메뉴 건너뛰기




Volumn 154, Issue 4, 2013, Pages

XAltered ribostasis: RNA-protein granules in degenerative disorders

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; MESSENGER RNA; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN;

EID: 84882801549     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2013.07.038     Document Type: Review
Times cited : (491)

References (106)
  • 1
    • 72149125838 scopus 로고    scopus 로고
    • The transcellular spread of cytosolic amyloids, prions, and prionoids
    • A. Aguzzi, and L. Rajendran The transcellular spread of cytosolic amyloids, prions, and prionoids Neuron 64 2009 783 790
    • (2009) Neuron , vol.64 , pp. 783-790
    • Aguzzi, A.1    Rajendran, L.2
  • 3
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • W.E. Balch, R.I. Morimoto, A. Dillin, and J.W. Kelly Adapting proteostasis for disease intervention Science 319 2008 916 919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 4
    • 80052967905 scopus 로고    scopus 로고
    • TDP-43: The relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • R.H. Baloh TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration FEBS J. 278 2011 3539 3549
    • (2011) FEBS J. , vol.278 , pp. 3539-3549
    • Baloh, R.H.1
  • 7
    • 80855131505 scopus 로고    scopus 로고
    • Model organisms reveal insight into human neurodegenerative disease: Ataxin-2 intermediate-length polyglutamine expansions are a risk factor for ALS
    • N.M. Bonini, and A.D. Gitler Model organisms reveal insight into human neurodegenerative disease: Ataxin-2 intermediate-length polyglutamine expansions are a risk factor for ALS J. Mol. Neurosci. 45 2011 676 683
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 676-683
    • Bonini, N.M.1    Gitler, A.D.2
  • 9
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • P. Brundin, R. Melki, and R. Kopito Prion-like transmission of protein aggregates in neurodegenerative diseases Nat. Rev. Mol. Cell Biol. 11 2010 301 307
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 10
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • J.R. Buchan, and R. Parker Eukaryotic stress granules: the ins and outs of translation Mol. Cell 36 2009 932 941
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 11
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • J.R. Buchan, D. Muhlrad, and R. Parker P bodies promote stress granule assembly in Saccharomyces cerevisiae J. Cell Biol. 183 2008 441 455
    • (2008) J. Cell Biol. , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 12
    • 84879349589 scopus 로고    scopus 로고
    • Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function
    • J.R. Buchan, R.M. Kolaitis, J.P. Taylor, and R. Parker Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function Cell 153 2013 1461 1474
    • (2013) Cell , vol.153 , pp. 1461-1474
    • Buchan, J.R.1    Kolaitis, R.M.2    Taylor, J.P.3    Parker, R.4
  • 13
    • 84860661767 scopus 로고    scopus 로고
    • The local transcriptome in the synaptic neuropil revealed by deep sequencing and high-resolution imaging
    • I.J. Cajigas, G. Tushev, T.J. Will, S. tom Dieck, N. Fuerst, and E.M. Schuman The local transcriptome in the synaptic neuropil revealed by deep sequencing and high-resolution imaging Neuron 74 2012 453 466
    • (2012) Neuron , vol.74 , pp. 453-466
    • Cajigas, I.J.1    Tushev, G.2    Will, T.J.3    Tom Dieck, S.4    Fuerst, N.5    Schuman, E.M.6
  • 14
    • 33646768641 scopus 로고    scopus 로고
    • A Drosophila model of oculopharyngeal dystrophy reveals intrinsic toxicity of PABN1
    • A. Chartier, B. Benoit, and M. Simonelig A Drosophila model of oculopharyngeal dystrophy reveals intrinsic toxicity of PABN1 EMBO J. 25 2006 2253 2262
    • (2006) EMBO J. , vol.25 , pp. 2253-2262
    • Chartier, A.1    Benoit, B.2    Simonelig, M.3
  • 17
    • 84874531814 scopus 로고    scopus 로고
    • RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations
    • J.G. Daigle, N.A. Lanson Jr., R.B. Smith, I. Casci, A. Maltare, J. Monaghan, C.D. Nichols, D. Kryndushkin, F. Shewmaker, and U.B. Pandey RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations Hum. Mol. Genet. 22 2013 1193 1205
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 1193-1205
