메뉴 건너뛰기




Volumn 3, Issue 6, 2007, Pages 331-338

Small molecules enhance autophagy and reduce toxicity in Huntington's disease models

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; BAFILOMYCIN A1; CENTRAL NERVOUS SYSTEM AGENTS; HUNTINGTIN; MUTANT PROTEIN; RAPAMYCIN; SMALL MOLECULE ENHANCER OF RAPAMYCIN 10; SMALL MOLECULE ENHANCER OF RAPAMYCIN 18; SMALL MOLECULE ENHANCER OF RAPAMYCIN 28; UNCLASSIFIED DRUG;

EID: 34248994604     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio883     Document Type: Article
Times cited : (532)

References (29)
  • 1
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky, D.J. & Emr, S.D. Autophagy as a regulated pathway of cellular degradation. Science 290, 1717-1721 (2000).
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 3
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar, B., Duden, R. & Rubinsztein, D.C. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11, 1107-1117 (2002).
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 4
    • 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. Nat. Genet. 36, 585-595 (2004).
    • (2004) Nat. Genet , vol.36 , pp. 585-595
    • Ravikumar, B.1
  • 6
    • 25444483066 scopus 로고    scopus 로고
    • Lithium induces autophagy by inhibiting inositol monophosphatase
    • Sarkar, S. et al. Lithium induces autophagy by inhibiting inositol monophosphatase. J. Cell Biol. 170, 1101-1111 (2005).
    • (2005) J. Cell Biol , vol.170 , pp. 1101-1111
    • Sarkar, S.1
  • 7
    • 0036533795 scopus 로고    scopus 로고
    • Lessons from animal models of Huntington's disease
    • Rubinsztein, D.C. Lessons from animal models of Huntington's disease. Trends Genet. 18, 202-209 (2002).
    • (2002) Trends Genet , vol.18 , pp. 202-209
    • Rubinsztein, D.C.1
  • 8
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein
    • Sarkar, S., Davies, J.E., Huang, Z., Tunnacliffe, A. & Rubinsztein, D.C. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and α-synuclein. J. Biol. Chem. 282, 5641-5652 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 9
    • 31544454404 scopus 로고    scopus 로고
    • Rapamycin alleviates toxicity of different aggregate-prone proteins
    • Berger, Z. et al. Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum. Mol. Genet. 15, 433-442 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 433-442
    • Berger, Z.1
  • 10
    • 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
  • 11
    • 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
  • 12
    • 33644609471 scopus 로고    scopus 로고
    • PKR-dependent autophagic degradation of herpes simplex virus type 1
    • Talloczy, Z., Virgin, H.W.T. & Levine, B. PKR-dependent autophagic degradation of herpes simplex virus type 1. Autophagy 2, 24-29 (2006).
    • (2006) Autophagy , vol.2 , pp. 24-29
    • Talloczy, Z.1    Virgin, H.W.T.2    Levine, B.3
  • 14
    • 9344247454 scopus 로고    scopus 로고
    • Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips
    • Huang, J. et al. Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips. Proc. Natl. Acad. Sci. USA 101, 16594-16599 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16594-16599
    • Huang, J.1
  • 15
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima, N. et al. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J. Cell Biol. 152, 657-668 (2001).
    • (2001) J. Cell Biol , vol.152 , pp. 657-668
    • Mizushima, N.1
  • 16
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific aminoterminal threonine modification by lactacystin
    • Fenteany, G. et al. Inhibition of proteasome activities and subunit-specific aminoterminal threonine modification by lactacystin. Science 268, 726-731 (1995).
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1
  • 17
    • 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
  • 18
    • 4344712684 scopus 로고    scopus 로고
    • Methods for monitoring autophagy
    • Mizushima, N. Methods for monitoring autophagy. Int. J. Biochem. Cell Biol. 36, 2491-2502 (2004).
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 2491-2502
    • Mizushima, N.1
  • 19
    • 19444382327 scopus 로고    scopus 로고
    • The dynamics of autophagy visualised in live cells: From autophagosome formation to fusion with endo/lysosomes
    • Bampton, E.T.W., Goemans, C.G., Niranjan, D., Mizushima, N. & Tolkovsky, A.M. The dynamics of autophagy visualised in live cells: from autophagosome formation to fusion with endo/lysosomes. Autophagy 1, 23-36 (2005).
    • (2005) Autophagy , vol.1 , pp. 23-36
    • Bampton, E.T.W.1    Goemans, C.G.2    Niranjan, D.3    Mizushima, N.4    Tolkovsky, A.M.5
  • 20
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto, A. et al. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct. Funct. 23, 33-42 (1998).
    • (1998) Cell Struct. Funct , vol.23 , pp. 33-42
    • Yamamoto, A.1
  • 21
    • 0021691112 scopus 로고
    • Inhibition of fast axonal transport by erythro-9-[3-(2-hydroxynonyl)]adenine
    • Ekstrom, P. & Kanje, M. Inhibition of fast axonal transport by erythro-9-[3-(2-hydroxynonyl)]adenine. J. Neurochem. 43, 1342-1345 (1984).
    • (1984) J. Neurochem , vol.43 , pp. 1342-1345
    • Ekstrom, P.1    Kanje, M.2
  • 22
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • Jackson, G.R. et al. Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Neuron 21, 633-642 (1998).
    • (1998) Neuron , vol.21 , pp. 633-642
    • Jackson, G.R.1
  • 23
    • 33749242234 scopus 로고    scopus 로고
    • Drosophila in the study of neurodegenerative disease
    • Marsh, J.L. & Thompson, L.M. Drosophila in the study of neurodegenerative disease. Neuron 52, 169-178 (2006).
    • (2006) Neuron , vol.52 , pp. 169-178
    • Marsh, J.L.1    Thompson, L.M.2
  • 24
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmelzle, T. & Hall, M.N. TOR, a central controller of cell growth. Cell 103, 253-262 (2000).
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 25
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome- dependent proteolysis in living cells
    • Dantuma, N.P., Lindsten, K., Glas, R., Jellne, M. & Masucci, M.G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome- dependent proteolysis in living cells. Nat. Biotechnol. 18, 538-543 (2000).
    • (2000) Nat. Biotechnol , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 26
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata, A., Riley, B.E., Johnston, J.A. & Kopito, R.R. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J. Biol. Chem. 280, 40282-40292 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 28
    • 2942743598 scopus 로고    scopus 로고
    • The DrosDel collection: A set of P-element insertions for generating custom chromosomal aberrations in Drosophila melanogaster
    • Ryder, E. et al. The DrosDel collection: a set of P-element insertions for generating custom chromosomal aberrations in Drosophila melanogaster. Genetics 167, 797-813 (2004).
    • (2004) Genetics , vol.167 , pp. 797-813
    • Ryder, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.