로고
    • Chemical genetic analysis of Apg1 reveals a non-kinase role in the induction of autophagy
    • Abeliovich H, Zhang C, Dunn WA Jr, Shokat KM, Klionsky DJ. Chemical genetic analysis of Apg1 reveals a non-kinase role in the induction of autophagy. Mol Biol Cell 2003; 14:477-490.
    • (2003) Mol Biol Cell , vol.14 , pp. 477-490
    • Abeliovich, H.1    Zhang, C.2    Dunn Jr., W.A.3    Shokat, K.M.4    Klionsky, D.J.5
  • 65
    • 29644435706 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of specific and nonspecific autophagy pathways in yeast
    • Nair U, Klionsky DJ. Molecular mechanisms and regulation of specific and nonspecific autophagy pathways in yeast. J Biol Chem 2005; 280:41785-41788.
    • (2005) J Biol Chem , vol.280 , pp. 41785-41788
    • Nair, U.1    Klionsky, D.J.2
  • 66
    • 70350128436 scopus 로고    scopus 로고
    • The Tor and PKA signaling pathways independently target the Atg1/Atg13 protein kinase complex to control autophagy
    • Stephan JS, Yeh YY, Ramachandran V, Deminoff SJ, Herman PK. The Tor and PKA signaling pathways independently target the Atg1/Atg13 protein kinase complex to control autophagy. Proc Natl Acad Sci USA 2009; 106:17049-17054.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17049-17054
    • Stephan, J.S.1    Yeh, Y.Y.2    Ramachandran, V.3    Deminoff, S.J.4    Herman, P.K.5
  • 67
    • 78349245944 scopus 로고    scopus 로고
    • Autophosphorylation within the Atg1 activation loop is required for both kinase activity and the induction of autophagy in Saccharomyces cerevisiae
    • Yeh YY, Wrasman K, Herman PK. Autophosphorylation within the Atg1 activation loop is required for both kinase activity and the induction of autophagy in Saccharomyces cerevisiae. Genetics 2010; 185:871-882.
    • (2010) Genetics , vol.185 , pp. 871-882
    • Yeh, Y.Y.1    Wrasman, K.2    Herman, P.K.3
  • 68
    • 78649299852 scopus 로고    scopus 로고
    • Activation of Atg1 kinase in autophagy by regulated phosphorylation
    • Kijanska M, Dohnal I, Reiter W, et al. Activation of Atg1 kinase in autophagy by regulated phosphorylation. Autophagy 2010; 6:1168-1178.
    • (2010) Autophagy , vol.6 , pp. 1168-1178
    • Kijanska, M.1    Dohnal, I.2    Reiter, W.3
  • 69
    • 75749090429 scopus 로고    scopus 로고
    • Tor directly controls the Atg1 kinase complex to regulate autophagy
    • Kamada Y, Yoshino K, Kondo C, et al. Tor directly controls the Atg1 kinase complex to regulate autophagy. Mol Cell Biol 2010; 30:1049-1058.
    • (2010) Mol Cell Biol , vol.30 , pp. 1049-1058
    • Kamada, Y.1    Yoshino, K.2    Kondo, C.3
  • 70
    • 25444459688 scopus 로고    scopus 로고
    • An evolutionary proteomics approach identifies substrates of the cAMP-dependent protein kinase
    • Budovskaya YV, Stephan JS, Deminoff SJ, Herman PK. An evolutionary proteomics approach identifies substrates of the cAMP-dependent protein kinase. Proc Natl Acad Sci USA 2005; 102:13933-13938.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13933-13938
    • Budovskaya, Y.V.1    Stephan, J.S.2    Deminoff, S.J.3    Herman, P.K.4
  • 71
    • 0034682772 scopus 로고    scopus 로고
    • Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting
    • Scott SV, Nice DC, III, Nau JJ, et al. Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting. J Biol Chem 2000; 275:25840-25849.
    • (2000) J Biol Chem , vol.275 , pp. 25840-25849
    • Scott, S.V.1    Nice III, D.C.2    Nau, J.J.3
  • 72
    • 84866426794 scopus 로고    scopus 로고
    • Binding of the Atg1/ ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy
    • Kraft C, Kijanska M, Kalie E, et al. Binding of the Atg1/ ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy. EMBO J 2012; 31:3691-3703.
    • (2012) EMBO J , vol.31 , pp. 3691-3703
    • Kraft, C.1    Kijanska, M.2    Kalie, E.3
  • 73
    • 67650234502 scopus 로고    scopus 로고
    • A multiple ATG gene knockout strain for yeast two-hybrid analysis
    • Cao Y, Nair U, Yasumura-Yorimitsu K, Klionsky DJ. A multiple ATG gene knockout strain for yeast two-hybrid analysis. Autophagy 2009; 5:699-705.
    • (2009) Autophagy , vol.5 , pp. 699-705
    • Cao, Y.1    Nair, U.2    Yasumura-Yorimitsu, K.3    Klionsky, D.J.4
  • 74
    • 70349739560 scopus 로고    scopus 로고
    • Characterization of the Atg17-Atg29-Atg31 complex specifically required for starvation-induced autophagy in Saccharomyces cerevisiae
    • Kabeya Y, Noda NN, Fujioka Y, et al. Characterization of the Atg17-Atg29-Atg31 complex specifically required for starvation-induced autophagy in Saccharomyces cerevisiae. Biochem Biophys Res Commun 2009; 389:612-615.
    • (2009) Biochem Biophys Res Commun , vol.389 , pp. 612-615
    • Kabeya, Y.1    Noda, N.N.2    Fujioka, Y.3
  • 75
    • 84871581862 scopus 로고    scopus 로고
    • Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis
    • Ragusa MJ, Stanley RE, Hurley JH. Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis. Cell 2012; 151:1501-1512.
