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Volumn 46, Issue 2, 2014, Pages 152-160

Therapeutic modulation of eIF2α phosphorylation rescues TDP-43 toxicity in amyotrophic lateral sclerosis disease models

Author keywords

[No Author keywords available]

Indexed keywords

7 METHYL 5 [1 [[3 (TRIFLUOROMETHYL)PHENYL]ACETYL] 2,3 DIHYDRO 1H INDOL 5 YL] 7H PYRROLO[2,3 D]PYRIMIDIN 4 AMINE; ATAXIN 2; BINDING PROTEIN; CYTOPLASM PROTEIN; GSK 2606414; INITIATION FACTOR 2ALPHA; PROTEIN KINASE INHIBITOR; PROTEIN PABPC1; PYRROLO[2,3 D]PYRIMIDINE DERIVATIVE; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84895822652     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng.2853     Document Type: Article
Times cited : (293)

References (63)
  • 1
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A disease of motor neurons and their nonneuronal neighbors
    • Boillée, S., Vande Velde, C. & Cleveland, D.W. ALS: A disease of motor neurons and their nonneuronal neighbors. Neuron 52, 39-59 (2006
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillée, S.1    Vande Velde, C.2    Cleveland, D.W.3
  • 2
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • Cleveland, D.W. & Rothstein, J.D. From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2, 806-819 (2001
    • (2001) Nat. Rev. Neurosci , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 3
    • 84865843186 scopus 로고    scopus 로고
    • The genetics and neuropathology of amyotrophic lateral sclerosis
    • Al-Chalabi, A. et al. The genetics and neuropathology of amyotrophic lateral sclerosis. Acta Neuropathol. 124, 339-352 (2012
    • (2012) Acta Neuropathol , vol.124 , pp. 339-352
    • Al-Chalabi, A.1
  • 4
    • 84863507711 scopus 로고    scopus 로고
    • Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis
    • Couthouis, J. et al. Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis. Hum. Mol. Genet. 21, 2899-2911 (2012
    • (2012) Hum. Mol. Genet , vol.21 , pp. 2899-2911
    • Couthouis, J.1
  • 5
    • 84862908655 scopus 로고    scopus 로고
    • A yeast functional screen predicts new candidate ALS disease genes
    • Couthouis, J. et al. A yeast functional screen predicts new candidate ALS disease genes. Proc. Natl. Acad. Sci. USA 108, 20881-20890 (2011
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20881-20890
    • Couthouis, J.1
  • 6
    • 84875605133 scopus 로고    scopus 로고
    • Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
    • Kim, H.J. et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 495, 467-473 (2013
    • (2013) Nature , vol.495 , pp. 467-473
    • Kim, H.J.1
  • 7
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King, O.D., Gitler, A.D. & Shorter, J. The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res. 1462, 61-80 (2012
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 8
    • 77956181850 scopus 로고    scopus 로고
    • TDP-43: A DNA and RNA binding protein with roles in neurodegenerative diseases
    • Warraich, S.T., Yang, S., Nicholson, G.A. & Blair, I.P. TDP-43: A DNA and RNA binding protein with roles in neurodegenerative diseases. Int. J. Biochem. Cell Biol. 42, 1606-1609 (2010
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , pp. 1606-1609
    • Warraich, S.T.1    Yang, S.2    Nicholson, G.A.3    Blair, I.P.4
  • 9
    • 84867686875 scopus 로고    scopus 로고
    • Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP
    • Aulas, A., Stabile, S. & Vande Velde, C. Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP. Mol. Neurodegener. 7, 54 (2012
    • (2012) Mol. Neurodegener , vol.7 , Issue.54
    • Aulas, A.1    Stabile, S.2    Vande Velde, C.3
  • 10
    • 84863309952 scopus 로고    scopus 로고
    • Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43
    • Bentmann, E. et al. Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43). J. Biol. Chem. 287, 23079-23094 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 23079-23094
    • Bentmann, E.1
  • 11
    • 84857124994 scopus 로고    scopus 로고
    • Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates
    • Parker, S.J. et al. Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates. Neurochem. Int. 60, 415-424 (2012
    • (2012) Neurochem. Int , vol.60 , pp. 415-424