    • Daigle, J.G.1    Lanson, Jr.N.A.2    Smith, R.B.3    Casci, I.4    Maltare, A.5    Monaghan, J.6    Nichols, C.D.7    Kryndushkin, D.8    Shewmaker, F.9    Pandey, U.B.10
  • 19
    • 82355181107 scopus 로고    scopus 로고
    • TDP-43 pathological changes in early onset familial and sporadic Alzheimer's disease, late onset Alzheimer's disease and Down's syndrome: Association with age, hippocampal sclerosis and clinical phenotype
    • Y.S. Davidson, S. Raby, P.G. Foulds, A. Robinson, J.C. Thompson, S. Sikkink, I. Yusuf, H. Amin, D. DuPlessis, and C. Troakes TDP-43 pathological changes in early onset familial and sporadic Alzheimer's disease, late onset Alzheimer's disease and Down's syndrome: association with age, hippocampal sclerosis and clinical phenotype Acta Neuropathol. 122 2011 703 713
    • (2011) Acta Neuropathol. , vol.122 , pp. 703-713
    • Davidson, Y.S.1    Raby, S.2    Foulds, P.G.3    Robinson, A.4    Thompson, J.C.5    Sikkink, S.6    Yusuf, I.7    Amin, H.8    Duplessis, D.9    Troakes, C.10
  • 20
    • 0030841672 scopus 로고    scopus 로고
    • Expansion of a CUG trinucleotide repeat in the 3′ untranslated region of myotonic dystrophy protein kinase transcripts results in nuclear retention of transcripts
    • B.M. Davis, M.E. McCurrach, K.L. Taneja, R.H. Singer, and D.E. Housman Expansion of a CUG trinucleotide repeat in the 3′ untranslated region of myotonic dystrophy protein kinase transcripts results in nuclear retention of transcripts Proc. Natl. Acad. Sci. USA 94 1997 7388 7393
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7388-7393
    • Davis, B.M.1    McCurrach, M.E.2    Taneja, K.L.3    Singer, R.H.4    Housman, D.E.5
  • 22
    • 84861398901 scopus 로고    scopus 로고
    • Explaining the length threshold of polyglutamine aggregation
    • P. De Los Rios, M. Hafner, and A. Pastore Explaining the length threshold of polyglutamine aggregation J. Phys. Condens. Matter 24 2012 244105
    • (2012) J. Phys. Condens. Matter , vol.24 , pp. 244105
    • De Los Rios, P.1    Hafner, M.2    Pastore, A.3
  • 23
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • C.J. Decker, D. Teixeira, and R. Parker Edc3p and a glutamine/asparagine- rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae J. Cell Biol. 179 2007 437 449
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 25
    • 84862128438 scopus 로고    scopus 로고
    • TDP-43 aggregation in neurodegeneration: Are stress granules the key?
    • C.M. Dewey, B. Cenik, C.F. Sephton, B.A. Johnson, J. Herz, and G. Yu TDP-43 aggregation in neurodegeneration: are stress granules the key? Brain Res. 1462 2012 16 25
    • (2012) Brain Res. , vol.1462 , pp. 16-25
    • Dewey, C.M.1    Cenik, B.2    Sephton, C.F.3    Johnson, B.A.4    Herz, J.5    Yu, G.6
  • 27
    • 77956362155 scopus 로고    scopus 로고
    • Protein homeostasis and aging in neurodegeneration
    • P.M. Douglas, and A. Dillin Protein homeostasis and aging in neurodegeneration J. Cell Biol. 190 2010 719 729
    • (2010) J. Cell Biol. , vol.190 , pp. 719-729
    • Douglas, P.M.1    Dillin, A.2
  • 28
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • D. Eisenberg, and M. Jucker The amyloid state of proteins in human diseases Cell 148 2012 1188 1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 30
    • 0036537492 scopus 로고    scopus 로고
    • Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci of expanded-repeat transcripts in DM1 and DM2 cells
    • M. Fardaei, M.T. Rogers, H.M. Thorpe, K. Larkin, M.G. Hamshere, P.S. Harper, and J.D. Brook Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci of expanded-repeat transcripts in DM1 and DM2 cells Hum. Mol. Genet. 11 2002 805 814
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 805-814
    • Fardaei, M.1    Rogers, M.T.2    Thorpe, H.M.3    Larkin, K.4    Hamshere, M.G.5    Harper, P.S.6    Brook, J.D.7
  • 31
    • 71849091749 scopus 로고    scopus 로고
    • Proteostasis therapeutics
    • K. Garber Proteostasis therapeutics Nat. Biotechnol. 27 2009 1070
    • (2009) Nat. Biotechnol. , vol.27 , pp. 1070
    • Garber, K.1
  • 34
    • 33746516731 scopus 로고    scopus 로고
    • HnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • S. Guil, J.C. Long, and J.F. Cáceres hnRNP A1 relocalization to the stress granules reflects a role in the stress response Mol. Cell. Biol. 26 2006 5744 5758
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Cáceres, J.F.3
  • 36
    • 2342635196 scopus 로고    scopus 로고
    • The fragile-X premutation: A maturing perspective
    • P.J. Hagerman, and R.J. Hagerman The fragile-X premutation: a maturing perspective Am. J. Hum. Genet. 74 2004 805 816
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 805-816
    • Hagerman, P.J.1    Hagerman, R.J.2
  • 38
    • 70849088746 scopus 로고    scopus 로고
    • Subcellular mRNA localization in animal cells and why it matters
    • C.E. Holt, and S.L. Bullock Subcellular mRNA localization in animal cells and why it matters Science 326 2009 1212 1216
    • (2009) Science , vol.326 , pp. 1212-1216
    • Holt, C.E.1    Bullock, S.L.2
  • 40
    • 84881518613 scopus 로고    scopus 로고
    • Decreased number of Gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis
    • 10.1093/hmg/ddt262 Published online June 19, 2013
    • T. Ishihara, Y. Ariizumi, A. Shiga, T. Kato, C.F. Tan, T. Sato, Y. Miki, M. Yokoo, T. Fujino, and A. Koyama Decreased number of Gemini of coiled bodies and U12 snRNA level in amyotrophic lateral sclerosis Hum. Mol. Genet 2013 10.1093/hmg/ddt262 Published online June 19, 2013
    • (2013) Hum. Mol. Genet
    • Ishihara, T.1    Ariizumi, Y.2    Shiga, A.3    Kato, T.4    Tan, C.F.5    Sato, T.6    Miki, Y.7    Yokoo, M.8    Fujino, T.9    Koyama, A.10
  • 42
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • B.S. Johnson, D. Snead, J.J. Lee, J.M. McCaffery, J. Shorter, and A.D. Gitler TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity J. Biol. Chem. 284 2009 20329 20339
    • (2009) J. Biol. Chem. , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5    Gitler, A.D.6
  • 44
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • M. Kato, T.W. Han, S. Xie, K. Shi, X. Du, L.C. Wu, H. Mirzaei, E.J. Goldsmith, J. Longgood, and J. Pei Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels Cell 149 2012 753 767
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5    Wu, L.C.6    Mirzaei, H.7    Goldsmith, E.J.8    Longgood, J.9    Pei, J.10
  • 46
    • 77954149731 scopus 로고    scopus 로고
    • Abnormal TDP-43 expression is identified in the neocortex in cases of dementia pugilistica, but is mainly confined to the limbic system when identified in high and moderate stages of Alzheimer's disease
    • A. King, F. Sweeney, I. Bodi, C. Troakes, S. Maekawa, and S. Al-Sarraj Abnormal TDP-43 expression is identified in the neocortex in cases of dementia pugilistica, but is mainly confined to the limbic system when identified in high and moderate stages of Alzheimer's disease Neuropathology 30 2010 408 419
    • (2010) Neuropathology , vol.30 , pp. 408-419
    • King, A.1    Sweeney, F.2    Bodi, I.3    Troakes, C.4    Maekawa, S.5    Al-Sarraj, S.6
  • 51
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein
    • J. Li, V.N. Uversky, and A.L. Fink Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein Biochemistry 40 2001 11604 11613
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 52
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Y.R. Li, O.D. King, J. Shorter, and A.D. Gitler Stress granules as crucibles of ALS pathogenesis J. Cell Biol. 201 2013 361 372
    • (2013) J. Cell Biol. , vol.201 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 53
    • 46549085203 scopus 로고    scopus 로고
    • Function and regulation of local axonal translation
    • A.C. Lin, and C.E. Holt Function and regulation of local axonal translation Curr. Opin. Neurobiol. 18 2008 60 68
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 60-68
    • Lin, A.C.1    Holt, C.E.2
  • 54
    • 84862908426 scopus 로고    scopus 로고
    • Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin
    • J. Liu, Y. Xu, D. Stoleru, and A. Salic Imaging protein synthesis in cells and tissues with an alkyne analog of puromycin Proc. Natl. Acad. Sci. USA 109 2012 413 418
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 413-418
    • Liu, J.1    Xu, Y.2    Stoleru, D.3    Salic, A.4
  • 58
