메뉴 건너뛰기




Volumn 3, Issue 3, 2007, Pages 181-206

Methods for monitoring autophagy from yeast to human

Author keywords

Assay; Lysosome; Protein degradation; Protein targeting; Trafficking; Vacuole

Indexed keywords

3 METHYLADENINE; ACETYL COENZYME A ACYLTRANSFERASE; ALKALINE PHOSPHATASE; ALPHA MANNOSIDASE; CALCIUM CHELATING AGENT; CHAPERONE; CYCLIC AMP; CYSTEINE; DANSYLCADAVERINE; GREEN FLUORESCENT PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 1; OKADAIC ACID; PHOSPHATIDYLETHANOLAMINE; PROTEINASE; SERINE; THAPSIGARGIN;

EID: 34248583762     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.3678     Document Type: Review
Times cited : (590)

References (249)
  • 1
    • 0033791650 scopus 로고    scopus 로고
    • Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells
    • Kim J, Klionsky DJ. Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells. Annu Rev Biochem 2000; 69:303-42.
    • (2000) Annu Rev Biochem , vol.69 , pp. 303-342
    • Kim, J.1    Klionsky, D.J.2
  • 2
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky DJ, Emr SD. Autophagy as a regulated pathway of cellular degradation. Science 2000; 290:1717-21.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 3
    • 0033280667 scopus 로고    scopus 로고
    • Vacuolar import of proteins and organelles from the cytoplasm
    • Klionsky DJ, Ohsumi Y. Vacuolar import of proteins and organelles from the cytoplasm. Annu Rev Cell Dev Biol 1999; 15:1-32.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 1-32
    • Klionsky, D.J.1    Ohsumi, Y.2
  • 4
    • 0036463736 scopus 로고    scopus 로고
    • Autophagy in the eukaryotic cell
    • Reggiori F, Klionsky DJ. Autophagy in the eukaryotic cell. Eukaryot Cell 2002; 1:11-21.
    • (2002) Eukaryot Cell , vol.1 , pp. 11-21
    • Reggiori, F.1    Klionsky, D.J.2
  • 5
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine B, Klionsky DJ. Development by self-digestion: Molecular mechanisms and biological functions of autophagy. Dev Cell 2004; 6:463-77.
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 6
    • 0442323561 scopus 로고    scopus 로고
    • Cuervo AM. Autophagy. In sickness and in health. Trends Cell Biol 2004; 14:70-7.
    • Cuervo AM. Autophagy. In sickness and in health. Trends Cell Biol 2004; 14:70-7.
  • 7
    • 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; 306:990-5.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 9
    • 0038309329 scopus 로고    scopus 로고
    • The molecular mechanism of autophagy
    • Wang CW, Klionsky DJ. The molecular mechanism of autophagy. Mol Med 2003; 9:65-76.
    • (2003) Mol Med , vol.9 , pp. 65-76
    • Wang, C.W.1    Klionsky, D.J.2
  • 10
    • 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
  • 11
    • 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; 280:41785-8.
    • (2005) J Biol Chem , vol.280 , pp. 41785-41788
    • Nair, U.1    Klionsky, D.J.2
  • 12
    • 1342321743 scopus 로고    scopus 로고
    • Two ubiquitin-like conjugation systems essential for autophagy
    • Ohsumi Y, Mizushima N. Two ubiquitin-like conjugation systems essential for autophagy. Semin Cell Dev Biol 2004; 15:231-6.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 231-236
    • Ohsumi, Y.1    Mizushima, N.2
  • 13
    • 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; 12:1542-52.
    • (2005) Cell Death Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 14
    • 1842419925 scopus 로고    scopus 로고
    • Regulation of autophagy by the target of rapamycin (Tor) proteins
    • Klionsky DJ, ed, Georgetown, TX: Landes Bioscience
    • Abeliovich H. Regulation of autophagy by the target of rapamycin (Tor) proteins. In: Klionsky DJ, ed. Autophagy. Georgetown, TX: Landes Bioscience, 2004. Pg. 60-9.
    • (2004) Autophagy , pp. 60-69
    • Abeliovich, H.1
  • 15
    • 0345825057 scopus 로고    scopus 로고
    • Signaling pathways in mammalian autophagy
    • Klionsky DJ, ed, Georgetown, TX: Landes Bioscience
    • Codogno P, Meijer AJ. Signaling pathways in mammalian autophagy. In: Klionsky DJ, ed. Autophagy. Georgetown, TX: Landes Bioscience, 2004. Pg.26-47.
    • (2004) Autophagy , pp. 26-47
    • Codogno, P.1    Meijer, A.J.2
  • 16
    • 1842419926 scopus 로고    scopus 로고
    • Structural aspects of mammalian autophagy
    • Klionsky DJ, ed, Georgetown, TX: Landes Bioscience
    • Fengsrud M, Sneve ML, Øverbye A, Seglen PO. Structural aspects of mammalian autophagy. In: Klionsky DJ, ed. Autophagy. Georgetown, TX: Landes Bioscience, 2004. Pg. 11-25.
    • (2004) Autophagy , pp. 11-25
    • Fengsrud, M.1    Sneve, M.L.2    Øverbye, A.3    Seglen, P.O.4
  • 17
    • 85011939675 scopus 로고    scopus 로고
    • Wang C-W, Klionsky DJ. Microautophagy. In: Klionsky DJ, ed. Autophagy. Georgetown, TX: Landes Bioscience, 2004. 107-14.
    • Wang C-W, Klionsky DJ. Microautophagy. In: Klionsky DJ, ed. Autophagy. Georgetown, TX: Landes Bioscience, 2004. Pg. 107-14.
  • 18
    • 22044442015 scopus 로고    scopus 로고
    • Autophagosomes: Biogenesis from scratch?
    • Reggiori F, Klionsky DJ. Autophagosomes: Biogenesis from scratch? Curr Opin Cell Biol 2005; 17:415-22.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 415-422
    • Reggiori, F.1    Klionsky, D.J.2
  • 19
    • 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
  • 20
    • 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; 3:825-37.
    • (2002) Dev Cell , vol.3 , pp. 825-837
    • Shintani, T.1    Huang, W.-P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 21
    • 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
  • 22
    • 0037086618 scopus 로고    scopus 로고
    • Yeast vacuoles and membrane fusion pathways
    • Wickner W. Yeast vacuoles and membrane fusion pathways. EMBO J 2002; 21:1241-7.
    • (2002) EMBO J , vol.21 , pp. 1241-1247
    • Wickner, W.1
  • 23
    • 0014939582 scopus 로고
    • Inhibition by insulin of valine turnover in liver: Evidence for a general control of proteolysis
    • Mortimore GE, Mondon CE. Inhibition by insulin of valine turnover in liver: Evidence for a general control of proteolysis. J Biol Chem 1970; 245:2375-83.
    • (1970) J Biol Chem , vol.245 , pp. 2375-2383
    • Mortimore, G.E.1    Mondon, C.E.2
  • 24
    • 0018746575 scopus 로고
    • Glucagon-induced autophagy and proteolysis in rat liver: Mediation by selective deprivation of intracellular amino acids
    • Schworer CM, Mortimore GE. Glucagon-induced autophagy and proteolysis in rat liver: Mediation by selective deprivation of intracellular amino acids. Proc Natl Acad Sci USA 1979; 76:3169-73.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3169-3173
    • Schworer, C.M.1    Mortimore, G.E.2
  • 25
    • 0005677775 scopus 로고
    • 3-Methyladenine: Specific inhibitor of autophagic/lysosomal pro-tein degradation in isolated rat hepatocytes
    • Seglen PO, Gordon PB. 3-Methyladenine: Specific inhibitor of autophagic/lysosomal pro-tein degradation in isolated rat hepatocytes. Proc Natl Acad Sci USA 1982; 79:1889-92.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Gordon, P.B.2
  • 26
    • 0022356564 scopus 로고
    • Use of digitonin extraction to distinguish between autophagic-lysosomal sequestration and mitochondrial uptake of [14C]sucrose in hepatocytes
    • Gordon PB, Tolleshaug H, Seglen PO. Use of digitonin extraction to distinguish between autophagic-lysosomal sequestration and mitochondrial uptake of [14C]sucrose in hepatocytes. Biochem J 1985; 232:773-80.
    • (1985) Biochem J , vol.232 , pp. 773-780
    • Gordon, P.B.1    Tolleshaug, H.2    Seglen, P.O.3
  • 29
    • 0025051251 scopus 로고
    • Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes
    • Kopitz J, Kisen GØ, Gordon PB, Bohley P, Seglen PO. Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes. J Cell Biol 1990; 111:941-53.
    • (1990) J Cell Biol , vol.111 , pp. 941-953
    • Kopitz, J.1    Kisen, G.2    Gordon, P.B.3    Bohley, P.4    Seglen, P.O.5
  • 30
    • 0025858399 scopus 로고
    • Inhibition of autophagic-lysosomal delivery and autophagic lactolysis by aspatagine
    • Høyvik H, Gordon PB, Berg TO, Strømhaug PE, Seglen PO. Inhibition of autophagic-lysosomal delivery and autophagic lactolysis by aspatagine. J Cell Biol 1991; 113:1305-12.
    • (1991) J Cell Biol , vol.113 , pp. 1305-1312
    • Høyvik, H.1    Gordon, P.B.2    Berg, T.O.3    Strømhaug, P.E.4    Seglen, P.O.5
  • 31
    • 0027716683 scopus 로고
    • Tracing intracellular proteolytic pathways: Proteolysis of fatty acid synthase and other cytoplasmic proteins in the yeast Saccharomyces cerevisiae
    • Egner R, Thumm M, Straub M, Simeon A, Schuller HJ, Wolf DH. Tracing intracellular proteolytic pathways: Proteolysis of fatty acid synthase and other cytoplasmic proteins in the yeast Saccharomyces cerevisiae. J Biol Chem 1993; 268:27269-76.
    • (1993) J Biol Chem , vol.268 , pp. 27269-27276
    • Egner, R.1    Thumm, M.2    Straub, M.3    Simeon, A.4    Schuller, H.J.5    Wolf, D.H.6
  • 32
    • 0029036915 scopus 로고
    • Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae
    • Noda T, Matsuura A, Wada Y, Ohsumi Y. Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun 1995; 210:126-32.