    • Parker, S.J.1
  • 12
    • 79952268025 scopus 로고    scopus 로고
    • TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor
    • Dewey, C.M. et al. TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Mol. Cell Biol. 31, 1098-1108 (2011
    • (2011) Mol. Cell Biol , vol.31 , pp. 1098-1108
    • Dewey, C.M.1
  • 14
    • 84863431578 scopus 로고    scopus 로고
    • ALS-Associated ataxin 2 polyQ expansions enhance stress-induced caspase 3 activation and increase TDP-43 pathological modifications
    • Hart, M.P. & Gitler, A.D. ALS-Associated ataxin 2 polyQ expansions enhance stress-induced caspase 3 activation and increase TDP-43 pathological modifications. J. Neurosci. 32, 9133-9142 (2012
    • (2012) J. Neurosci , vol.32 , pp. 9133-9142
    • Hart, M.P.1    Gitler, A.D.2
  • 15
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li, Y.R., King, O.D., Shorter, J. & Gitler, A.D. Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201, 361-372 (2013
    • (2013) J. Cell Biol , vol.201 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 16
    • 78149461229 scopus 로고    scopus 로고
    • TAR DNA binding protein-43 (TDP-43) associates with stress granules: Analysis of cultured cells and pathological brain tissue
    • Liu-Yesucevitz, L. et al. TAR DNA binding protein-43 (TDP-43) associates with stress granules: Analysis of cultured cells and pathological brain tissue. PLoS ONE 5, e13250 (2010
    • (2010) PLoS ONE , vol.5
    • Liu-Yesucevitz, L.1
  • 17
    • 84869192353 scopus 로고    scopus 로고
    • Regulated protein aggregation: Stress granules and neurodegeneration
    • Wolozin, B. Regulated protein aggregation: Stress granules and neurodegeneration. Mol. Neurodegener. 7, 56 (2012
    • (2012) Mol. Neurodegener , vol.7 , Issue.56
    • Wolozin, B.1
  • 18
    • 84883446343 scopus 로고    scopus 로고
    • Stress granules in neurodegeneration-lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma
    • Bentmann, E., Haass, C. & Dormann, D. Stress granules in neurodegeneration-lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma. FEBS J. 280, 4348-4370 (2013
    • (2013) FEBS J. , vol.280 , pp. 4348-4370
    • Bentmann, E.1    Haass, C.2    Dormann, D.3
  • 19
    • 84882801549 scopus 로고    scopus 로고
    • Altered ribostasis: RNA-protein granules in degenerative disorders
    • Ramaswami, M., Taylor, J.P. & Parker, R. Altered ribostasis: RNA-protein granules in degenerative disorders. Cell 154, 727-736 (2013
    • (2013) Cell , vol.154 , pp. 727-736
    • Ramaswami, M.1    Taylor, J.P.2    Parker, R.3
  • 20
    • 84877250175 scopus 로고    scopus 로고
    • RNA dysfunction and aggrephagy at the centre of an amyotrophic lateral sclerosis/frontotemporal dementia disease continuum
    • Thomas, M., Alegre-Abarrategui, J. & Wade-Martins, R. RNA dysfunction and aggrephagy at the centre of an amyotrophic lateral sclerosis/frontotemporal dementia disease continuum. Brain 136, 1345-1360 (2013
    • (2013) Brain , vol.136 , pp. 1345-1360
    • Thomas, M.1    Alegre-Abarrategui, J.2    Wade-Martins, R.3
  • 21
    • 84885463900 scopus 로고    scopus 로고
    • Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice
    • Moreno, J.A. et al. Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice. Sci. Transl. Med. 5, 206ra138 (2013
    • (2013) Sci. Transl. Med , vol.5
    • Moreno, J.A.1
  • 22
    • 84861450392 scopus 로고    scopus 로고
    • Sustained translational repression by eIF2a-P mediates prion neurodegeneration
    • Moreno, J.A. et al. Sustained translational repression by eIF2a-P mediates prion neurodegeneration. Nature 485, 507-511 (2012
    • (2012) Nature , vol.485 , pp. 507-511
    • Moreno, J.A.1
  • 23
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of a-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck, P.K., Chan, H.Y., Trojanowski, J.Q., Lee, V.M. & Bonini, N.M. Chaperone suppression of a-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295, 865-868 (2002
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 24
    • 33746533924 scopus 로고    scopus 로고
    • A.-Synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models
    • Cooper, A.A. et al. a-Synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 313, 324-328 (2006
