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Volumn 7, Issue 11, 2012, Pages

Large-Scale Screen for Modifiers of Ataxin-3-Derived Polyglutamine-Induced Toxicity in Drosophila

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EID: 84868368482     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047452     Document Type: Article
Times cited : (33)

References (56)
  • 1
    • 77955636420 scopus 로고    scopus 로고
    • Autosomal dominant cerebellar ataxias: polyglutamine expansions and beyond
    • Durr A, Autosomal dominant cerebellar ataxias: polyglutamine expansions and beyond. Lancet Neurol 9: 885-894.
    • Lancet Neurol , vol.9 , pp. 885-894
    • Durr, A.1
  • 2
    • 0028143527 scopus 로고
    • CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1
    • Kawaguchi Y, Okamoto T, Taniwaki M, Aizawa M, Inoue M, et al. (1994) CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. Nat Genet 8: 221-228.
    • (1994) Nat Genet , vol.8 , pp. 221-228
    • Kawaguchi, Y.1    Okamoto, T.2    Taniwaki, M.3    Aizawa, M.4    Inoue, M.5
  • 3
    • 77949775195 scopus 로고    scopus 로고
    • Repeat expansion disease: progress and puzzles in disease pathogenesis
    • La Spada AR, Taylor JP, (2010) Repeat expansion disease: progress and puzzles in disease pathogenesis. Nat Rev Genet 11: 247-258.
    • (2010) Nat Rev Genet , vol.11 , pp. 247-258
    • La Spada, A.R.1    Taylor, J.P.2
  • 4
    • 16044373842 scopus 로고    scopus 로고
    • Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice
    • Mangiarini L, Sathasivam K, Seller M, Cozens B, Harper A, et al. (1996) Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 87: 493-506.
    • (1996) Cell , vol.87 , pp. 493-506
    • Mangiarini, L.1    Sathasivam, K.2    Seller, M.3    Cozens, B.4    Harper, A.5
  • 5
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr HT, Zoghbi HY, (2007) Trinucleotide repeat disorders. Annu Rev Neurosci 30: 575-621.
    • (2007) Annu Rev Neurosci , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 6
    • 0035871295 scopus 로고    scopus 로고
    • Beyond the Qs in the polyglutamine diseases
    • Orr HT, (2001) Beyond the Qs in the polyglutamine diseases. Genes Dev 15: 925-932.
    • (2001) Genes Dev , vol.15 , pp. 925-932
    • Orr, H.T.1
  • 7
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: mechanisms and common principles
    • Gatchel JR, Zoghbi HY, (2005) Diseases of unstable repeat expansion: mechanisms and common principles. Nat Rev Genet 6: 743-755.
    • (2005) Nat Rev Genet , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 8
    • 0033551063 scopus 로고    scopus 로고
    • Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology
    • Scherzinger E, Sittler A, Schweiger K, Heiser V, Lurz R, et al. (1999) Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology. Proc Natl Acad Sci U S A 96: 4604-4609.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 4604-4609
    • Scherzinger, E.1    Sittler, A.2    Schweiger, K.3    Heiser, V.4    Lurz, R.5
  • 9
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA, (2004) Protein aggregation and neurodegenerative disease. Nat Med 10 (Suppl):: S10-17.
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 10
    • 38349158062 scopus 로고    scopus 로고
    • Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic
    • Takahashi T, Kikuchi S, Katada S, Nagai Y, Nishizawa M, et al. (2008) Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum Mol Genet 17: 345-356.
    • (2008) Hum Mol Genet , vol.17 , pp. 345-356
    • Takahashi, T.1    Kikuchi, S.2    Katada, S.3    Nagai, Y.4    Nishizawa, M.5
  • 11
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME, (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95: 55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 12
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement IA, Skinner PJ, Kaytor MD, Yi H, Hersch SM, et al. (1998) Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95: 41-53.
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5
  • 13
    • 33747884761 scopus 로고    scopus 로고
    • Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes
    • Satterfield TF, Pallanck LJ, (2006) Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes. Hum Mol Genet 15: 2523-2532.
    • (2006) Hum Mol Genet , vol.15 , pp. 2523-2532
    • Satterfield, T.F.1    Pallanck, L.J.2
  • 14
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR, (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292: 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 15
    • 34547807613 scopus 로고    scopus 로고
    • Global changes to the ubiquitin system in Huntington's disease
    • Bennett EJ, Shaler TA, Woodman B, Ryu KY, Zaitseva TS, et al. (2007) Global changes to the ubiquitin system in Huntington's disease. Nature 448: 704-708.
