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Volumn 277, Issue 6, 2010, Pages 1369-1379

Amyloid oligomers: Dynamics and toxicity in the cytosol and nucleus

Author keywords

Live cell imaging; Misfolded protein; Molecular chaperone; Neurodegenerative disease; Neuronal cell death; Oligomer; Protein aggregation; Protein degradation; Protein interaction; Spectroscopic analysis

Indexed keywords

AMYLOID; CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; MONOMER; OLIGOMER; POLYGLUTAMINE;

EID: 77749316908     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07570.x     Document Type: Short Survey
Times cited : (23)

References (77)
  • 1
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor JP, Hardy J Fischbeck KH (2002) Toxic proteins in neurodegenerative disease. Science 296, 1991 1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA Poirier MA (2004) Protein aggregation and neurodegenerative disease. Nat Med Suppl 10, S10 S17.
    • (2004) Nat Med , Issue.SUPPL. 10
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75, 333 366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 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
  • 5
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • Williams AJ Paulson HL (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci 31, 521 528.
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 6
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A disease of motor neurons and their nonneuronal neighbors
    • Boillee S, Vande Velde C Cleveland DW (2006) ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron 52, 39 59.
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillee, S.1    Vande Velde, C.2    Cleveland, D.W.3
  • 7
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • Shaw BF Valentine JS (2007) How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem Sci 32, 78 85.
    • (2007) Trends Biochem Sci , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 9
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low background: Analysis of translational diffusion
    • Rigler R, Mets U, Widengren J Kask P (1993) Fluorescence correlation spectroscopy with high count rate and low background: analysis of translational diffusion. Eur Biophys J 22, 169 175.
    • (1993) Eur Biophys J , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, U.2    Widengren, J.3    Kask, P.4
  • 10
    • 0242404444 scopus 로고    scopus 로고
    • Intracellular applications of fluorescence correlation spectroscopy: Prospects for neuroscience
    • Kim SA Schwille P (2003) Intracellular applications of fluorescence correlation spectroscopy: prospects for neuroscience. Curr Opin Neurobiol 13, 583 590.
    • (2003) Curr Opin Neurobiol , vol.13 , pp. 583-590
    • Kim, S.A.1    Schwille, P.2
  • 11
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira H, Breuer P, Hayer-Hartl MK Hartl FU (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc Natl Acad Sci U S A 99 Suppl 4, 16412 16418.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.SUPPL. 4 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 12
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6, 11 22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 13
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto RI (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 22, 1427 1438.
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 15
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • Ross CA Poirier MA (2005) Opinion: what is the role of protein aggregation in neurodegeneration? Nat Rev Mol Cell Biol 6, 891 898.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 16
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A Brundin P (2003) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40, 427 446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 17
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 10, 524 530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 18
    • 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 (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 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
  • 19
    • 26444471905 scopus 로고    scopus 로고
    • Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates
    • Matsumoto G, Stojanovic A, Holmberg CI, Kim S Morimoto RI (2005) Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates. J Cell Biol 171, 75 85.
    • (2005) J Cell Biol , vol.171 , pp. 75-85
    • Matsumoto, G.1    Stojanovic, A.2    Holmberg, C.I.3    Kim, S.4    Morimoto, R.I.5
  • 22
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A Yao TP (2003) The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115, 727 738.
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 23
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443, 780 786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 24
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451, 1069 1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 26
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA Kopito RR (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 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