    • (2006) Science , vol.313 , pp. 324-328
    • Cooper, A.A.1
  • 25
    • 77956155218 scopus 로고    scopus 로고
    • Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS
    • Elden, A.C. et al. Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS. Nature 466, 1069-1075 (2010
    • (2010) Nature , vol.466 , pp. 1069-1075
    • Elden, A.C.1
  • 26
    • 61349147706 scopus 로고    scopus 로고
    • A-Synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity
    • Gitler, A.D. et al. a-Synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat. Genet. 41, 308-315 (2009
    • (2009) Nat. Genet , vol.41 , pp. 308-315
    • Gitler, A.D.1
  • 27
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into a-synuclein biology and pathobiology
    • Outeiro, T.F. & Lindquist, S. Yeast cells provide insight into a-synuclein biology and pathobiology. Science 302, 1772-1775 (2003
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 28
    • 82755197062 scopus 로고    scopus 로고
    • Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast
    • Treusch, S. et al. Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast. Science 334, 1241-1245 (2011
    • (2011) Science , vol.334 , pp. 1241-1245
    • Treusch, S.1
  • 29
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • Johnson, B.S., McCaffery, J.M., Lindquist, S. & Gitler, A.D. A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc. Natl. Acad. Sci. USA 105, 6439-6444 (2008
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6439-6444
    • Johnson, B.S.1    McCaffery, J.M.2    Lindquist, S.3    Gitler, A.D.4
  • 30
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson, B.S. et al. TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284, 20329-20339 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 20329-20339
    • Johnson, B.S.1
  • 32
    • 34249053477 scopus 로고    scopus 로고
    • Genetic dissection of ethanol tolerance in the budding yeast Saccharomyces cerevisiae
    • Hu, X.H. et al. Genetic dissection of ethanol tolerance in the budding yeast Saccharomyces cerevisiae. Genetics 175, 1479-1487 (2007
    • (2007) Genetics , vol.175 , pp. 1479-1487
    • Hu, X.H.1
  • 33
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Sun, Z. et al. Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol. 9, e1000614 (2011
    • (2011) PLoS Biol , vol.9
    • Sun, Z.1
  • 34
    • 84873532024 scopus 로고    scopus 로고
    • The discovery and analysis of P bodies
    • Jain, S. & Parker, R. The discovery and analysis of P bodies. Adv. Exp. Med. Biol. 768, 23-43 (2013
    • (2013) Adv. Exp. Med. Biol , vol.768 , pp. 23-43
    • Jain, S.1    Parker, R.2
  • 35
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne, C., Polymenidou, M. & Cleveland, D.W. TDP-43 and FUS/TLS: Emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 19, R46-R64 (2010
    • (2010) Hum. Mol. Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 36
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis
    • Ling, S.C., Polymenidou, M. & Cleveland, D.W. Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis. Neuron 79, 416-438 (2013
    • (2013) Neuron , vol.79 , pp. 416-438
    • Ling, S.C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 37
    • 84885818460 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and spinocerebellar ataxia type 2 in a family with full CAG repeat expansions of ATXN2
    • doi:10.1001/jamaneurol.2013.443 (19 August 2013
    • Tazen, S. et al. Amyotrophic lateral sclerosis and spinocerebellar ataxia type 2 in a family with full CAG repeat expansions of ATXN2. JAMA Neurol. doi:10.1001/jamaneurol.2013.443 (19 August 2013
    • JAMA Neurol
    • Tazen, S.1
  • 38
    • 0037020244 scopus 로고    scopus 로고
    • Characterization of mammalian eIF2A and identification of the yeast homolog
    • Zoll, W.L., Horton, L.E., Komar, A.A., Hensold, J.O. & Merrick, W.C. Characterization of mammalian eIF2A and identification of the yeast homolog. J. Biol. Chem. 277, 37079-37087 (2002
    • (2002) J. Biol. Chem , vol.277 , pp. 37079-37087
    • Zoll, W.L.1    Horton, L.E.2    Komar, A.A.3    Hensold, J.O.4    Merrick, W.C.5
  • 39
    • 84862128438 scopus 로고    scopus 로고
    • TDP-43 aggregation in neurodegeneration: Are stress granules the key?