    • (2007) Nature , vol.448 , pp. 704-708
    • Bennett, E.J.1    Shaler, T.A.2    Woodman, B.3    Ryu, K.Y.4    Zaitseva, T.S.5
  • 16
    • 45749147456 scopus 로고    scopus 로고
    • RNA toxicity is a component of ataxin-3 degeneration in Drosophila
    • Li LB, Yu Z, Teng X, Bonini NM, (2008) RNA toxicity is a component of ataxin-3 degeneration in Drosophila. Nature 453: 1107-1111.
    • (2008) Nature , vol.453 , pp. 1107-1111
    • Li, L.B.1    Yu, Z.2    Teng, X.3    Bonini, N.M.4
  • 17
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey UB, Nie Z, Batlevi Y, McCray BA, Ritson GP, et al. (2007) HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447: 859-863.
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3    McCray, B.A.4    Ritson, G.P.5
  • 18
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • Bilen J, Bonini NM, (2007) Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila. PLoS Genet 3: 1950-1964.
    • (2007) PLoS Genet , vol.3 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 20
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P, Benzer S, (2000) Genetic suppression of polyglutamine toxicity in Drosophila. Science 287: 1837-1840.
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 21
    • 40149101562 scopus 로고    scopus 로고
    • Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila
    • Lessing D, Bonini NM, (2008) Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila. PLoS Biol 6: e29.
    • (2008) PLoS Biol , vol.6
    • Lessing, D.1    Bonini, N.M.2
  • 22
    • 34447530305 scopus 로고    scopus 로고
    • A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila
    • Dietzl G, Chen D, Schnorrer F, Su KC, Barinova Y, et al. (2007) A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila. Nature 448: 151-156.
    • (2007) Nature , vol.448 , pp. 151-156
    • Dietzl, G.1    Chen, D.2    Schnorrer, F.3    Su, K.C.4    Barinova, Y.5
  • 23
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • Warrick JM, Paulson HL, Gray-Board GL, Bui QT, Fischbeck KH, et al. (1998) Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 93: 939-949.
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1    Paulson, H.L.2    Gray-Board, G.L.3    Bui, Q.T.4    Fischbeck, K.H.5
  • 24
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M, Lendon CL, Rizzu P, Baker M, Froelich S, et al. (1998) Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393: 702-705.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3    Baker, M.4    Froelich, S.5
  • 25
    • 0035958642 scopus 로고    scopus 로고
    • Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles
    • Wittmann CW, Wszolek MF, Shulman JM, Salvaterra PM, Lewis J, et al. (2001) Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles. Science 293: 711-714.
    • (2001) Science , vol.293 , pp. 711-714
    • Wittmann, C.W.1    Wszolek, M.F.2    Shulman, J.M.3    Salvaterra, P.M.4    Lewis, J.5
  • 26
    • 81855172495 scopus 로고    scopus 로고
    • Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation
    • Ambegaokar SS, Jackson GR, (2011) Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation. Hum Mol Genet 20: 4947-4977.
    • (2011) Hum Mol Genet , vol.20 , pp. 4947-4977
    • Ambegaokar, S.S.1    Jackson, G.R.2
  • 27
    • 0346361872 scopus 로고    scopus 로고
    • Genetic modifiers of tauopathy in Drosophila
    • Shulman JM, Feany MB, (2003) Genetic modifiers of tauopathy in Drosophila. Genetics 165: 1233-1242.
    • (2003) Genetics , vol.165 , pp. 1233-1242
    • Shulman, J.M.1    Feany, M.B.2
  • 28
    • 77949879488 scopus 로고    scopus 로고
    • Nuclear aggregation of polyglutamine-expanded ataxin-3: fragments escape the cytoplasmic quality control
    • Breuer P, Haacke A, Evert BO, Wullner U, (2010) Nuclear aggregation of polyglutamine-expanded ataxin-3: fragments escape the cytoplasmic quality control. J Biol Chem 285: 6532-6537.
    • (2010) J Biol Chem , vol.285 , pp. 6532-6537
    • Breuer, P.1    Haacke, A.2    Evert, B.O.3    Wullner, U.4
  • 29
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation
    • Perez MK, Paulson HL, Pendse SJ, Saionz SJ, Bonini NM, et al. (1998) Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J Cell Biol 143: 1457-1470.
    • (1998) J Cell Biol , vol.143 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3    Saionz, S.J.4    Bonini, N.M.5
  • 30
    • 0038701684 scopus 로고    scopus 로고
    • Huntingtin aggregation and toxicity in Huntington's disease
    • Bates G, (2003) Huntingtin aggregation and toxicity in Huntington's disease. Lancet 361: 1642-1644.
    • (2003) Lancet , vol.361 , pp. 1642-1644
    • Bates, G.1
  • 31
    • 0032879437 scopus 로고    scopus 로고
    • Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates
    • Wanker EE, Scherzinger E, Heiser V, Sittler A, Eickhoff H, et al. (1999) Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates. Methods Enzymol 309: 375-386.
