메뉴 건너뛰기




Volumn 14, Issue 5, 2007, Pages 887-894

Constitutive autophagy: Vital role in clearance of unfavorable proteins in neurons

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SYNUCLEIN; CATHEPSIN D; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; HUNTINGTIN; INSULIN RECEPTOR SUBSTRATE 2; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; MAMMALIAN TARGET OF RAPAMYCIN; MICROTUBULE ASSOCIATED PROTEIN 1; PHOSPHATIDYLINOSITOL 3 KINASE; POLYGLUTAMINE; PRESENILIN 1; PROTEASOME; PROTEIN P62; RAPAMYCIN; SOMATOMEDIN C; UBIQUITIN;

EID: 34247398719     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/sj.cdd.4402120     Document Type: Review
Times cited : (142)

References (52)
  • 1
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 2003; 426: 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 2
    • 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: 463-477.
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 3
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • Cuervo AM. Autophagy: In sickness and in health. Trends Cell Biol 2004; 14: 70-77.
    • (2004) Trends Cell Biol , vol.14 , pp. 70-77
    • Cuervo, A.M.1
  • 5
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige K, Baba M, Tsuboi S, Noda T, Ohsumi Y. Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J Cell Biol 1992; 119: 301-311.
    • (1992) J Cell Biol , vol.119 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 6
    • 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: 1101-1111.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 7
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue 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 homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 2000; 19: 5720-5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6
  • 9
    • 4344604111 scopus 로고    scopus 로고
    • HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates
    • Tanida I, Sou YS, Ezaki J, Minematsu-Ikeguchi N, Ueno T, Kominami E. HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates. J Biol Chem 2004; 279: 36268-36276.
    • (2004) J Biol Chem , vol.279 , pp. 36268-36276
    • Tanida, I.1    Sou, Y.S.2    Ezaki, J.3    Minematsu-Ikeguchi, N.4    Ueno, T.5    Kominami, E.6
  • 11
    • 0035910423 scopus 로고    scopus 로고
    • The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3
    • Tanida I, Tanida-Miyake E, Ueno T, Kominami E. The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3. J Biol Chem 2001; 276: 1701-1706.
    • (2001) J Biol Chem , vol.276 , pp. 1701-1706
    • Tanida, I.1    Tanida-Miyake, E.2    Ueno, T.3    Kominami, E.4
  • 12
    • 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: 13739-13744.
    • (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
  • 13
    • 0020510501 scopus 로고
    • Quantitative correlation between proteolysis and macro- and microautophagy in mouse hepatocytes during starvation and refeeding
    • Mortimore GE, Hutson NJ, Surmacz CA. Quantitative correlation between proteolysis and macro- and microautophagy in mouse hepatocytes during starvation and refeeding. Proc Natl Acad Sci USA 1993; 80: 2179-2183.
    • (1993) Proc Natl Acad Sci USA , vol.80 , pp. 2179-2183
    • Mortimore, G.E.1    Hutson, N.J.2    Surmacz, C.A.3
  • 14
    • 21044455137 scopus 로고    scopus 로고
    • Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice
    • Komatsu M, Waguri S, Ueno T, Iwata J, Murata S, Tanida I et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J Cell Biol 2005; 169: 425-434.
    • (2005) J Cell Biol , vol.169 , pp. 425-434
    • Komatsu, M.1    Waguri, S.2    Ueno, T.3    Iwata, J.4    Murata, S.5    Tanida, I.6
  • 15
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada M, Ohsumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 1993; 333: 169-174.
    • (1993) FEBS Lett , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 16
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • Kuma A, Hatano M, Matsui M, Yamamoto A, Nakaya H, Yoshimori T et al. The role of autophagy during the early neonatal starvation period. Nature 2004; 432: 1032-1036.
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1    Hatano, M.2    Matsui, M.3    Yamamoto, A.4    Nakaya, H.5    Yoshimori, T.6
  • 17
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and cell survival in the absence of apoptosis