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 126-132
    • Noda, T.1    Matsuura, A.2    Wada, Y.3    Ohsumi, Y.4
  • 36
    • 2142752480 scopus 로고    scopus 로고
    • Cellular autophagy: Surtender, avoidance and subversion by microorganisms
    • Kirkegaard K, Taylor MP, Jackson WT. Cellular autophagy: Surtender, avoidance and subversion by microorganisms. Nat Rev Microbiol 2004; 2:301-14.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 301-314
    • Kirkegaard, K.1    Taylor, M.P.2    Jackson, W.T.3
  • 37
    • 4344712684 scopus 로고    scopus 로고
    • Methods for monitoring autophagy
    • Mizushima N. Methods for monitoring autophagy. Int J Biochem Cell Biol 2004; 36:2491-502.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2491-2502
    • Mizushima, N.1
  • 38
    • 0002549377 scopus 로고
    • The lysosome
    • de Duve C. The lysosome. Sci Am 1963; 208:64-72.
    • (1963) Sci Am , vol.208 , pp. 64-72
    • de Duve, C.1
  • 40
    • 0014359297 scopus 로고
    • Studies on cellular autophagocytosis: The formation of autophagic vacuoles in the liver after glucagon administration
    • Arstila AU, Trump BF. Studies on cellular autophagocytosis: The formation of autophagic vacuoles in the liver after glucagon administration. Am J Pathol 1968; 53:687-733.
    • (1968) Am J Pathol , vol.53 , pp. 687-733
    • Arstila, A.U.1    Trump, B.F.2
  • 41
    • 0034721869 scopus 로고    scopus 로고
    • Selective degtadation of annexins by chaperone-mediated autophagy
    • Cuervo AM, Gomes AV, Barnes JA, Dice JF. Selective degtadation of annexins by chaperone-mediated autophagy. J Biol Chem 2000; 275:33329-35.
    • (2000) J Biol Chem , vol.275 , pp. 33329-33335
    • Cuervo, A.M.1    Gomes, A.V.2    Barnes, J.A.3    Dice, J.F.4
  • 42
    • 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
  • 43
    • 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
  • 44
    • 0023665218 scopus 로고
    • Amino acid and hormonal control of macromolecular turnover in perfused rat liver: Evidence for selective autophagy
    • Lardeux BR, Mortimore GE. Amino acid and hormonal control of macromolecular turnover in perfused rat liver: Evidence for selective autophagy. J Biol Chem 1987; 262:14514-9.
    • (1987) J Biol Chem , vol.262 , pp. 14514-14519
    • Lardeux, B.R.1    Mortimore, G.E.2
  • 45
    • 0018763480 scopus 로고
    • Inhibition of the lysosomal pathway of ptotein degtadation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin
    • Seglen PO, Gtinde B, Solheim AE. Inhibition of the lysosomal pathway of ptotein degtadation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin. Eur J Biochem 1979; 95:215-25.
    • (1979) Eur J Biochem , vol.95 , pp. 215-225
    • Seglen, P.O.1    Gtinde, B.2    Solheim, A.E.3
  • 46
    • 0018927246 scopus 로고
    • Amino acid inhibition of the autophagic/lysosomal pathway of protein degradation in isolated rat hepatocytes
    • Seglen PO, Gordon PB, Poli A. Amino acid inhibition of the autophagic/lysosomal pathway of protein degradation in isolated rat hepatocytes. Biochim Biophys Acta 1980; 630:103-18.
    • (1980) Biochim Biophys Acta , vol.630 , pp. 103-118
    • Seglen, P.O.1    Gordon, P.B.2    Poli, A.3
  • 47
    • 0018533425 scopus 로고
    • Protein synthesis and protein degradation through the cell cycle of human NHIK 3025 cells in vitro
    • Rønning ØW, Pettersen EO, Seglen PO. Protein synthesis and protein degradation through the cell cycle of human NHIK 3025 cells in vitro. Exp Cell Res 1979; 123:63-72.
    • (1979) Exp Cell Res , vol.123 , pp. 63-72
    • Rønning, O.1    Pettersen, E.O.2    Seglen, P.O.3
  • 48
    • 0019417043 scopus 로고
    • Inhibition of autophagic vacuole formation and protein degradation by amino acids in isolated hepatocytes
    • Kovács AL, Grinde B, Seglen PO. Inhibition of autophagic vacuole formation and protein degradation by amino acids in isolated hepatocytes. Exp Cell Res 1981; 133:431-6.
    • (1981) Exp Cell Res , vol.133 , pp. 431-436
    • Kovács, A.L.1    Grinde, B.2    Seglen, P.O.3
  • 49
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • Fuertes G, Martin De Llano JJ, Villarroya A, Rivett AJ, Knecht E. Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem J 2003; 375:75-86.
    • (2003) Biochem J , vol.375 , pp. 75-86
    • Fuertes, G.1    Martin De Llano, J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 51
    • 0022384018 scopus 로고
    • Reduced autophagic activity, improved protein balance and enhanced in vitro survival of hepatocytes isolated from carcinogen-treated rats
    • Schwarze PE, Seglen PO. Reduced autophagic activity, improved protein balance and enhanced in vitro survival of hepatocytes isolated from carcinogen-treated rats. Exp Cell Res 1985; 157:15-28.
    • (1985) Exp Cell Res , vol.157 , pp. 15-28
    • Schwarze, P.E.1    Seglen, P.O.2
  • 52
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • Blommaart EFC, Krause U, Schellens JPM, Vreeling- Sindelárová 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.C.1    Krause, U.2    Schellens, J.P.M.3    Vreeling- Sindelárová, H.4    Meijer, A.J.5
  • 54
    • 0036685158 scopus 로고    scopus 로고
    • Inhibition of mitochondrial permeability transition and release of cytochrome c by anti-apoptotic nucleoside analogues
    • Xue L, Borutaite V, Tolkovsky AM. Inhibition of mitochondrial permeability transition and release of cytochrome c by anti-apoptotic nucleoside analogues. Biochem Pharmacol 2002; 64:441-9.
    • (2002) Biochem Pharmacol , vol.64 , pp. 441-449
    • Xue, L.1    Borutaite, V.2    Tolkovsky, A.M.3
  • 55
    • 0025694803 scopus 로고
    • Both endocytic and endogenous protein degradation in fibroblasts is stimulated by serum/amino acid deprivation and inhibited by 3-methyladenine
    • Hendil KB, Lauridsen AMB, Seglen PO. Both endocytic and endogenous protein degradation in fibroblasts is stimulated by serum/amino acid deprivation and inhibited by 3-methyladenine. Biochem J 1990; 272:577-81.
    • (1990) Biochem J , vol.272 , pp. 577-581
    • Hendil, K.B.1    Lauridsen, A.M.B.2    Seglen, P.O.3
  • 56
    • 0027945432 scopus 로고
    • 3-Methyladenine inhibits transport from late endosomes to lysosomes in cultured rat and mouse fibroblasts
    • Punnonen E-L, Marjomäki VS, Reunanen H. 3-Methyladenine inhibits transport from late endosomes to lysosomes in cultured rat and mouse fibroblasts. Eur J Cell Biol 1994; 65:14-25.
    • (1994) Eur J Cell Biol , vol.65 , pp. 14-25
    • Punnonen, E.-L.1    Marjomäki, V.S.2    Reunanen, H.3
  • 57
    • 0022447864 scopus 로고
    • Use of a hydrolysable probe, [14C]lactose, to distinguish between prelysosomal and lysosomal sreps in the autophagic pathway
    • Høyvik H, Gordon PB, Seglen PO. Use of a hydrolysable probe, [14C]lactose, to distinguish between prelysosomal and lysosomal sreps in the autophagic pathway. Exp Cell Res 1986; 166:1-14.
    • (1986) Exp Cell Res , vol.166 , pp. 1-14
    • Høyvik, H.1    Gordon, P.B.2    Seglen, P.O.3
  • 58
    • 0027513693 scopus 로고
    • Evidence for acidity of prelysosomal autophagic/endocytic vacuoles (amphisomes)
    • Strømhaug PE, Seglen PO. Evidence for acidity of prelysosomal autophagic/endocytic vacuoles (amphisomes). Biochem J 1993; 291:115-21.
    • (1993) Biochem J , vol.291 , pp. 115-121
    • Strømhaug, P.E.1    Seglen, P.O.2
  • 59
    • 0017667822 scopus 로고
    • Evidence for the autophagy of microinjected proteins in HeLA cells
    • Stacey DW, Allfrey VG. Evidence for the autophagy of microinjected proteins in HeLA cells. J Cell Biol 1977; 75:807-17.
    • (1977) J Cell Biol , vol.75 , pp. 807-817
    • Stacey, D.W.1    Allfrey, V.G.2
  • 61
    • 0020334810 scopus 로고
    • Autophagic sequestration of [14C]sucrose, introduced into rat hepatocytes by reversible electro-permeabilization
    • Gordon PB, Seglen PO. Autophagic sequestration of [14C]sucrose, introduced into rat hepatocytes by reversible electro-permeabilization. Exp Cell Res 1982; 142:1-14.
    • (1982) Exp Cell Res , vol.142 , pp. 1-14
    • Gordon, P.B.1    Seglen, P.O.2
  • 62
    • 0022268071 scopus 로고
    • Autophagic sequestration of [14C]sucrose introduced into isolated rat hepatocytes by electrical and nonelectrical methods
    • Gordon PB, Tolleshaug H, Seglen PO. Autophagic sequestration of [14C]sucrose introduced into isolated rat hepatocytes by electrical and nonelectrical methods. Exp Cell Res 1985; 160:449-58.
    • (1985) Exp Cell Res , vol.160 , pp. 449-458
    • Gordon, P.B.1    Tolleshaug, H.2    Seglen, P.O.3
  • 63
    • 0032996570 scopus 로고    scopus 로고
    • Parasitophorous vacuoles of Leishmania mexicana acquire macro molecules from the host cell cytosol via two independent routes
    • Schaible UE, Schlesinger PH, Steinberg TH, Mangel WF, Kobayashi T, Russell DG. Parasitophorous vacuoles of Leishmania mexicana acquire macro molecules from the host cell cytosol via two independent routes. J Cell Sci 1999; 112:681-93.
