메뉴 건너뛰기




Volumn 441, Issue 7095, 2006, Pages 880-884

Loss of autophagy in the central nervous system causes neurodegeneration in mice

Author keywords

[No Author keywords available]

Indexed keywords

BIODIVERSITY; BIOMEDICAL ENGINEERING; CELLS; DEGRADATION; DISEASES; PROTEINS;

EID: 33646800306     PISSN: 00280836     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/nature04723     Document Type: Article
Times cited : (3041)

References (30)
  • 1
    • 7044238416 scopus 로고    scopus 로고
    • Neurodegenerative diseases: A decade of discoveries paves the way for therapeutic breakthroughs
    • Forman, M. S., Trojanowski, J. Q. & Lee, V. M. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nature Med. 10, 1055-1063 (2004).
    • (2004) Nature Med. , vol.10 , pp. 1055-1063
    • Forman, M.S.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 2
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • Shintani, T. & Klionsky, D. J. Autophagy in health and disease: a double-edged sword. Science 306, 990-995 (2004).
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 3
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899 (2003).
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 4
    • 22044442015 scopus 로고    scopus 로고
    • Autophagosomes: Biogenesis from scratch?
    • Reggiori, F. & Klionsky, D. J. Autophagosomes: biogenesis from scratch? Curr. Opin. Cell Biol. 17, 415-422 (2005).
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 415-422
    • 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, D. J. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell 6, 463-477 (2004).
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 6
    • 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. 333, 169-174 (1993).
    • (1993) FEBS Lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 7
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • Kuma, A. et al. The role of autophagy during the early neonatal starvation period. Nature 432, 1032-1036 (2004).
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1
  • 8
    • 21044455137 scopus 로고    scopus 로고
    • Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice
    • Komatsu, M. et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169, 425-434 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 425-434
    • Komatsu, M.1
  • 9
    • 0042691506 scopus 로고    scopus 로고
    • Autophagy genes are essential for dauer development and life-span extension in C. elegans
    • Melendez, A. et al. Autophagy genes are essential for dauer development and life-span extension in C. elegans. Science 301, 1387-1391 (2003).
    • (2003) Science , vol.301 , pp. 1387-1391
    • Melendez, A.1
  • 10
    • 0038393057 scopus 로고    scopus 로고
    • The Drosophila homolog of Aut1 is essential for autophagy and development
    • Juhasz, G., Csikos, G., Sinka, R., Erdelyi, M. & Sass, M. The Drosophila homolog of Aut1 is essential for autophagy and development. FEBS Lett. 543, 154-158 (2003).
    • (2003) FEBS Lett. , vol.543 , pp. 154-158
    • Juhasz, G.1    Csikos, G.2    Sinka, R.3    Erdelyi, M.4    Sass, M.5
  • 11
    • 12844275079 scopus 로고    scopus 로고
    • Endogenous MHC class II processing of a viral nuclear antigen after autophagy
    • Paludan, C. et al. Endogenous MHC class II processing of a viral nuclear antigen after autophagy. Science 307, 593-596 (2005).
    • (2005) Science , vol.307 , pp. 593-596
    • Paludan, C.1
  • 12
    • 8344247016 scopus 로고    scopus 로고
    • Autophagy defends cells against invading group A Streptococcus
    • Nakagawa, I. et al. Autophagy defends cells against invading group A Streptococcus. Science 306, 1037-1040 (2004).
    • (2004) Science , vol.306 , pp. 1037-1040
    • Nakagawa, I.1
  • 13
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • Gutierrez, M. G. et al. Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119, 753-766 (2004).
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1
  • 14
    • 0030267396 scopus 로고    scopus 로고
    • Bypass of lethality with mosaic mice generated by Cre-loxP-mediated recombination
    • Betz, U. A., Vosshenrich, C. A., Rajewsky, K. & Muller, W. Bypass of lethality with mosaic mice generated by Cre-loxP-mediated recombination. Curr. Biol. 6, 1307-1316 (1996).
    • (1996) Curr. Biol. , vol.6 , pp. 1307-1316