    • Lum JJ, Bauer DE, Kong M, Harris MH, Li C, Lindsten T et al. Growth factor regulation of autophagy and cell survival in the absence of apoptosis. Cell 2005; 120: 237-248.
    • (2005) Cell , vol.120 , pp. 237-248
    • Lum, J.J.1    Bauer, D.E.2    Kong, M.3    Harris, M.H.4    Li, C.5    Lindsten, T.6
  • 18
    • 0027419879 scopus 로고
    • Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport
    • Hollenbeck PJ. Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport. J Cell Biol 1993; 121: 305-315.
    • (1993) J Cell Biol , vol.121 , pp. 305-315
    • Hollenbeck, P.J.1
  • 20
    • 0037734370 scopus 로고    scopus 로고
    • Mutations in dynein link motor neuron degeneration to defects in retrograde transport
    • Hafezparast M, Klocke R, Ruhrberg C, Marquardt A, Ahmad-Annuar A, Bowen S et al. Mutations in dynein link motor neuron degeneration to defects in retrograde transport. Science 2003; 300: 808-812.
    • (2003) Science , vol.300 , pp. 808-812
    • Hafezparast, M.1    Klocke, R.2    Ruhrberg, C.3    Marquardt, A.4    Ahmad-Annuar, A.5    Bowen, S.6
  • 22
    • 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: 40282-40292.
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 24
    • 0030045552 scopus 로고    scopus 로고
    • Properties of the endosomal-lysosomal system in the human central nervous system: Disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease
    • Cataldo AM, Hamilton DJ, Barnett JL, Paskevich PA, Nixon RA. Properties of the endosomal-lysosomal system in the human central nervous system: disturbances mark most neurons in populations at risk to degenerate in Alzheimer's disease. J Neurosci 1996; 16: 186-199.
    • (1996) J Neurosci , vol.16 , pp. 186-199
    • Cataldo, A.M.1    Hamilton, D.J.2    Barnett, J.L.3    Paskevich, P.A.4    Nixon, R.A.5
  • 26
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E, McIntyre C, Castano JG, Aronin N et al. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 2000; 20: 7268-7278.
    • (2000) J Neurosci , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6
  • 27
    • 0035364748 scopus 로고    scopus 로고
    • Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration
    • Petersen A, Larsen KE, Behr GG, Romero N, Przedborski S, Brundin P et al. Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration. Hum Mol Genet 2001; 10: 1243-1254.
    • (2001) Hum Mol Genet , vol.10 , pp. 1243-1254
    • Petersen, A.1    Larsen, K.E.2    Behr, G.G.3    Romero, N.4    Przedborski, S.5    Brundin, P.6
  • 28
    • 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
  • 29
    • 17044440789 scopus 로고    scopus 로고
    • Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)
    • Nishino I, Fu J, Tanji K, Yamada T, Shimojo S, Koori T et al. Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease). Nature 2000; 406: 906-910.
    • (2000) Nature , vol.406 , pp. 906-910
    • Nishino, I.1    Fu, J.2    Tanji, K.3    Yamada, T.4    Shimojo, S.5    Koori, T.6
  • 30
  • 31
    • 0030058208 scopus 로고    scopus 로고
    • Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo
    • Ikeda H, Yamaguchi M, Sugai S, Aze Y, Narumiya S, Kakizuka A. Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Nat Genet 1996; 13: 196-202.
    • (1996) Nat Genet , vol.13 , pp. 196-202
    • Ikeda, H.1    Yamaguchi, M.2    Sugai, S.3    Aze, Y.4    Narumiya, S.5    Kakizuka, A.6
  • 32
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I, Mahlke C, Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 2003; 421: 373-379.
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 33
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004; 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 34
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B, Duden R, Rubinsztein DC. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 2002; 11: 1107-1117.
    • (2002) Hum Mol Genet , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 35
    • 11244297916 scopus 로고    scopus 로고
    • Dysregulation of the TSC-mTOR pathway in human disease
    • Inoki K, Corradetti MN, Guan KL. Dysregulation of the TSC-mTOR pathway in human disease. Nat Genet 2005; 37: 19-24.
    • (2005) Nat Genet , vol.37 , pp. 19-24
    • Inoki, K.1    Corradetti, M.N.2    Guan, K.L.3
  • 36
    • 33749055522 scopus 로고    scopus 로고