    • (1999) J Cell Sci , vol.112 , pp. 681-693
    • Schaible, U.E.1    Schlesinger, P.H.2    Steinberg, T.H.3    Mangel, W.F.4    Kobayashi, T.5    Russell, D.G.6
  • 64
    • 0020321716 scopus 로고
    • Introduction of mactomolecules into cultured mammalian cells by osmotic lysis of pinocytic vesicles
    • Okada CY, Rechsteiner M. Introduction of mactomolecules into cultured mammalian cells by osmotic lysis of pinocytic vesicles. Cell 1982; 29:33-41.
    • (1982) Cell , vol.29 , pp. 33-41
    • Okada, C.Y.1    Rechsteiner, M.2
  • 66
    • 33645120442 scopus 로고    scopus 로고
    • Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes
    • Köchl R, Hu XW, Chan EYW, Tooze SA. Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes. Traffic 2006; 7:129-45.
    • (2006) Traffic , vol.7 , pp. 129-145
    • Köchl, R.1    Hu, X.W.2    Chan, E.Y.W.3    Tooze, S.A.4
  • 67
    • 0027296748 scopus 로고
    • Inhibition of hepatocytic autophagy by okadaic acid and othet protein phosphatase inhibitots
    • Holen I, Gordon PB, Seglen PO. Inhibition of hepatocytic autophagy by okadaic acid and othet protein phosphatase inhibitots. Eur J Biochem 1993; 215:113-22.
    • (1993) Eur J Biochem , vol.215 , pp. 113-122
    • Holen, I.1    Gordon, P.B.2    Seglen, P.O.3
  • 68
    • 0028957045 scopus 로고
    • Protection by naringin and some othet flavonoids of hepatocytic autophagy and endocytosis against inhibition by okadaic acid
    • Gordon PB, Holen I, Seglen PO. Protection by naringin and some othet flavonoids of hepatocytic autophagy and endocytosis against inhibition by okadaic acid. J Biol Chem 1995; 270:5830-8.
    • (1995) J Biol Chem , vol.270 , pp. 5830-5838
    • Gordon, P.B.1    Holen, I.2    Seglen, P.O.3
  • 70
    • 0033556037 scopus 로고    scopus 로고
    • αi3 ptotein and G alpha interacting protein, two proteins involved in the control of macroautophagy in human colon cancer HT-29 cells
    • αi3 ptotein and G alpha interacting protein, two proteins involved in the control of macroautophagy in human colon cancer HT-29 cells. Biochem J 1999; 337:289-95.
    • (1999) Biochem J , vol.337 , pp. 289-295
    • Petiot, A.1    Ogier-Denis, E.2    Bauvy, C.3    Cluzeaud, F.4    Vandewalle, A.5    Codogno, P.6
  • 72
    • 0029044483 scopus 로고
    • Vanadate inhibition of hepatocytic autophagy: Calcium-modulated and osmolality-modulated antagonism by asparagine
    • Fosse M, Berg TO, O'Reilly DS, Seglen PO. Vanadate inhibition of hepatocytic autophagy: Calcium-modulated and osmolality-modulated antagonism by asparagine. Eur J Biochem 1995; 230:17-24.
    • (1995) Eur J Biochem , vol.230 , pp. 17-24
    • Fosse, M.1    Berg, T.O.2    O'Reilly, D.S.3    Seglen, P.O.4
  • 73
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A, Ogier-Denis E, Blommaart EFC, Meijer AJ, Codogno P. Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 2000; 275:992-8.
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.C.3    Meijer, A.J.4    Codogno, P.5
  • 75
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky DJ, Herman PK, Emr SD. The fungal vacuole: Composition, function, and biogenesis. Microbiol Rev 1990; 54:266-92.
    • (1990) Microbiol Rev , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 76
    • 0024447838 scopus 로고
    • Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase
    • Klionsky DJ, Emr SD. Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase. EMBO J 1989; 8:2241-50.
    • (1989) EMBO J , vol.8 , pp. 2241-2250
    • Klionsky, D.J.1    Emr, S.D.2
  • 79
    • 34250900953 scopus 로고    scopus 로고
    • Kuma A, Matsui M, Mizushima N. LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy Caution in the interpretation of LC3 localization. Autophagy 2007; in press:
    • Kuma A, Matsui M, Mizushima N. LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy Caution in the interpretation of LC3 localization. Autophagy 2007; in press:
  • 80
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • Tanida I, Minematsu-Ikeguchi N, Ueno T, Kominami E. Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy 2005; 1:84-91.
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 82
    • 0030863299 scopus 로고    scopus 로고
    • Nutrient deprivation of cultured rat hepatocytes increases the desferrioxamine-available iron pool and augments the sensitivity ro hydrogen peroxide
    • Öllinger K, Roberg K. Nutrient deprivation of cultured rat hepatocytes increases the desferrioxamine-available iron pool and augments the sensitivity ro hydrogen peroxide. J Biol Chem 1997; 272:23707-11.
    • (1997) J Biol Chem , vol.272 , pp. 23707-23711
    • Öllinger, K.1    Roberg, K.2
  • 83
    • 1942424799 scopus 로고    scopus 로고
    • Inhibition of platelet-derived growth factor signalling induces autophagy in malignant glioma cells
    • Takeuchi H, Kanzawa T, Kondo Y, Kondo S. Inhibition of platelet-derived growth factor signalling induces autophagy in malignant glioma cells. Br J Cancer 2004; 90:1069-75.
    • (2004) Br J Cancer , vol.90 , pp. 1069-1075
    • Takeuchi, H.1    Kanzawa, T.2    Kondo, Y.3    Kondo, S.4
  • 84
    • 0020040519 scopus 로고
    • Accumulation of autophagosomes after inhibition of hepatocytic protein degradation by vinblastine, leupeptin or a lysosomotropic amine
    • Kovács AL, Reith A, Seglen PO. Accumulation of autophagosomes after inhibition of hepatocytic protein degradation by vinblastine, leupeptin or a lysosomotropic amine. Exp Cell Res 1982; 137:191-201.
    • (1982) Exp Cell Res , vol.137 , pp. 191-201
    • Kovács, A.L.1    Reith, A.2    Seglen, P.O.3
  • 85
    • 0028856914 scopus 로고
    • Ultrastructural and immunocytochemical characterization of autophagic vacuoles in isolated hepatocytes: Effects of vinblastine and asparagine on vacuole distributions
    • Fengsrud M, Roos N, Berg T, Liou W, Slot JW, Seglen PO. Ultrastructural and immunocytochemical characterization of autophagic vacuoles in isolated hepatocytes: Effects of vinblastine and asparagine on vacuole distributions. Exp Cell Res 1995; 221:504-19.
    • (1995) Exp Cell Res , vol.221 , pp. 504-519
    • Fengsrud, M.1    Roos, N.2    Berg, T.3    Liou, W.4    Slot, J.W.5    Seglen, P.O.6
  • 86
    • 0026668042 scopus 로고
    • Autophagy in yeasr demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige K, Baba M, Tsuboi S, Noda T, Ohsumi Y. Autophagy in yeasr demonstrated with proteinase-deficient mutants and conditions for its induction. J Cell Biol 1992; 119:301-11.
    • (1992) J Cell Biol , vol.119 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 87
    • 0020973226 scopus 로고
    • Inhibitors of lysosomal function
    • Seglen PO. Inhibitors of lysosomal function. Methods Enzymol 1983; 96:737-64.
    • (1983) Methods Enzymol , vol.96 , pp. 737-764
    • Seglen, P.O.1
  • 88
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: Their role in cell survival and cell death
    • Codogno P, Meijer AJ. Autophagy and signaling: Their role in cell survival and cell death. Cell Death Differ 2005; 12:1509-18.
    • (2005) Cell Death Differ , vol.12 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 89
    • 0032508564 scopus 로고    scopus 로고
    • Inhibition of hepatocytic autophagy by adenosine, aminoimidazole-4-carboxamide riboside, and N6-mer cap top urine 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-mer cap top urine 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
  • 90
    • 0015523795 scopus 로고
    • Suppression of protein turnover by amino acids in the perfused rat liver
    • Woodside KH, Mortimore GE. Suppression of protein turnover by amino acids in the perfused rat liver. J Biol Chem 1972; 247:6474-81.
    • (1972) J Biol Chem , vol.247 , pp. 6474-6481
    • Woodside, K.H.1    Mortimore, G.E.2
  • 91
    • 0019518137 scopus 로고
    • Leucine inhibition of autophagic vacuole formation in isolated rat hepatocytes
    • Grinde B, Seglen PO. Leucine inhibition of autophagic vacuole formation in isolated rat hepatocytes. Exp Cell Res 1981; 134:33-9.
    • (1981) Exp Cell Res , vol.134 , pp. 33-39
    • Grinde, B.1    Seglen, P.O.2
  • 92
    • 0020412799 scopus 로고
    • Multifunctional control of amino acids of deprivation-induced proteolysis in liver: Role of leucine
    • Pösö AR, Wert Jr JJ, Mortimore GE. Multifunctional control of amino acids of deprivation-induced proteolysis in liver: Role of leucine. J Biol Chem 1982; 257:12114-20.
    • (1982) J Biol Chem , vol.257 , pp. 12114-12120
    • Pösö, A.R.1    Wert Jr, J.J.2    Mortimore, G.E.3
  • 93
    • 0021271399 scopus 로고
    • Amino acid control of autophagic sequestration and protein degradation in isolated rat hepatocytes
    • Seglen PO, Gordon PB. Amino acid control of autophagic sequestration and protein degradation in isolated rat hepatocytes. J Cell Biol 1984; 99:435-44.
    • (1984) J Cell Biol , vol.99 , pp. 435-444
    • Seglen, P.O.1    Gordon, P.B.2
  • 94
    • 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; 151:40-7.
