메뉴 건너뛰기




Volumn 123, Issue 6, 2013, Pages 366-374

Protein SUMOylation, an emerging pathway in amyotrophic lateral sclerosis

Author keywords

ALS; Hypoxia; Oxidative stress; SUMO; Ubiquitin

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; EXCITATORY AMINO ACID TRANSPORTER 2; FUSED IN SARCOMA PROTEIN; GLUTAMATE TRANSPORTER; GLUTAMIC ACID; PROTEASOME; TAR DNA BINDING PROTEIN;

EID: 84878086454     PISSN: 00207454     EISSN: 15635279     Source Type: Journal    
DOI: 10.3109/00207454.2012.761984     Document Type: Article
Times cited : (26)

References (95)
  • 1
    • 80755128213 scopus 로고    scopus 로고
    • Clinicaldiagnosis and management of amyotrophic lateral sclerosis
    • Hardiman O, Van den Berg LH, Kiernan MC. Clinicaldiagnosis and management of amyotrophic lateral sclerosis. NatRev Neurol 2011;7(11):639-49.
    • (2011) NatRev Neurol , vol.7 , Issue.11 , pp. 639-649
    • Den Van, H.O.1    Berg, L.H.2    Kiernan, M.C.3
  • 2
    • 33745924415 scopus 로고    scopus 로고
    • SUMO-1 modification increaseshuman SOD1 stability and aggregation
    • Fei E, Jia N, Yan M, et al. SUMO-1 modification increaseshuman SOD1 stability and aggregation. Biochem Biophys ResCommun 2006;347(2):406-12.
    • (2006) Biochem Biophys ResCommun , vol.347 , Issue.2 , pp. 406-412
    • Fei, E.1    Jia, N.2    Yan, M.3
  • 3
    • 77950658888 scopus 로고    scopus 로고
    • Multiplex SILA Canalysis of a cellular TDP-43 proteinopathy model reveals proteininclusions associated with SUMOylation and diversepolyubiquitin chains
    • Seyfried NT, Gozal YM, Dammer EB, et al. Multiplex SILACanalysis of a cellular TDP-43 proteinopathy model reveals proteininclusions associated with SUMOylation and diversepolyubiquitin chains. Mol Cell Proteomics 2010;9(4):705-18.
    • (2010) Mol Cell Proteomics , vol.9 , Issue.4 , pp. 705-718
    • Seyfried, N.T.1    Gozal, Y.M.2    Dammer, E.B.3
  • 4
    • 77149134314 scopus 로고    scopus 로고
    • Ebp1 sumoylation, regulated byTLS/FUS E3 ligase, is required for its anti-proliferative activity
    • Oh S-M, Liu Z,Okada M, et al. Ebp1 sumoylation, regulated byTLS/FUS E3 ligase, is required for its anti-proliferative activity.Oncogene 2010;29(7):1017-30.
    • (2010) Oncogene , vol.29 , Issue.7 , pp. 1017-1030
    • Oh, S.-M.1    Liu Zokada, M.2
  • 5
    • 61349156118 scopus 로고    scopus 로고
    • Mutationsin the FUS/TLS gene on chromosome 16 cause familial amyotrophiclateral sclerosis
    • Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, et al. Mutationsin the FUS/TLS gene on chromosome 16 cause familial amyotrophiclateral sclerosis. Science 2009;323(5918):1205-8.
    • (2009) Science , vol.323 , Issue.5918 , pp. 1205-1208
    • Kwiatkowski Jr., T.J.1    Bosco, D.A.2    Leclerc, A.L.3
  • 6
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosistype 6
    • Vance C, Rogelj B, Hortob́agyi T, et al. Mutations in FUS, anRNA processing protein, cause familial amyotrophic lateral sclerosistype 6. Science 2009;323(5918):1208-11.
    • (2009) Science , vol.323 , Issue.5918 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortob́agyi, T.3
  • 7
    • 84863067477 scopus 로고    scopus 로고
    • SOD1 ANG TARDBPand FUS mutations in amyotrophic lateral sclerosis: A UnitedStates clinical testing lab experience
    • Brown JA, Min J, Staropoli JF, et al. SOD1, ANG, TARDBPand FUS mutations in amyotrophic lateral sclerosis: a UnitedStates clinical testing lab experience. Amyotroph Lateral Scler2012;13(2):217-22.
    • (2012) Amyotroph Lateral Scler , vol.13 , Issue.2 , pp. 217-222
    • Brown, J.A.1    Min, J.2    Staropoli, J.F.3
  • 8
    • 79151482596 scopus 로고    scopus 로고
    • Linking hypoxic and oxidativeinsults to cell death mechanisms in models of ALS
    • Xu R, Wu C, Zhang X, et al. Linking hypoxic and oxidativeinsults to cell death mechanisms in models of ALS. Brain Res2011;1372:133-44.
    • (2011) Brain Res , vol.1372 , pp. 133-144
    • Xu, R.1    Wu, C.2    Zhang, X.3
  • 9
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphismin a novel SUMO gene (SUMO-4) differentiallyactivates heat shock transcription factors and is associatedwith susceptibility to type i diabetes mellitus
    • Bohren KM, Nadkarni V, Song JH, et al. A M55V polymorphismin a novel SUMO gene (SUMO-4) differentiallyactivates heat shock transcription factors and is associatedwith susceptibility to type I diabetes mellitus. J Biol Chem2004;279(26):27233-8.
    • J Biol Chem2004 , vol.279 , Issue.26 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3
  • 10
    • 0031104910 scopus 로고    scopus 로고
    • SMT3A ahuman homologue of the S. cerevisiae SMT3 gene maps tochromosome 21qter and defines a novel gene family
    • Lapenta V, Chiurazzi P, Van der Spek P, et al. SMT3A, ahuman homologue of the S. cerevisiae SMT3 gene, maps tochromosome 21qter and defines a novel gene family. Genomics1997;40(2):362-6.