    • Autophagy: A cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically
    • Bergamini E. Autophagy: A cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically. Mol Aspects Med 2006; 27: 403-410.
    • (2006) Mol Aspects Med , vol.27 , pp. 403-410
    • Bergamini, E.1
  • 37
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B, Vacher C, Berger Z, Davies JE, Luo S, Oroz LG et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 2004; 36: 585-595.
    • (2004) Nat Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6
  • 38
    • 33644540193 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway
    • Yamamoto A, Cremona ML, Rothman JE. Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway. J Cell Biol 2006; 172: 719-731.
    • (2006) J Cell Biol , vol.172 , pp. 719-731
    • Yamamoto, A.1    Cremona, M.L.2    Rothman, J.E.3
  • 39
    • 2442421944 scopus 로고    scopus 로고
    • Degradative organelles containing mislocalized alpha-and beta-synuclein proliferate in presenilin-1 null neurons
    • Wilson CA, Murphy DD, Giasson BI, Zhang B, Trojanowski JQ, Lee VM. Degradative organelles containing mislocalized alpha-and beta-synuclein proliferate in presenilin-1 null neurons. J Cell Biol 2004; 165 335-346.
    • (2004) J Cell Biol , vol.165 , pp. 335-346
    • Wilson, C.A.1    Murphy, D.D.2    Giasson, B.I.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 40
    • 4644257963 scopus 로고    scopus 로고
    • Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway
    • Esselens C, Oorschot V, Baert V, Raemaekers T, Spittaels K, Serneels L et al. Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway. J Cell Biol 2004; 166: 1041-1054.
    • (2004) J Cell Biol , vol.166 , pp. 1041-1054
    • Esselens, C.1    Oorschot, V.2    Baert, V.3    Raemaekers, T.4    Spittaels, K.5    Serneels, L.6
  • 41
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy - a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease
    • Yu WH, Cuervo AM, Kumar A, Peterhoff CM, Schmidt SD, Lee JH et al. Macroautophagy - a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease. J Cell Biol 2005; 171: 87-98.
    • (2005) J Cell Biol , vol.171 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3    Peterhoff, C.M.4    Schmidt, S.D.5    Lee, J.H.6
  • 42
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • Jenner P, Olanow CW. Understanding cell death in Parkinson's disease. Ann Neurol 1998; 44: S72-S84.
    • (1998) Ann Neurol , vol.44
    • Jenner, P.1    Olanow, C.W.2
  • 43
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger R, Kuhn W, Muller T, Woitalla D, Graeber M, Kosel S et al. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet 1998; 18: 106-108.
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 44
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A et al. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 1997; 276: 2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 45
    • 2942618660 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders
    • Chung KK, Dawson VL, Dawson TM. The role of the ubiquitin-proteasomal pathway in Parkinson's disease and other neurodegenerative disorders. Trends Neurosci 2001; 24: S7-S14.
    • (2001) Trends Neurosci , vol.24
    • Chung, K.K.1    Dawson, V.L.2    Dawson, T.M.3
  • 46
    • 0037154184 scopus 로고    scopus 로고
    • Recent advances in the genetics and pathogenesis of Parkinson disease
    • Mouradian MM. Recent advances in the genetics and pathogenesis of Parkinson disease. Neurology 2002; 58: 179-185.
    • (2002) Neurology , vol.58 , pp. 179-185
    • Mouradian, M.M.1
  • 47
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, Greene LA. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci 2001; 21: 9549-9560.
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 49
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004; 305: 1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 50
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441: 880-884.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 51
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006; 441: 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 52
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A 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: 603-614.
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.