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Volumn 9, Issue 6, 2010, Pages 779-790

Genetic determinants of amyotrophic lateral sclerosis as therapeutic targets

Author keywords

Amyotrophic lateral sclerosis; Genome wide association; Neurodegeneration; Therapy

Indexed keywords

ANGIOGENIC FACTOR; ANGIOGENIN; ARIMOCLOMOL; COPPER ZINC SUPEROXIDE DISMUTASE; DNA BINDING PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; KINESIN ASSOCIATED PROTEIN 3A; KINESIN ASSOCIATED PROTEIN 3B; MICRORNA; PROTEIN BCL 2; PROTEIN UNC 13 HOMOLOG A; RILUZOLE; SB 509; SMALL INTERFERING RNA; SNARE PROTEIN; TAR DNA BINDING PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 78649277728     PISSN: 18715273     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152710793237494     Document Type: Article
Times cited : (34)

References (158)
  • 1
    • 0021809173 scopus 로고
    • Amyotrophic lateral sclerosis: Part 1. Clinical features, pathology and ethical issues in management
    • Tandan, R.; Bradley, W.G. Amyotrophic lateral sclerosis: Part 1. Clinical features, pathology and ethical issues in management. Ann. Neurol., 1985, 18, 271-280.
    • (1985) Ann. Neurol , vol.18 , pp. 271-280
    • Tandan, R.1    Bradley, W.G.2
  • 2
  • 4
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A disease of motor neurons and their nonneuronal neighbors
    • Boillee, S.; Vande Velde, C.; Cleveland, D.W. ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron, 2006, 52, 39-59.
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillee, S.1    vande Velde, C.2    Cleveland, D.W.3
  • 5
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein, J.D. Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann. Neurol., 2009, 65(Suppl 1), S3-S9.
    • (2009) Ann. Neurol , vol.65 , Issue.SUPPL. 1
    • Rothstein, J.D.1
  • 7
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • Pasinelli, P.; Brown, R.H. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci., 2006, 7, 710-723.
    • (2006) Nat. Rev. Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 8
    • 0030806863 scopus 로고    scopus 로고
    • 2-.), superoxide dismutases and related matters
    • 2-.), superoxide dismutases and related matters. J. Biol. Chem., 1997, 272, 18515-18517.
    • (1997) J. Biol. Chem , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 12
    • 66749133370 scopus 로고    scopus 로고
    • Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS
    • Chattopadhyay, M.; Valentine, J.S. Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS. Antioxid. Redox. Signal., 2009, 11, 1603-1614.
    • (2009) Antioxid. Redox. Signal , vol.11 , pp. 1603-1614
    • Chattopadhyay, M.1    Valentine, J.S.2
  • 13
    • 68749083546 scopus 로고    scopus 로고
    • Variation in aggregation propensities among ALS-associated variants of SOD1: Correlation to human disease
    • Prudencio, M.; Hart, P.J.; Borchelt, D.R.; Andersen, P.M. Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease. Hum. Mol. Genet., 2009, 18, 3217-3226.
    • (2009) Hum. Mol. Genet , vol.18 , pp. 3217-3226
    • Prudencio, M.1    Hart, P.J.2    Borchelt, D.R.3    Andersen, P.M.4
  • 14
    • 3242703300 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria
    • Pasinelli, P.; Belford, M.E.; Lennon, N.; Bacskai, B.J.; Hyman, B.T.; Trotti, D.; Brown, R.H., Jr. Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron, 2004, 43, 19-30.
