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Volumn 6, Issue 4, 2010, Pages 438-448

A comprehensive glossary of autophagy-related molecules and processes

(13)  Klionsky, Daniel J a   Codogno, Patrice b   Cuervo, Ana Maria c   Deretic, Vojo d   Elazar, Zvulun e   Fueyo Margareto, Juan f   Gewirtz, David A g   Kroemer, Guido h   Levine, Beth i   Mizushima, Noboru j   Rubinsztein, David C k   Thumm, Michael l   Tooze, Sharon A m  

b INSERM   (France)

Author keywords

Autophagy; Definitions; Glossary; Lexicon; Terms

Indexed keywords

3 METHYLADENINE; 4 [4 (4' CHLORO 2 BIPHENYLYLMETHYL) 1 PIPERAZINYL] N [4 [3 DIMETHYLAMINO 1 (PHENYLTHIOMETHYL)PROPYLAMINO] 3 NITROBENZENESULFONYL]BENZAMIDE; ATM PROTEIN; AUTOPHAGY PROTEIN; AUTOPHAGY PROTEIN 5; BECLIN 1; BH3 PROTEIN; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE BETA; DEATH ASSOCIATED PROTEIN KINASE; ENDOPHILIN; ENDOPHILIN B 1; EVEROLIMUS; FORKHEAD TRANSCRIPTION FACTOR; GLYCOGEN SYNTHASE KINASE 3; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 90; HYPOXIA INDUCIBLE FACTOR 1; INITIATION FACTOR 2ALPHA; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; MEMBRANE COFACTOR PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN; PROTEIN C JUN; STRESS ACTIVATED PROTEIN KINASE 1; TEMSIROLIMUS; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR GCN4; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 77953724901     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.6.4.12244     Document Type: Review
Times cited : (136)

References (176)
  • 1
    • 0005677775 scopus 로고
    • 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated hepatocytes
    • Seglen P, Gordon P. 3-Methyladenine: Specific inhibitor of autophagic/lysosomal protein degradation in isolated hepatocytes. Proc Nat Acad Sci USA 1982; 79:1889-92.
    • (1982) Proc Nat Acad Sci USA , vol.79 , pp. 1889-1892
    • Seglen, P.1    Gordon, P.2
  • 3
    • 34250828455 scopus 로고    scopus 로고
    • Proteomic analysis of membrane-associated proteins from rat liver autophagosomes
    • Overbye A, Fengsrud M, Seglen PO. Proteomic analysis of membrane-associated proteins from rat liver autophagosomes. Autophagy 2007; 3:300-22.
    • (2007) Autophagy , vol.3 , pp. 300-322
    • Overbye, A.1    Fengsrud, M.2    Seglen, P.O.3
  • 4
    • 77950484269 scopus 로고    scopus 로고
    • Atg8-family interacting motif crucial for selective autophagy
    • Noda NN, Ohsumi Y, Inagaki F. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett 2010; 584:1379-85.
    • (2010) FEBS Lett , vol.584 , pp. 1379-1385
    • Noda, N.N.1    Ohsumi, Y.2    Inagaki, F.3
  • 5
    • 4944247868 scopus 로고    scopus 로고
    • Alfy, A novel FYVE-domain- containing protein associated with protein granules and autophagic membranes
    • Simonsen A, Birkeland HC, Gillooly DJ, Mizushima N, Kuma A, Yoshimori T, et al. Alfy, a novel FYVE-domain- containing protein associated with protein granules and autophagic membranes. J Cell Sci 2004; 117:4239-51.
    • (2004) J Cell Sci , vol.117 , pp. 4239-4251
    • Simonsen, A.1    Birkeland, H.C.2    Gillooly, D.J.3    Mizushima, N.4    Kuma, A.5    Yoshimori, T.6
  • 8
    • 34248593475 scopus 로고    scopus 로고
    • AMP-activated protein kinase and autophagy
    • Meijer AJ, Codogno P. AMP-activated protein kinase and autophagy. Autophagy 2007; 3:238-40.
    • (2007) Autophagy , vol.3 , pp. 238-240
    • Meijer, A.J.1    Codogno, P.2
  • 9
    • 0032508564 scopus 로고    scopus 로고
    • Inhibition of hepatocytic autophagy by adenosine, aminoimidazole-4- carboxamide riboside, and N6-mercaptopurine riboside. Evidence for involvement of AMP-activated protein kinase
    • Samari HR, Seglen PO. Inhibition of hepatocytic autophagy by adenosine, aminoimidazole-4-carboxamide riboside, and N6-mercaptopurine riboside. Evidence for involvement of AMP-activated protein kinase. J Biol Chem 1998; 273:23758-63.
    • (1998) J Biol Chem , vol.273 , pp. 23758-23763
    • Samari, H.R.1    Seglen, P.O.2
  • 10
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic V, Levine B. Autophagy, immunity, and microbial adaptations. Cell Host Microbe 2009; 5:527-49.
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 11
    • 77951643083 scopus 로고    scopus 로고
    • ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR signaling pathway
    • Kuo ea. ARD1 stabilization of TSC2 suppresses tumorigenesis through the mTOR signaling pathway. Sci Signal 2010; 3:ra9.
    • (2010) Sci Signal , vol.3
    • Kuo, E.A.1
  • 13
    • 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; 192:245-50.
    • (1997) Gene , vol.192 , pp. 245-250
    • Matsuura, A.1    Tsukada, M.2    Wada, Y.3    Ohsumi, Y.4
  • 14
    • 0035839430 scopus 로고    scopus 로고
    • Apg2 is a novel protein required for the cytoplasm to vacuole targeting, autophagy, and pexophagy pathways
    • Wang C-W, Kim J, Huang W-P, Abeliovich H, Stromhaug PE, Dunn WA, Jr., et al. Apg2 is a novel protein required for the cytoplasm to vacuole targeting, autophagy, and pexophagy pathways. J Biol Chem 2001; 276:30442-51.
    • (2001) J Biol Chem , vol.276 , pp. 30442-30451
    • Wang, C.-W.1    Kim, J.2    Huang, W.-P.3    Abeliovich, H.4    Stromhaug, P.E.5    Dunn Jr., W.A.6
  • 15
    • 0035839551 scopus 로고    scopus 로고
    • Apg2p functions in autophagosome formation on the perivacuolar structure
    • Shintani T, Suzuki K, Kamada Y, Noda T, Ohsumi Y. Apg2p functions in autophagosome formation on the perivacuolar structure. J Biol Chem 2001; 276:30452-60.
    • (2001) J Biol Chem , vol.276 , pp. 30452-30460
    • Shintani, T.1    Suzuki, K.2    Kamada, Y.3    Noda, T.4    Ohsumi, Y.5
  • 18
    • 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, Kabeya Y, Mizushima N, Yoshimori T, 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; 151:263-76.