    • 74249085705 scopus 로고    scopus 로고
    • Prion neurodegeneration: Starts and stops at the synapse
    • G.R. Mallucci Prion neurodegeneration: starts and stops at the synapse Prion 3 2009 195 201
    • (2009) Prion , vol.3 , pp. 195-201
    • Mallucci, G.R.1
  • 63
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • H. Meyer, M. Bug, and S. Bremer Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system Nat. Cell Biol. 14 2012 117 123
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 65
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: The complex lives of eukaryotic mRNAs
    • M.J. Moore From birth to death: the complex lives of eukaryotic mRNAs Science 309 2005 1514 1518
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 67
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • P.J. Muchowski, and J.L. Wacker Modulation of neurodegeneration by molecular chaperones Nat. Rev. Neurosci. 6 2005 11 22
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 68
    • 1542380523 scopus 로고    scopus 로고
    • The spinocerebellar ataxia 8 noncoding RNA causes neurodegeneration and associates with staufen in Drosophila
    • M. Mutsuddi, C.M. Marshall, K.A. Benzow, M.D. Koob, and I. Rebay The spinocerebellar ataxia 8 noncoding RNA causes neurodegeneration and associates with staufen in Drosophila Curr. Biol. 14 2004 302 308
    • (2004) Curr. Biol. , vol.14 , pp. 302-308
    • Mutsuddi, M.1    Marshall, C.M.2    Benzow, K.A.3    Koob, M.D.4    Rebay, I.5
  • 70
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • T. Ohn, N. Kedersha, T. Hickman, S. Tisdale, and P. Anderson A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly Nat. Cell Biol. 10 2008 1224 1231
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Anderson, P.5
  • 72
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • H.T. Orr, and H.Y. Zoghbi Trinucleotide repeat disorders Annu. Rev. Neurosci. 30 2007 575 621
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 74
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • R. Parker, and U. Sheth P bodies and the control of mRNA translation and degradation Mol. Cell 25 2007 635 646
    • (2007) Mol. Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 75
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: Exosomes, microvesicles, and friends
    • G. Raposo, and W. Stoorvogel Extracellular vesicles: exosomes, microvesicles, and friends J. Cell Biol. 200 2013 373 383
    • (2013) J. Cell Biol. , vol.200 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 76
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • M.A. Reijns, R.D. Alexander, M.P. Spiller, and J.D. Beggs A role for Q/N-rich aggregation-prone regions in P-body localization J. Cell Sci. 121 2008 2463 2472
    • (2008) J. Cell Sci. , vol.121 , pp. 2463-2472
    • Reijns, M.A.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 80
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • C.A. Ross, and M.A. Poirier Protein aggregation and neurodegenerative disease Nat. Med. 10 Suppl 2004 S10 S17
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 81
    • 0035511932 scopus 로고    scopus 로고
    • Induction, assembly, maturation and maintenance of a postsynaptic apparatus
    • J.R. Sanes, and J.W. Lichtman Induction, assembly, maturation and maintenance of a postsynaptic apparatus Nat. Rev. Neurosci. 2 2001 791 805
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 791-805
    • Sanes, J.R.1    Lichtman, J.W.2
  • 84
    • 84865468329 scopus 로고    scopus 로고
    • The genetics and neuropathology of Alzheimer's disease
    • G.D. Schellenberg, and T.J. Montine The genetics and neuropathology of Alzheimer's disease Acta Neuropathol. 124 2012 305 323
    • (2012) Acta Neuropathol. , vol.124 , pp. 305-323
    • Schellenberg, G.D.1    Montine, T.J.2
  • 86
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • D.J. Selkoe Alzheimer's disease is a synaptic failure Science 298 2002 789 791
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 89
    • 33751203862 scopus 로고    scopus 로고
    • SnapShot: Cellular bodies
    • D.L. Spector SnapShot: Cellular bodies Cell 127 2006 1071
    • (2006) Cell , vol.127 , pp. 1071
    • Spector, D.L.1