    • (1997) Genomics , vol.40 , Issue.2 , pp. 362-366
    • Lapenta, V.1    Chiurazzi, P.2    Van Der Spek, P.3
  • 11
    • 70349191359 scopus 로고    scopus 로고
    • Differential SUMOylationof LXRalpha and LXRbeta mediates transrepression of STAT1inflammatory signaling in IFN-gamma-stimulated brain astrocytes
    • Lee JH, Park SM, Kim OS, et al. Differential SUMOylationof LXRalpha and LXRbeta mediates transrepression of STAT1inflammatory signaling in IFN-gamma-stimulated brain astrocytes.Mol Cell 2009;35(6):806-17.
    • (2009) Mol Cell , vol.35 , Issue.6 , pp. 806-817
    • Lee, J.H.1    Park, S.M.2    Kim, O.S.3
  • 12
    • 84863435384 scopus 로고    scopus 로고
    • Protein SUMOylation in spine structureand function
    • Craig TJ, Henley JM. Protein SUMOylation in spine structureand function. Curr Opin Neurobiol 2012;22(3):480-7.
    • Curr Opin Neurobiol 2012 , vol.22 , Issue.3 , pp. 480-487
    • Craig, T.J.1    Henley, J.M.2
  • 13
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains ofSUMO-2 and SUMO-3 are conjugated to protein substrates bySAE1/SAE2 and Ubc9
    • Tatham MH, Jaffray E, Vaughan OA, et al. Polymeric chains ofSUMO-2 and SUMO-3 are conjugated to protein substrates bySAE1/SAE2 and Ubc9. J Biol Chem 2001;276(38):35368-74.
    • (2001) J Biol Chem , vol.276 , Issue.38 , pp. 35368-35374
    • Tatham, M.H.1    Jaffray, E.2    Vaughan, O.A.3
  • 14
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identificationof human small ubiquitin-like modifier polymerization sites byhigh accuracy mass spectrometry and an in vitro to in vivo strategy
    • Matic I, Van Hagen M, Schimmel J, et al. In vivo identificationof human small ubiquitin-like modifier polymerization sites byhigh accuracy mass spectrometry and an in vitro to in vivo strategy.Mol Cell Proteomics 2008;7(1):132-44.
    • (2008) Mol Cell Proteomics , vol.7 , Issue.1 , pp. 132-144
    • Matic, I.1    Van Hagen, M.2    Schimmel, J.3
  • 15
    • 0033060826 scopus 로고    scopus 로고
    • Molecular cloningand characterization of human AOS1 and UBA2 componentsof the sentrin-activating enzyme complex
    • Gong L, Li B, Millas S, Yeh ET. Molecular cloningand characterization of human AOS1 and UBA2, componentsof the sentrin-activating enzyme complex. FEBS Lett1999;448(1):185-9.
    • (1999) FEBS Lett , vol.448 , Issue.1 , pp. 185-189
    • Gong, L.1    Li, B.2    Millas, S.3    Yeh, E.T.4
  • 16
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzymefor the ubiquitin-like protein Smt3p
    • Johnson ES, Blobel G. Ubc9p is the conjugating enzymefor the ubiquitin-like protein Smt3p. J Biol Chem1997;272(43):26799-802.
    • (1997) J Biol Chem , vol.272 , Issue.43 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 17
    • 67449091213 scopus 로고    scopus 로고
    • What was theset of ubiquitin and ubiquitin-like conjugating enzymes in theeukaryote common ancestor?
    • Michelle C, Vourc'h P, Mignon L, Andres CR. What was theset of ubiquitin and ubiquitin-like conjugating enzymes in theeukaryote common ancestor? J Mol Evol 2009;68(6):616-28.
    • (2009) J Mol Evol , vol.68 , Issue.6 , pp. 616-628
    • Michelle, C.1    Vourc'H, P.2    Mignon, L.3    Andres, C.R.4
  • 18
    • 0033571214 scopus 로고    scopus 로고
    • SUMO-1 modificationactivates the transcriptional response of p53
    • Rodriguez MS, Desterro JM, Lain S, et al. SUMO-1 modificationactivates the transcriptional response of p53. EMBO J1999;18(22):6455-61.
    • (1999) EMBO J , vol.18 , Issue.22 , pp. 6455-6461
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3
  • 19
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitinlikemodifier-1 (SUMO-1) consensus sequence mediates Ubc9binding and is essential for SUMO-1 modification
    • Sampson DA, Wang M, Matunis MJ. The small ubiquitinlikemodifier-1 (SUMO-1) consensus sequence mediates Ubc9binding and is essential for SUMO-1 modification. J Biol Chem2001;276(24):21664-9.
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 20
    • 30444440554 scopus 로고    scopus 로고
    • PDSM, a motiffor phosphorylation-dependent SUMO modification
    • Hietakangas V, Anckar J, Blomster HA, et al. PDSM, a motiffor phosphorylation-dependent SUMO modification. Proc NatlAcad Sci USA 2006;103(1):45-50.
    • (2006) Proc NatlAcad Sci USA , vol.103 , Issue.1 , pp. 45-50
    • Hietakangas, V.1    Anckar, J.2    Blomster, H.A.3
  • 21
    • 33645213038 scopus 로고    scopus 로고
    • SUMO-3 enhances androgenreceptor transcriptional activity through a sumoylationindependentmechanism in prostate cancer cells
    • Zheng Z, Cai C, Omwancha J, et al. SUMO-3 enhances androgenreceptor transcriptional activity through a sumoylationindependentmechanism in prostate cancer cells. J Biol Chem2006;281(7):4002-12.
    • (2006) J Biol Chem , vol.281 , Issue.7 , pp. 4002-4012
    • Zheng, Z.1    Cai, C.2    Omwancha, J.3
  • 22
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modificationof IkappaBalpha inhibits NF-kappaB activation
    • Desterro JM, Rodriguez MS, Hay RT. SUMO-1 modificationof IkappaBalpha inhibits NF-kappaB activation. Mol Cell1998;2(2):233-9.
    • (1998) Mol Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 23
    • 0035873076 scopus 로고    scopus 로고
    • Neuronspecificexpression of mutant superoxide dismutase 1 in transgenicmice does not lead to motor impairment
    • Pramatarova A, Laganìere J, Roussel J, et al. Neuronspecificexpression of mutant superoxide dismutase 1 in transgenicmice does not lead to motor impairment. J Neurosci2001;21(10):3369-74.