    • (2012) Cell , vol.151 , pp. 1501-1512
    • Ragusa, M.J.1    Stanley, R.E.2    Hurley, J.H.3
  • 76
    • 65249119430 scopus 로고    scopus 로고
    • Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy
    • Hosokawa N, Hara T, Kaizuka T, et al. Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy. Mol Biol Cell 2009; 20:1981-1991.
    • (2009) Mol Biol Cell , vol.20 , pp. 1981-1991
    • Hosokawa, N.1    Hara, T.2    Kaizuka, T.3
  • 77
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • Mizushima N. The role of the Atg1/ULK1 complex in autophagy regulation. Curr Opin Cell Biol 2010; 22:132-139.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 78
    • 70349644856 scopus 로고    scopus 로고
    • Atg101, a novel mammalian autophagy protein interacting with Atg13
    • Hosokawa N, Sasaki T, Iemura S, et al. Atg101, a novel mammalian autophagy protein interacting with Atg13. Autophagy 2009; 5:973-979.
    • (2009) Autophagy , vol.5 , pp. 973-979
    • Hosokawa, N.1    Sasaki, T.2    Iemura, S.3
  • 79
    • 67549110195 scopus 로고    scopus 로고
    • A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy
    • Mercer CA, Kaliappan A, Dennis PB. A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy. Autophagy 2009; 5:649-662.
    • (2009) Autophagy , vol.5 , pp. 649-662
    • Mercer, C.A.1    Kaliappan, A.2    Dennis, P.B.3
  • 80
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
    • Hara T, Takamura A, Kishi C, et al. FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells. J Cell Biol 2008; 181:497-510.
    • (2008) J Cell Biol , vol.181 , pp. 497-510
    • Hara, T.1    Takamura, A.2    Kishi, C.3
  • 81
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • Jung CH, Jun CB, Ro SH, et al. ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell 2009; 20:1992-2003.
    • (2009) Mol Biol Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3
  • 82
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J, Kundu M, Viollet B, Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 2011; 13:132-141.
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 83
    • 77957728513 scopus 로고    scopus 로고
    • The dynamic interaction of AMBRA1 with the dynein motor complex regulates mammalian autophagy
    • Di Bartolomeo S, Corazzari M, Nazio F, et al. The dynamic interaction of AMBRA1 with the dynein motor complex regulates mammalian autophagy. J Cell Biol 2010; 191:155-168.
    • (2010) J Cell Biol , vol.191 , pp. 155-168
    • Di Bartolomeo, S.1    Corazzari, M.2    Nazio, F.3
  • 84
    • 84880331368 scopus 로고    scopus 로고
    • ULK1 induces autophagy by phosphorylating Beclin-1 and activating VPS34 lipid kinase
    • Russell RC, Tian Y, Yuan H, et al. ULK1 induces autophagy by phosphorylating Beclin-1 and activating VPS34 lipid kinase. Nat Cell Biol 2013; 15:741-750.
    • (2013) Nat Cell Biol , vol.15 , pp. 741-750
    • Russell, R.C.1    Tian, Y.2    Yuan, H.3
  • 85
    • 27644544004 scopus 로고    scopus 로고
    • Atg9 cycles between mitochondria and the pre-autophagosomal structure in yeasts
    • Reggiori F, Shintani T, Nair U, Klionsky DJ. Atg9 cycles between mitochondria and the pre-autophagosomal structure in yeasts. Autophagy 2005; 1:101-109.
    • (2005) Autophagy , vol.1 , pp. 101-109
    • Reggiori, F.1    Shintani, T.2    Nair, U.3    Klionsky, D.J.4
  • 86
    • 59449097721 scopus 로고    scopus 로고
    • Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy
    • He C, Baba M, Cao Y, Klionsky DJ. Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy. Mol Biol Cell 2008; 19:5506-5516.
    • (2008) Mol Biol Cell , vol.19 , pp. 5506-5516
    • He, C.1    Baba, M.2    Cao, Y.3    Klionsky, D.J.4
  • 87
    • 33845692364 scopus 로고    scopus 로고
    • Recruitment of Atg9 to the preautophagosomal structure by Atg11 is essential for selective autophagy in budding yeast
    • He C, Song H, Yorimitsu T, et al. Recruitment of Atg9 to the preautophagosomal structure by Atg11 is essential for selective autophagy in budding yeast. J Cell Biol 2006; 175:925-935.
    • (2006) J Cell Biol , vol.175 , pp. 925-935
    • He, C.1    Song, H.2    Yorimitsu, T.3
  • 88
    • 34548082024 scopus 로고    scopus 로고
    • A cycling protein complex required for selective autophagy
    • Legakis JE, Yen W-L, Klionsky DJ. A cycling protein complex required for selective autophagy. Autophagy 2007; 3:422-432.
    • (2007) Autophagy , vol.3 , pp. 422-432
    • Legakis, J.E.1    Yen, W.-L.2    Klionsky, D.J.3
  • 89
    • 33846807374 scopus 로고    scopus 로고
    • Atg27 is required for autophagy-dependent cycling of Atg9
    • Yen WL, Legakis JE, Nair U, Klionsky DJ. Atg27 is required for autophagy-dependent cycling of Atg9. Mol Biol Cell 2007; 18:581-593.
    • (2007) Mol Biol Cell , vol.18 , pp. 581-593
    • Yen, W.L.1    Legakis, J.E.2    Nair, U.3    Klionsky, D.J.4
  • 90
    • 84861158462 scopus 로고    scopus 로고
    • Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy
    • Orsi A, Razi M, Dooley HC, et al. Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy. Mol Biol Cell 2012; 23:1860-1873.