  • 29
    • 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, Stenmark H Johansen T (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 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    Stenmark, H.7    Johansen, T.8
  • 31
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross CA (2002) Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron 35, 819 822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 32
    • 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
  • 33
    • 0033613212 scopus 로고    scopus 로고
    • Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells
    • Kazantsev A, Preisinger E, Dranovsky A, Goldgaber D Housman D (1999) Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammalian cells. Proc Natl Acad Sci U S A 96, 11404 11409.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11404-11409
    • Kazantsev, A.1    Preisinger, E.2    Dranovsky, A.3    Goldgaber, D.4    Housman, D.5
  • 36
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity
    • Nekooki-Machida Y, Kurosawa M, Nukina N, Ito K, Oda T Tanaka M (2009) Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc Natl Acad Sci U S A 106, 9679 9684.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Oda, T.5    Tanaka, M.6
  • 40
    • 33744800848 scopus 로고    scopus 로고
    • Cytosolic chaperonin protects folding intermediates of Gbeta from aggregation by recognizing hydrophobic beta-strands
    • Kubota S, Kubota H Nagata K (2006) Cytosolic chaperonin protects folding intermediates of Gbeta from aggregation by recognizing hydrophobic beta-strands. Proc Natl Acad Sci U S A 103, 8360 8365.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8360-8365
    • Kubota, S.1    Kubota, H.2    Nagata, K.3
  • 44
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • Tam S, Geller R, Spiess C Frydman J (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8, 1155 1162.
    • (2006) Nat Cell Biol , vol.8 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 45
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • Lagier-Tourenne C Cleveland DW (2009) Rethinking ALS: the FUS about TDP-43. Cell 136, 1001 1004.
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 47
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • Cleveland DW Rothstein JD (2001) From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat Rev Neurosci 2, 806 819.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 48
    • 33645225597 scopus 로고    scopus 로고
    • Pathogenic superoxide dismutase structure, folding, aggregation and turnover
    • Hart PJ (2006) Pathogenic superoxide dismutase structure, folding, aggregation and turnover. Curr Opin Chem Biol 10, 131 138.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 131-138
    • Hart, P.J.1
  • 50
    • 59249098430 scopus 로고    scopus 로고
    • An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans
    • Wang J, Farr GW, Hall DH, Li F, Furtak K, Dreier L Horwich AL (2009) An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans. PLoS Genet 5, e1000350.
    • (2009) PLoS Genet , vol.5 , pp. 1000350
    • Wang, J.1    Farr, G.W.2    Hall, D.H.3    Li, F.4    Furtak, K.5    Dreier, L.6    Horwich, A.L.7
  • 51
    • 33144484368 scopus 로고    scopus 로고
    • Synaptic targeting by Abeta oligomers (ADDLS) as a basis for memory loss in early Alzheimer's disease
    • Klein WL (2006) Synaptic targeting by Abeta oligomers (ADDLS) as a basis for memory loss in early Alzheimer's disease. Alzheimers Dement 2, 43 55.
    • (2006) Alzheimers Dement , vol.2 , pp. 43-55
    • Klein, W.L.1
  • 52
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8, 101 112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 53
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • Ferreira ST, Vieira MN De Felice FG (2007) Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases. IUBMB Life 59, 332 345.
    • (2007) IUBMB Life , vol.59 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 54
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani M, Sik A, Sakurai T, Nukina N, Takahashi R Julien JP (2006) Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat Neurosci 9, 108 118.
    • (2006) Nat Neurosci , vol.9 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.P.6
  • 56
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis
    • Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV Nukina N (2008) Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. J Biol Chem 283, 24167 24176.
    • (2008) J Biol Chem , vol.283 , pp. 24167-24176
    • Furukawa, Y.1    Kaneko, K.2    Yamanaka, K.3    O'Halloran, T.V.4    Nukina, N.5
  • 58
    • 0037047123 scopus 로고    scopus 로고
    • Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis
    • Chai Y, Shao J, Miller VM, Williams A Paulson HL (2002) Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. Proc Natl Acad Sci U S A 99, 9310 9315.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 9310-9315
    • Chai, Y.1    Shao, J.2    Miller, V.M.3    Williams, A.4    Paulson, H.L.5
  • 59
    • 0036798685 scopus 로고    scopus 로고
    • Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