    • (2001) J Neurosci , vol.21 , Issue.10 , pp. 3369-3374
    • Pramatarova, A.1    Laganìere, J.2    Roussel, J.3
  • 24
    • 84864018984 scopus 로고    scopus 로고
    • Identification of estrogenreceptor ? as a SUMO-1 target reveals a novel phosphorylatedsumoylation motif and regulation by glycogen synthase kinase3?
    • Picard N, Caron V, Bilodeau S, et al. Identification of estrogenreceptor ? as a SUMO-1 target reveals a novel phosphorylatedsumoylation motif and regulation by glycogen synthase kinase3?. Mol Cell Biol 2012;32(14):2709-21.
    • (2012) Mol Cell Biol , vol.32 , Issue.14 , pp. 2709-2721
    • Picard, N.1    Caron, V.2    Bilodeau, S.3
  • 25
    • 78951474065 scopus 로고    scopus 로고
    • Estrogen receptor agonistsand estrogen attenuate TNF-?-induced apoptosis in VSC4.1motoneurons
    • Das A, Smith JA, Gibson C, et al. Estrogen receptor agonistsand estrogen attenuate TNF-?-induced apoptosis in VSC4.1motoneurons. J Endocrinol 2011;208(2):171-82.
    • (2011) J Endocrinol , vol.208 , Issue.2 , pp. 171-182
    • Das, A.1    Smith, J.A.2    Gibson, C.3
  • 26
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism andconsequences for paralog-specific sumoylation of ubiquitinspecificprotease 25
    • Meulmeester E, Kunze M, Hsiao HH, et al. Mechanism andconsequences for paralog-specific sumoylation of ubiquitinspecificprotease 25. Mol Cell 2008;30(5):610-9.
    • (2008) Mol Cell , vol.30 , Issue.5 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3
  • 27
    • 48349117947 scopus 로고    scopus 로고
    • Ubc9 sumoylationregulates SUMO target discrimination
    • Knipscheer P, Flotho A, Klug H, et al. Ubc9 sumoylationregulates SUMO target discrimination. Mol Cell2008;31(3):371-82.
    • (2008) Mol Cell , vol.31 , Issue.3 , pp. 371-382
    • Knipscheer, P.1    Flotho, A.2    Klug, H.3
  • 28
    • 77952544821 scopus 로고    scopus 로고
    • Mutant superoxide dismutase1 overexpression in NSC-34 cells: Effect of trehalose on aggregation,TDP-43 localization and levels of co-expressed glycoproteins
    • Gomes C, Escrevente C, Costa J. Mutant superoxide dismutase1 overexpression in NSC-34 cells: effect of trehalose on aggregation,TDP-43 localization and levels of co-expressed glycoproteins.Neurosci Lett 2010;475(3):145-9.
    • (2010) Neurosci Lett , vol.475 , Issue.3 , pp. 145-149
    • Gomes, C.1    Escrevente, C.2    Costa, J.3
  • 29
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteinsin Saccharomyces cerevisiae. Induction of protein sumoylationby cellular stresses
    • Zhou W, Ryan JJ, Zhou H. Global analyses of sumoylated proteinsin Saccharomyces cerevisiae. Induction of protein sumoylationby cellular stresses. J Biol Chem 2004;279(31):32262-8.
    • (2004) J Biol Chem , vol.279 , Issue.31 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3
  • 30
    • 0037108967 scopus 로고    scopus 로고
    • Higher order arrangementof the eukaryotic nuclear bodies
    • Wang I-F, Reddy NM, Shen C-KJ. Higher order arrangementof the eukaryotic nuclear bodies. Proc Natl Acad Sci USA2002;99(21):13583-8.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.21 , pp. 13583-13588
    • Wang, I.-F.1    Reddy, N.M.2    Shen, C.-K.J.3
  • 31
    • 33748990136 scopus 로고    scopus 로고
    • SUSP1 antagonizesformation of highly SUMO2/3-conjugated species
    • Mukhopadhyay D, Ayaydin F, Kolli N, et al. SUSP1 antagonizesformation of highly SUMO2/3-conjugated species. J CellBiol 2006;174(7):939-49.
    • (2006) J CellBiol , vol.174 , Issue.7 , pp. 939-949
    • Mukhopadhyay, D.1    Ayaydin, F.2    Kolli, N.3
  • 32
    • 4043051557 scopus 로고    scopus 로고
    • A proteomic study ofSUMO-2 target proteins
    • Vertegaal ACO, Ogg SC, Jaffray E, et al. A proteomic study ofSUMO-2 target proteins. J Biol Chem 2004;279(32):33791-8.
    • (2004) J Biol Chem , vol.279 , Issue.32 , pp. 33791-33798
    • Aco, V.1    Ogg, S.C.2    Jaffray, E.3
  • 33
    • 67649173012 scopus 로고    scopus 로고
    • System-widechanges to SUMO modifications in response to heat shock
    • Golebiowski F, Matic I, Tatham MH, et al. System-widechanges to SUMO modifications in response to heat shock. SciSignal 2009;2(72):ra24.
    • (2009) Sci Signal , vol.2 , Issue.72
    • Golebiowski, F.1    Matic, I.2    Tatham, M.H.3
  • 34
    • 67650720512 scopus 로고    scopus 로고
    • Systematic study of protein sumoylation:development of a site-specific predictor of SUMOsp 2.0
    • Ren J, Gao X, Jin C, et al. Systematic study of protein sumoylation:development of a site-specific predictor of SUMOsp 2.0.Proteomics 2009;9(12):3409-12.
    • (2009) Proteomics , vol.9 , Issue.12 , pp. 3409-3412
    • Ren, J.1    Gao, X.2    Jin, C.3
  • 35
    • 80755163102 scopus 로고    scopus 로고
    • Molecular pathways ofmotor neuron injury in amyotrophic lateral sclerosis
    • Ferraiuolo L, Kirby J, Grierson AJ, et al.Molecular pathways ofmotor neuron injury in amyotrophic lateral sclerosis. Nat RevNeurol 2011;7(11):616-30.