    • Dewey, C.M. et al. TDP-43 aggregation in neurodegeneration: Are stress granules the key? Brain Res. 1462, 16-25 (2012
    • (2012) Brain Res , vol.1462 , pp. 16-25
    • Dewey, C.M.1
  • 40
    • 0036556757 scopus 로고    scopus 로고
    • Visibly stressed: The role of eIF2, TIA-1, and stress granules in protein translation
    • Anderson, P. & Kedersha, N. Visibly stressed: The role of eIF2, TIA-1, and stress granules in protein translation. Cell Stress Chaperones 7, 213-221 (2002
    • (2002) Cell Stress Chaperones , vol.7 , pp. 213-221
    • Anderson, P.1    Kedersha, N.2
  • 41
    • 0027265545 scopus 로고
    • The developmentally-regulated Drosophila gene rox8 encodes an RRM-Type RNA binding protein structurally related to human TIA-1-Type nucleolysins
    • Brand, S. & Bourbon, H.M. The developmentally-regulated Drosophila gene rox8 encodes an RRM-Type RNA binding protein structurally related to human TIA-1-Type nucleolysins. Nucleic Acids Res. 21, 3699-3704 (1993
    • (1993) Nucleic Acids Res , vol.21 , pp. 3699-3704
    • Brand, S.1    Bourbon, H.M.2
  • 43
    • 78951492184 scopus 로고    scopus 로고
    • Modulation of stress granules and P bodies during dicistrovirus infection
    • Khong, A. & Jan, E. Modulation of stress granules and P bodies during dicistrovirus infection. J. Virol. 85, 1439-1451 (2011
    • (2011) J. Virol , vol.85 , pp. 1439-1451
    • Khong, A.1    Jan, E.2
  • 44
  • 45
    • 0034638837 scopus 로고    scopus 로고
    • Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules
    • Kedersha, N. et al. Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules. J. Cell Biol. 151, 1257-1268 (2000
    • (2000) J. Cell Biol , vol.151 , pp. 1257-1268
    • Kedersha, N.1
  • 46
    • 84867167962 scopus 로고    scopus 로고
    • Dynamic oscillation of translation and stress granule formation mark the cellular response to virus infection
    • Ruggieri, A. et al. Dynamic oscillation of translation and stress granule formation mark the cellular response to virus infection. Cell Host Microbe 12, 71-85 (2012
    • (2012) Cell Host Microbe , vol.12 , pp. 71-85
    • Ruggieri, A.1
  • 47
    • 34247229733 scopus 로고    scopus 로고
    • Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and interferes with P-bodies and stress granules
    • Nonhoff, U. et al. Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and interferes with P-bodies and stress granules. Mol. Biol. Cell 18, 1385-1396 (2007
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1385-1396
    • Nonhoff, U.1
  • 48
    • 77955099645 scopus 로고    scopus 로고
    • Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae
    • Swisher, K.D. & Parker, R. Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae. PLoS ONE 5, e10006 (2010
    • (2010) PLoS ONE , vol.5
    • Swisher, K.D.1    Parker, R.2
  • 49
    • 77349089667 scopus 로고    scopus 로고
    • Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein
    • Kozlov, G., Menade, M., Rosenauer, A., Nguyen, L. & Gehring, K. Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein. J. Mol. Biol. 397, 397-407 (2010
    • (2010) J. Mol. Biol , vol.397 , pp. 397-407
    • Kozlov, G.1    Menade, M.2    Rosenauer, A.3    Nguyen, L.4    Gehring, K.5
  • 50
    • 84859978033 scopus 로고    scopus 로고
    • Both Sm-domain and C-Terminal extension of Lsm1 are important for the RNA-binding activity of the Lsm1-7-Pat1 complex
    • Chowdhury, A., Raju, K.K., Kalurupalle, S. & Tharun, S. Both Sm-domain and C-Terminal extension of Lsm1 are important for the RNA-binding activity of the Lsm1-7-Pat1 complex. RNA 18, 936-944 (2012
    • (2012) RNA , vol.18 , pp. 936-944
    • Chowdhury, A.1    Raju, K.K.2    Kalurupalle, S.3    Tharun, S.4
  • 51
    • 33747884761 scopus 로고    scopus 로고
    • Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes
    • Satterfield, T.F. & Pallanck, L.J. Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes. Hum. Mol. Genet. 15, 2523-2532 (2006