    • (2012) Mol Biol Cell , pp. 23
    • Orsi, A.1    Razi, M.2    Dooley, H.C.3
  • 91
    • 84884220705 scopus 로고    scopus 로고
    • Diverse autophagosome membrane sources coalesce in recycling endosomes
    • Puri C, Renna M, Bento CF, Moreau K, Rubinsztein DC. Diverse autophagosome membrane sources coalesce in recycling endosomes. Cell 2013; 154:1285-1299.
    • (2013) Cell , vol.154 , pp. 1285-1299
    • Puri, C.1    Renna, M.2    Bento, C.F.3    Moreau, K.4    Rubinsztein, D.C.5
  • 92
    • 33745086418 scopus 로고    scopus 로고
    • Assortment of phosphatidylinositol 3-kinase complexes-Atg14p directs association of complex i to the pre-autophagosomal structure in Saccharomyces cerevisiae
    • Obara K, Sekito T, Ohsumi Y. Assortment of phosphatidylinositol 3-kinase complexes-Atg14p directs association of complex I to the pre-autophagosomal structure in Saccharomyces cerevisiae. Mol Biol Cell 2006; 17:1527-1539.
    • (2006) Mol Biol Cell , vol.17 , pp. 1527-1539
    • Obara, K.1    Sekito, T.2    Ohsumi, Y.3
  • 93
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase y sorting in Saccharomyces cerevisiae
    • Kihara A, Noda T, Ishihara N, Ohsumi Y. Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J Cell Biol 2001; 152:519-530.
    • (2001) J Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 94
    • 84887543464 scopus 로고    scopus 로고
    • Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase complex integrity
    • Araki Y, Ku WC, Akioka M, et al. Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase complex integrity. J Cell Biol 2013; 203:299-313.
    • (2013) J Cell Biol , vol.203 , pp. 299-313
    • Araki, Y.1    Ku, W.C.2    Akioka, M.3
  • 95
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura E, Kishi C, Inoue K, Mizushima N. Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol Biol Cell 2008; 19:5360-5372.
    • (2008) Mol Biol Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 96
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang Z, Klionsky DJ. Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol 2010; 22:124-131.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 97
    • 84892569830 scopus 로고    scopus 로고
    • An overview of autophagy: Morphology, mechanism, and regulation
    • doi:10.1089/ars.2013.5371
    • Parzych KR, Klionsky DJ. An overview of autophagy: Morphology, mechanism, and regulation. Antioxid Redox Signal 2013 Aug 2. doi:10.1089/ars.2013.5371
    • Antioxid Redox Signal 2013 Aug 2
    • Parzych, K.R.1    Klionsky, D.J.2
  • 98
    • 47549092694 scopus 로고    scopus 로고
    • Atg8 controls phagophore expansion during autophagosome formation
    • Xie Z, Nair U, Klionsky DJ. Atg8 controls phagophore expansion during autophagosome formation. Mol Biol Cell 2008; 19:3290-3298.
    • (2008) Mol Biol Cell , vol.19 , pp. 3290-3298
    • Xie, Z.1    Nair, U.2    Klionsky, D.J.3
  • 99
    • 0036901104 scopus 로고    scopus 로고
    • Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway
    • Shintani T, Huang W-P, Stromhaug PE, Klionsky DJ. Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway. Dev Cell 2002; 3:825-837.
    • (2002) Dev Cell , vol.3 , pp. 825-837
    • Shintani, T.1    Huang, W.-P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 100
    • 0032896760 scopus 로고    scopus 로고
    • Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways
    • Kim J, Dalton VM, Eggerton KP, Scott SV, Klionsky DJ. Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways. Mol Biol Cell 1999; 10:1337-1351.
    • (1999) Mol Biol Cell , vol.10 , pp. 1337-1351
    • Kim, J.1    Dalton, V.M.2    Eggerton, K.P.3    Scott, S.V.4    Klionsky, D.J.5
  • 101
    • 0034676037 scopus 로고    scopus 로고
    • The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway
    • Kirisako T, Ichimura Y, Okada H, et al. The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway. J Cell Biol 2000; 151:263-276.
    • (2000) J Cell Biol , vol.151 , pp. 263-276
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3
  • 102
    • 0034707036 scopus 로고    scopus 로고
    • A ubiquitin-like system mediates protein lipidation
    • Ichimura Y, Kirisako T, Takao T, et al. A ubiquitin-like system mediates protein lipidation. Nature 2000; 408:488-492.
    • (2000) Nature , vol.408 , pp. 488-492
    • Ichimura, Y.1    Kirisako, T.2    Takao, T.3
  • 103
    • 0032563798 scopus 로고    scopus 로고
    • A protein conjugation system essential for autophagy
    • Mizushima N, Noda T, Yoshimori T, et al. A protein conjugation system essential for autophagy. Nature 1998; 395:395-398.
    • (1998) Nature , vol.395 , pp. 395-398
    • Mizushima, N.1    Noda, T.2    Yoshimori, T.3
  • 104
    • 0032898636 scopus 로고    scopus 로고
    • Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy
    • Tanida I, Mizushima N, Kiyooka M, et al. Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy. Mol Biol Cell 1999; 10:1367-1379.
    • (1999) Mol Biol Cell , vol.10 , pp. 1367-1379
    • Tanida, I.1    Mizushima, N.2    Kiyooka, M.3
  • 105
    • 0033214582 scopus 로고    scopus 로고
    • Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast
    • Shintani T, Mizushima N, Ogawa Y, et al. Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 1999; 18:5234-5241.