    • (2011) Nat RevNeurol , vol.7 , Issue.11 , pp. 616-630
    • Ferraiuolo, L.1    Kirby, J.2    Grierson, A.J.3
  • 36
    • 46749152929 scopus 로고    scopus 로고
    • SUMO-1 transientlylocalizes to Cajal bodies in mammalian neurons
    • Navascues J, Bengoechea R, Tapia O, et al. SUMO-1 transientlylocalizes to Cajal bodies in mammalian neurons. J Struct Biol2008;163(2):137-46.
    • (2008) J Struct Biol , vol.163 , Issue.2 , pp. 137-146
    • Navascues, J.1    Bengoechea, R.2    Tapia, O.3
  • 37
    • 84860428058 scopus 로고    scopus 로고
    • P53 and cell cycle proteins participatein spinal motor neuron cell death in ALS
    • Ranganathan S, Bowser R. p53 and cell cycle proteins participatein spinal motor neuron cell death in ALS. Open Pathol J2010;4:11-22.
    • (2010) Open Pathol J , vol.4 , pp. 11-22
    • Ranganathan, S.1    Bowser, R.2
  • 38
    • 36349022018 scopus 로고    scopus 로고
    • Emergingextranuclear roles of protein SUMOylation in neuronal functionand dysfunction
    • Martin S, Wilkinson KA, Nishimune A, Henley JM. Emergingextranuclear roles of protein SUMOylation in neuronal functionand dysfunction. Nat Rev Neurosci 2007;8(12):948-59.
    • (2007) Nat Rev Neurosci , vol.8 , Issue.12 , pp. 948-959
    • Martin, S.1    Wilkinson, K.A.2    Nishimune, A.3    Henley, J.M.4
  • 39
  • 40
    • 33645422711 scopus 로고    scopus 로고
    • ANG mutationssegregate with familial and sporadic amyotrophic lateralsclerosis
    • Greenway MJ, Andersen PM, Russ C, et al. ANG mutationssegregate with familial and sporadic amyotrophic lateralsclerosis. Nat Genet 2006;38(4):411-3.
    • (2006) Nat Genet , vol.38 , Issue.4 , pp. 411-413
    • Greenway, M.J.1    Andersen, P.M.2    Russ, C.3
  • 41
    • 54049119245 scopus 로고    scopus 로고
    • Mutations of the ANG genein French patients with sporadic amyotrophic lateral sclerosis
    • Paubel A, Violette J, Amy M, et al. Mutations of the ANG genein French patients with sporadic amyotrophic lateral sclerosis.Arch Neurol 2008;65(10):1333-6.
    • (2008) Arch Neurol , vol.65 , Issue.10 , pp. 1333-1336
    • Paubel, A.1    Violette, J.2    Amy, M.3
  • 42
    • 35348904953 scopus 로고    scopus 로고
    • RSUMEa small RWD-containing protein enhances SUMO conjugationand stabilizes HIF-1alpha during hypoxia
    • Carbia-Nagashima A, Gerez J, Perez-Castro C, et al. RSUME,a small RWD-containing protein, enhances SUMO conjugationand stabilizes HIF-1alpha during hypoxia. Cell2007;131(2):309-23.
    • (2007) Cell , vol.131 , Issue.2 , pp. 309-323
    • Carbia-Nagashima, A.1    Gerez, J.2    Perez-Castro, C.3
  • 43
    • 79551524400 scopus 로고    scopus 로고
    • SUMO-1 interacts with mutant ataxin-1 andcolocalizes to its aggregates in Purkinje cells of SCA1 transgenicmice
    • Kang S, Hong S. SUMO-1 interacts with mutant ataxin-1 andcolocalizes to its aggregates in Purkinje cells of SCA1 transgenicmice. Arch Ital Biol 2010;148(4):351-63.
    • (2010) Arch Ital Biol , vol.148 , Issue.4 , pp. 351-363
    • Kang, S.1    Hong, S.2
  • 44
    • 35548935098 scopus 로고    scopus 로고
    • SUMO-specific protease1 is essential for stabilization of HIF1alpha during hypoxia
    • Cheng J, Kang X, Zhang S, Yeh ETH. SUMO-specific protease1 is essential for stabilization of HIF1alpha during hypoxia. Cell2007;131(3):584-95.
    • (2007) Cell , vol.131 , Issue.3 , pp. 584-595
    • Cheng, J.1    Kang, X.2    Zhang, S.3    Yeh, E.T.H.4
  • 45
    • 79953002264 scopus 로고    scopus 로고
    • Small ubiquitinrelatedmodifier (SUMO)-1 promotes glycolysis in hypoxia
    • Agbor TA, Cheong A, Comerford KM, et al. Small ubiquitinrelatedmodifier (SUMO)-1 promotes glycolysis in hypoxia.J Biol Chem 2011;286(6):4718-26.
    • J Biol Chem 2011 , vol.286 , Issue.6 , pp. 4718-4726
    • Agbor, T.A.1    Cheong, A.2    Comerford, K.M.3
  • 46
    • 0033967220 scopus 로고    scopus 로고
    • The sentrinconjugatingenzyme mUbc9 interacts with GLUT4 andGLUT1 glucose transporters and regulates transporter levelsin skeletal muscle cells
    • Giorgino F, De Robertis O, Laviola L, et al. The sentrinconjugatingenzyme mUbc9 interacts with GLUT4 andGLUT1 glucose transporters and regulates transporter levelsin skeletal muscle cells. Proc Natl Acad Sci USA2000;97(3):1125-30.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.3 , pp. 1125-1130
    • Giorgino, F.1    De Robertis, O.2    Laviola, L.3
  • 47
    • 84865501729 scopus 로고    scopus 로고
    • Impaired response ofhypoxic sensor protein HIF-1? and its downstream proteinsin the spinal motor neurons of ALS model mice
    • Sato K, Morimoto N, Kurata T, et al. Impaired response ofhypoxic sensor protein HIF-1? and its downstream proteinsin the spinal motor neurons of ALS model mice. Brain Res2012;1473:55-62.