  • 90
  • 92
    • 82455188194 scopus 로고    scopus 로고
    • Long-term consequences of repetitive brain trauma: Chronic traumatic encephalopathy
    • R.A. Stern, D.O. Riley, D.H. Daneshvar, C.J. Nowinski, R.C. Cantu, and A.C. McKee Long-term consequences of repetitive brain trauma: chronic traumatic encephalopathy PM R 3 10, Suppl 2 2011 S460 S467
    • (2011) PM R , vol.3 , Issue.10 SUPPL. 2
    • Stern, R.A.1    Riley, D.O.2    Daneshvar, D.H.3    Nowinski, C.J.4    Cantu, R.C.5    McKee, A.C.6
  • 93
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Z. Sun, Z. Diaz, X. Fang, M.P. Hart, A. Chesi, J. Shorter, and A.D. Gitler Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS PLoS Biol. 9 2011 e1000614
    • (2011) PLoS Biol. , vol.9 , pp. 1000614
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5    Shorter, J.6    Gitler, A.D.7
  • 94
    • 77955099645 scopus 로고    scopus 로고
    • Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae
    • K.D. Swisher, and R. Parker Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae PLoS One 5 2010 e10006
    • (2010) PLoS One , vol.5 , pp. 10006
    • Swisher, K.D.1    Parker, R.2
  • 95
    • 23944431645 scopus 로고    scopus 로고
    • FMR1 RNA within the intranuclear inclusions of fragile X-associated tremor/ataxia syndrome (FXTAS)
    • F. Tassone, C. Iwahashi, and P.J. Hagerman FMR1 RNA within the intranuclear inclusions of fragile X-associated tremor/ataxia syndrome (FXTAS) RNA Biol. 1 2004 103 105
    • (2004) RNA Biol. , vol.1 , pp. 103-105
    • Tassone, F.1    Iwahashi, C.2    Hagerman, P.J.3
  • 97
    • 80052185880 scopus 로고    scopus 로고
    • Accumulation of transactive response DNA binding protein 43 in mild cognitive impairment and Alzheimer disease
    • C. Tremblay, I. St-Amour, J. Schneider, D.A. Bennett, and F. Calon Accumulation of transactive response DNA binding protein 43 in mild cognitive impairment and Alzheimer disease J. Neuropathol. Exp. Neurol. 70 2011 788 798
    • (2011) J. Neuropathol. Exp. Neurol. , vol.70 , pp. 788-798
    • Tremblay, C.1    St-Amour, I.2    Schneider, J.3    Bennett, D.A.4    Calon, F.5
  • 99
    • 79951630982 scopus 로고    scopus 로고
    • The case for therapeutic proteostasis modulators
    • N. Vij The case for therapeutic proteostasis modulators Expert Opin. Ther. Targets 15 2011 233 236
    • (2011) Expert Opin. Ther. Targets , vol.15 , pp. 233-236
    • Vij, N.1
  • 101
    • 84855877969 scopus 로고    scopus 로고
    • Transgenic mice with SCA10 pentanucleotide repeats show motor phenotype and susceptibility to seizure: A toxic RNA gain-of-function model
    • M. White, G. Xia, R. Gao, M. Wakamiya, P.S. Sarkar, K. McFarland, and T. Ashizawa Transgenic mice with SCA10 pentanucleotide repeats show motor phenotype and susceptibility to seizure: a toxic RNA gain-of-function model J. Neurosci. Res. 90 2012 706 714
    • (2012) J. Neurosci. Res. , vol.90 , pp. 706-714
    • White, M.1    Xia, G.2    Gao, R.3    Wakamiya, M.4    Sarkar, P.S.5    McFarland, K.6    Ashizawa, T.7
  • 103
    • 84869192353 scopus 로고    scopus 로고
    • Regulated protein aggregation: Stress granules and neurodegeneration
    • B. Wolozin Regulated protein aggregation: stress granules and neurodegeneration Mol. Neurodegener. 7 2012 56
    • (2012) Mol. Neurodegener. , vol.7 , pp. 56
    • Wolozin, B.1
  • 104
    • 84855206731 scopus 로고    scopus 로고
    • Recent advances in p97/VCP/Cdc48 cellular functions
    • K. Yamanaka, Y. Sasagawa, and T. Ogura Recent advances in p97/VCP/Cdc48 cellular functions Biochim. Biophys. Acta 1823 2012 130 137
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 130-137
    • Yamanaka, K.1    Sasagawa, Y.2    Ogura, T.3
  • 106
    • 58249085224 scopus 로고    scopus 로고
    • SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. Elegans
    • Y. Zhang, L. Yan, Z. Zhou, P. Yang, E. Tian, K. Zhang, Y. Zhao, Z. Li, B. Song, and J. Han SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans Cell 136 2009 308 321
    • (2009) Cell , vol.136 , pp. 308-321
    • Zhang, Y.1    Yan, L.2    Zhou, Z.3    Yang, P.4    Tian, E.5    Zhang, K.6    Zhao, Y.7    Li, Z.8    Song, B.9    Han, J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.