    • (1999) EMBO J , vol.18 , pp. 5234-5241
    • Shintani, T.1    Mizushima, N.2    Ogawa, Y.3
  • 106
    • 0032545292 scopus 로고    scopus 로고
    • A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy
    • Mizushima N, Sugita H, Yoshimori T, Ohsumi Y. A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy. J Biol Chem 1998; 273:33889-33892.
    • (1998) J Biol Chem , vol.273 , pp. 33889-33892
    • Mizushima, N.1    Sugita, H.2    Yoshimori, T.3    Ohsumi, Y.4
  • 107
    • 0035910423 scopus 로고    scopus 로고
    • The human homolog of Saccharomyces cerevisiae Apg7p is a protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3
    • Tanida I, Tanida-Miyake E, Ueno T, Kominami E. The human homolog of Saccharomyces cerevisiae Apg7p is a protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3. J Biol Chem 2001; 276:1701-1706.
    • (2001) J Biol Chem , vol.276 , pp. 1701-1706
    • Tanida, I.1    Tanida-Miyake, E.2    Ueno, T.3    Kominami, E.4
  • 108
    • 0037132504 scopus 로고    scopus 로고
    • Mouse Apg10 as an Apg12-conjugating enzyme: Analysis by the conjugation-mediated yeast two-hybrid method
    • Mizushima N, Yoshimori T, Ohsumi Y. Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method. FEBS Lett 2002; 532:450-454.
    • (2002) FEBS Lett , vol.532 , pp. 450-454
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 109
    • 0038325675 scopus 로고    scopus 로고
    • Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate
    • Mizushima N, Kuma A, Kobayashi Y, et al. Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate. J Cell Sci 2003; 116:1679-1688.
    • (2003) J Cell Sci , vol.116 , pp. 1679-1688
    • Mizushima, N.1    Kuma, A.2    Kobayashi, Y.3
  • 110
    • 77953122645 scopus 로고    scopus 로고
    • LC3 and GATE-16/ GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis
    • Weidberg H, Shvets E, Shpilka T, et al. LC3 and GATE-16/ GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J 2010; 29:1792-1802.
    • (2010) EMBO J , vol.29 , pp. 1792-1802
    • Weidberg, H.1    Shvets, E.2    Shpilka, T.3
  • 111
    • 79953190772 scopus 로고    scopus 로고
    • Kinetics comparisons of mammalian Atg4 homologues indicate selective preferences toward diverse Atg8 substrates
    • Li M, Hou Y, Wang J, et al. Kinetics comparisons of mammalian Atg4 homologues indicate selective preferences toward diverse Atg8 substrates. J Biol Chem 2011; 286:7327-7338.
    • (2011) J Biol Chem , vol.286 , pp. 7327-7338
    • Li, M.1    Hou, Y.2    Wang, J.3
  • 112
    • 3242888703 scopus 로고    scopus 로고
    • LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
    • Kabeya Y, Mizushima N, Yamamoto A, et al. LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation. J Cell Sci 2004; 117:2805-2812.
    • (2004) J Cell Sci , vol.117 , pp. 2805-2812
    • Kabeya, Y.1    Mizushima, N.2    Yamamoto, A.3
  • 113
    • 0034964443 scopus 로고    scopus 로고
    • Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway
    • Scott SV, Guan J, Hutchins MU, Kim J, Klionsky DJ. Cvt19 is a receptor for the cytoplasm-to-vacuole targeting pathway. Mol Cell 2001; 7:1131-1141.
    • (2001) Mol Cell , vol.7 , pp. 1131-1141
    • Scott, S.V.1    Guan, J.2    Hutchins, M.U.3    Kim, J.4    Klionsky, D.J.5
  • 114
    • 77956913181 scopus 로고    scopus 로고
    • Selective transport of ?-mannosidase by autophagic pathways: Structural basis for cargo recognition by Atg19 and Atg34
    • Watanabe Y, Noda NN, Kumeta H, et al. Selective transport of ?-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34. J Biol Chem 2010; 285:30026-30033.
    • (2010) J Biol Chem , vol.285 , pp. 30026-30033
    • Watanabe, Y.1    Noda, N.N.2    Kumeta, H.3
  • 115
    • 57749121573 scopus 로고    scopus 로고
    • Mitophagy in yeast occurs through a selective mechanism
    • Kanki T, Klionsky DJ. Mitophagy in yeast occurs through a selective mechanism. J Biol Chem 2008; 283:32386-32393.
    • (2008) J Biol Chem , vol.283 , pp. 32386-32393
    • Kanki, T.1    Klionsky, D.J.2
  • 116
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K, Kondo-Okamoto N, Ohsumi Y. Mitochondriaanchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev Cell 2009; 17:87-97.
    • (2009) Dev Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 117
    • 84863843241 scopus 로고    scopus 로고
    • Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
    • Motley AM, Nuttall JM, Hettema EH. Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae. EMBO J 2012; 31:2852-2868.
    • (2012) EMBO J , vol.31 , pp. 2852-2868
    • Motley, A.M.1    Nuttall, J.M.2    Hettema, E.H.3
  • 118
    • 84869472835 scopus 로고    scopus 로고
    • Receptor protein complexes are in control of autophagy
    • Mijaljica D, Nazarko TY, Brumell JH, et al. Receptor protein complexes are in control of autophagy. Autophagy 2012; 8:1701-1705.
    • (2012) Autophagy , vol.8 , pp. 1701-1705
    • Mijaljica, D.1    Nazarko, T.Y.2    Brumell, J.H.3
  • 119
    • 77950510302 scopus 로고    scopus 로고
    • The Cvt pathway as a model for selective autophagy
    • Lynch-Day MA, Klionsky DJ. The Cvt pathway as a model for selective autophagy. FEBS Lett 2010; 584:1359-1366.