    • (2000) J Cell Biol , vol.151 , pp. 263-276
    • Kirisako, T.1    Ichimura, Y.2    Okada, H.3    Kabeya, Y.4    Mizushima, N.5    Yoshimori, T.6
  • 20
    • 0032575551 scopus 로고    scopus 로고
    • Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae
    • Kametaka S, Okano T, Ohsumi M, Ohsumi Y. Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae. J Biol Chem 1998; 273:22284-91.
    • (1998) J Biol Chem , vol.273 , pp. 22284-22291
    • Kametaka, S.1    Okano, T.2    Ohsumi, M.3    Ohsumi, Y.4
  • 22
    • 0032896760 scopus 로고    scopus 로고
    • Apg7p/Cvt2p is required for the cytoplasm-tovacuole targeting, macroautophagy, and peroxisome degradation pathways
    • Kim J, Dalton VM, Eggerton KP, Scott SV, Klionsky DJ. Apg7p/Cvt2p is required for the cytoplasm-tovacuole targeting, macroautophagy, and peroxisome degradation pathways. Mol Biol Cell 1999; 10:1337-51.
    • (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
  • 23
    • 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; 275:5845-51.
    • (2000) J Biol Chem , vol.275 , pp. 5845-5851
    • Huang, W.-P.1    Scott, S.V.2    Kim, J.3    Klionsky, D.J.4
  • 25
    • 0034614934 scopus 로고    scopus 로고
    • Apg9p/Cvt7p is an integral membrane protein required for transport vesicle formation in the Cvt and autophagy pathways
    • Noda T, Kim J, Huang W-P, Baba M, Tokunaga C, Ohsumi Y, et al. Apg9p/Cvt7p is an integral membrane protein required for transport vesicle formation in the Cvt and autophagy pathways. J Cell Biol 2000; 148:465-80.
    • (2000) J Cell Biol , vol.148 , pp. 465-480
    • Noda, T.1    Kim, J.2    Huang, W.-P.3    Baba, M.4    Tokunaga, C.5    Ohsumi, Y.6
  • 26
    • 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; 1:101-9.
    • (2005) Autophagy , vol.1 , pp. 101-109
    • Reggiori, F.1    Shintani, T.2    Nair, U.3    Klionsky, D.J.4
  • 27
    • 0033214582 scopus 로고    scopus 로고
    • Apg10p, A novel protein-conjugating enzyme essential for autophagy in yeast
    • Shintani T, Mizushima N, Ogawa Y, Matsuura A, Noda T, Ohsumi Y. Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J 1999; 18:5234-41.
    • (1999) EMBO J , vol.18 , pp. 5234-5241
    • Shintani, T.1    Mizushima, N.2    Ogawa, Y.3    Matsuura, A.4    Noda, T.5    Ohsumi, Y.6
  • 28
    • 0035897414 scopus 로고    scopus 로고
    • Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for the vacuole
    • Kim J, Kamada Y, Stromhaug PE, Guan J, Hefner-Gravink A, Baba M, et al. Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for the vacuole. J Cell Biol 2001; 153:381-96.
    • (2001) J Cell Biol , vol.153 , pp. 381-396
    • Kim, J.1    Kamada, Y.2    Stromhaug, P.E.3    Guan, J.4    Hefner-Gravink, A.5    Baba, M.6
  • 29
    • 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, Weisman LS, Kamada Y, Keizer-Gunnink I, et al. Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting. J Biol Chem 2000; 275:25840-9.
    • (2000) J Biol Chem , vol.275 , pp. 25840-25849
    • Scott, S.V.1    Nice III, D.C.2    Nau, J.J.3    Weisman, L.S.4    Kamada, Y.5    Keizer-Gunnink, I.6
  • 30
    • 0030919092 scopus 로고    scopus 로고
    • Analyses of APG13 gene involved in autophagy in yeast, Saccharomyces cerevisiae
    • Funakoshi T, Matsuura A, Noda T, Ohsumi Y. Analyses of APG13 gene involved in autophagy in yeast, Saccharomyces cerevisiae. Gene 1997; 192:207-13.
    • (1997) Gene , vol.192 , pp. 207-213
    • Funakoshi, T.1    Matsuura, A.2    Noda, T.3    Ohsumi, Y.4
  • 31
    • 0035910577 scopus 로고    scopus 로고
    • Degradation of lipid vesicles in the yeast vacuole requires function of Cvt17, A putative lipase
    • Teter SA, Eggerton KP, Scott SV, Kim J, Fischer AM, Klionsky DJ. Degradation of lipid vesicles in the yeast vacuole requires function of Cvt17, a putative lipase. J Biol Chem 2001; 276:2083-7.
    • (2001) J Biol Chem , vol.276 , pp. 2083-2087
    • Teter, S.A.1    Eggerton, K.P.2    Scott, S.V.3    Kim, J.4    Fischer, A.M.5    Klionsky, D.J.6
  • 32
    • 0034809331 scopus 로고    scopus 로고
    • Aut5/Cvt17p, A putative lipase essential for disintegration of autophagic bodies inside the vacuole
    • Epple UD, Suriapranata I, Eskelinen E-L, Thumm M. Aut5/Cvt17p, a putative lipase essential for disintegration of autophagic bodies inside the vacuole. J Bacteriol 2001; 183:5942-55.
    • (2001) J Bacteriol , vol.183 , pp. 5942-5955
    • Epple, U.D.1    Suriapranata, I.2    Eskelinen, E.-L.3    Thumm, M.4
  • 33
    • 0033565655 scopus 로고    scopus 로고
    • Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway
    • Mizushima N, Noda T, Ohsumi Y. Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway. EMBO J 1999; 18:3888-96.
    • (1999) EMBO J , vol.18 , pp. 3888-3896
    • Mizushima, N.1    Noda, T.2    Ohsumi, Y.3
  • 34
    • 35848970794 scopus 로고    scopus 로고
    • Genome-wide association scanning highlights two autophagy genes, ATG16L1 and IRGM, as being significantly associated with Crohn's disease
    • Massey DC, Parkes M. Genome-wide association scanning highlights two autophagy genes, ATG16L1 and IRGM, as being significantly associated with Crohn's disease. Autophagy 2007; 3:649-51.
    • (2007) Autophagy , vol.3 , pp. 649-651
    • Massey, D.C.1    Parkes, M.2
  • 37
    • 0035661648 scopus 로고    scopus 로고
    • Cvt18/Gsa12 is required for cytoplasm-to-vacuole transport, pexophagy, and autophagy in Saccharomyces cerevisiae and Pichia pastoris
    • Guan J, Stromhaug PE, George MD, Habibzadegah-Tari P, Bevan A, Dunn WA, Jr., et al. Cvt18/Gsa12 is required for cytoplasm-to-vacuole transport, pexophagy, and autophagy in Saccharomyces cerevisiae and Pichia pastoris. Mol Biol Cell 2001; 12:3821-38.