    • (1988) Biochem Biophys Res Commun , vol.151 , pp. 40-47
    • Gordon, P.B.1    Seglen, P.O.2
  • 95
    • 0017738395 scopus 로고
    • Inhibitor of protein degradation formed during incubarion of isolated rat hepatocytes in a cell culture medium: Its identification as ammonia
    • Seglen PO. Inhibitor of protein degradation formed during incubarion of isolated rat hepatocytes in a cell culture medium: Its identification as ammonia. Exp Cell Res 1977; 107:207-17.
    • (1977) Exp Cell Res , vol.107 , pp. 207-217
    • Seglen, P.O.1
  • 96
    • 0021136882 scopus 로고
    • Requirement for alanine in the amino acid control of deprivation-induced protein degradation in liver
    • Pösö AR, Mortimore GE. Requirement for alanine in the amino acid control of deprivation-induced protein degradation in liver. Proc Natl Acad Sci USA 1984; 81:4270-4.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4270-4274
    • Pösö, A.R.1    Mortimore, G.E.2
  • 97
    • 1542289063 scopus 로고    scopus 로고
    • Amino acids and insulin control autophagic proteolysis through different signaling pathways in relation to mTOR in isolated rat hepatocytes
    • Kanazawa T, Taneike I, Akaishi R, Yoshizawa F, Furuya N, Fujimura S, Kadowaki M. Amino acids and insulin control autophagic proteolysis through different signaling pathways in relation to mTOR in isolated rat hepatocytes. J Biol Chem 2004; 279:8452-9.
    • (2004) J Biol Chem , vol.279 , pp. 8452-8459
    • Kanazawa, T.1    Taneike, I.2    Akaishi, R.3    Yoshizawa, F.4    Furuya, N.5    Fujimura, S.6    Kadowaki, M.7
  • 98
    • 0033965924 scopus 로고    scopus 로고
    • Intracellular protein degradation and autophagy in isolated pancreatic acini of the rat
    • Telbisz A, Kovács AL. Intracellular protein degradation and autophagy in isolated pancreatic acini of the rat. Cell Biochem Funct 2000; 18:29-40.
    • (2000) Cell Biochem Funct , vol.18 , pp. 29-40
    • Telbisz, A.1    Kovács, A.L.2
  • 99
    • 0002697457 scopus 로고
    • Regulation of autophagic protein degtadation in isolated liver cells
    • Glaumann H, Ballard FJ, eds, London, UK: Academic Press
    • Seglen PO. Regulation of autophagic protein degtadation in isolated liver cells. In: Glaumann H, Ballard FJ, eds. Lysosomes: their role in protein breakdown. London, UK: Academic Press, 1987. Pg. 371-414.
    • (1987) Lysosomes: Their role in protein breakdown , pp. 371-414
    • Seglen, P.O.1
  • 100
    • 0020467237 scopus 로고
    • 6-substituted purines: A novel class of inhibitors of endogenous protein degradation in isolated rat hepatocytes
    • Gordon PB, Seglen PO. 6-substituted purines: A novel class of inhibitors of endogenous protein degradation in isolated rat hepatocytes. Arch Biochem Biophys 1982; 217:282-94.
    • (1982) Arch Biochem Biophys , vol.217 , pp. 282-294
    • Gordon, P.B.1    Seglen, P.O.2
  • 101
    • 0019853118 scopus 로고
    • Inhibition of autophagic sequestration and endogenous protein degradation in isolated tat hepatocytes by methylated adenosine derivatives
    • Kovács AL, Molnar K, Seglen PO. Inhibition of autophagic sequestration and endogenous protein degradation in isolated tat hepatocytes by methylated adenosine derivatives. FEBS Lett 1981; 134:194-6.
    • (1981) FEBS Lett , vol.134 , pp. 194-196
    • Kovács, A.L.1    Molnar, K.2    Seglen, P.O.3
  • 102
    • 0019481713 scopus 로고
    • Inhibition of hepatocytic protein degradation by methylaminopurines and inhibitors of protein synthesis
    • Kovács AL, Seglen PO. Inhibition of hepatocytic protein degradation by methylaminopurines and inhibitors of protein synthesis. Biochim Biophys Acta 1981; 676:213-20.
    • (1981) Biochim Biophys Acta , vol.676 , pp. 213-220
    • Kovács, A.L.1    Seglen, P.O.2
  • 103
    • 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; 152:519-30.
    • (2001) J Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 104
    • 0037119448 scopus 로고    scopus 로고
    • Cooperative binding of the cytoplasm to vacuole targeting pathway proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the pte-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 pte-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
  • 107
    • 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
  • 108
    • 0029077946 scopus 로고
    • Disruption of the cytokeratin cytoskeleton and inhibition of hepatocytic autophagy by okadaic acid
    • Blankson H, Holen I, Seglen PO. Disruption of the cytokeratin cytoskeleton and inhibition of hepatocytic autophagy by okadaic acid. Exp Cell Res 1995; 218:522-30.
    • (1995) Exp Cell Res , vol.218 , pp. 522-530
    • Blankson, H.1    Holen, I.2    Seglen, P.O.3
  • 109
    • 0037144405 scopus 로고    scopus 로고
    • Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes
    • Ruud Larsen AK, Møller MT, Blankson H, Samari HR, Holden L, Seglen PO. Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes. J Biol Chem 2002; 277:34826-35.
    • (2002) J Biol Chem , vol.277 , pp. 34826-34835
    • Ruud Larsen, A.K.1    Møller, M.T.2    Blankson, H.3    Samari, H.R.4    Holden, L.5    Seglen, P.O.6
  • 110
    • 0034898851 scopus 로고    scopus 로고
    • Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p
    • Wang Z, Wilson WA, Fujino MA, Roach PJ. Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p. Mol Cell Biol 2001; 21:5742-52.
    • (2001) Mol Cell Biol , vol.21 , pp. 5742-5752
    • Wang, Z.1    Wilson, W.A.2    Fujino, M.A.3    Roach, P.J.4
  • 112
    • 0033902938 scopus 로고    scopus 로고
    • Prevention of toxin-induced cytoskeletal disruption and apoptotic liver cell death by the grapefruit flavonoid, naringin
    • Blankson H, Grotterød EM, Seglen PO. Prevention of toxin-induced cytoskeletal disruption and apoptotic liver cell death by the grapefruit flavonoid, naringin. Cell Death Differ 2000; 7:739-46.
    • (2000) Cell Death Differ , vol.7 , pp. 739-746
    • Blankson, H.1    Grotterød, E.M.2    Seglen, P.O.3
  • 113
    • 0027495705 scopus 로고
    • Dependence of hepatocytic autophagy on intracellularly sequestered calcium
    • Gordon PB, Holen I, Fosse M, Røtnes JS, Seglen PO. Dependence of hepatocytic autophagy on intracellularly sequestered calcium. J Biol Chem 1993; 268:26107-12.
    • (1993) J Biol Chem , vol.268 , pp. 26107-26112
    • Gordon, P.B.1    Holen, I.2    Fosse, M.3    Røtnes, J.S.4    Seglen, P.O.5
  • 114
    • 0032512636 scopus 로고    scopus 로고
    • Noda T, Ohsumi Y. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J Biol Chem 1998; 273:3963-6.
    • Noda T, Ohsumi Y. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J Biol Chem 1998; 273:3963-6.
  • 115
    • 2442645050 scopus 로고    scopus 로고
    • The Ras/cAMP-dependent protein kinase signaling pathway regulates an early step of the autophagy process in Saccharomyces cerevisiae
    • Budovskaya YV, Stephan JS, Reggiori F, Klionsky DJ, Herman PK. The Ras/cAMP-dependent protein kinase signaling pathway regulates an early step of the autophagy process in Saccharomyces cerevisiae. J Biol Chem 2004; 279:20663-71.
    • (2004) J Biol Chem , vol.279 , pp. 20663-20671
    • Budovskaya, Y.V.1    Stephan, J.S.2    Reggiori, F.3    Klionsky, D.J.4    Herman, P.K.5
  • 116
    • 0026059005 scopus 로고
    • Role of cyclic nucleotides in the control of hepatic autophagy
    • Holen I, Gordon PB, Seglen PO. Role of cyclic nucleotides in the control of hepatic autophagy. Biomed Biochim Acta 1991; 50:389-92.
    • (1991) Biomed Biochim Acta , vol.50 , pp. 389-392
    • Holen, I.1    Gordon, P.B.2    Seglen, P.O.3
  • 118
    • 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; 102:13933-8.
    • (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
  • 120
    • 0016778074 scopus 로고
    • Protein degradation in isolated rat hepatocytes is inhibited by ammonia
    • Seglen PO. Protein degradation in isolated rat hepatocytes is inhibited by ammonia. Biochem Biophys Res Commun 1975; 66:44-52.
    • (1975) Biochem Biophys Res Commun , vol.66 , pp. 44-52
    • Seglen, P.O.1
  • 121
    • 0017082272 scopus 로고
    • Ammonia inhibition of protein degradation in isolated rat hepatocytes: Quantitative ultrastructural alterations in the lysosomal system
    • Seglen PO, Reith A. Ammonia inhibition of protein degradation in isolated rat hepatocytes: Quantitative ultrastructural alterations in the lysosomal system. Exp Cell Res 1976; 100:276-80.
    • (1976) Exp Cell Res , vol.100 , pp. 276-280
    • Seglen, P.O.1    Reith, A.2
  • 122
    • 0017062911 scopus 로고
    • Selective control of the degradation of normal and aberrant proteins in Reuber H35 hepatoma cells
    • Knowles SE, Ballard FJ. Selective control of the degradation of normal and aberrant proteins in Reuber H35 hepatoma cells. Biochem J 1976; 156:609-17.
    • (1976) Biochem J , vol.156 , pp. 609-617
    • Knowles, S.E.1    Ballard, F.J.2
  • 124
    • 0019209783 scopus 로고
    • Effects of lysosomotropic monoamines, diamines, amino alcohols, and other amino compounds on protein degradation and protein synthesis in isolated rat hepatocytes
    • Seglen PO, Gordon PB. Effects of lysosomotropic monoamines, diamines, amino alcohols, and other amino compounds on protein degradation and protein synthesis in isolated rat hepatocytes. Mol Pharmacol 1980; 18:468-75.