    • (2010) FEBS Lett , vol.584 , pp. 1359-1366
    • Lynch-Day, M.A.1    Klionsky, D.J.2
  • 120
    • 0026640551 scopus 로고
    • Aminopeptidase i of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
    • Klionsky DJ, Cueva R, Yaver DS. Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway. J Cell Biol 1992; 119:287-299.
    • (1992) J Cell Biol , vol.119 , pp. 287-299
    • Klionsky, D.J.1    Cueva, R.2    Yaver, D.S.3
  • 122
    • 0029913505 scopus 로고    scopus 로고
    • Cytoplasmto- vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
    • Scott SV, Hefner-Gravink A, Morano KA, et al. Cytoplasmto- vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc Natl Acad Sci USA 1996; 93:12304-12308.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12304-12308
    • Scott, S.V.1    Hefner-Gravink, A.2    Morano, K.A.3
  • 123
    • 0031417385 scopus 로고    scopus 로고
    • Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome
    • Baba M, Osumi M, Scott SV, Klionsky DJ, Ohsumi Y. Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome. J Cell Biol 1997; 139:1687-1695.
    • (1997) J Cell Biol , vol.139 , pp. 1687-1695
    • Baba, M.1    Osumi, M.2    Scott, S.V.3    Klionsky, D.J.4    Ohsumi, Y.5
  • 124
    • 0030852279 scopus 로고    scopus 로고
    • Aminopeptidase i is targeted to the vacuole by a nonclassical vesicular mechanism
    • Scott SV, Baba M, Ohsumi Y, Klionsky DJ. Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism. J Cell Biol 1997; 138:37-44.
    • (1997) J Cell Biol , vol.138 , pp. 37-44
    • Scott, S.V.1    Baba, M.2    Ohsumi, Y.3    Klionsky, D.J.4
  • 125
    • 0030997923 scopus 로고    scopus 로고
    • Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway
    • Kim J, Scott SV, Oda MN, Klionsky DJ. Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway. J Cell Biol 1997; 137:609-618.
    • (1997) J Cell Biol , vol.137 , pp. 609-618
    • Kim, J.1    Scott, S.V.2    Oda, M.N.3    Klionsky, D.J.4
  • 126
    • 0035897414 scopus 로고    scopus 로고
    • Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for the vacuole
    • Kim J, Kamada Y, Stromhaug PE, et al. Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for the vacuole. J Cell Biol 2001; 153:381-396.
    • (2001) J Cell Biol , vol.153 , pp. 381-396
    • Kim, J.1    Kamada, Y.2    Stromhaug, P.E.3
  • 127
    • 53549088312 scopus 로고    scopus 로고
    • Quantitative regulation of vesicle formation in yeast nonspecific autophagy
    • Geng J, Klionsky DJ. Quantitative regulation of vesicle formation in yeast nonspecific autophagy. Autophagy 2008; 4:955-957.
    • (2008) Autophagy , vol.4 , pp. 955-957
    • Geng, J.1    Klionsky, D.J.2
  • 128
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mito phagy
    • Kanki T, Wang K, Cao Y, Baba M, Klionsky DJ. Atg32 is a mitochondrial protein that confers selectivity during mito phagy. Dev Cell 2009; 17:98-109.
    • (2009) Dev Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 129
    • 73949122199 scopus 로고    scopus 로고
    • A genomic screen for yeast mutants defective in selective mitochondria autophagy
    • Kanki T, Wang K, Baba M, et al. A genomic screen for yeast mutants defective in selective mitochondria autophagy. Mol Biol Cell 2009; 20:4730-4738.
    • (2009) Mol Biol Cell , vol.20 , pp. 4730-4738
    • Kanki, T.1    Wang, K.2    Baba, M.3
  • 130
    • 79958219318 scopus 로고    scopus 로고
    • Two MAPKsignaling pathways are required for mitophagy in Saccharomyces cerevisiae
    • Mao K, Wang K, Zhao M, Xu T, Klionsky DJ. Two MAPKsignaling pathways are required for mitophagy in Saccharomyces cerevisiae. J Cell Biol 2011; 193:755-767.
    • (2011) J Cell Biol , vol.193 , pp. 755-767
    • Mao, K.1    Wang, K.2    Zhao, M.3    Xu, T.4    Klionsky, D.J.5
  • 131
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissova I, Deffieu M, Manon S, Camougrand N. Uth1p is involved in the autophagic degradation of mitochondria. J Biol Chem 2004; 279:39068-39074.
    • (2004) J Biol Chem , vol.279 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 132
    • 34247172582 scopus 로고    scopus 로고
    • Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival
    • Tal R, Winter G, Ecker N, Klionsky DJ, Abeliovich H. Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival. J Biol Chem 2007; 282:5617-5624.
    • (2007) J Biol Chem , vol.282 , pp. 5617-5624
    • Tal, R.1    Winter, G.2    Ecker, N.3    Klionsky, D.J.4    Abeliovich, H.5
  • 133
    • 72149110062 scopus 로고    scopus 로고
    • Aup1-mediated regulation of Rtg3 during mitophagy
    • Journo D, Mor A, Abeliovich H. Aup1-mediated regulation of Rtg3 during mitophagy. J Biol Chem 2009; 284:35885-35895.
    • (2009) J Biol Chem , vol.284 , pp. 35885-35895
    • Journo, D.1    Mor, A.2    Abeliovich, H.3
  • 135
    • 77953641544 scopus 로고    scopus 로고
    • Mitochondrial clearance by autophagy in developing erythrocytes: Clearly important, but just how much so?
    • Mortensen M, Ferguson DJ, Simon AK. Mitochondrial clearance by autophagy in developing erythrocytes: clearly important, but just how much so? Cell Cycle 2010; 9:1901-1906.