    • (2004) Neuron , vol.43 , pp. 19-30
    • Pasinelli, P.1    Belford, M.E.2    Lennon, N.3    Bacskai, B.J.4    Hyman, B.T.5    Trotti, D.6    Brown Jr., R.H.7
  • 15
    • 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, J.P. Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci., 2006, 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
  • 16
    • 41649086378 scopus 로고    scopus 로고
    • Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria
    • Vande Velde, C.; Miller, T.M.; Cashman, N.R.; Cleveland, D.W. Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria. Proc. Natl. Acad. Sci. USA, 2008, 105, 4022-4027.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4022-4027
    • vande Velde, C.1    Miller, T.M.2    Cashman, N.R.3    Cleveland, D.W.4
  • 17
    • 70449417623 scopus 로고    scopus 로고
    • Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities
    • Magrane, J.; Hervias, I.; Henning, M.S.; Damiano, M.; Kawamata, H.; Manfredi, G. Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities. Hum. Mol. Genet., 2009, 18, 4552-4564.
    • (2009) Hum. Mol. Genet , vol.18 , pp. 4552-4564
    • Magrane, J.1    Hervias, I.2    Henning, M.S.3    Damiano, M.4    Kawamata, H.5    Manfredi, G.6
  • 18
    • 66749104344 scopus 로고    scopus 로고
    • Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis
    • Magrane, J.; Manfredi, G. Mitochondrial function, morphology, and axonal transport in amyotrophic lateral sclerosis. Antioxid. Redox. Signal., 2009, 11, 1615-1626.
    • (2009) Antioxid. Redox. Signal , vol.11 , pp. 1615-1626
    • Magrane, J.1    Manfredi, G.2
  • 20
    • 60549104791 scopus 로고    scopus 로고
    • Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3
    • Tateno, M.; Kato, S.; Sakurai, T.; Nukina, N.; Takahashi, R.; Araki, T. Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3. Hum. Mol. Genet., 2009, 18, 942-955.
    • (2009) Hum. Mol. Genet , vol.18 , pp. 942-955
    • Tateno, M.1    Kato, S.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Araki, T.6
  • 21
    • 33751013740 scopus 로고    scopus 로고
    • Transgenic mouse models of amyotrophic lateral sclerosis
    • Julien, J.P.; Kriz, J. Transgenic mouse models of amyotrophic lateral sclerosis. Biochim. Biophys. Acta, 2006, 1762, 1013-1024.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 1013-1024
    • Julien, J.P.1    Kriz, J.2
  • 22
    • 0035575761 scopus 로고    scopus 로고
    • Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: Associated mutations develop motor neuron disease
    • Nagai, M.; Aoki, M.; Miyoshi, I.; Kato, M.; Pasinelli, P.; Kasai, N.; Brown, R.H., Jr.; Itoyama, Y. Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: associated mutations develop motor neuron disease. J. Neurosci., 2001, 21, 9246-9254.
    • (2001) J. Neurosci , vol.21 , pp. 9246-9254
    • Nagai, M.1    Aoki, M.2    Miyoshi, I.3    Kato, M.4    Pasinelli, P.5    Kasai, N.6    Brown Jr., R.H.7    Itoyama, Y.8
  • 24
    • 70649097387 scopus 로고    scopus 로고
    • RNAi applications in therapy development for neurodegenerative disease
    • Maxwell, M.M. RNAi applications in therapy development for neurodegenerative disease. Curr. Pharm. Des., 2009, 15, 3977-3991.
    • (2009) Curr. Pharm. Des , vol.15 , pp. 3977-3991
    • Maxwell, M.M.1
  • 25
    • 14644393684 scopus 로고    scopus 로고
    • Perspective: Machines for RNAi
    • Tomari, Y.; Zamore, P.D. Perspective: machines for RNAi. Genes Dev., 2005, 19, 517-529.
    • (2005) Genes Dev , vol.19 , pp. 517-529
    • Tomari, Y.1    Zamore, P.D.2
  • 26
    • 0032700656 scopus 로고    scopus 로고
    • Molecular mechanisms of action of antisense drugs
    • Crooke, S.T. Molecular mechanisms of action of antisense drugs. Biochim. Biophys. Acta, 1999, 1489, 31-44.