    • (1980) Mol Pharmacol , vol.18 , pp. 468-475
    • Seglen, P.O.1    Gordon, P.B.2
  • 125
    • 0030925772 scopus 로고    scopus 로고
    • Differences between fluid-phase endocytosis (pinocytosis) and receptor-mediated endocytosis in isolated rat hepatocytes
    • Strømhaug PE, Berg TO, Gjøen T, Seglen PO. Differences between fluid-phase endocytosis (pinocytosis) and receptor-mediated endocytosis in isolated rat hepatocytes. Eur J Cell Biol 1997; 73:28-39.
    • (1997) Eur J Cell Biol , vol.73 , pp. 28-39
    • Strømhaug, P.E.1    Berg, T.O.2    Gjøen, T.3    Seglen, P.O.4
  • 126
    • 0017619319 scopus 로고
    • Ammonia inhibits protein secretion in isolated rat hepatocytes
    • Seglen PO, Reith A. Ammonia inhibits protein secretion in isolated rat hepatocytes. Biochim Biophys Acta 1977; 496:29-35.
    • (1977) Biochim Biophys Acta , vol.496 , pp. 29-35
    • Seglen, P.O.1    Reith, A.2
  • 127
    • 0018666229 scopus 로고
    • Inhibition of cell spreading by lysosomotropic amines
    • Seglen PO, Gordon PB. Inhibition of cell spreading by lysosomotropic amines. FEBS Lett 1979; 105:345-8.
    • (1979) FEBS Lett , vol.105 , pp. 345-348
    • Seglen, P.O.1    Gordon, P.B.2
  • 129
    • 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; 333:169-74.
    • (1993) FEBS Lett , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 134
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required fot autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR. HDAC6 and microtubules are required fot 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
  • 136
    • 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
  • 138
    • 0032895859 scopus 로고    scopus 로고
    • Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein
    • Yuan W, Stromhaug PE, Dunn Jr WA. Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein. Mol Biol Cell 1999; 10:1353-66.
    • (1999) Mol Biol Cell , vol.10 , pp. 1353-1366
    • Yuan, W.1    Stromhaug, P.E.2    Dunn Jr, W.A.3
  • 139
    • 0037134443 scopus 로고    scopus 로고
    • Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p
    • Tanida I, Tanida-Miyake E, Komatsu M, Ueno T, Kominami E. Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p. J Biol Chem 2002; 277:13739-44.
    • (2002) J Biol Chem , vol.277 , pp. 13739-13744
    • Tanida, I.1    Tanida-Miyake, E.2    Komatsu, M.3    Ueno, T.4    Kominami, E.5
  • 140
    • 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
  • 142
    • 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; 276:1701-6.
    • (2001) J Biol Chem , vol.276 , pp. 1701-1706
    • Tanida, I.1    Tanida-Miyake, E.2    Ueno, T.3    Kominami, E.4
  • 143
    • 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
  • 144
    • 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
    • Strømhaug 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
    • Strømhaug, P.E.1    Reggiori, F.2    Guan, J.3    Wang, C.-W.4    Klionsky, D.J.5
  • 145
    • 19444382327 scopus 로고    scopus 로고
    • The dynamics of autophagy visualized in live cells: From autophagosome formation to fusion with endo/lysosomes
    • Bampton ETW, Goemans CG, Niranjan D, Mizushima N, Tolkovsky AM. The dynamics of autophagy visualized in live cells: From autophagosome formation to fusion with endo/lysosomes. Autophagy 2005; 1:11-22.
    • (2005) Autophagy , vol.1 , pp. 11-22
    • Bampton, E.T.W.1    Goemans, C.G.2    Niranjan, D.3    Mizushima, N.4    Tolkovsky, A.M.5
  • 146
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 2004; 15:1101-11.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 147
    • 0035870257 scopus 로고    scopus 로고
    • Beclin 1 contains a leucine-rich nuclear export signal that is required for its autophagy and tumor suppressor function
    • Liang XH, Yu J, Brown K, Levine B. Beclin 1 contains a leucine-rich nuclear export signal that is required for its autophagy and tumor suppressor function. Cancer Res 2001; 61:3443-9.
    • (2001) Cancer Res , vol.61 , pp. 3443-3449
    • Liang, X.H.1    Yu, J.2    Brown, K.3    Levine, B.4
  • 148
    • 0037194894 scopus 로고    scopus 로고
    • A novel protein complex linking the δ2 glutamate receptor and autophagy: Implications for neurodegeneration in lurcher mice
    • Yue Z, Horton A, Bravin M, DeJager PL, Selimi F, Heintz N. A novel protein complex linking the δ2 glutamate receptor and autophagy: Implications for neurodegeneration in lurcher mice. Neuron 2002; 35:921-33.
    • (2002) Neuron , vol.35 , pp. 921-933
    • Yue, Z.1    Horton, A.2    Bravin, M.3    DeJager, P.L.4    Selimi, F.5    Heintz, N.6
  • 150
    • 0036017758 scopus 로고    scopus 로고
    • Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24
    • Munafo DB, Colombo MI. Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24. Traffic 2002; 3:472-82.
    • (2002) Traffic , vol.3 , pp. 472-482
    • Munafo, D.B.1    Colombo, M.I.2
  • 151
    • 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 W-P, 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; 277:763-73.
    • (2002) J Biol Chem , vol.277 , pp. 763-773
    • Kim, J.1    Huang, W.-P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 152
    • 0035503594 scopus 로고    scopus 로고
    • The pre-autophagosomal structure organized by concerted functions of APG genes is essential fot 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 fot 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
  • 153
    • 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; 12:231-5.
    • (2002) Trends Cell Biol , vol.12 , pp. 231-235
    • Noda, T.1    Suzuki, K.2    Ohsumi, Y.3
  • 154
    • 0034614934 scopus 로고    scopus 로고
    • Apg9p/Cvt7p is an integral membrane protein requited for transport vesicle formation in the Cvt and autophagy pathways
    • Noda T, Kim J, Huang W-P, Baba M, Tokunaga C, Ohsumi Y, Klionsky DJ. Apg9p/Cvt7p is an integral membrane protein requited 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    Klionsky, D.J.7
  • 155
    • 0347611578 scopus 로고    scopus 로고
    • Atg23 is essential for the cytoplasm to vacuole tatgeting pathway and efficient autophagy but not pexophagy
    • Tucker KA, Reggiori F, Dunn Jt WA, Klionsky DJ. Atg23 is essential for the cytoplasm to vacuole tatgeting 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, J.W.3    Klionsky, D.J.4
  • 156
    • 0033747489 scopus 로고    scopus 로고
    • Autophagy in the epithelial cells of murine seminal vesicle in vitro: Formation of large sheets of nascent isolation membranes, sequestration of the nucleus and inhibition by wortmannin and 3-methyladenine
    • Kovács AL, Réz G, Pálfia Z, Kovács J. Autophagy in the epithelial cells of murine seminal vesicle in vitro: Formation of large sheets of nascent isolation membranes, sequestration of the nucleus and inhibition by wortmannin and 3-methyladenine. Cell Tissue Res 2000; 302:253-61.
    • (2000) Cell Tissue Res , vol.302 , pp. 253-261
    • Kovács, A.L.1    Réz, G.2    Pálfia, Z.3    Kovács, J.4
  • 157
    • 0034529528 scopus 로고    scopus 로고
    • Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy
    • Fengsrud M, Erichsen ES, Berg TO, Raiborg C, Seglen PO. Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy. Eur J Cell Biol 2000; 79:871-82.
    • (2000) Eur J Cell Biol , vol.79 , pp. 871-882
    • Fengsrud, M.1    Erichsen, E.S.2    Berg, T.O.3    Raiborg, C.4    Seglen, P.O.5
  • 159
    • 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
  • 160
    • 0028987672 scopus 로고
    • Physiological functions of endosomal proteolysis
    • Betg T, Gjøen T, Bakke O. Physiological functions of endosomal proteolysis. Biochem J 1995; 307:313-26.
    • (1995) Biochem J , vol.307 , pp. 313-326
    • Betg, T.1    Gjøen, T.2    Bakke, O.3
  • 161
    • 0017650088 scopus 로고
    • Lysosomal sequestration of intracellular protein as a regulatory step in hepatic proteolysis
    • Ward WF, Cox JR, Mortimore GE. Lysosomal sequestration of intracellular protein as a regulatory step in hepatic proteolysis. J Biol Chem 1977; 252:6955-61.
    • (1977) J Biol Chem , vol.252 , pp. 6955-6961
    • Ward, W.F.1    Cox, J.R.2    Mortimore, G.E.3
  • 162
    • 0019900928 scopus 로고
    • Appearance of autolysosomes in rat liver after leupeptin treatment
    • Futuno K, Ishikawa T, Kato K. Appearance of autolysosomes in rat liver after leupeptin treatment. J Biochem (Tokyo) 1982; 91:1485-94.
    • (1982) J Biochem (Tokyo) , vol.91 , pp. 1485-1494
    • Futuno, K.1    Ishikawa, T.2    Kato, K.3
  • 163
    • 0020584354 scopus 로고
    • Sequestration of cytoplasmic enzymes in an autophagic vacuole-lysosomal system induced by injection of leupeptin
    • Kominami E, Hashida S, Khairallah EA, Katunuma N. Sequestration of cytoplasmic enzymes in an autophagic vacuole-lysosomal system induced by injection of leupeptin. J Biol Chem 1983; 258:6093-100.
    • (1983) J Biol Chem , vol.258 , pp. 6093-6100
    • Kominami, E.1    Hashida, S.2    Khairallah, E.A.3    Katunuma, N.4
  • 164
    • 0020085949 scopus 로고
    • Isolation of autophagic vacuoles from rat liver: Morphological and biochemical characterization
    • Marzella L, Ahlberg J, Glaumann H. Isolation of autophagic vacuoles from rat liver: Morphological and biochemical characterization. J Cell Biol 1982; 93:144-54.
    • (1982) J Cell Biol , vol.93 , pp. 144-154
    • Marzella, L.1    Ahlberg, J.2    Glaumann, H.3
  • 165
    • 0032532323 scopus 로고    scopus 로고
    • Purification and characterization of autophagosomes from rat hepatocytes
    • Strømhaug PE, Berg TO, Fengsrud M, Seglen PO. Purification and characterization of autophagosomes from rat hepatocytes. Biochem J 1998; 335:217-24.