    • (2001) Mol Biol Cell , vol.12 , pp. 3821-3838
    • Guan, J.1    Stromhaug, P.E.2    George, M.D.3    Habibzadegah-Tari, P.4    Bevan, A.5    Dunn Jr., W.A.6
  • 38
    • 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; 7:1131-41.
    • (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
  • 39
    • 0035800870 scopus 로고    scopus 로고
    • Yol082p, A novel CVT protein involved in the selective targeting of aminopeptidase I to the yeast vacuole
    • Leber R, Silles E, Sandoval IV, Mazon MJ. Yol082p, a novel CVT protein involved in the selective targeting of aminopeptidase I to the yeast vacuole. J Biol Chem 2001; 276:29210-7.
    • (2001) J Biol Chem , vol.276 , pp. 29210-29217
    • Leber, R.1    Silles, E.2    Sandoval, I.V.3    Mazon, M.J.4
  • 40
    • 0037119448 scopus 로고    scopus 로고
    • Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy
    • Nice DC, Sato TK, Stromhaug PE, Emr SD, Klionsky DJ. Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pre-autophagosomal structure is required for selective autophagy. J Biol Chem 2002; 277:30198-207.
    • (2002) J Biol Chem , vol.277 , pp. 30198-30207
    • Nice, D.C.1    Sato, T.K.2    Stromhaug, P.E.3    Emr, S.D.4    Klionsky, D.J.5
  • 41
    • 3342951135 scopus 로고    scopus 로고
    • Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy
    • Stromhaug PE, Reggiori F, Guan J, Wang C-W, Klionsky DJ. Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy. Mol Biol Cell 2004; 15:3553-66.
    • (2004) Mol Biol Cell , vol.15 , pp. 3553-3566
    • Stromhaug, P.E.1    Reggiori, F.2    Guan, J.3    Wang, C.-W.4    Klionsky, D.J.5
  • 42
    • 33845407202 scopus 로고    scopus 로고
    • Atg22 recycles amino acids to link the degradative and recycling functions of autophagy
    • Yang Z, Huang J, Geng J, Nair U, Klionsky DJ. Atg22 recycles amino acids to link the degradative and recycling functions of autophagy. Mol Biol Cell 2006; 17:5094-104.
    • (2006) Mol Biol Cell , vol.17 , pp. 5094-5104
    • Yang, Z.1    Huang, J.2    Geng, J.3    Nair, U.4    Klionsky, D.J.5
  • 44
    • 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; 3:422-32.
    • (2007) Autophagy , vol.3 , pp. 422-432
    • Legakis, J.E.1    Yen, W.-L.2    Klionsky, D.J.3
  • 45
    • 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
  • 46
    • 0347611578 scopus 로고    scopus 로고
    • Atg23 is essential for the cytoplasm to vacuole targeting pathway and efficient autophagy but not pexophagy
    • Tucker KA, Reggiori F, Dunn WA, Jr., Klionsky DJ. Atg23 is essential for the cytoplasm to vacuole targeting pathway and efficient autophagy but not pexophagy. J Biol Chem 2003; 278:48445-52.
    • (2003) J Biol Chem , vol.278 , pp. 48445-48452
    • Tucker, K.A.1    Reggiori, F.2    Dunn Jr., W.A.3    Klionsky, D.J.4
  • 48
    • 33846140410 scopus 로고    scopus 로고
    • Atg26 is not involved in autophagy-related pathways in Saccharomyces cerevisiae
    • Cao Y, Klionsky DJ. Atg26 is not involved in autophagy-related pathways in Saccharomyces cerevisiae. Autophagy 2007; 3:17-20.
    • (2007) Autophagy , vol.3 , pp. 17-20
    • Cao, Y.1    Klionsky, D.J.2
  • 49
    • 33747402357 scopus 로고    scopus 로고
    • PI4P-signaling pathway for the synthesis of a nascent membrane structure in selective autophagy
    • Yamashita S, Oku M, Wasada Y, Ano Y, Sakai Y. PI4P-signaling pathway for the synthesis of a nascent membrane structure in selective autophagy. J Cell Biol 2006; 173:709-17.
    • (2006) J Cell Biol , vol.173 , pp. 709-717
    • Yamashita, S.1    Oku, M.2    Wasada, Y.3    Ano, Y.4    Sakai, Y.5
  • 50
    • 33846807374 scopus 로고    scopus 로고
    • Atg27 is required for autophagy-dependent cycling of Atg9
    • Yen W-L, Legakis JE, Nair U, Klionsky DJ. Atg27 is required for autophagy-dependent cycling of Atg9. Mol Biol Cell 2007; 18:581-93.
    • (2007) Mol Biol Cell , vol.18 , pp. 581-593
    • Yen, W.-L.1    Legakis, J.E.2    Nair, U.3    Klionsky, D.J.4
  • 51
    • 33644587420 scopus 로고    scopus 로고
    • Atg28, A novel coiledcoil protein involved in autophagic degradation of peroxisomes in the methylotrophic yeast Pichia pastoris
    • Stasyk OV, Stasyk OG, Mathewson RD, Farre JC, Nazarko VY, Krasovska OS, et al. Atg28, a novel coiledcoil protein involved in autophagic degradation of peroxisomes in the methylotrophic yeast Pichia pastoris. Autophagy 2006; 2:30-8.
    • (2006) Autophagy , vol.2 , pp. 30-38
    • Stasyk, O.V.1    Stasyk, O.G.2    Mathewson, R.D.3    Farre, J.C.4    Nazarko, V.Y.5    Krasovska, O.S.6
  • 53
  • 54
    • 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; 356:405-10.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 405-410
    • Kabeya, Y.1    Kawamata, T.2    Suzuki, K.3    Ohsumi, Y.4
  • 55
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T, Wang K, Cao Y, Baba M, Klionsky DJ. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. 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
  • 56
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K, Kondo-Okamoto N, Ohsumi Y. Mitochondria-anchored 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
  • 57
    • 73949122199 scopus 로고    scopus 로고
    • A genomic screen for yeast mutants defective in selective mitochondria autophagy
    • Kanki T, Wang K, Baba M, Bartholomew CR, Lynch- Day MA, Du Z, et al. A genomic screen for yeast mutants defective in selective mitochondria autophagy. Mol Biol Cell 2009; 20:4730-8.
    • (2009) Mol Biol Cell , vol.20 , pp. 4730-4738
    • Kanki, T.1    Wang, K.2    Baba, M.3    Bartholomew, C.R.4    Lynch- Day, M.A.5    Du, Z.6
  • 59
    • 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; 5:649-62.