    • (2012) Brain Res , vol.1473 , pp. 55-62
    • Sato, K.1    Morimoto, N.2    Kurata, T.3
  • 48
    • 77957562993 scopus 로고    scopus 로고
    • The role of oxidativestress in amyotrophic lateral sclerosis and Parkinson's disease
    • Baillet A, Chanteperdrix V, Trocḿe C, et al. The role of oxidativestress in amyotrophic lateral sclerosis and Parkinson's disease.Neurochem Res 2010;35(10):1530-7.
    • (2010) Neurochem Res , vol.35 , Issue.10 , pp. 1530-1537
    • Baillet, A.1    Chanteperdrix, V.2    Trocḿe, C.3
  • 50
    • 55849125016 scopus 로고    scopus 로고
    • Arf-inducedturnover of the nucleolar nucleophosmin-associated SUMO-2/3protease Senp3
    • KuoM-L, Den BestenW, ThomasMC, Sherr CJ. Arf-inducedturnover of the nucleolar nucleophosmin-associated SUMO-2/3protease Senp3. Cell Cycle 2008;7(21):3378-87.
    • (2008) Cell Cycle , vol.7 , Issue.21 , pp. 3378-3387
    • Kuo, M.-L.1    Den Besten, W.2    Thomas, M.C.3    Sherr, C.J.4
  • 51
    • 0037961625 scopus 로고    scopus 로고
    • P300transcriptional repression is mediated by SUMO modification
    • Girdwood D, Bumpass D, Vaughan OA, Thain A, et al. P300transcriptional repression is mediated by SUMO modification.Mol Cell 2003;11(4):1043-54.
    • (2003) Mol Cell , vol.11 , Issue.4 , pp. 1043-1054
    • Girdwood, D.1    Bumpass, D.2    Vaughan, O.A.3    Thain, A.4
  • 52
    • 70349168446 scopus 로고    scopus 로고
    • Hypoxia-induciblemir-210 regulates normoxic gene expression involved in tumorinitiation
    • Huang X, Ding L, Bennewith KL, et al. Hypoxia-induciblemir-210 regulates normoxic gene expression involved in tumorinitiation. Mol Cell 2009;35(6):856-67.
    • (2009) Mol Cell , vol.35 , Issue.6 , pp. 856-867
    • Huang, X.1    Ding, L.2    Bennewith, K.L.3
  • 53
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversibleoxidation of SUMO conjugating enzymes
    • Bossis G, Melchior F. Regulation of SUMOylation by reversibleoxidation of SUMO conjugating enzymes. Mol Cell2006;21(3):349-57.
    • (2006) Mol Cell , vol.21 , Issue.3 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 54
    • 23244436178 scopus 로고    scopus 로고
    • Role of GSK-3beta activityin motor neuronal cell death induced by G93A or A4V mutanthSOD1 gene
    • Koh S-H, Lee Y-B, Kim KS, et al. Role of GSK-3beta activityin motor neuronal cell death induced by G93A or A4V mutanthSOD1 gene. Eur J Neurosci 2005;22(2):301-9.
    • (2005) Eur J Neurosci , vol.22 , Issue.2 , pp. 301-309
    • Koh, S.-H.1    Lee, Y.-B.2    Kim, K.S.3
  • 55
    • 84864610364 scopus 로고    scopus 로고
    • The neuroprotective effect ofthe GSK-3? inhibitor and influence on the extrinsic apoptosisin the ALS transgenic mice
    • Ahn S-W, Kim J-E, Park KS, et al. The neuroprotective effect ofthe GSK-3? inhibitor and influence on the extrinsic apoptosisin the ALS transgenic mice. J Neurol Sci 2012;320(1-2):1-5.
    • (2012) J Neurol Sci , vol.320 , Issue.1-2 , pp. 1-5
    • Ahn, S.-W.1    Kim, J.-E.2    Park, K.S.3
  • 56
    • 77955365630 scopus 로고    scopus 로고
    • The small heat shock proteinB8 (HspB8) promotes autophagic removal of misfoldedproteins involved in amyotrophic lateral sclerosis (ALS)
    • Crippa V, Sau D, Rusmini P, et al. The small heat shock proteinB8 (HspB8) promotes autophagic removal of misfoldedproteins involved in amyotrophic lateral sclerosis (ALS). HumMol Genet 2010;19(17):3440-56.
    • (2010) Hum Mol Genet , vol.19 , Issue.17 , pp. 3440-3456
    • Crippa, V.1    Sau, D.2    Rusmini, P.3
  • 57
    • 78449275359 scopus 로고    scopus 로고
    • Redox regulation of the stabilityof the SUMO protease SENP3 via interactions with CHIP andHsp90
    • Yan S, Sun X, Xiang B, et al. Redox regulation of the stabilityof the SUMO protease SENP3 via interactions with CHIP andHsp90. EMBO J 2010;29(22):3773-86.
    • (2010) EMBO J , vol.29 , Issue.22 , pp. 3773-3786
    • Yan, S.1    Sun, X.2    Xiang, B.3
  • 58
    • 33846930615 scopus 로고    scopus 로고
    • The causes and mechanism of selective motorneuron death in amyotrophic lateral sclerosis
    • Van den Bosch L. [The causes and mechanism of selective motorneuron death in amyotrophic lateral sclerosis]. Verh K AcadGeneeskd Belg 2006;68(4):249-69.
    • (2006) Verh K AcadGeneeskd Belg , vol.68 , Issue.4 , pp. 249-269
    • Van Den Bosch, L.1
  • 59
    • 80052809771 scopus 로고    scopus 로고
    • Motor neuron impairmentmediated by a sumoylated fragment of the glial glutamatetransporter EAAT2
    • Foran E, Bogush A, Goffredo M, et al. Motor neuron impairmentmediated by a sumoylated fragment of the glial glutamatetransporter EAAT2. Glia 2011;59(11):1719-31.
    • (2011) Glia , vol.59 , Issue.11 , pp. 1719-1731
    • Foran, E.1    Bogush, A.2    Goffredo, M.3
  • 60
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurinin amyotrophic lateral sclerosis
    • Maruyama H, Morino H, Ito H, et al. Mutations of optineurinin amyotrophic lateral sclerosis. Nature 2010;465(7295):223-6.