    • (2010) Cell Cycle , pp. 9
    • Mortensen, M.1    Ferguson, D.J.2    Simon, A.K.3
  • 137
    • 74049153002 scopus 로고    scopus 로고
    • Nix is a selective autophagy receptor for mitochondrial clearance
    • Novak I, Kirkin V, McEwan DG, et al. Nix is a selective autophagy receptor for mitochondrial clearance. EMBO Rep 2010; 11:45-51.
    • (2010) EMBO Rep , vol.11 , pp. 45-51
    • Novak, I.1    Kirkin, V.2    McEwan, D.G.3
  • 138
    • 79952356168 scopus 로고    scopus 로고
    • Autophagy receptors in developmental clearance of mitochondria
    • Novak I, Dikic I. Autophagy receptors in developmental clearance of mitochondria. Autophagy 2011; 7:301-303.
    • (2011) Autophagy , vol.7 , pp. 301-303
    • Novak, I.1    Dikic, I.2
  • 139
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, Asakawa S, Hattori N, et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998; 392:605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3
  • 140
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinsons disease caused by mutations in PINK1
    • Valente EM, Abou-Sleiman PM, Caputo V, et al. Hereditary early-onset Parkinsons disease caused by mutations in PINK1. Science 2004; 304:1158-1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3
  • 141
    • 84885653993 scopus 로고    scopus 로고
    • Defective quality control mechanisms and accumulation of damaged mitochondria link Gaucher and Parkinson diseases
    • Osellame LD, Duchen MR. Defective quality control mechanisms and accumulation of damaged mitochondria link Gaucher and Parkinson diseases. Autophagy 2013; 9:1633-1635.
    • (2013) Autophagy , vol.9 , pp. 1633-1635
    • Osellame, L.D.1    Duchen, M.R.2
  • 142
    • 0033490110 scopus 로고    scopus 로고
    • Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway
    • Hutchins MU, Veenhuis M, Klionsky DJ. Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway. J Cell Sci 1999; 112:4079-4087.
    • (1999) J Cell Sci , vol.112 , pp. 4079-4087
    • Hutchins, M.U.1    Veenhuis, M.2    Klionsky, D.J.3
  • 143
    • 42049094041 scopus 로고    scopus 로고
    • PpAtg30 tags peroxisomes for turnover by selective autophagy
    • Farr JC, Manjithaya R, Mathewson RD, Subramani S. PpAtg30 tags peroxisomes for turnover by selective autophagy. Dev Cell 2008; 14:365-376.
    • (2008) Dev Cell , vol.14 , pp. 365-376
    • Farr, J.C.1    Manjithaya, R.2    Mathewson, R.D.3    Subramani, S.4
  • 144
    • 70349334586 scopus 로고    scopus 로고
    • Peroxisome size provides insights into the function of autophagy-related proteins
    • Nazarko TY, Farre JC, Subramani S. Peroxisome size provides insights into the function of autophagy-related proteins. Mol Biol Cell 2009; 20:3828-3839.
    • (2009) Mol Biol Cell , vol.20 , pp. 3828-3839
    • Nazarko, T.Y.1    Farre, J.C.2    Subramani, S.3
  • 145
    • 55149097659 scopus 로고    scopus 로고
    • The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes
    • Hara-Kuge S, Fujiki Y. The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes. Exp Cell Res 2008; 314:3531-3541.
    • (2008) Exp Cell Res , vol.314 , pp. 3531-3541
    • Hara-Kuge, S.1    Fujiki, Y.2
  • 147
    • 84875834380 scopus 로고    scopus 로고
    • A HORMA domain in Atg13 mediates PI 3-kinase recruitment in autophagy
    • Jao CC, Ragusa MJ, Stanley RE, Hurley JH. A HORMA domain in Atg13 mediates PI 3-kinase recruitment in autophagy. Proc Natl Acad Sci USA 2013; 110:5486-5491.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 5486-5491
    • Jao, C.C.1    Ragusa, M.J.2    Stanley, R.E.3    Hurley, J.H.4
  • 148
    • 84885622585 scopus 로고    scopus 로고
    • Structural characterization of the Saccharomyces cerevisiae autophagy regulatory complex Atg17-Atg31-Atg29
    • Chew LH, Setiaputra D, Klionsky DJ, Yip CK. Structural characterization of the Saccharomyces cerevisiae autophagy regulatory complex Atg17-Atg31-Atg29. Autophagy 2013; 9:1467-1474.
    • (2013) Autophagy , vol.9 , pp. 1467-1474
    • Chew, L.H.1    Setiaputra, D.2    Klionsky, D.J.3    Yip, C.K.4
  • 149
    • 80051692531 scopus 로고    scopus 로고
    • An Atg13 protein-mediated self-association of the Atg1 protein kinase is important for the induction of autophagy
    • Yeh YY, Shah KH, Herman PK. An Atg13 protein-mediated self-association of the Atg1 protein kinase is important for the induction of autophagy. J Biol Chem 2011; 286:28931-28939.
    • (2011) J Biol Chem , vol.286 , pp. 28931-28939
    • Yeh, Y.Y.1    Shah, K.H.2    Herman, P.K.3
  • 150
    • 84864337089 scopus 로고    scopus 로고
    • Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a ?-propeller protein family
    • Krick R, Busse RA, Scacioc A, et al. Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a ?-propeller protein family. Proc Natl Acad Sci USA 2012; 109:E2042-E2049.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Krick, R.1    Busse, R.A.2    Scacioc, A.3
  • 151
    • 84866419794 scopus 로고    scopus 로고
    • Structurebased analyses reveal distinct binding sites for Atg2 and phosphoinositides in Atg18
    • Watanabe Y, Kobayashi T, Yamamoto H, et al. Structurebased analyses reveal distinct binding sites for Atg2 and phosphoinositides in Atg18. J Biol Chem 2012; 287:31681-31690.