    • (2009) Autophagy , vol.5 , pp. 649-662
    • Mercer, C.A.1    Kaliappan, A.2    Dennis, P.B.3
  • 61
    • 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; 110:1935-45.
    • (1990) J Cell Biol , vol.110 , pp. 1935-1945
    • Dunn Jr., W.A.1
  • 62
    • 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; 20:465-71.
    • (1995) Cell Struct Funct , vol.20 , pp. 465-471
    • Baba, M.1    Osumi, M.2    Ohsumi, Y.3
  • 63
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A, Tagawa Y, Yoshimori T, Moriyama Y, Masaki R, Tashiro Y. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct 1998; 23:33-42.
    • (1998) Cell Struct Funct , vol.23 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 64
    • 53549084325 scopus 로고    scopus 로고
    • Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?
    • Klionsky DJ, Elazar Z, Seglen PO, Rubinsztein DC. Does bafilomycin A1 block the fusion of autophagosomes with lysosomes? Autophagy 2008; 4:849-950.
    • (2008) Autophagy , vol.4 , pp. 849-950
    • Klionsky, D.J.1    Elazar, Z.2    Seglen, P.O.3    Rubinsztein, D.C.4
  • 65
    • 58049192897 scopus 로고    scopus 로고
    • Identification of Barkor as a mammalian autophagyspecific factor for Beclin 1 and class III phosphatidylinositol 3-kinase
    • Sun Q, Fan W, Chen K, Ding X, Chen S, Zhong Q. Identification of Barkor as a mammalian autophagyspecific factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 2008; 105:19211-6.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19211-19216
    • Sun, Q.1    Fan, W.2    Chen, K.3    Ding, X.4    Chen, S.5    Zhong, Q.6
  • 67
    • 34848899280 scopus 로고    scopus 로고
    • Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis
    • Takahashi Y, Coppola D, Matsushita N, Cualing HD, Sun M, Sato Y, et al. Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and tumorigenesis. Nat Cell Biol 2007; 9:1142-51.
    • (2007) Nat Cell Biol , vol.9 , pp. 1142-1151
    • Takahashi, Y.1    Coppola, D.2    Matsushita, N.3    Cualing, H.D.4    Sun, M.5    Sato, Y.6
  • 69
    • 3042562282 scopus 로고    scopus 로고
    • Pivotal role of the cell death factor BNIP3 in ceramide-induced autophagic cell death in malignant glioma cells
    • Daido S, Kanzawa T, Yamamoto A, Takeuchi H, Kondo Y, Kondo S. Pivotal role of the cell death factor BNIP3 in ceramide-induced autophagic cell death in malignant glioma cells. Cancer Res 2004; 64:4286-93.
    • (2004) Cancer Res , vol.64 , pp. 4286-4293
    • Daido, S.1    Kanzawa, T.2    Yamamoto, A.3    Takeuchi, H.4    Kondo, Y.5    Kondo, S.6
  • 70
    • 0026645413 scopus 로고
    • Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity
    • Holen I, Gordon PB, Seglen PO. Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity. Biochem J 1992; 284:633-6.
    • (1992) Biochem J , vol.284 , pp. 633-636
    • Holen, I.1    Gordon, P.B.2    Seglen, P.O.3
  • 72
    • 77949328788 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: Selectivity pays off
    • Cuervo AM. Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol Metab 2010; 21:142-50.
    • (2010) Trends Endocrinol Metab , vol.21 , pp. 142-150
    • Cuervo, A.M.1
  • 73
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice J. Chaperone-mediated autophagy. Autophagy 2007; 3:295-9.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.1
  • 74
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes F, Terlecky S, Dice J. An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 1997; 137:825-34.
    • (1997) J Cell Biol , vol.137 , pp. 825-834
    • Agarraberes, F.1    Terlecky, S.2    Dice, J.3
  • 75
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo A, Dice J. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996; 273:501-3.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.1    Dice, J.2
  • 76
    • 0014189413 scopus 로고
    • Effect of chloroquine on morphology of cytoplasmic granules in maturing human leukocytes - An ultrastructural study
    • Fedorko M. Effect of chloroquine on morphology of cytoplasmic granules in maturing human leukocytes - an ultrastructural study. J Clin Invest 1967; 46:1932-42.
    • (1967) J Clin Invest , vol.46 , pp. 1932-1942
    • Fedorko, M.1
  • 77
    • 77950228149 scopus 로고    scopus 로고
    • Jun proteins are starvation-regulated inhibitors of autophagy
    • Yogev O, Goldberg R, Anzi S, Shaulian E. Jun proteins are starvation-regulated inhibitors of autophagy. Cancer Res; 70:2318-27.
    • Cancer Res , vol.70 , pp. 2318-2327
    • Yogev, O.1    Goldberg, R.2    Anzi, S.3    Shaulian, E.4
  • 78
    • 77951001692 scopus 로고    scopus 로고
    • Positive or negative regulatory roles of different cyclindependent kinase Pho85-cyclin complexes orchestrate induction of autophagy in Saccharomyces cerevisiae
    • Yang Z, Geng J, Yen W-L, Wang K, Klionsky DJ. Positive or negative regulatory roles of different cyclindependent kinase Pho85-cyclin complexes orchestrate induction of autophagy in Saccharomyces cerevisiae. Mol Cell 2010; 38:250-64.
    • (2010) Mol Cell , vol.38 , pp. 250-264
    • Yang, Z.1    Geng, J.2    Yen, W.-L.3    Wang, K.4    Klionsky, D.J.5
  • 79
    • 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, Cao Y, Richardson BC, Li Z, et al. The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy. J Cell Biol 2010; 188:101-14.
    • (2010) J Cell Biol , vol.188 , pp. 101-114
    • Yen, W.-L.1    Shintani, T.2    Nair, U.3    Cao, Y.4    Richardson, B.C.5    Li, Z.6
  • 80
    • 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
  • 81
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • Inbal B, Bialik S, Sabanay I, Shani G, Kimchi A. DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death. J Cell Biol 2002; 157:455-68.
    • (2002) J Cell Biol , vol.157 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 82
    • 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, Chandra P, Roderick HL, Habermann A, 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    Chandra, P.4    Roderick, H.L.5    Habermann, A.6
  • 83
    • 74049129024 scopus 로고    scopus 로고
    • The nuclear cofactor DOR regulates autophagy in mammalian and Drosophila cells
    • Mauvezin C, Orpinell M, Francis VA, Mansilla F, Duran J, Ribas V, et al. The nuclear cofactor DOR regulates autophagy in mammalian and Drosophila cells. EMBO Rep 2010; 11:37-44.