    • (2010) Nature , vol.465 , Issue.7295 , pp. 223-226
    • Maruyama, H.1    Morino, H.2    Ito, H.3
  • 61
    • 33744909882 scopus 로고    scopus 로고
    • Caspase-3cleaves and inactivates the glutamate transporter EAAT2
    • Boston-Howes W, Gibb SL, Williams EO, et al. Caspase-3cleaves and inactivates the glutamate transporter EAAT2. J BiolChem 2006;281(20):14076-84.
    • (2006) J BiolChem , vol.281 , Issue.20 , pp. 14076-14084
    • Boston-Howes, W.1    Gibb, S.L.2    Williams, E.O.3
  • 62
    • 36148957860 scopus 로고    scopus 로고
    • A caspase-3-cleaved fragment of the glial glutamate transporter EAAT2 issumoylated and targeted to promyelocytic leukemia nuclearbodies in mutant SOD1-linked amyotrophic lateral sclerosis
    • Gibb SL, Boston-Howes W, Lavina ZS, et al. A caspase-3-cleaved fragment of the glial glutamate transporter EAAT2 issumoylated and targeted to promyelocytic leukemia nuclearbodies in mutant SOD1-linked amyotrophic lateral sclerosis.J Biol Chem 2007;282(44):32480-90.
    • (2007) J Biol Chem , vol.282 , Issue.44 , pp. 32480-32490
    • Gibb, S.L.1    Boston-Howes, W.2    Lavina, Z.S.3
  • 63
    • 0036944699 scopus 로고    scopus 로고
    • Smad3-dependent inductionof plasminogen activator inhibitor-1 in astrocytes mediatesneuroprotective activity of transforming growth factorbeta1 against NMDA-induced necrosis
    • Docagne F, Nicole O, Gabriel C, et al. Smad3-dependent inductionof plasminogen activator inhibitor-1 in astrocytes mediatesneuroprotective activity of transforming growth factorbeta1 against NMDA-induced necrosis. Mol Cell Neurosci2002;21(4):634-44.
    • (2002) Mol Cell Neurosci , vol.21 , Issue.4 , pp. 634-644
    • Docagne, F.1    Nicole, O.2    Gabriel, C.3
  • 64
    • 39749124883 scopus 로고    scopus 로고
    • Phosphorylated Smad2/3immunoreactivity in sporadic and familial amyotrophic lateralsclerosis and its mouse model
    • Nakamura M, Ito H, Wate R, et al. Phosphorylated Smad2/3immunoreactivity in sporadic and familial amyotrophic lateralsclerosis and its mouse model. Acta Neuropathol2008;115(3):327-34.
    • (2008) Acta Neuropathol , vol.115 , Issue.3 , pp. 327-334
    • Nakamura, M.1    Ito, H.2    Wate, R.3
  • 65
    • 42249101377 scopus 로고    scopus 로고
    • Sumoylation of Smad3stimulates its nuclear export during PIASy-mediated suppressionof TGF-beta signaling
    • Imoto S, Ohbayashi N, Ikeda O, et al. Sumoylation of Smad3stimulates its nuclear export during PIASy-mediated suppressionof TGF-beta signaling. Biochem Biophys Res Commun2008;370(2):359-65.
    • (2008) Biochem Biophys Res Commun , vol.370 , Issue.2 , pp. 359-365
    • Imoto, S.1    Ohbayashi, N.2    Ikeda, O.3
  • 66
    • 84876416652 scopus 로고    scopus 로고
    • Activation of transforminggrowth factor-?/Smad signaling reduces aggregate formation ofmislocalized TAR DNA-binding protein-43
    • [Epub before print] DOI 10.1159/000338151
    • Nakamura M, Kaneko S, Ito H, et al. Activation of transforminggrowth factor-?/Smad signaling reduces aggregate formation ofmislocalized TAR DNA-binding protein-43. Neurodegener Dis2012. [Epub before print] DOI 10.1159/000338151.
    • (2012) Neurodegener Dis
    • Nakamura, M.1    Kaneko, S.2    Ito, H.3
  • 67
    • 80755189921 scopus 로고    scopus 로고
    • How can we improve clinicaltrials in amyotrophic lateral sclerosis?
    • Gordon PH, Meininger V. How can we improve clinicaltrials in amyotrophic lateral sclerosis? Nat Rev Neurol2011;7(11):650-4.
    • Nat Rev Neurol2011 , vol.7 , Issue.11 , pp. 650-654
    • Gordon, P.H.1    Meininger, V.2
  • 68
    • 33645822300 scopus 로고    scopus 로고
    • Chronic activation inpresymptomatic amyotrophic lateral sclerosis (ALS) mice of afeedback loop involving Fas
    • Raoul C, Buhler E, Sadeghi C, et al. Chronic activation inpresymptomatic amyotrophic lateral sclerosis (ALS) mice of afeedback loop involving Fas, Daxx, and FasL. Proc Natl AcadSci USA 2006;103(15):6007-12.
    • (2006) Daxx, and FasL. Proc Natl AcadSci USA , vol.103 , Issue.15 , pp. 6007-6012
    • Raoul, C.1    Buhler, E.2    Sadeghi, C.3
  • 69
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interactingmotif in Daxx SUMO modification subnuclear localizationand repression of sumoylated transcription factors
    • Lin D-Y, Huang Y-S, Jeng J-C, et al. Role of SUMO-interactingmotif in Daxx SUMO modification, subnuclear localization,and repression of sumoylated transcription factors. Mol Cell2006;24(3):341-54.
    • (2006) Mol Cell , vol.24 , Issue.3 , pp. 341-354
    • Lin, D.-Y.1    Huang, Y.-S.2    Jeng, J.-C.3
  • 70
    • 84862798314 scopus 로고    scopus 로고
    • DeSUMOylating isopeptidase: A second class of SUMO protease
    • Shin EJ, Shin HM, Nam E, et al. DeSUMOylating isopeptidase:a second class of SUMO protease. EMBO Rep2012;13(4):339-46.