    • (1999) Methods Enzymol , vol.309 , pp. 375-386
    • Wanker, E.E.1    Scherzinger, E.2    Heiser, V.3    Sittler, A.4    Eickhoff, H.5
  • 32
    • 76249110159 scopus 로고    scopus 로고
    • Gene networks in Drosophila melanogaster: integrating experimental data to predict gene function
    • Costello JC, Dalkilic MM, Beason SM, Gehlhausen JR, Patwardhan R, et al. (2009) Gene networks in Drosophila melanogaster: integrating experimental data to predict gene function. Genome Biol 10: R97.
    • (2009) Genome Biol , vol.10
    • Costello, J.C.1    Dalkilic, M.M.2    Beason, S.M.3    Gehlhausen, J.R.4    Patwardhan, R.5
  • 33
    • 77955858671 scopus 로고    scopus 로고
    • Improved activities of CREB binding protein, heterogeneous nuclear ribonucleoproteins and proteasome following downregulation of noncoding hsromega transcripts help suppress poly(Q) pathogenesis in fly models
    • Mallik M, Lakhotia SC, (2010) Improved activities of CREB binding protein, heterogeneous nuclear ribonucleoproteins and proteasome following downregulation of noncoding hsromega transcripts help suppress poly(Q) pathogenesis in fly models. Genetics 184: 927-945.
    • (2010) Genetics , vol.184 , pp. 927-945
    • Mallik, M.1    Lakhotia, S.C.2
  • 34
    • 77955870526 scopus 로고    scopus 로고
    • A genomewide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila
    • Zhang S, Binari R, Zhou R, Perrimon N, (2010) A genomewide RNA interference screen for modifiers of aggregates formation by mutant Huntingtin in Drosophila. Genetics 184: 1165-1179.
    • (2010) Genetics , vol.184 , pp. 1165-1179
    • Zhang, S.1    Binari, R.2    Zhou, R.3    Perrimon, N.4
  • 35
    • 2342652188 scopus 로고    scopus 로고
    • Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation
    • Nollen EA, Garcia SM, van Haaften G, Kim S, Chavez A, et al. (2004) Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation. Proc Natl Acad Sci U S A 101: 6403-6408.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6403-6408
    • Nollen, E.A.1    Garcia, S.M.2    van Haaften, G.3    Kim, S.4    Chavez, A.5
  • 36
    • 0033030565 scopus 로고    scopus 로고
    • Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
    • Chai Y, Koppenhafer SL, Shoesmith SJ, Perez MK, Paulson HL, (1999) Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum Mol Genet 8: 673-682.
    • (1999) Hum Mol Genet , vol.8 , pp. 673-682
    • Chai, Y.1    Koppenhafer, S.L.2    Shoesmith, S.J.3    Perez, M.K.4    Paulson, H.L.5
  • 38
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman P, Wetzel R, Tanaka M, Nukina N, Goldberg AL, (2004) Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 14: 95-104.
    • (2004) Mol Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 39
    • 77949352928 scopus 로고    scopus 로고
    • Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation
    • Ortega Z, Diaz-Hernandez M, Maynard CJ, Hernandez F, Dantuma NP, et al. Acute polyglutamine expression in inducible mouse model unravels ubiquitin/proteasome system impairment and permanent recovery attributable to aggregate formation. J Neurosci 30: 3675-3688.
    • J Neurosci , vol.30 , pp. 3675-3688
    • Ortega, Z.1    Diaz-Hernandez, M.2    Maynard, C.J.3    Hernandez, F.4    Dantuma, N.P.5
  • 40
    • 15944419824 scopus 로고    scopus 로고
    • Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophila by a ubiquitin-associated mechanism
    • Warrick JM, Morabito LM, Bilen J, Gordesky-Gold B, Faust LZ, et al. (2005) Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophila by a ubiquitin-associated mechanism. Mol Cell 18: 37-48.
    • (2005) Mol Cell , vol.18 , pp. 37-48
    • Warrick, J.M.1    Morabito, L.M.2    Bilen, J.3    Gordesky-Gold, B.4    Faust, L.Z.5
  • 41
    • 79954464577 scopus 로고    scopus 로고
    • Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1
    • Chan WM, Tsoi H, Wu CC, Wong CH, Cheng TC, et al. (2011) Expanded polyglutamine domain possesses nuclear export activity which modulates subcellular localization and toxicity of polyQ disease protein via exportin-1. Hum Mol Genet 20: 1738-1750.
    • (2011) Hum Mol Genet , vol.20 , pp. 1738-1750
    • Chan, W.M.1    Tsoi, H.2    Wu, C.C.3    Wong, C.H.4    Cheng, T.C.5
  • 42
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies SW, Turmaine M, Cozens BA, DiFiglia M, Sharp AH, et al. (1997) Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90: 537-548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3    DiFiglia, M.4    Sharp, A.H.5
  • 43
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson HL, Perez MK, Trottier Y, Trojanowski JQ, Subramony SH, et al. (1997) Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19: 333-344.