    • (2010) EMBO Rep , vol.11 , pp. 37-44
    • Mauvezin, C.1    Orpinell, M.2    Francis, V.A.3    Mansilla, F.4    Duran, J.5    Ribas, V.6
  • 84
    • 33745885329 scopus 로고    scopus 로고
    • DRAM, A p53-induced modulator of autophagy, is critical for apoptosis
    • Crighton D, Wilkinson S, O'Prey J, Syed N, Smith P, Harrison PR, et al. DRAM, a p53-induced modulator of autophagy, is critical for apoptosis. Cell 2006; 126:121-34.
    • (2006) Cell , vol.126 , pp. 121-134
    • Crighton, D.1    Wilkinson, S.2    O'Prey, J.3    Syed, N.4    Smith, P.5    Harrison, P.R.6
  • 85
    • 49649121765 scopus 로고    scopus 로고
    • E2F1 regulates autophagy and the transcription of autophagy genes
    • Polager S, Ofir M, Ginsberg D. E2F1 regulates autophagy and the transcription of autophagy genes. Oncogene 2008; 27:4860-4.
    • (2008) Oncogene , vol.27 , pp. 4860-4864
    • Polager, S.1    Ofir, M.2    Ginsberg, D.3
  • 87
    • 33846211417 scopus 로고    scopus 로고
    • ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation
    • Kouroku Y, Fujita E, Tanida I, Ueno T, Isoai A, Kumagai H, et al. ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ 2007; 14:230-9.
    • (2007) Cell Death Differ , vol.14 , pp. 230-239
    • Kouroku, Y.1    Fujita, E.2    Tanida, I.3    Ueno, T.4    Isoai, A.5    Kumagai, H.6
  • 88
    • 0034672063 scopus 로고    scopus 로고
    • Erk1/2-dependent phosphorylation of Gα-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells
    • Ogier-Denis E, Pattingre S, El Benna J, Codogno P. Erk1/2-dependent phosphorylation of Gα-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells. J Biol Chem 2000; 275:39090-5.
    • (2000) J Biol Chem , vol.275 , pp. 39090-39095
    • Ogier-Denis, E.1    Pattingre, S.2    El Benna, J.3    Codogno, P.4
  • 89
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, A ULK-interacting protein is required for autophagosome formation in mammalian cells
    • Hara T, Takamura A, Kishi C, Iemura S, Natsume T, Guan JL, 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    Iemura, S.4    Natsume, T.5    Guan, J.L.6
  • 90
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao J, Brault JJ, Schild A, Cao P, Sandri M, Schiaffino S, et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 2007; 6:472-83.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6
  • 91
    • 36549042562 scopus 로고    scopus 로고
    • FoxO3 controls dangerous proteolytic liaisons
    • Attaix D, Bechet D. FoxO3 controls dangerous proteolytic liaisons. Cell Metab 2007; 6:425-7.
    • (2007) Cell Metab , vol.6 , pp. 425-427
    • Attaix, D.1    Bechet, D.2
  • 92
    • 76149086512 scopus 로고    scopus 로고
    • FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport
    • Pankiv S, Alemu EA, Brech A, Bruun JA, Lamark T, Øvervatn A, et al. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J Cell Biol; 188:253-69.
    • J Cell Biol , vol.188 , pp. 253-269
    • Pankiv, S.1    Alemu, E.A.2    Brech, A.3    Bruun, J.A.4    Lamark, T.5    Øvervatn, A.6
  • 93
    • 0034727876 scopus 로고    scopus 로고
    • Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: Possible role of vesicular transport in axonal elongation
    • Okazaki N, Yan J, Yuasa S, Ueno T, Kominami E, Masuho Y, et al. Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation. Brain Res Mol Brain Res 2000; 85:1-12.
    • (2000) Brain Res Mol Brain Res , vol.85 , pp. 1-12
    • Okazaki, N.1    Yan, J.2    Yuasa, S.3    Ueno, T.4    Kominami, E.5    Masuho, Y.6
  • 94
    • 0035910423 scopus 로고    scopus 로고
    • The human homologue 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 homologue 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; 276:1701-6.
    • (2001) J Biol Chem , vol.276 , pp. 1701-1706
    • Tanida, I.1    Tanida-Miyake, E.2    Ueno, T.3    Kominami, E.4
  • 95
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey UB, Nie Z, Batlevi Y, McCray BA, Ritson GP, Nedelsky NB, et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 2007; 447:859-63.
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3    McCray, B.A.4    Ritson, G.P.5    Nedelsky, N.B.6
  • 96
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 2005; 280:40282-92.
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 97
    • 77649337122 scopus 로고    scopus 로고
    • HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy
    • Lee JY, Koga H, Kawaguchi Y, Tang W, Wong E, Gao YS, et al. HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy. EMBO J 2010; 29:969-80.
    • (2010) EMBO J , vol.29 , pp. 969-980
    • Lee, J.Y.1    Koga, H.2    Kawaguchi, Y.3    Tang, W.4    Wong, E.5    Gao, Y.S.6
  • 98
    • 36148954660 scopus 로고    scopus 로고
    • The role of the hypoxia-inducible BH3-only proteins BNIP3 and BNIP3L in cancer
    • Mellor HR, Harris AL. The role of the hypoxia-inducible BH3-only proteins BNIP3 and BNIP3L in cancer. Cancer Metastasis Rev 2007; 26:553-66.
    • (2007) Cancer Metastasis Rev , vol.26 , pp. 553-566
    • Mellor, H.R.1    Harris, A.L.2
  • 100
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang H, Terlecky S, Plant C, et al. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 1989; 246:382-5.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.1    Terlecky, S.2    Plant, C.3
  • 101
    • 33748374920 scopus 로고    scopus 로고
    • Lysosome membrane lipid microdomains: Novel regulators of chaperone-mediated autophagy
    • Kaushik S, Massey AC, Cuervo AM. Lysosome membrane lipid microdomains: novel regulators of chaperone-mediated autophagy. EMBO J 2006; 25:3921-33.
    • (2006) EMBO J , vol.25 , pp. 3921-3933
    • Kaushik, S.1    Massey, A.C.2    Cuervo, A.M.3
  • 102
    • 51349130544 scopus 로고    scopus 로고
    • Dynamic organization of the receptor for chaperone- mediated autophagy at the lysosomal membrane
    • Bandhyopadhyay U, Kaushik S, Vartikovsky L, Cuervo AM. Dynamic organization of the receptor for chaperone- mediated autophagy at the lysosomal membrane. Mol Cell Biol 2008; 28:5747-63.
    • (2008) Mol Cell Biol , vol.28 , pp. 5747-5763
    • Bandhyopadhyay, U.1    Kaushik, S.2    Vartikovsky, L.3    Cuervo, A.M.4
  • 103
  • 105
    • 24744463111 scopus 로고    scopus 로고
    • Autophagy in innate and adaptive immunity
    • Deretic V. Autophagy in innate and adaptive immunity. Trends Immunol 2005; 26:523-8.