    • (2006) Hum. Mol. Genet , vol.15 , pp. 2523-2532
    • Satterfield, T.F.1    Pallanck, L.J.2
  • 52
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti, E. & Baralle, F.E. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem. 276, 36337-36343 (2001
    • (2001) J. Biol. Chem , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 53
    • 84866905708 scopus 로고    scopus 로고
    • Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3- dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-Amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK
    • Axten, J.M. et al. Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl) phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-Amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK). J. Med. Chem. 55, 7193-7207 (2012
    • (2012) J. Med. Chem , vol.55 , pp. 7193-7207
    • Axten, J.M.1
  • 54
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E.S., Segal, M.R. & Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810 (2004
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 55
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
    • Barmada, S.J. et al. Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J. Neurosci. 30, 639-649 (2010
    • (2010) J. Neurosci , vol.30 , pp. 639-649
    • Barmada, S.J.1
  • 56
    • 84883575046 scopus 로고    scopus 로고
    • GeneMANIA prediction server 2013 update
    • Zuberi, K. et al. GeneMANIA prediction server 2013 update. Nucleic Acids Res. 41, W115-W122 (2013
    • (2013) Nucleic Acids Res , vol.41
    • Zuberi, K.1
  • 57
    • 84867186265 scopus 로고    scopus 로고
    • Translation suppression promotes stress granule formation and cell survival in response to cold shock
    • Hofmann, S., Cherkasova, V., Bankhead, P., Bukau, B. & Stoecklin, G. Translation suppression promotes stress granule formation and cell survival in response to cold shock. Mol. Biol. Cell 23, 3786-3800 (2012
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3786-3800
    • Hofmann, S.1    Cherkasova, V.2    Bankhead, P.3    Bukau, B.4    Stoecklin, G.5
  • 58
    • 79251554956 scopus 로고    scopus 로고
    • Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae
    • Buchan, J.R., Yoon, J.H. & Parker, R. Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae. J. Cell Sci. 124, 228-239 (2011
    • (2011) J. Cell Sci , vol.124 , pp. 228-239
    • Buchan, J.R.1    Yoon, J.H.2    Parker, R.3
  • 59
    • 17444372666 scopus 로고    scopus 로고
    • Seizure suppression by gain-of-function escargot mutations
    • Hekmat-Scafe, D.S., Dang, K.N. & Tanouye, M.A. Seizure suppression by gain-of-function escargot mutations. Genetics 169, 1477-1493 (2005
    • (2005) Genetics , vol.169 , pp. 1477-1493
    • Hekmat-Scafe, D.S.1    Dang, K.N.2    Tanouye, M.A.3
  • 60
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H. & Perrimon, N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415 (1993
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 61
    • 78951477322 scopus 로고    scopus 로고
    • Refinement of tools for targeted gene expression in Drosophila
    • Pfeiffer, B.D. et al. Refinement of tools for targeted gene expression in Drosophila. Genetics 186, 735-755 (2010
    • (2010) Genetics , vol.186 , pp. 735-755
    • Pfeiffer, B.D.1
  • 62
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany, M.B. & Bender, W.W. A Drosophila model of Parkinson's disease. Nature 404, 394-398 (2000
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 63
    • 14844359962 scopus 로고    scopus 로고
    • Automated microscope system for determining factors that predict neuronal fate
    • Arrasate, M. & Finkbeiner, S. Automated microscope system for determining factors that predict neuronal fate. Proc. Natl. Acad. Sci. USA 102, 3840-3845 (2005.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3840-3845
    • Arrasate, M.1    Finkbeiner, S.2


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