    • (1999) Biochim. Biophys. Acta , vol.1489 , pp. 31-44
    • Crooke, S.T.1
  • 28
    • 17644383664 scopus 로고    scopus 로고
    • Lentiviral-mediated silencing of SOD1 through RNA interference retards disease onset and progression in a mouse model of ALS
    • Raoul, C.; Abbas-Terki, T.; Bensadoun, J.C.; Guillot, S.; Haase, G.; Szulc, J.; Henderson, C.E.; Aebischer, P. Lentiviral-mediated silencing of SOD1 through RNA interference retards disease onset and progression in a mouse model of ALS. Nat. Med., 2005, 11, 423-428.
    • (2005) Nat. Med , vol.11 , pp. 423-428
    • Raoul, C.1    Abbas-Terki, T.2    Bensadoun, J.C.3    Guillot, S.4    Haase, G.5    Szulc, J.6    Henderson, C.E.7    Aebischer, P.8
  • 29
    • 47049099443 scopus 로고    scopus 로고
    • Therapeutic gene silencing delivered by a chemically modified small interfering RNA against mutant SOD1 slows amyotrophic lateral sclerosis progression
    • Wang, H.; Ghosh, A.; Baigude, H.; Yang, C.S.; Qiu, L.; Xia, X.; Zhou, H.; Rana, T.M.; Xu, Z. Therapeutic gene silencing delivered by a chemically modified small interfering RNA against mutant SOD1 slows amyotrophic lateral sclerosis progression. J. Biol. Chem., 2008, 283, 15845-15852.
    • (2008) J. Biol. Chem , vol.283 , pp. 15845-15852
    • Wang, H.1    Ghosh, A.2    Baigude, H.3    Yang, C.S.4    Qiu, L.5    Xia, X.6    Zhou, H.7    Rana, T.M.8    Xu, Z.9
  • 31
    • 33747201641 scopus 로고    scopus 로고
    • Allele-specific RNAi selectively silences mutant SOD1 and achieves significant therapeutic benefit in vivo
    • Xia, X.; Zhou, H.; Huang, Y.; Xu, Z. Allele-specific RNAi selectively silences mutant SOD1 and achieves significant therapeutic benefit in vivo. Neurobiol. Dis., 2006, 23, 578-586.
    • (2006) Neurobiol. Dis , vol.23 , pp. 578-586
    • Xia, X.1    Zhou, H.2    Huang, Y.3    Xu, Z.4
  • 33
    • 33751003518 scopus 로고    scopus 로고
    • Oxidative stress in ALS: A mechanism of neurodegeneration and a therapeutic target
    • Barber, S.C.; Mead, R.J.; Shaw, P.J. Oxidative stress in ALS: a mechanism of neurodegeneration and a therapeutic target. Biochim. Biophys. Acta, 2006, 1762, 1051-1067.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 1051-1067
    • Barber, S.C.1    Mead, R.J.2    Shaw, P.J.3
  • 34
    • 33847787621 scopus 로고    scopus 로고
    • Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis
    • Urushitani, M.; Ezzi, S.A.; Julien, J.P. Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA, 2007, 104, 2495-2500.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2495-2500
    • Urushitani, M.1    Ezzi, S.A.2    Julien, J.P.3
  • 35
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong, P.C.; Pardo, C.A.; Borchelt, D.R.; Lee, M.K.; Copeland, N.G.; Jenkins, N.A.; Sisodia, S.S.; Cleveland, D.W.; Price, D.L. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron, 1995, 14, 1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 37
    • 33845240108 scopus 로고    scopus 로고
    • Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants
    • Sawkar, A.R.; Schmitz, M.; Zimmer, K.P.; Reczek, D.; Edmunds, T.; Balch, W.E.; Kelly, J.W. Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants. ACS Chem. Biol., 2006, 1, 235-251.
    • (2006) ACS Chem. Biol , vol.1 , pp. 235-251
    • Sawkar, A.R.1    Schmitz, M.2    Zimmer, K.P.3    Reczek, D.4    Edmunds, T.5    Balch, W.E.6    Kelly, J.W.7
  • 38
    • 0346333094 scopus 로고    scopus 로고
    • Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis
    • Adamski-Werner, S.L.; Palaninathan, S.K.; Sacchettini, J.C.; Kelly, J.W. Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis. J. Med. Chem., 2004, 47, 355-374.