    • (2005) Trends Immunol , vol.26 , pp. 523-528
    • Deretic, V.1
  • 107
    • 33748506089 scopus 로고    scopus 로고
    • Human IRGM induces autophagy to eliminate intracellular mycobacteria
    • Singh SB, Davis AS, Taylor GA, Deretic V. Human IRGM induces autophagy to eliminate intracellular mycobacteria. Science 2006; 313:1438-41.
    • (2006) Science , vol.313 , pp. 1438-1441
    • Singh, S.B.1    Davis, A.S.2    Taylor, G.A.3    Deretic, V.4
  • 108
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • Wei Y, Pattingre S, Sinha S, Bassik M, Levine B. JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol Cell 2008; 30:678-88.
    • (2008) Mol Cell , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 112
    • 3042760943 scopus 로고    scopus 로고
    • Disturbed cholesterol traffic but normal proteolytic function in LAMP-1/ LAMP-2 double-deficient fibroblasts
    • Eskelinen E-L, Schmidt C, Neu S, Willenborg M, Fuertes G, Salvador N, et al. Disturbed cholesterol traffic but normal proteolytic function in LAMP-1/ LAMP-2 double-deficient fibroblasts. Mol Biol Cell 2004; 15:3132-45.
    • (2004) Mol Biol Cell , vol.15 , pp. 3132-3145
    • Eskelinen, E.-L.1    Schmidt, C.2    Neu, S.3    Willenborg, M.4    Fuertes, G.5    Salvador, N.6
  • 114
    • 0034329418 scopus 로고    scopus 로고
    • LC3, A mammalian homologueue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, et al. LC3, a mammalian homologueue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19:5720-8.
    • (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
  • 116
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin V, Lamark T, Sou YS, Bjørkøy G, Nunn JL, Bruun JA, et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell 2009; 33:505-16.
    • (2009) Mol Cell , vol.33 , pp. 505-516
    • Kirkin, V.1    Lamark, T.2    Sou, Y.S.3    Bjørkøy, G.4    Nunn, J.L.5    Bruun, J.A.6
  • 117
    • 33947250696 scopus 로고    scopus 로고
    • The energy sensing LKB1-AMPK pathway regulates p27(kip1) phosphorylation mediating the decision to enter autophagy or apoptosis
    • Liang J, Shao SH, Xu ZX, Hennessy B, Ding Z, Larrea M, et al. The energy sensing LKB1-AMPK pathway regulates p27(kip1) phosphorylation mediating the decision to enter autophagy or apoptosis. Nat Cell Biol 2007; 9:218-24.
    • (2007) Nat Cell Biol , vol.9 , pp. 218-224
    • Liang, J.1    Shao, S.H.2    Xu, Z.X.3    Hennessy, B.4    Ding, Z.5    Larrea, M.6
  • 118
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • Blommaart EF, Krause U, Schellens JP, Vreeling- Sindelarova H, Meijer AJ. The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes. Eur J Biochem 1997; 243:240-6.
    • (1997) Eur J Biochem , vol.243 , pp. 240-246
    • Blommaart, E.F.1    Krause, U.2    Schellens, J.P.3    Vreeling- Sindelarova, H.4    Meijer, A.J.5
  • 119
    • 0028836002 scopus 로고
    • Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles
    • Biederbick A, Kern HF, Elsasser HP. Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles. Eur J Cell Biol 1995; 66:3-14.
    • (1995) Eur J Cell Biol , vol.66 , pp. 3-14
    • Biederbick, A.1    Kern, H.F.2    Elsasser, H.P.3
  • 120
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky DJ, Abeliovich H, Agostinis P, Agrawal DK, Aliev G, Askew DS, et al. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 2008; 4:151-75.
    • (2008) Autophagy , vol.4 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3    Agrawal, D.K.4    Aliev, G.5    Askew, D.S.6
  • 121
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters JJ. Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res 2005; 8:3-5.
    • (2005) Rejuvenation Res , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 122
  • 123
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston TL, Ryzhakov G, Bloor S, von Muhlinen N, Randow F. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat Immunol 2009; 10:1215-21.
    • (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
  • 126
    • 73849121209 scopus 로고    scopus 로고
    • Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry
    • Travassos LH, Carneiro LA, Ramjeet M, Hussey S, Kim YG, Magalhaes JG, et al. Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry. Nat Immunol 2010; 11:55-62.
    • (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
  • 127
    • 75649085703 scopus 로고    scopus 로고
    • Coordinated regulation of autophagy by p38α MAPK through mAtg9 and p38IP
    • Webber JL, Tooze SA. Coordinated regulation of autophagy by p38α MAPK through mAtg9 and p38IP. EMBO J; 29:27-40.
    • EMBO J , vol.29 , pp. 27-40
    • Webber, J.L.1    Tooze, S.A.2
  • 129
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy G, Lamark T, Brech A, Outzen H, Perander M, Øvervatn A, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005; 171:603-14.
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Øvervatn, A.6
  • 130
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, Youle RJ. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 2008; 183:795-803.
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 131
    • 34248581861 scopus 로고    scopus 로고
    • Atg9 trafficking in autophagy-related pathways
    • He C, Klionsky DJ. Atg9 trafficking in autophagy-related pathways. Autophagy 2007; 3:271-4.
    • (2007) Autophagy , vol.3 , pp. 271-274
    • He, C.1    Klionsky, D.J.2
  • 132
    • 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, Mizushima N, Noda T, Ohsumi Y. The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO J 2001; 20:5971-81.
    • (2001) EMBO J , vol.20 , pp. 5971-5981
    • Suzuki, K.1    Kirisako, T.2    Kamada, Y.3    Mizushima, N.4    Noda, T.5    Ohsumi, Y.6
  • 133
    • 0030917085 scopus 로고    scopus 로고
    • Protein transport from the cytoplasm into the vacuole
    • Klionsky DJ. Protein transport from the cytoplasm into the vacuole. J Membr Biol 1997; 157:105-15.
    • (1997) J Membr Biol , vol.157 , pp. 105-115
    • Klionsky, D.J.1
  • 137
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda RK, Cherra SJ, 3rd, Kulich SM, Tandon A, Park D, Chu CT. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem 2009; 284:13843-55.
    • (2009) J Biol Chem , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra III, S.J.2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 138
    • 33644609471 scopus 로고    scopus 로고
    • PKR-dependent autophagic degradation of herpes simplex virus type 1
    • Tallóczy Z, Virgin HW, IV, Levine B. PKR-dependent autophagic degradation of herpes simplex virus type 1. Autophagy 2006; 2:24-9.