    • (2012) J Biol Chem , vol.287 , pp. 31681-31690
    • Watanabe, Y.1    Kobayashi, T.2    Yamamoto, H.3
  • 152
    • 84864960430 scopus 로고    scopus 로고
    • Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in autophagy
    • Baskaran S, Ragusa MJ, Boura E, Hurley JH. Two-site recognition of phosphatidylinositol 3-phosphate by PROPPINs in autophagy. Mol Cell 2012; 47:339-348.
    • (2012) Mol Cell , vol.47 , pp. 339-348
    • Baskaran, S.1    Ragusa, M.J.2    Boura, E.3    Hurley, J.H.4
  • 153
    • 3142583199 scopus 로고    scopus 로고
    • Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors
    • Dove SK, Piper RC, McEwen RK, et al. Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors. EMBO J 2004; 23:1922-1933.
    • (2004) EMBO J , vol.23 , pp. 1922-1933
    • Dove, S.K.1    Piper, R.C.2    McEwen, R.K.3
  • 154
    • 84876087626 scopus 로고    scopus 로고
    • Atg18 function in autophagy is regulated by specific sites within its b-propeller
    • Rieter E, Vinke F, Bakula D, et al. Atg18 function in autophagy is regulated by specific sites within its b-propeller. J Cell Sci 2013; 126:593-604.
    • (2013) J Cell Sci , vol.126 , pp. 593-604
    • Rieter, E.1    Vinke, F.2    Bakula, D.3
  • 155
    • 4344696843 scopus 로고    scopus 로고
    • The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8
    • Sugawara K, Suzuki NN, Fujioka Y, et al. The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8. Genes Cells 2004; 9:611-618.
    • (2004) Genes Cells , vol.9 , pp. 611-618
    • Sugawara, K.1    Suzuki, N.N.2    Fujioka, Y.3
  • 156
    • 28844502647 scopus 로고    scopus 로고
    • Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy
    • Sugawara K, Suzuki NN, Fujioka Y, et al. Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy. J Biol Chem 2005; 280:40058-40065.
    • (2005) J Biol Chem , vol.280 , pp. 40058-40065
    • Sugawara, K.1    Suzuki, N.N.2    Fujioka, Y.3
  • 157
    • 65649136884 scopus 로고    scopus 로고
    • The structure of Atg4BLC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy
    • Satoo K, Noda NN, Kumeta H, et al. The structure of Atg4BLC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy. EMBO J 2009; 28:1341-1350.
    • (2009) EMBO J , vol.28 , pp. 1341-1350
    • Satoo, K.1    Noda, N.N.2    Kumeta, H.3
  • 158
    • 80555144181 scopus 로고    scopus 로고
    • Structural basis of Atg8 activation by a homodimeric E1, Atg7
    • Noda NN, Satoo K, Fujioka Y, et al. Structural basis of Atg8 activation by a homodimeric E1, Atg7. Mol Cell 2011; 44:462-475.
    • (2011) Mol Cell , vol.44 , pp. 462-475
    • Noda, N.N.1    Satoo, K.2    Fujioka, Y.3
  • 159
    • 82955247613 scopus 로고    scopus 로고
    • Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8
    • Hong SB, Kim BW, Lee KE, et al. Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8. Nat Struct Mol Biol 2011; 18:1323-1330.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1323-1330
    • Hong, S.B.1    Kim, B.W.2    Lee, K.E.3
  • 160
    • 80555144189 scopus 로고    scopus 로고
    • Atg8 transfer from Atg7 to Atg3: A distinctive E1-E2 architecture and mechanism in the autophagy pathway
    • Taherbhoy AM, Tait SW, Kaiser SE, et al. Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Mol Cell 2011; 44:451-461.
    • (2011) Mol Cell , vol.44 , pp. 451-461
    • Taherbhoy, A.M.1    Tait, S.W.2    Kaiser, S.E.3
  • 161
    • 34247237202 scopus 로고    scopus 로고
    • The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation
    • Yamada Y, Suzuki NN, Hanada T, et al. The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. J Biol Chem 2007; 282:8036-8043.
    • (2007) J Biol Chem , vol.282 , pp. 8036-8043
    • Yamada, Y.1    Suzuki, N.N.2    Hanada, T.3
  • 162
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita N, Itoh T, Omori H, et al. The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol Biol Cell 2008; 19:2092-2100.
    • (2008) Mol Biol Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3
  • 163
    • 84876191754 scopus 로고    scopus 로고
    • Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site
    • Sakoh-Nakatogawa M, Matoba K, Asai E, et al. Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site. Nat Struct Mol Biol 2013; 20:433-439.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 433-439
    • Sakoh-Nakatogawa, M.1    Matoba, K.2    Asai, E.3
  • 164
    • 33644590635 scopus 로고    scopus 로고
    • The crystal structure of plant ATG12 and its biological implication in autophagy
    • Suzuki NN, Yoshimoto K, Fujioka Y, Ohsumi Y, Inagaki F. The crystal structure of plant ATG12 and its biological implication in autophagy. Autophagy 2005; 1:119-126.
    • (2005) Autophagy , vol.1 , pp. 119-126
    • Suzuki, N.N.1    Yoshimoto, K.2    Fujioka, Y.3    Ohsumi, Y.4    Inagaki, F.5
  • 165
    • 84863519526 scopus 로고    scopus 로고
    • Structural insights into Atg10-mediated formation of the autophagyessential Atg12-Atg5 conjugate
    • Yamaguchi M, Noda NN, Yamamoto H, et al. Structural insights into Atg10-mediated formation of the autophagyessential Atg12-Atg5 conjugate. Structure 2012; 20:1244-1254.