    • (1998) Biochem J , vol.335 , pp. 217-224
    • Strømhaug, P.E.1    Berg, T.O.2    Fengsrud, M.3    Seglen, P.O.4
  • 166
    • 0028261473 scopus 로고
    • Separation of lysosomes and autophagosomes by means of glycyl-phenylalanine-naphthylamide, a lysosome-disrupting cathepsin-C substrate
    • Berg TO, Strømhaug PE, Berg T, Seglen PO. Separation of lysosomes and autophagosomes by means of glycyl-phenylalanine-naphthylamide, a lysosome-disrupting cathepsin-C substrate. Eur J Biochem 1994; 221:595-602.
    • (1994) Eur J Biochem , vol.221 , pp. 595-602
    • Berg, T.O.1    Strømhaug, P.E.2    Berg, T.3    Seglen, P.O.4
  • 167
    • 0032555641 scopus 로고    scopus 로고
    • Isolation and characterization of rat liver amphisomes: Evidence for fusion of autophagosomes with both early and late endosomes
    • Berg TO, Fengsrud M, Stroømhaug PE, Berg T, Seglen PO. Isolation and characterization of rat liver amphisomes: Evidence for fusion of autophagosomes with both early and late endosomes. J Biol Chem 1998; 273:21883-92.
    • (1998) J Biol Chem , vol.273 , pp. 21883-21892
    • Berg, T.O.1    Fengsrud, M.2    Stroømhaug, P.E.3    Berg, T.4    Seglen, P.O.5
  • 168
    • 0027287640 scopus 로고    scopus 로고
    • Araki N, Ohno J, Lee T, Takashima Y, Ogawa K. Nematolysosomes (elongate lysosomes) in rat hepatocytes: Their distribution, microtubule dependence, and role in endocytic transport pathway. Exp Cell Res 1993; 204:181-91.
    • Araki N, Ohno J, Lee T, Takashima Y, Ogawa K. Nematolysosomes (elongate lysosomes) in rat hepatocytes: Their distribution, microtubule dependence, and role in endocytic transport pathway. Exp Cell Res 1993; 204:181-91.
  • 169
    • 0021815646 scopus 로고
    • Conversion of dense lysosomes inro light lysosomes during hepatocytic autophagy
    • Seglen PO, Solheim AE. Conversion of dense lysosomes inro light lysosomes during hepatocytic autophagy. Exp Cell Res 1985; 157:550-5.
    • (1985) Exp Cell Res , vol.157 , pp. 550-555
    • Seglen, P.O.1    Solheim, A.E.2
  • 170
    • 0027396017 scopus 로고
    • The differential degradation of two cytosolic proteins as a tool to monitor autophagy in hepatocytes by immunocytochemistry
    • Rabouille C, Strous GJ, Crapo JD, Geuze HJ, Slot JW. The differential degradation of two cytosolic proteins as a tool to monitor autophagy in hepatocytes by immunocytochemistry. J Cell Biol 1993; 120:897-908.
    • (1993) J Cell Biol , vol.120 , pp. 897-908
    • Rabouille, C.1    Strous, G.J.2    Crapo, J.D.3    Geuze, H.J.4    Slot, J.W.5
  • 171
    • 1842865745 scopus 로고    scopus 로고
    • Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells
    • Kanzawa T, Germano IM, Komata T, Ito H, Kondo Y, Kondo S. Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells. Cell Death Differ 2004; 11:448-57.
    • (2004) Cell Death Differ , vol.11 , pp. 448-457
    • Kanzawa, T.1    Germano, I.M.2    Komata, T.3    Ito, H.4    Kondo, Y.5    Kondo, S.6
  • 173
    • 0034757896 scopus 로고    scopus 로고
    • A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation
    • Munafo DB, Colombo MI. A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation. J Cell Sci 2001; 114:3619-29.
    • (2001) J Cell Sci , vol.114 , pp. 3619-3629
    • Munafo, D.B.1    Colombo, M.I.2
  • 174
    • 33644606491 scopus 로고    scopus 로고
    • Tracker dyes to probe mitochondrial autophagy (mitophagy) in tat hepatocytes
    • Rodriguez-Enriquez S, Kim I, Currin RT, Lemasters JJ. Tracker dyes to probe mitochondrial autophagy (mitophagy) in tat hepatocytes. Autophagy 2006; 2:39-46.
    • (2006) Autophagy , vol.2 , pp. 39-46
    • Rodriguez-Enriquez, S.1    Kim, I.2    Currin, R.T.3    Lemasters, J.J.4
  • 175
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in rhe Drosophila fat body
    • Scott RC, Schuldiner O, Neufeld TP. Role and regulation of starvation-induced autophagy in rhe 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
  • 176
    • 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. Eut J Cell Biol 1995; 66:3-14.
    • (1995) Eut J Cell Biol , vol.66 , pp. 3-14
    • Biederbick, A.1    Kern, H.F.2    Elsasser, H.P.3
  • 177
    • 0034722378 scopus 로고    scopus 로고
    • Dissection of autophagosome biogenesis into distinct nucleation and expansion steps
    • Abeliovich H, Dunn Jr WA, Kim J, Klionsky DJ. Dissection of autophagosome biogenesis into distinct nucleation and expansion steps. J Cell Biol 2000; 151:1025-34.
    • (2000) J Cell Biol , vol.151 , pp. 1025-1034
    • Abeliovich, H.1    Dunn Jr, W.A.2    Kim, J.3    Klionsky, D.J.4
  • 178
    • 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
  • 181
    • 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
  • 182
    • 0037329201 scopus 로고    scopus 로고
    • Chemical genetic analysis of Apg1 reveals a nonkinase role in the induction of autophagy
    • Abeliovich H, Zhang C, Dunn Jr WA, Shokat KM, Klionsky DJ. Chemical genetic analysis of Apg1 reveals a nonkinase role in the induction of autophagy. Mol Biol Cell 2003; 14:477-90.
    • (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
  • 184
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the preautophagosomal structure
    • Reggiori F, Tucker KA, Stromhaug PE, Klionsky DJ. The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the preautophagosomal 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
  • 186
    • 3142677196 scopus 로고    scopus 로고
    • Cargo proteins facilitate the fotmation of transport vesicles in the cytoplasm to vacuole targeting pathway
    • Shintani T, Klionsky DJ. Cargo proteins facilitate the fotmation of transport vesicles in the cytoplasm to vacuole targeting pathway. J Biol Chem 2004; 279:29889-94.
    • (2004) J Biol Chem , vol.279 , pp. 29889-29894
    • Shintani, T.1    Klionsky, D.J.2
  • 187
    • 0032126632 scopus 로고    scopus 로고
    • Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole
    • Lang T, Schaeffeler E, Bernreuther D, Bredschneider M, Wolf DH, Thumm M. Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole. Embo J 1998; 17:3597-607.
    • (1998) Embo J , vol.17 , pp. 3597-3607
    • Lang, T.1    Schaeffeler, E.2    Bernreuther, D.3    Bredschneider, M.4    Wolf, D.H.5    Thumm, M.6
  • 188
    • 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
  • 191
    • 0035825175 scopus 로고    scopus 로고
    • Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex
    • Kim J, Huang W-P, Klionsky DJ. Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex. J Cell Biol 2001; 152:51-64.
    • (2001) J Cell Biol , vol.152 , pp. 51-64
    • Kim, J.1    Huang, W.-P.2    Klionsky, D.J.3
  • 193
    • 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, Ohsumi M, Takao T, Noda T, Ohsumi Y. 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    Ohsumi, M.7    Takao, T.8    Noda, T.9    Ohsumi, Y.10
  • 194
    • 0026559695 scopus 로고
    • Prelysosomal and lysosomal connections between autophagy and endocytosis
    • Gordon PB, Høyvik H, Seglen PO. Prelysosomal and lysosomal connections between autophagy and endocytosis. Biochem J 1992; 283:361-9.
    • (1992) Biochem J , vol.283 , pp. 361-369
    • Gordon, P.B.1    Høyvik, H.2    Seglen, P.O.3
  • 195
    • 0008853116 scopus 로고
    • Convergence of autophagic and endocytic pathways at the level of the lysosome
    • Høyvik H, Gordon PB, Seglen PO. Convergence of autophagic and endocytic pathways at the level of the lysosome. Biochem Soc Trans 1987; 15:964-5.
    • (1987) Biochem Soc Trans , vol.15 , pp. 964-965
    • Høyvik, H.1    Gordon, P.B.2    Seglen, P.O.3
  • 196
    • 33646204392 scopus 로고    scopus 로고
    • Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size
    • Hosokawa N, Hara Y, Mizushima N. Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size. FEBS Lett 2006; 580:2623-9.
    • (2006) FEBS Lett , vol.580 , pp. 2623-2629
    • Hosokawa, N.1    Hara, Y.2    Mizushima, N.3
  • 197
    • 0020510501 scopus 로고
    • Quantitative correlation between ptoteolysis and macro- and microautophagy in mouse hepatocytes during starvation and refeeding
    • Mottimore GE, Hutson NJ, Surmacz CA. Quantitative correlation between ptoteolysis and macro- and microautophagy in mouse hepatocytes during starvation and refeeding. Proc Natl Acad Sci USA 1983; 80:2179-83.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 2179-2183
    • Mottimore, G.E.1    Hutson, N.J.2    Surmacz, C.A.3
  • 198
    • 0022568933 scopus 로고
    • Quantitative changes in the lysosomal vacuolar system of rat hepatocytes during short-term starvation: A morphometric analysis with special reference ro macro- and microautophagy
    • de Waal EJ, Vreeling-Sindelárová H, Schellens JPM, Hourkooper JM, James J. Quantitative changes in the lysosomal vacuolar system of rat hepatocytes during short-term starvation: A morphometric analysis with special reference ro macro- and microautophagy. Cell Tissue Res 1986; 243:641-8.