    • (2006) Autophagy , vol.2 , pp. 24-29
    • Tallóczy, Z.1    Virgin IV, H.W.2    Levine, B.3
  • 139
    • 47849094901 scopus 로고    scopus 로고
    • Autophagic control of listeria through intracellular innate immune recognition in drosophila
    • Yano T, Mita S, Ohmori H, Oshima Y, Fujimoto Y, Ueda R, et al. Autophagic control of listeria through intracellular innate immune recognition in drosophila. Nat Immunol 2008; 9:908-16.
    • (2008) Nat Immunol , vol.9 , pp. 908-916
    • Yano, T.1    Mita, S.2    Ohmori, H.3    Oshima, Y.4    Fujimoto, Y.5    Ueda, R.6
  • 141
    • 52449146523 scopus 로고
    • Filipin labelling and intramembrane particles on the membranes of early and later autophagic vacuoles in Ehrlich ascites cells
    • Punnonen E-L, Reunanen H, Hirsimaki P, Lounatmaa K. Filipin labelling and intramembrane particles on the membranes of early and later autophagic vacuoles in Ehrlich ascites cells. Virchows Arch B Cell Pathol Incl Mol Pathol 1988; 54:317-26.
    • (1988) Virchows Arch B Cell Pathol Incl Mol Pathol , vol.54 , pp. 317-326
    • Punnonen, E.-L.1    Reunanen, H.2    Hirsimaki, P.3    Lounatmaa, K.4
  • 144
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in the Drosophila fat body
    • Scott RC, Schuldiner O, Neufeld TP. Role and regulation of starvation-induced autophagy in the Drosophila fat body. Dev Cell 2004; 7:167-78.
    • (2004) Dev Cell , vol.7 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3
  • 145
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • Kraft C, Deplazes A, Sohrmann M, Peter M. Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat Cell Biol 2008; 10:602-10.
    • (2008) Nat Cell Biol , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 146
    • 34948828483 scopus 로고    scopus 로고
    • Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae
    • Yorimitsu T, Zaman S, Broach JR, Klionsky DJ. Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae. Mol Biol Cell 2007; 18:4180-9.
    • (2007) Mol Biol Cell , vol.18 , pp. 4180-4189
    • Yorimitsu, T.1    Zaman, S.2    Broach, J.R.3    Klionsky, D.J.4
  • 147
    • 64049086758 scopus 로고    scopus 로고
    • Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
    • Matsunaga K, Saitoh T, Tabata K, Omori H, Satoh T, Kurotori N, et al. Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol 2009; 11:385-96.
    • (2009) Nat Cell Biol , vol.11 , pp. 385-396
    • Matsunaga, K.1    Saitoh, T.2    Tabata, K.3    Omori, H.4    Satoh, T.5    Kurotori, N.6
  • 148
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol- 3-kinase complex
    • Zhong Y, Wang QJ, Li X, Yan Y, Backer JM, Chait BT, et al. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol- 3-kinase complex. Nat Cell Biol 2009; 11:468-76.
    • (2009) Nat Cell Biol , vol.11 , pp. 468-476
    • Zhong, Y.1    Wang, Q.J.2    Li, X.3    Yan, Y.4    Backer, J.M.5    Chait, B.T.6
  • 149
    • 58249085224 scopus 로고    scopus 로고
    • SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans
    • Zhang Y, Yan L, Zhou Z, Yang P, Tian E, Zhang K, et al. SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans. Cell 2009; 136:308-21.
    • (2009) Cell , vol.136 , pp. 308-321
    • Zhang, Y.1    Yan, L.2    Zhou, Z.3    Yang, P.4    Tian, E.5    Zhang, K.6
  • 152
    • 0029867412 scopus 로고    scopus 로고
    • The metabolism of sphingo(glyco)lipids is correlated with the differentiation- dependent autophagic pathway in HT-29 cells
    • Ghidoni R, Houri JJ, Giuliani A, Ogier-Denis E, Parolari E, Botti S, et al. The metabolism of sphingo(glyco)lipids is correlated with the differentiation- dependent autophagic pathway in HT-29 cells. Eur J Biochem 1996; 237:454-9.
    • (1996) Eur J Biochem , vol.237 , pp. 454-459
    • Ghidoni, R.1    Houri, J.J.2    Giuliani, A.3    Ogier-Denis, E.4    Parolari, E.5    Botti, S.6
  • 153
    • 33846192839 scopus 로고    scopus 로고
    • Is autophagy the key mechanism by which the sphingolipid rheostat controls the cell fate decision?
    • Lavieu G, Scarlatti F, Sala G, Levade T, Ghidoni R, Botti J, et al. Is autophagy the key mechanism by which the sphingolipid rheostat controls the cell fate decision? Autophagy 2007; 3:45-7.
    • (2007) Autophagy , vol.3 , pp. 45-47
    • Lavieu, G.1    Scarlatti, F.2    Sala, G.3    Levade, T.4    Ghidoni, R.5    Botti, J.6
  • 155
    • 58149374223 scopus 로고    scopus 로고
    • High-throughput functional screening for autophagy-related genes and identification of TM9SF1 as an autophagosome-inducing gene
    • He P, Peng Z, Luo Y, Wang L, Yu P, Deng W, et al. High-throughput functional screening for autophagy-related genes and identification of TM9SF1 as an autophagosome-inducing gene. Autophagy 2009; 5:52-60.
    • (2009) Autophagy , vol.5 , pp. 52-60
    • He, P.1    Peng, Z.2    Luo, Y.3    Wang, L.4    Yu, P.5    Deng, W.6
  • 156
    • 40949132464 scopus 로고    scopus 로고
    • TMEM74, A lysosome and autophagosome protein, regulates autophagy
    • Yu C, Wang L, Lv B, Lu Y, Zeng L, Chen Y, et al. TMEM74, a lysosome and autophagosome protein, regulates autophagy. Biochem Biophys Res Commun 2008; 369:622-9.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 622-629
    • Yu, C.1    Wang, L.2    Lv, B.3    Lu, Y.4    Zeng, L.5    Chen, Y.6
  • 157
    • 34250824671 scopus 로고    scopus 로고
    • TMEM166, A novel transmembrane protein, regulates cell autophagy and apoptosis
    • Wang L, Yu C, Lu Y, He P, Guo J, Zhang C, et al. TMEM166, a novel transmembrane protein, regulates cell autophagy and apoptosis. Apoptosis 2007; 12:1489-502.
    • (2007) Apoptosis , vol.12 , pp. 1489-1502
    • Wang, L.1    Yu, C.2    Lu, Y.3    He, P.4    Guo, J.5    Zhang, C.6
  • 158
    • 52049091512 scopus 로고    scopus 로고
    • What controls TOR?
    • Jacinto E. What controls TOR? IUBMB Life 2008; 60:483-96.