    • (2012) EMBO Rep , vol.13 , Issue.4 , pp. 339-346
    • Shin, E.J.1    Shin, H.M.2    Nam, E.3
  • 71
    • 0027401203 scopus 로고
    • Mutations in Cu/Znsuperoxide dismutase gene are associated with familial amyotrophiclateral sclerosis
    • Rosen DR, Siddique T, Patterson D, et al. Mutations in Cu/Znsuperoxide dismutase gene are associated with familial amyotrophiclateral sclerosis. Nature 1993;362:59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 72
    • 33645422711 scopus 로고    scopus 로고
    • ANG mutationssegregate with familial and sporadic amyotrophic lateral sclerosis
    • Greenway MJ, Andersen PM, Russ C, et al. ANG mutationssegregate with familial and "sporadic" amyotrophic lateral sclerosis.Nat Genet 2006;38:411-3.
    • (2006) Nat Genet , vol.38 , pp. 411-413
    • Greenway, M.J.1    Andersen, P.M.2    Russ, C.3
  • 73
    • 84908016489 scopus 로고    scopus 로고
    • TDP-43 mutationsin familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J, Blair IP, Tripathi VB, et al. TDP-43 mutationsin familial and sporadic amyotrophic lateral sclerosis. Science2008;3191668-72.
    • Science2008 , pp. 3191668-3191672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3
  • 74
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurinin amyotrophic lateral sclerosis
    • Maruyama H, Morino H, Ito H, et al. Mutations of optineurinin amyotrophic lateral sclerosis. Nature 2010;465:223-6.
    • (2010) Nature , vol.465 , pp. 223-226
    • Maruyama, H.1    Morino, H.2    Ito, H.3
  • 75
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2cause dominant X-linked juvenile and adult-onset ALS andALS/dementia
    • Deng H-X, Chen W, Hong S-T, et al. Mutations in UBQLN2cause dominant X-linked juvenile and adult-onset ALS andALS/dementia. Nature 2011;477:211-5.
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.-X.1    Chen, W.2    Hong, S.-T.3
  • 76
    • 0034785509 scopus 로고    scopus 로고
    • The gene encoding alsin aprotein with three guanine-nucleotide exchange factor domains,is mutated in a form of recessive amyotrophic lateral sclerosis
    • Yang Y, Hentati A, Deng HX, et al. The gene encoding alsin, aprotein with three guanine-nucleotide exchange factor domains,is mutated in a form of recessive amyotrophic lateral sclerosis.Nat Genet 2001;29:160-5.
    • (2001) Nat Genet , vol.29 , pp. 160-165
    • Yang, Y.1    Hentati, A.2    Deng, H.X.3
  • 77
    • 2442658908 scopus 로고    scopus 로고
    • DNA/RNA helicasegene mutations in a form of juvenile amyotrophic lateral sclerosis(ALS4
    • Chen Y-Z, Bennett CL, Huynh HM, et al. DNA/RNA helicasegene mutations in a form of juvenile amyotrophic lateral sclerosis(ALS4). Am J Hum Genet 2004;74:1128-35.
    • (2004) Am J Hum Genet , vol.74 , pp. 1128-1135
    • Chen, Y.-Z.1    Bennett, C.L.2    Huynh, H.M.3
  • 78
    • 77249126425 scopus 로고    scopus 로고
    • SPATACSIN mutationscause autosomal recessive juvenile amyotrophic lateralsclerosis
    • Orlacchio A, Babalini C, Borreca A, et al. SPATACSIN mutationscause autosomal recessive juvenile amyotrophic lateralsclerosis. Brain 2010;133:591-8.
    • (2010) Brain , vol.133 , pp. 591-598
    • Orlacchio, A.1    Babalini, C.2    Borreca, A.3
  • 79
    • 6344257200 scopus 로고    scopus 로고
    • A mutationin the vesicle-trafficking protein VAPB causes late-onset spinalmuscular atrophy and amyotrophic lateral sclerosis
    • Nishimura AL, Mitne-Neto M, Silva HCA et al. A mutationin the vesicle-trafficking protein VAPB causes late-onset spinalmuscular atrophy and amyotrophic lateral sclerosis. Am J HumGenet 2004;75:822-31.
    • (2004) Am J HumGenet , vol.75 , pp. 822-831
    • Nishimura, A.L.1    Mitne-Neto, M.2    Hca, S.3
  • 80
    • 58049192812 scopus 로고    scopus 로고
    • Deleterious variantsof FIG4, a phosphoinositide phosphatase in patients with ALS
    • Chow CY, Landers JE, Bergren SK, et al. Deleterious variantsof FIG4, a phosphoinositide phosphatase, in patients with ALS.Am J Hum Genet 2009;84:85-8.
    • (2009) Am J Hum Genet , vol.84 , pp. 85-88
    • Chow, C.Y.1    Landers, J.E.2    Bergren, S.K.3
  • 81
    • 78249273602 scopus 로고    scopus 로고
    • Sigma nonopioidintracellular receptor 1 mutations cause frontotemporallobar degeneration-motor neuron disease
    • Luty AA, Kwok JBJ, Dobson-Stone C, et al. Sigma nonopioidintracellular receptor 1 mutations cause frontotemporallobar degeneration-motor neuron disease. Ann Neurol2010;68:639-49.
    • (2010) Ann Neurol , vol.68 , pp. 639-649
    • Luty, A.A.1    Kwok, J.B.J.2    Dobson-Stone, C.3
  • 82
    • 84155163741 scopus 로고    scopus 로고
    • A mutation in sigma-1 receptorcauses juvenile amyotrophic lateral sclerosis
    • Al-Saif A, Al-Mohanna F, Bohlega S. A mutation in sigma-1 receptorcauses juvenile amyotrophic lateral sclerosis. Ann Neurol2011;70:913-9.
    • (2011) Ann Neurol , vol.70 , pp. 913-919
    • Al-Saif, A.1    Al-Mohanna, F.2    Bohlega, S.3
  • 83
    • 80054837386 scopus 로고    scopus 로고
    • A hex nucleotide repeatexpansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD
    • Renton AE, Majounie E, Waite A, et al. A hex nucleotide repeatexpansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 2011;72:257-68.