    • (2012) Structure , vol.20 , pp. 1244-1254
    • Yamaguchi, M.1    Noda, N.N.2    Yamamoto, H.3
  • 166
    • 84870815734 scopus 로고    scopus 로고
    • Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures
    • Kaiser SE, Mao K, Taherbhoy AM, et al. Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. Nat Struct Mol Biol 2012; 19:1242-1249.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1242-1249
    • Kaiser, S.E.1    Mao, K.2    Taherbhoy, A.M.3
  • 167
    • 34248203863 scopus 로고    scopus 로고
    • Structure of Atg5Atg16, a complex essential for autophagy
    • Matsushita M, Suzuki NN, Obara K, et al. Structure of Atg5Atg16, a complex essential for autophagy. J Biol Chem 2007; 282:6763-6772.
    • (2007) J Biol Chem , vol.282 , pp. 6763-6772
    • Matsushita, M.1    Suzuki, N.N.2    Obara, K.3
  • 168
    • 84873405258 scopus 로고    scopus 로고
    • Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation
    • Noda NN, Fujioka Y, Hanada T, Ohsumi Y, Inagaki F. Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation. EMBO Rep 2013; 14:206-211.
    • (2013) EMBO Rep , vol.14 , pp. 206-211
    • Noda, N.N.1    Fujioka, Y.2    Hanada, T.3    Ohsumi, Y.4    Inagaki, F.5
  • 169
    • 74049140368 scopus 로고    scopus 로고
    • Dimeric coiled-coil structure of Saccharomyces cerevisiae Atg16 and its functional significance in autophagy
    • Fujioka Y, Noda NN, Nakatogawa H, Ohsumi Y, Inagaki F. Dimeric coiled-coil structure of Saccharomyces cerevisiae Atg16 and its functional significance in autophagy. J Biol Chem 2010; 285:1508-1515.
    • (2010) J Biol Chem , vol.285 , pp. 1508-1515
    • Fujioka, Y.1    Noda, N.N.2    Nakatogawa, H.3    Ohsumi, Y.4    Inagaki, F.5
  • 170
    • 84872036691 scopus 로고    scopus 로고
    • Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy
    • Otomo C, Metlagel Z, Takaesu G, Otomo T. Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy. Nat Struct Mol Biol 2013; 20:59-66.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 59-66
    • Otomo, C.1    Metlagel, Z.2    Takaesu, G.3    Otomo, T.4
  • 171
    • 84878562770 scopus 로고    scopus 로고
    • Autophagic processes in yeast: Mechanism, machinery and regulation
    • Reggiori F, Klionsky DJ. Autophagic processes in yeast: mechanism, machinery and regulation. Genetics 2013; 194:341-361.
    • (2013) Genetics , vol.194 , pp. 341-361
    • Reggiori, F.1    Klionsky, D.J.2
  • 172
    • 77950212231 scopus 로고    scopus 로고
    • Shaping development of autophagy inhibitors with the structure of the lipid kinase Vps34
    • Miller S, Tavshanjian B, Oleksy A, et al. Shaping development of autophagy inhibitors with the structure of the lipid kinase Vps34. Science 2010; 327:1638-1642.
    • (2010) Science , vol.327 , pp. 1638-1642
    • Miller, S.1    Tavshanjian, B.2    Oleksy, A.3
  • 173
    • 84862777560 scopus 로고    scopus 로고
    • Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein
    • Huang W, Choi W, Hu W, et al. Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein. Cell Res 2012; 22:473-489.
    • (2012) Cell Res , vol.22 , pp. 473-489
    • Huang, W.1    Choi, W.2    Hu, W.3
  • 174
    • 34249037565 scopus 로고    scopus 로고
    • Crystal structure of the Bcl- XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein
    • Oberstein A, Jeffrey PD, Shi Y. Crystal structure of the Bcl- XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J Biol Chem 2007; 282:13123-13132.
    • (2007) J Biol Chem , vol.282 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 175
    • 84862023791 scopus 로고    scopus 로고
    • Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG
    • Li X, He L, Che KH, et al. Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG. Nat Commun 2012; 3:662.
    • (2012) Nat Commun , vol.3 , pp. 662
    • Li, X.1    He, L.2    Che, K.H.3
  • 176
    • 67650070480 scopus 로고    scopus 로고
    • Structure and function of Vps15 in the endosomal G protein signaling pathway
    • Heenan EJ, Vanhooke JL, Temple BR, et al. Structure and function of Vps15 in the endosomal G protein signaling pathway. Biochemistry 2009; 48:6390-6401.
    • (2009) Biochemistry , vol.48 , pp. 6390-6401
    • Heenan, E.J.1    Vanhooke, J.L.2    Temple, B.R.3
  • 177
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • Itakura E, Kishi-Itakura C, Mizushima N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 2012; 151:1256-1269.
    • (2012) Cell , vol.151 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 178
    • 77955880894 scopus 로고    scopus 로고
    • Finding a fitting shoe for Cinderella: Searching for an autophagy inhibitor
    • Miller S, Oleksy A, Perisic O, Williams RL. Finding a fitting shoe for Cinderella: searching for an autophagy inhibitor. Autophagy 2010; 6:805-807.
    • (2010) Autophagy , vol.6 , pp. 805-807
    • Miller, S.1    Oleksy, A.2    Perisic, O.3    Williams, R.L.4
  • 179
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein DC, Codogno P, Levine B. Autophagy modulation as a potential therapeutic target for diverse diseases. Nat Rev Drug Discov 2012; 11:709-730.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.