    • (2008) IUBMB Life , vol.60 , pp. 483-496
    • Jacinto, E.1
  • 159
    • 67349241955 scopus 로고    scopus 로고
    • DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival
    • Peterson TR, Laplante M, Thoreen CC, Sancak Y, Kang SA, Kuehl WM, et al. DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell 2009; 137:873-86.
    • (2009) Cell , vol.137 , pp. 873-886
    • Peterson, T.R.1    Laplante, M.2    Thoreen, C.C.3    Sancak, Y.4    Kang, S.A.5    Kuehl, W.M.6
  • 160
    • 34347210090 scopus 로고    scopus 로고
    • Identification of Protor as a novel Rictor-binding component of mTOR complex- 2
    • Pearce LR, Huang X, Boudeau J, Pawlowski R, Wullschleger S, Deak M, et al. Identification of Protor as a novel Rictor-binding component of mTOR complex- 2. Biochem J 2007; 405:513-22.
    • (2007) Biochem J , vol.405 , pp. 513-522
    • Pearce, L.R.1    Huang, X.2    Boudeau, J.3    Pawlowski, R.4    Wullschleger, S.5    Deak, M.6
  • 161
    • 65549145048 scopus 로고    scopus 로고
    • An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1
    • Thoreen CC, Kang SA, Chang JW, Liu Q, Zhang J, Gao Y, et al. An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1. J Biol Chem 2009; 284:8023-32.
    • (2009) J Biol Chem , vol.284 , pp. 8023-8032
    • Thoreen, C.C.1    Kang, S.A.2    Chang, J.W.3    Liu, Q.4    Zhang, J.5    Gao, Y.6
  • 164
    • 59649110865 scopus 로고    scopus 로고
    • PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation
    • N'Diaye EN, Kajihara KK, Hsieh I, Morisaki H, Debnath J, Brown EJ. PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation. EMBO Rep 2009; 10:173-9.
    • (2009) EMBO Rep , vol.10 , pp. 173-179
    • N'Diaye, E.N.1    Kajihara, K.K.2    Hsieh, I.3    Morisaki, H.4    Debnath, J.5    Brown, E.J.6
  • 165
    • 34548482499 scopus 로고    scopus 로고
    • siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy
    • Chan EYW, Kir S, Tooze SA. siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy. J Biol Chem 2007; 282:25464-74.
    • (2007) J Biol Chem , vol.282 , pp. 25464-25474
    • Chan, E.Y.W.1    Kir, S.2    Tooze, S.A.3
  • 166
    • 33750366092 scopus 로고    scopus 로고
    • Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
    • Young ARJ, Chan EYW, Hu XW, Köchl R, Crawshaw SG, High S, et al. Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci 2006; 119:3888-900.
    • (2006) J Cell Sci , vol.119 , pp. 3888-3900
    • Young, A.R.J.1    Chan, E.Y.W.2    Hu, X.W.3    Köchl, R.4    Crawshaw, S.G.5    High, S.6
  • 167
    • 84883055574 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.
    • Curr Opin Cell Biol
    • Mizushima, N.1
  • 168
    • 33745751085 scopus 로고    scopus 로고
    • Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
    • Liang C, Feng P, Ku B, Dotan I, Canaani D, Oh BH, et al. Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG. Nat Cell Biol 2006; 8:688-99.
    • (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
  • 169
    • 0029844569 scopus 로고    scopus 로고
    • Isolation of degradationdeficient mutants defective in the targeting of fructose- 1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae
    • Hoffman M, Chiang H-L. Isolation of degradationdeficient mutants defective in the targeting of fructose- 1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae. Genetics 1996; 143:1555-66.
    • (1996) Genetics , vol.143 , pp. 1555-1566
    • Hoffman, M.1    Chiang, H.-L.2
  • 170
    • 41449102022 scopus 로고    scopus 로고
    • A novel mammalian trans-membrane protein reveals an alternative initiation pathway for autophagy
    • Vaccaro MI, Ropolo A, Grasso D, Iovanna JL. A novel mammalian trans-membrane protein reveals an alternative initiation pathway for autophagy. Autophagy 2008; 4:388-90.
    • (2008) Autophagy , vol.4 , pp. 388-390
    • Vaccaro, M.I.1    Ropolo, A.2    Grasso, D.3    Iovanna, J.L.4
  • 171
    • 37549012209 scopus 로고    scopus 로고
    • The pancreatitis-induced vacuole membrane protein 1 triggers autophagy in mammalian cells
    • Ropolo A, Grasso D, Pardo R, Sacchetti ML, Archange C, Lo Re A, et al. The pancreatitis-induced vacuole membrane protein 1 triggers autophagy in mammalian cells. J Biol Chem 2007; 282:37124-33.
    • (2007) J Biol Chem , vol.282 , pp. 37124-37133
    • Ropolo, A.1    Grasso, D.2    Pardo, R.3    Sacchetti, M.L.4    Archange, C.5    Lo Re, A.6
  • 172
    • 11244289333 scopus 로고    scopus 로고
    • WIPI-1α (WIPI49), A member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy
    • Proikas-Cezanne T, Waddell S, Gaugel A, Frickey T, Lupas A, Nordheim A. WIPI-1α (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy. Oncogene 2004; 23:9314-25.
    • (2004) Oncogene , vol.23 , pp. 9314-9325
    • Proikas-Cezanne, T.1    Waddell, S.2    Gaugel, A.3    Frickey, T.4    Lupas, A.5    Nordheim, A.6
  • 173
    • 57249083972 scopus 로고    scopus 로고
    • Structural basis of target recognition by Atg8/LC3 during selective autophagy
    • Noda NN, Kumeta H, Nakatogawa H, Satoo K, Adachi W, Ishii J, et al. Structural basis of target recognition by Atg8/LC3 during selective autophagy. Genes Cells 2008; 13:1211-8.
    • (2008) Genes Cells , vol.13 , pp. 1211-1218
    • Noda, N.N.1    Kumeta, H.2    Nakatogawa, H.3    Satoo, K.4    Adachi, W.5    Ishii, J.6
  • 174
    • 65749101996 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in the intestinal epithelium and inflammatory bowel disease
    • Kaser A, Blumberg RS. Endoplasmic reticulum stress in the intestinal epithelium and inflammatory bowel disease. Semin Immunol 2009; 21:156-63.
    • (2009) Semin Immunol , vol.21 , pp. 156-163
    • Kaser, A.1    Blumberg, R.S.2
  • 175
    • 12944308330 scopus 로고    scopus 로고
    • Eating oneself and uninvited guests: Autophagy-related pathways in cellular defense
    • Levine B. Eating oneself and uninvited guests: autophagy-related pathways in cellular defense. Cell 2005; 120:159-62.
    • (2005) Cell , vol.120 , pp. 159-162
    • Levine, B.1


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