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1    Perez, M.K.2    Trottier, Y.3    Trojanowski, J.Q.4    Subramony, S.H.5
  • 44
    • 0031446233 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases?
    • Ross CA, (1997) Intranuclear neuronal inclusions: a common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron 19: 1147-1150.
    • (1997) Neuron , vol.19 , pp. 1147-1150
    • Ross, C.A.1
  • 45
    • 3242892160 scopus 로고    scopus 로고
    • The multifaceted role of mTOR in cellular stress responses
    • Proud CG, (2004) The multifaceted role of mTOR in cellular stress responses. DNA Repair (Amst) 3: 927-934.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 927-934
    • Proud, C.G.1
  • 46
    • 41749089797 scopus 로고    scopus 로고
    • Reprogramming mRNA translation during stress
    • Yamasaki S, Anderson P, (2008) Reprogramming mRNA translation during stress. Curr Opin Cell Biol 20: 222-226.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 222-226
    • Yamasaki, S.1    Anderson, P.2
  • 47
    • 84859169870 scopus 로고    scopus 로고
    • The mitochondrial chaperone protein TRAP1 mitigates alpha-Synuclein toxicity
    • Butler EK, Voigt A, Lutz AK, Toegel JP, Gerhardt E, et al. (2012) The mitochondrial chaperone protein TRAP1 mitigates alpha-Synuclein toxicity. PLoS Genet 8: e1002488.
    • (2012) PLoS Genet , vol.8
    • Butler, E.K.1    Voigt, A.2    Lutz, A.K.3    Toegel, J.P.4    Gerhardt, E.5
  • 48
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, et al. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 23: 425-428.
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5
  • 49
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R, (1998) Repression of heat shock transription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94: 471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 50
    • 0033044001 scopus 로고    scopus 로고
    • Expression of ataxin-2 in brains from normal individuals and patients with Alzheimer's disease and spinocerebellar ataxia 2
    • Huynh DP, Del Bigio MR, Ho DH, Pulst SM, (1999) Expression of ataxin-2 in brains from normal individuals and patients with Alzheimer's disease and spinocerebellar ataxia 2. Ann Neurol 45: 232-241.
    • (1999) Ann Neurol , vol.45 , pp. 232-241
    • Huynh, D.P.1    Del Bigio, M.R.2    Ho, D.H.3    Pulst, S.M.4
  • 51
    • 84855258498 scopus 로고    scopus 로고
    • A genetic screening strategy identifies novel regulators of the proteostasis network
    • Silva MC, Fox S, Beam M, Thakkar H, Amaral MD, et al. (2011) A genetic screening strategy identifies novel regulators of the proteostasis network. PLoS Genet 7: e1002438.
    • (2011) PLoS Genet , vol.7
    • Silva, M.C.1    Fox, S.2    Beam, M.3    Thakkar, H.4    Amaral, M.D.5
  • 52
    • 75949094261 scopus 로고    scopus 로고
    • A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation
    • Hageman J, Rujano MA, van Waarde MA, Kakkar V, Dirks RP, et al. (2010) A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation. Mol Cell 37: 355-369.
    • (2010) Mol Cell , vol.37 , pp. 355-369
    • Hageman, J.1    Rujano, M.A.2    van Waarde, M.A.3    Kakkar, V.4    Dirks, R.P.5
  • 53
    • 51349098915 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate-insoluble oligomers are involved in polyglutamine degeneration
    • Wong SL, Chan WM, Chan HY, (2008) Sodium dodecyl sulfate-insoluble oligomers are involved in polyglutamine degeneration. FASEB J 22: 3348-3357.
    • (2008) FASEB J , vol.22 , pp. 3348-3357
    • Wong, S.L.1    Chan, W.M.2    Chan, H.Y.3
  • 54
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2.8: new features for data integration and network visualization
    • Smoot ME, Ono K, Ruscheinski J, Wang PL, Ideker T, (2011) Cytoscape 2.8: new features for data integration and network visualization. Bioinformatics 27: 431-432.
    • (2011) Bioinformatics , vol.27 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3    Wang, P.L.4    Ideker, T.5
  • 55
    • 47049099111 scopus 로고    scopus 로고
    • Ontologizer 2.0-a multifunctional tool for GO term enrichment analysis and data exploration
    • Bauer S, Grossmann S, Vingron M, Robinson PN, (2008) Ontologizer 2.0-a multifunctional tool for GO term enrichment analysis and data exploration. Bioinformatics 24: 1650-1651.
    • (2008) Bioinformatics , vol.24 , pp. 1650-1651
    • Bauer, S.1    Grossmann, S.2    Vingron, M.3    Robinson, P.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.