    • (2011) Neuron , vol.72 , pp. 257-268
    • Renton, A.E.1    Majounie, E.2    Waite, A.3
  • 84
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hex nucleotide repeat in noncoding regionof C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez M, Mackenzie IR, Boeve BF, et al. ExpandedGGGGCC hex nucleotide repeat in noncoding regionof C9ORF72 causes chromosome 9p-linked FTD and ALS.Neuron 2011;72:245-56.
    • (2011) Neuron , vol.72 , pp. 245-256
    • Dejesus-Hernandez, M.1    MacKenzie, I.R.2    Boeve, B.F.3
  • 85
    • 0032543684 scopus 로고    scopus 로고
    • Association of missenseand 5'-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M, Lendon CL, Rizzu P, et al. Association of missenseand 5'-splice-site mutations in tau with the inherited dementiaFTDP-17. Nature 1998;393:702-5.
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 86
    • 78649941297 scopus 로고    scopus 로고
    • Exome sequencingreveals VCP mutations as a cause of familial ALS
    • Johnson JO, Mandrioli J, Benatar M, et al. Exome sequencingreveals VCP mutations as a cause of familial ALS. Neuron2010;68:857-64.
    • (2010) Neuron , vol.68 , pp. 857-864
    • Johnson, J.O.1    Mandrioli, J.2    Benatar, M.3
  • 87
    • 0041104778 scopus 로고    scopus 로고
    • ApolipoproteinE in Guamanian amyotrophic lateral sclerosis/ parkinsonismdementiacomplex: Genotype analysis and relationships toneuropathological changes
    • Búee L, Ṕerez-Tur J, Leveugle B, et al. ApolipoproteinE in Guamanian amyotrophic lateral sclerosis/parkinsonismdementiacomplex: genotype analysis and relationships toneuropathological changes. Acta Neuropathol 1996;91:247-53.
    • (1996) Acta Neuropathol , vol.91 , pp. 247-253
    • Búee, L.1    Ṕerez-Tur, J.2    Leveugle, B.3
  • 88
    • 77956155218 scopus 로고    scopus 로고
    • Ataxin-2 intermediatelengthpolyglutamine expansions are associated with increasedrisk for ALS
    • Elden AC, Kim H-J, Hart MP, et al. Ataxin-2 intermediatelengthpolyglutamine expansions are associated with increasedrisk for ALS. Nature 2010;466:1069-75.
    • (2010) Nature , vol.466 , pp. 1069-1075
    • Elden, A.C.1    Kim, H.-J.2    Hart, M.P.3
  • 89
    • 76049085112 scopus 로고    scopus 로고
    • ChromograninB P413L variant as risk factor and modifier of disease onsetfor amyotrophic lateral sclerosis
    • Gros-Louis F, Andersen PM, Dupre N, et al. ChromograninB P413L variant as risk factor and modifier of disease onsetfor amyotrophic lateral sclerosis. Proc Natl Acad Sci USA2009;106:21777-82.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 21777-21782
    • Gros-Louis, F.1    Andersen, P.M.2    Dupre, N.3
  • 90
    • 33749006845 scopus 로고    scopus 로고
    • ALS phenotypes withmutations in CHMP2B (charged multivesicular body protein2B
    • Parkinson N, Ince PG, Smith MO, et al. ALS phenotypes withmutations in CHMP2B (charged multivesicular body protein2B). Neurology 2006;67:1074-7.
    • (2006) Neurology , vol.67 , pp. 1074-1077
    • Parkinson, N.1    Ince, P.G.2    Smith, M.O.3
  • 91
    • 33748707208 scopus 로고    scopus 로고
    • Paraoxonase clusterpolymorphisms are associated with sporadic ALS
    • Saeed M, Siddique N, Hung WY, et al. Paraoxonase clusterpolymorphisms are associated with sporadic ALS. Neurology2006;67:771-6.
    • (2006) Neurology , vol.67 , pp. 771-776
    • Saeed, M.1    Siddique, N.2    Hung, W.Y.3
  • 92
    • 79952815816 scopus 로고    scopus 로고
    • Association between divalentmetal transport 1 encoding gene (SLC11A2) and diseaseduration in amyotrophic lateral sclerosis
    • Blasco H, Vourc'h P, Nadjar Y, et al. Association between divalentmetal transport 1 encoding gene (SLC11A2) and diseaseduration in amyotrophic lateral sclerosis. J Neurol Sci2011;303:124-7.
    • (2011) J Neurol Sci , vol.303 , pp. 124-127
    • Blasco, H.1    Vourc'H, P.2    Nadjar, Y.3
  • 93
    • 0036156999 scopus 로고    scopus 로고
    • Abnormal SMN1gene copy number is a susceptibility factor for amyotrophic lateralsclerosis
    • Corcia P, Mayeux-Portas V, Khoris J, et al. Abnormal SMN1gene copy number is a susceptibility factor for amyotrophic lateralsclerosis. Ann Neurol 2002;51:243-6.
    • (2002) Ann Neurol , vol.51 , pp. 243-246
    • Corcia, P.1    Mayeux-Portas, V.2    Khoris, J.3
  • 94
    • 0035957312 scopus 로고    scopus 로고
    • Homozygousdeletion of the survival motor neuron 2 gene isa prognostic factor in sporadic ALS
    • Veldink JH, van den Berg LH, Cobben JM, et al. Homozygousdeletion of the survival motor neuron 2 gene isa prognostic factor in sporadic ALS. Neurology 2001;56:749-52.
    • (2001) Neurology , vol.56 , pp. 749-752
    • Veldink, J.H.1    Van Den Berg, L.H.2    Cobben, J.M.3
  • 95
    • 70349592269 scopus 로고    scopus 로고
    • Genome-wide associationstudy identifies 19p13.3 (UNC13A) and 9p21.2 assusceptibility loci for sporadic amyotrophic lateral sclerosis
    • van Es MA, Veldink JH, Saris CGJ, et al. Genome-wide associationstudy identifies 19p13.3 (UNC13A) and 9p21.2 assusceptibility loci for sporadic amyotrophic lateral sclerosis. NatGenet 2009;41:1083-7.
    • (2009) NatGenet , vol.41 , pp. 1083-1087
    • Van Es, M.A.1    Veldink, J.H.2    Saris, C.G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.