    • Stenoien DL, Mielke M Mancini MA (2002) Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. Nat Cell Biol 4, 806 810.
    • (2002) Nat Cell Biol , vol.4 , pp. 806-810
    • Stenoien, D.L.1    Mielke, M.2    Mancini, M.A.3
  • 61
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D, Kopito R Frydman J (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454, 1088 1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 62
    • 33751229633 scopus 로고    scopus 로고
    • Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs
    • Pack C, Saito K, Tamura M Kinjo M (2006) Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs. Biophys J 91, 3921 3936.
    • (2006) Biophys J , vol.91 , pp. 3921-3936
    • Pack, C.1    Saito, K.2    Tamura, M.3    Kinjo, M.4
  • 63
    • 34548227453 scopus 로고    scopus 로고
    • Detection of polyglutamine protein oligomers in cells by fluorescence correlation spectroscopy
    • Takahashi Y, Okamoto Y, Popiel HA, Fujikake N, Toda T, Kinjo M Nagai Y (2007) Detection of polyglutamine protein oligomers in cells by fluorescence correlation spectroscopy. J Biol Chem 282, 24039 24048.
    • (2007) J Biol Chem , vol.282 , pp. 24039-24048
    • Takahashi, Y.1    Okamoto, Y.2    Popiel, H.A.3    Fujikake, N.4    Toda, T.5    Kinjo, M.6    Nagai, Y.7
  • 64
    • 31744436399 scopus 로고    scopus 로고
    • Fluorescence cross-correlation spectroscopy in living cells
    • Bacia K, Kim SA Schwille P (2006) Fluorescence cross-correlation spectroscopy in living cells. Nat Methods 3, 83 89.
    • (2006) Nat Methods , vol.3 , pp. 83-89
    • Bacia, K.1    Kim, S.A.2    Schwille, P.3
  • 65
    • 25444478296 scopus 로고    scopus 로고
    • Interaction of a small heat shock protein of the fission yeast, Schizosaccharomyces pombe, with a denatured protein at elevated temperature
    • Hirose M, Tohda H, Giga-Hama Y, Tsushima R, Zako T, Iizuka R, Pack C, Kinjo M, Ishii N Yohda M (2005) Interaction of a small heat shock protein of the fission yeast, Schizosaccharomyces pombe, with a denatured protein at elevated temperature. J Biol Chem 280, 32586 32593.
    • (2005) J Biol Chem , vol.280 , pp. 32586-32593
    • Hirose, M.1    Tohda, H.2    Giga-Hama, Y.3    Tsushima, R.4    Zako, T.5    Iizuka, R.6    Pack, C.7    Kinjo, M.8    Ishii, N.9    Yohda, M.10
  • 66
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan RS, Illing ME, Bence NF Kopito RR (2001) Specificity in intracellular protein aggregation and inclusion body formation. Proc Natl Acad Sci U S A 98, 13060 13065.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3    Kopito, R.R.4
  • 67
    • 33747053662 scopus 로고    scopus 로고
    • Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model
    • Brignull HR, Moore FE, Tang SJ Morimoto RI (2006) Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model. J Neurosci 26, 7597 7606.
    • (2006) J Neurosci , vol.26 , pp. 7597-7606
    • Brignull, H.R.1    Moore, F.E.2    Tang, S.J.3    Morimoto, R.I.4
  • 69
    • 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 Onodera O (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    Onodera, O.6
  • 70
  • 71
    • 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
  • 72
    • 33749054066 scopus 로고    scopus 로고
    • Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy
    • Yasuda R (2006) Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy. Curr Opin Neurobiol 16, 551 561.
    • (2006) Curr Opin Neurobiol , vol.16 , pp. 551-561
    • Yasuda, R.1
  • 73
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based Resonance Energy-Accepting Chromoprotein (REACh) for Forster resonance energy transfer with GFP
    • Ganesan S, Ameer-Beg SM, Ng TT, Vojnovic B Wouters FS (2006) A dark yellow fluorescent protein (YFP)-based Resonance Energy-Accepting Chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc Natl Acad Sci U S A 103, 4089 4094.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, F.S.5
  • 75
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston JA, Dalton MJ, Gurney ME Kopito RR (2000) Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 97, 12571 12576.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 76
    • 34948850962 scopus 로고    scopus 로고
    • Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1
    • Niwa J, Yamada S, Ishigaki S, Sone J, Takahashi M, Katsuno M, Tanaka F, Doyu M Sobue G (2007) Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. J Biol Chem 282, 28087 28095.
    • (2007) J Biol Chem , vol.282 , pp. 28087-28095
    • Niwa, J.1    Yamada, S.2    Ishigaki, S.3    Sone, J.4    Takahashi, M.5    Katsuno, M.6    Tanaka, F.7    Doyu, M.8    Sobue, G.9
  • 77
    • 33847324863 scopus 로고    scopus 로고
    • A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures
    • Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S Deniz AA (2007) A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proc Natl Acad Sci U S A 104, 2649 2654.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2649-2654
    • Mukhopadhyay, S.1    Krishnan, R.2    Lemke, E.A.3    Lindquist, S.4    Deniz, A.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.