    • (1986) Cell Tissue Res , vol.243 , pp. 641-648
    • de Waal, E.J.1    Vreeling-Sindelárová, H.2    Schellens, J.P.M.3    Hourkooper, J.M.4    James, J.5
  • 199
    • 0019506466 scopus 로고
    • Autophagy, hetetophagy, microautophagy and crinophagy as the means for intracellular degradation
    • Marzella L, Ahlbetg J, Glaumann H. Autophagy, hetetophagy, microautophagy and crinophagy as the means for intracellular degradation. Virchows Arch B Cell Pathol Incl Mol Pathol 1981; 36:219-34.
    • (1981) Virchows Arch B Cell Pathol Incl Mol Pathol , vol.36 , pp. 219-234
    • Marzella, L.1    Ahlbetg, J.2    Glaumann, H.3
  • 200
    • 0021718330 scopus 로고
    • Swainsonine inhibits glycoprotein degradation by isolated rat liver lysosomes
    • Winkler JR, Segal HL. Swainsonine inhibits glycoprotein degradation by isolated rat liver lysosomes. J Biol Chem 1984; 259:15369-72.
    • (1984) J Biol Chem , vol.259 , pp. 15369-15372
    • Winkler, J.R.1    Segal, H.L.2
  • 201
    • 0034735536 scopus 로고    scopus 로고
    • Autophagic tubes: Vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding
    • Muller O, Sattler T, Flotenmeyer M, Schwarz H, Plattner H, Mayer A. Autophagic tubes: Vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding. J Cell Biol 2000; 151:519-28.
    • (2000) J Cell Biol , vol.151 , pp. 519-528
    • Muller, O.1    Sattler, T.2    Flotenmeyer, M.3    Schwarz, H.4    Plattner, H.5    Mayer, A.6
  • 202
    • 0034735511 scopus 로고    scopus 로고
    • Cell-free reconstitution of microaurophagic vacuole invagination and vesicle formation
    • Sattler T, Mayer A. Cell-free reconstitution of microaurophagic vacuole invagination and vesicle formation, J Cell Biol 2000; 151:529-38.
    • (2000) J Cell Biol , vol.151 , pp. 529-538
    • Sattler, T.1    Mayer, A.2
  • 204
    • 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; 119:287-99.
    • (1992) J Cell Biol , vol.119 , pp. 287-299
    • Klionsky, D.J.1    Cueva, R.2    Yaver, D.S.3
  • 206
    • 0029913505 scopus 로고    scopus 로고
    • Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
    • Scott SV, Hefner-Gravink A, Morano KA, Noda T, Ohsumi Y, Klionsky DJ. Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc Natl Acad Sci USA 1996; 93:12304-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12304-12308
    • Scott, S.V.1    Hefner-Gravink, A.2    Morano, K.A.3    Noda, T.4    Ohsumi, Y.5    Klionsky, D.J.6
  • 207
    • 0242677719 scopus 로고    scopus 로고
    • A new class of mutants deficient in dodecamerization of aminopeptidase 1 and vacuolar transport
    • Andrei-Selmer C, Knuppel A, Satyanarayana C, Heese C, Schu PV. A new class of mutants deficient in dodecamerization of aminopeptidase 1 and vacuolar transport. J Biol Chem 2001; 276:11606-14.
    • (2001) J Biol Chem , vol.276 , pp. 11606-11614
    • Andrei-Selmer, C.1    Knuppel, A.2    Satyanarayana, C.3    Heese, C.4    Schu, P.V.5
  • 208
    • 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; 10:1337-51.
    • (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
  • 209
    • 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, Strømhaug PE, George MD, Habibzadegah-Tari P, Bevan A, Dunn Jr WA, Klionsky DJ. 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    Strømhaug, P.E.2    George, M.D.3    Habibzadegah-Tari, P.4    Bevan, A.5    Dunn Jr, W.A.6    Klionsky, D.J.7
  • 210
    • 0035827541 scopus 로고    scopus 로고
    • Vacuolar localization of oligomeric α-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae
    • Hutchins MU, Klionsky DJ. Vacuolar localization of oligomeric α-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae. J Biol Chem 2001; 276:20491-8.
    • (2001) J Biol Chem , vol.276 , pp. 20491-20498
    • Hutchins, M.U.1    Klionsky, D.J.2
  • 211
    • 0017825873 scopus 로고
    • α-D-Mannosidase of Saccharomyces cerevisiae: Characterization and modulation of activity
    • Opheim DJ. α-D-Mannosidase of Saccharomyces cerevisiae: Characterization and modulation of activity. Biochim Biophys Acta 1978; 524:121-30.
    • (1978) Biochim Biophys Acta , vol.524 , pp. 121-130
    • Opheim, D.J.1
  • 212
    • 0001199243 scopus 로고
    • A quantitative assay to measure homotypic vacuole fusion in vitro
    • Haas A. A quantitative assay to measure homotypic vacuole fusion in vitro. Methods in Cell Science 1995; 17:283-94.
    • (1995) Methods in Cell Science , vol.17 , pp. 283-294
    • Haas, A.1
  • 213
    • 33745834116 scopus 로고    scopus 로고
    • Vacuolar import and degradation
    • Klionsky DJ, ed, Georgetown, TX: Landes Bioscience
    • Brown CR, Chiang H-L. Vacuolar import and degradation. In: Klionsky DJ, ed. Autophagy. Georgetown, TX: Landes Bioscience, 2004. Pg. 176-86.
    • (2004) Autophagy , pp. 176-186
    • Brown, C.R.1    Chiang, H.-L.2
  • 214
    • 33745023775 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy in aging and in disease
    • Massey A, Zhang C, Cuervo AM. Chaperone-mediated autophagy in aging and in disease. Curr Topics Devel Biol 2006; 73:203-35.
    • (2006) Curr Topics Devel Biol , vol.73 , pp. 203-235
    • Massey, A.1    Zhang, C.2    Cuervo, A.M.3
  • 215
    • 21844440290 scopus 로고    scopus 로고
    • Ketone bodies srimulare chaperone-mediated autophagy
    • Finn PF, Dice JF. Ketone bodies srimulare chaperone-mediated autophagy. J Biol Chem 2005; 280:25864-70.
    • (2005) J Biol Chem , vol.280 , pp. 25864-25870
    • Finn, P.F.1    Dice, J.F.2
  • 217
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice JF. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990; 15:305-9.
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 218
    • 4344673498 scopus 로고    scopus 로고
    • Mechanisms of chaperone-mediated autophagy
    • Majeski AE, Dice JF. Mechanisms of chaperone-mediated autophagy. Int J Biochem Cell Biol 2004; 36:2435-44.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2435-2444
    • Majeski, A.E.1    Dice, J.F.2
  • 219
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible fot the selective uptake and degradation of cytosolic proteins
    • Cuervo AM, Dice JF, Knecht E. A population of rat liver lysosomes responsible fot the selective uptake and degradation of cytosolic proteins. J Biol Chem 1997; 272:5606-15.
    • (1997) J Biol Chem , vol.272 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 220
    • 0027280820 scopus 로고
    • Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes
    • Aniento F, Roche E, Cuervo AM, Knecht E. Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes. J Biol Chem 1993; 268:10463-70.
    • (1993) J Biol Chem , vol.268 , pp. 10463-10470
    • Aniento, F.1    Roche, E.2    Cuervo, A.M.3    Knecht, E.4
  • 221
    • 0027379661 scopus 로고
    • Polypeptide impott and degradation by isolated lysosomes
    • Terlecky SR, Dice JF. Polypeptide impott and degradation by isolated lysosomes. J Biol Chem 1993; 268:23490-5.
    • (1993) J Biol Chem , vol.268 , pp. 23490-23495
    • Terlecky, S.R.1    Dice, J.F.2
  • 222
    • 6344275803 scopus 로고    scopus 로고
    • Activation of chaperone-mediated autophagy during oxidarive sttess
    • Kiffin R, Christian C, Knecht E, Cuervo AM. Activation of chaperone-mediated autophagy during oxidarive sttess. Mol Biol Cell 2004; 15:4829-40.
    • (2004) Mol Biol Cell , vol.15 , pp. 4829-4840
    • Kiffin, R.1    Christian, C.2    Knecht, E.3    Cuervo, A.M.4
  • 223
    • 0034510572 scopus 로고    scopus 로고
    • Unique properties of lamp2a compared to othet lamp2 isoforms
    • Cuervo AM, Dice JF. Unique properties of lamp2a compared to othet lamp2 isoforms. J Cell Sci 2000; 113:4441-50.
    • (2000) J Cell Sci , vol.113 , pp. 4441-4450
    • Cuervo, A.M.1    Dice, J.F.2
  • 225
    • 0025767818 scopus 로고
    • Regulation of ttanscription of the gene coding fot peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cerevisiae
    • Einethand AW, Vootn-Btouwet TM, Erdmann R, Kunau WH, Tabak HF. Regulation of ttanscription of the gene coding fot peroxisomal 3-oxoacyl-CoA thiolase of Saccharomyces cerevisiae. Eur J Biochem 1991; 200:113-22.
    • (1991) Eur J Biochem , vol.200 , pp. 113-122
    • Einethand, A.W.1    Vootn-Btouwet, T.M.2    Erdmann, R.3    Kunau, W.H.4    Tabak, H.F.5
  • 226
    • 0033490110 scopus 로고    scopus 로고
    • Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of mactoautophagy and the Cvt pathway
    • Hutchins MU, Veenhuis M, Klionsky DJ. Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of mactoautophagy and the Cvt pathway. J Cell Sci 1999; 112:4079-87.
    • (1999) J Cell Sci , vol.112 , pp. 4079-4087
    • Hutchins, M.U.1    Veenhuis, M.2    Klionsky, D.J.3
  • 227
    • 28644447348 scopus 로고    scopus 로고
    • The actin cytoskeleton is essential for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae
    • Reggiori F, Monastytska I, Shintani T, Klionsky DJ. The actin cytoskeleton is essential for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae. Mol Biol Cell 2005; 16:5843-56.