    • Betz, U.A.1    Vosshenrich, C.A.2    Rajewsky, K.3    Muller, W.4
  • 15
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. Molecular dissection of autophagy: two ubiquitin-like systems. Nature Rev. Mol. Cell Biol. 2, 211-216 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 16
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya, Y. et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 19, 5720-5728 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5720-5728
    • Kabeya, Y.1
  • 17
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover, A. & Brundin, P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40, 427-446 (2003).
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 19
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N. F., Sampat, R. M. & Kopito, R. R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (2001).
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 20
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy-a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
    • Yu, W. H. et al. Macroautophagy-a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease. J. Cell Biol. 171, 87-98 (2005).
    • (2005) J. Cell Biol. , vol.171 , pp. 87-98
    • Yu, W.H.1
  • 21
    • 19244384656 scopus 로고    scopus 로고
    • Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice
    • Tanaka, Y. et al. Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice. Nature 406, 902-906 (2000).
    • (2000) Nature , vol.406 , pp. 902-906
    • Tanaka, Y.1
  • 22
    • 17044440789 scopus 로고    scopus 로고
    • Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)
    • Nishino, I. et al. Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease). Nature 406, 906-910 (2000).
    • (2000) Nature , vol.406 , pp. 906-910
    • Nishino, I.1
  • 24
    • 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. et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nature Genet. 36, 585-595 (2004).
    • (2004) Nature Genet. , vol.36 , pp. 585-595
    • Ravikumar, B.1
  • 25
    • 0344874551 scopus 로고    scopus 로고
    • Emerging role for autophagy in the removal of aggresomes in Schwann cells
    • Fortun, J., Dunn, W. A. Jr, Joy, S., Li, J. & Notterpek, L. Emerging role for autophagy in the removal of aggresomes in Schwann cells. J. Neurosci. 23, 10672-10680 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 10672-10680
    • Fortun, J.1    Dunn Jr., W.A.2    Joy, S.3    Li, J.4    Notterpek, L.5
  • 26
    • 25144506835 scopus 로고    scopus 로고
    • Autophagy in cell death: An innocent convict?
    • Levine, B. & Yuan, J. Autophagy in cell death: an innocent convict? J. Clin. Invest. 115, 2679-2688 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 2679-2688
    • Levine, B.1    Yuan, J.2
  • 27
    • 0036501460 scopus 로고    scopus 로고
    • Knockout mouse model for Fxr2: A model for menta retardation
    • Bontekoe, C. J. et al. Knockout mouse model for Fxr2: a model for menta retardation. Hum. Mol. Genet. 11, 487-498 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 487-498
    • Bontekoe, C.J.1
  • 28
    • 0037301337 scopus 로고    scopus 로고
    • Involvement of two different cell death pathways in retina atrophy of cathepsin D-deficient mice
    • Koike, M. et al. Involvement of two different cell death pathways in retina atrophy of cathepsin D-deficient mice. Mol. Cell. Neurosci. 22, 146-161 (2003).
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 146-161
    • Koike, M.1
  • 29
    • 0028990820 scopus 로고
    • Cysteine proteinases in GH4C1 cells, a rat pituitary tumour cell line, are secreted by the constitutive and regulated secretory pathways
    • Waguri, S. et al. Cysteine proteinases in GH4C1 cells, a rat pituitary tumour cell line, are secreted by the constitutive and regulated secretory pathways. Eur. J. Cell Biol. 67, 308-318 (1995).
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 308-318
    • Waguri, S.1
  • 30
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-γ and contribution to ATP-dependent proteolysis
    • Tanahashi, N. et al. Hybrid proteasomes. Induction by interferon-γ and contribution to ATP-dependent proteolysis. J. Biol. Chem. 275, 14336-14345 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14336-14345
    • Tanahashi, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.