    • (2005) Mol Biol Cell , vol.16 , pp. 5843-5856
    • Reggiori, F.1    Monastytska, I.2    Shintani, T.3    Klionsky, D.J.4
  • 228
    • 0000779492 scopus 로고
    • Isolation and characterization of a catabolite repression-insensitive mutant of a methanol yeast, Candida boidinii A5, ptoducing alcohol oxidase in glucose-containing medium
    • Sakai Y, Sawai T, Tani Y. Isolation and characterization of a catabolite repression-insensitive mutant of a methanol yeast, Candida boidinii A5, ptoducing alcohol oxidase in glucose-containing medium. Appl Environ Microbiol 1987; 53:1812-8.
    • (1987) Appl Environ Microbiol , vol.53 , pp. 1812-1818
    • Sakai, Y.1    Sawai, T.2    Tani, Y.3
  • 229
    • 0022780345 scopus 로고
    • A method of quantitative determination of alcohol oxidase and catalase in yeast colonies
    • Sibirnyi AA, Titotenko VI. A method of quantitative determination of alcohol oxidase and catalase in yeast colonies. Ukr Biokhim Zh 1986; 58:65-8.
    • (1986) Ukr Biokhim Zh , vol.58 , pp. 65-68
    • Sibirnyi, A.A.1    Titotenko, V.I.2
  • 230
    • 0022410916 scopus 로고
    • Degtadative inactivation of the peroxisomal enzyme, alcohol oxidase, during adaptation of methanol-grown Candida boidinii to ethanol
    • Hill DJ, Hann AC, Lloyd D. Degtadative inactivation of the peroxisomal enzyme, alcohol oxidase, during adaptation of methanol-grown Candida boidinii to ethanol. Biochem J 1985; 232:743-50.
    • (1985) Biochem J , vol.232 , pp. 743-750
    • Hill, D.J.1    Hann, A.C.2    Lloyd, D.3
  • 231
    • 0030846044 scopus 로고    scopus 로고
    • Impairment of peroxisome degradation in Pichia methanolica mutants defective in acetyl-CoA synthetase or isocitrate lyase
    • Kulachkovsky AR, Moroz OM, Sibirny AA. Impairment of peroxisome degradation in Pichia methanolica mutants defective in acetyl-CoA synthetase or isocitrate lyase. Yeast 1997; 13:1043-52.
    • (1997) Yeast , vol.13 , pp. 1043-1052
    • Kulachkovsky, A.R.1    Moroz, O.M.2    Sibirny, A.A.3
  • 232
    • 0032482219 scopus 로고    scopus 로고
    • Peroxisome degradation by microautophagy in Pichia pastoris: Identification of specific steps and morphological intermediates
    • Sakai Y, Koller A, Rangell LK, Keller GA, Subramani S. Peroxisome degradation by microautophagy in Pichia pastoris: Identification of specific steps and morphological intermediates. J Cell Biol 1998; 141:625-36.
    • (1998) J Cell Biol , vol.141 , pp. 625-636
    • Sakai, Y.1    Koller, A.2    Rangell, L.K.3    Keller, G.A.4    Subramani, S.5
  • 233
    • 0028855325 scopus 로고
    • Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris
    • Tuttle DL, Dunn Jr WA. Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris. J Cell Sci 1995; 108:25-35.
    • (1995) J Cell Sci , vol.108 , pp. 25-35
    • Tuttle, D.L.1    Dunn Jr, W.A.2
  • 234
    • 0033618147 scopus 로고    scopus 로고
    • The Hansenula polymorpha PDD1 gene product, essential for the selective degradation of peroxisomes, is a homologue of Saccharomyces cerevisiae Vps34p
    • Kiel JAKW, Rechinger KB, van der Klei IJ, Salomons FA, Titorenko VI, Veenhuis M. The Hansenula polymorpha PDD1 gene product, essential for the selective degradation of peroxisomes, is a homologue of Saccharomyces cerevisiae Vps34p. Yeast 1999; 15:741-54.
    • (1999) Yeast , vol.15 , pp. 741-754
    • Kiel, J.A.K.W.1    Rechinger, K.B.2    van der Klei, I.J.3    Salomons, F.A.4    Titorenko, V.I.5    Veenhuis, M.6
  • 235
    • 0027207680 scopus 로고
    • Selective autophagy of peroxisomes in methylotrophic yeasts
    • Tuttle DL, Lewin AS, Dunn Jr WA. Selective autophagy of peroxisomes in methylotrophic yeasts. Eur J Cell Biol 1993; 60:283-90.
    • (1993) Eur J Cell Biol , vol.60 , pp. 283-290
    • Tuttle, D.L.1    Lewin, A.S.2    Dunn Jr, W.A.3
  • 236
    • 33845345128 scopus 로고    scopus 로고
    • Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae
    • Nazarko TY, Huang J, Nicaud JM, Klionsky DJ, Sibirny AA. Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae. Autophagy 2005; 1:37-45.
    • (2005) Autophagy , vol.1 , pp. 37-45
    • Nazarko, T.Y.1    Huang, J.2    Nicaud, J.M.3    Klionsky, D.J.4    Sibirny, A.A.5
  • 237
    • 0033900939 scopus 로고    scopus 로고
    • The catabolite inactivation of Aspergillus nidulans isocitrate lyase occurs by specific autophagy of peroxisomes
    • Amor C, Dominguez AI, De Lucas JR, Laborda F. The catabolite inactivation of Aspergillus nidulans isocitrate lyase occurs by specific autophagy of peroxisomes. Arch Microbiol 2000; 174:59-66.
    • (2000) Arch Microbiol , vol.174 , pp. 59-66
    • Amor, C.1    Dominguez, A.I.2    De Lucas, J.R.3    Laborda, F.4
  • 238
    • 0028855063 scopus 로고
    • Isolation and characrerization of mutants impaired in the selective degradation of peroxisomes in the yeast Hansenula polymorpha
    • Titorenko VI, Keizer I, Harder W, Veenhuis M. Isolation and characrerization of mutants impaired in the selective degradation of peroxisomes in the yeast Hansenula polymorpha. J Bacteriol 1995; 177:357-63.
    • (1995) J Bacteriol , vol.177 , pp. 357-363
    • Titorenko, V.I.1    Keizer, I.2    Harder, W.3    Veenhuis, M.4
  • 239
    • 0026649636 scopus 로고
    • Autophagic degradation of peroxisomes in isolated rat hepatocytes
    • Luiken JJ, van den Berg M, Heikoop JC, Meijer AJ. Autophagic degradation of peroxisomes in isolated rat hepatocytes. FEBS Lett 1992; 304:93-7.
    • (1992) FEBS Lett , vol.304 , pp. 93-97
    • Luiken, J.J.1    van den Berg, M.2    Heikoop, J.C.3    Meijer, A.J.4
  • 241
    • 0037705403 scopus 로고    scopus 로고
    • Macroautophagy is required for multicellular development of the social amoeba Dictyostelium discoideum
    • Otto GP, Wu MY, Kazgan N, Anderson OR, Kessin RH. Macroautophagy is required for multicellular development of the social amoeba Dictyostelium discoideum. J Biol Chem 2003; 278:17636-45.
    • (2003) J Biol Chem , vol.278 , pp. 17636-17645
    • Otto, G.P.1    Wu, M.Y.2    Kazgan, N.3    Anderson, O.R.4    Kessin, R.H.5
  • 242
    • 1842577042 scopus 로고    scopus 로고
    • Dictyostelium macroautophagy mutants vary in the severity of their developmental defects
    • Otto GP, Wu MY, Kazgan N, Anderson OR, Kessin RH. Dictyostelium macroautophagy mutants vary in the severity of their developmental defects. J Biol Chem 2004; 279:15621-9.
    • (2004) J Biol Chem , vol.279 , pp. 15621-15629
    • Otto, G.P.1    Wu, M.Y.2    Kazgan, N.3    Anderson, O.R.4    Kessin, R.H.5
  • 243
    • 14744268915 scopus 로고    scopus 로고
    • Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy
    • Yoshimoto K, Hanaoka H, Sato S, Kato T, Tabata S, Noda T, Ohsumi Y. Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy. Plant Cell 2004; 16:2967-83.
    • (2004) Plant Cell , vol.16 , pp. 2967-2983
    • Yoshimoto, K.1    Hanaoka, H.2    Sato, S.3    Kato, T.4    Tabata, S.5    Noda, T.6    Ohsumi, Y.7
  • 244
    • 0037031843 scopus 로고    scopus 로고
    • The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana
    • Doelling JH, Walker JM, Friedman EM, Thompson AR, Vierstra RD. The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana. J Biol Chem 2002; 277:33105-14.
    • (2002) J Biol Chem , vol.277 , pp. 33105-33114
    • Doelling, J.H.1    Walker, J.M.2    Friedman, E.M.3    Thompson, A.R.4    Vierstra, R.D.5
  • 245
    • 0035983934 scopus 로고    scopus 로고
    • Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene
    • Hanaoka H, Noda T, Shirano Y, Kato T, Hayashi H, Shibata D, Tabata S, Ohsumi Y. Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene. Plant Physiol 2002; 129:1181-93.
    • (2002) Plant Physiol , vol.129 , pp. 1181-1193
    • Hanaoka, H.1    Noda, T.2    Shirano, Y.3    Kato, T.4    Hayashi, H.5    Shibata, D.6    Tabata, S.7    Ohsumi, Y.8
  • 246
    • 0042691506 scopus 로고    scopus 로고
    • Autophagy genes are essential for dauer development and life-span extension in C. elegans
    • Melendez A, Talloczy Z, Seaman M, Eskelinen E-L, Hall DH, Levine B. Autophagy genes are essential for dauer development and life-span extension in C. elegans. Science 2003; 301:1387-91.
    • (2003) Science , vol.301 , pp. 1387-1391
    • Melendez, A.1    Talloczy, Z.2    Seaman, M.3    Eskelinen, E.-L.4    Hall, D.H.5    Levine, B.6
  • 249
    • 0022904943 scopus 로고
    • Radiolabelled sugars as probes of hepatocytic autophagy
    • Seglen PO, Gordon PB, Høyvik H. Radiolabelled sugars as probes of hepatocytic autophagy. Biomed Biochim Acta 1986; 45:1647-56.
    • (1986) Biomed Biochim Acta , vol.45 , pp. 1647-1656
    • Seglen, P.O.1    Gordon, P.B.2    Høyvik, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.