    • (2004) J. Med. Chem , vol.47 , pp. 355-374
    • Adamski-Werner, S.L.1    Palaninathan, S.K.2    Sacchettini, J.C.3    Kelly, J.W.4
  • 39
    • 14844361966 scopus 로고    scopus 로고
    • Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    • Ray, S.S.; Nowak, R.J.; Brown, R.H., Jr.; Lansbury, P.T., Jr. Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Proc. Natl. Acad. Sci. USA, 2005, 102, 3639-3644.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3639-3644
    • Ray, S.S.1    Nowak, R.J.2    Brown Jr., R.H.3    Lansbury Jr., P.T.4
  • 40
    • 2142761528 scopus 로고    scopus 로고
    • An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis
    • Ray, S.S.; Nowak, R.J.; Strokovich, K.; Brown, R.H., Jr.; Walz, T.; Lansbury, P.T., Jr. An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Biochemistry, 2004, 43, 4899-4905.
    • (2004) Biochemistry , vol.43 , pp. 4899-4905
    • Ray, S.S.1    Nowak, R.J.2    Strokovich, K.3    Brown Jr., R.H.4    Walz, T.5    Lansbury Jr., P.T.6
  • 41
    • 2442624720 scopus 로고    scopus 로고
    • Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis
    • Rakhit, R.; Crow, J.P.; Lepock, J.R.; Kondejewski, L.H.; Cashman, N.R.; Chakrabartty, A. Monomeric Cu, Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. J. Biol. Chem., 2004, 279, 15499-15504.
    • (2004) J. Biol. Chem , vol.279 , pp. 15499-15504
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5    Chakrabartty, A.6    Monomeric, C.7
  • 43
    • 71449104857 scopus 로고    scopus 로고
    • A common property of amyotrophic lateral sclerosis-associated variants: Destabilization of the Cu/Zn superoxide dismutase electrostatic loop
    • Molnar, K.S.; Karabacak, N.M.; Johnson, J.L.; Wang, Q.; Tiwari, A.; Hayward, L.J.; Coales, S.J.; Hamuro, Y.; Agar, J.N. A common property of amyotrophic lateral sclerosis-associated variants: Destabilization of the Cu/Zn superoxide dismutase electrostatic loop. J. Biol. Chem., 2009, 284, 30965-30973.
    • (2009) J. Biol. Chem , vol.284 , pp. 30965-30973
    • Molnar, K.S.1    Karabacak, N.M.2    Johnson, J.L.3    Wang, Q.4    Tiwari, A.5    Hayward, L.J.6    Coales, S.J.7    Hamuro, Y.8    Agar, J.N.9
  • 44
    • 0344507132 scopus 로고    scopus 로고
    • Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis
    • Bruening, W.; Roy, J.; Giasson, B.; Figlewicz, D.A.; Mushynski, W.E.; Durham, H.D. Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis. J. Neurochem., 1999, 72, 693-699.
    • (1999) J. Neurochem , vol.72 , pp. 693-699
    • Bruening, W.1    Roy, J.2    Giasson, B.3    Figlewicz, D.A.4    Mushynski, W.E.5    Durham, H.D.6
  • 46
    • 53149114499 scopus 로고    scopus 로고
    • Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS
    • Kalmar, B.; Novoselov, S.; Gray, A.; Cheetham, M.E.; Margulis, B.; Greensmith, L. Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS. J. Neurochem., 2008, 107, 339-350.
    • (2008) J. Neurochem , vol.107 , pp. 339-350
    • Kalmar, B.1    Novoselov, S.2    Gray, A.3    Cheetham, M.E.4    Margulis, B.5    Greensmith, L.6
  • 47
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran, D.; Kalmar, B.; Dick, J.R.; Riddoch-Contreras, J.; Burnstock, G.; Greensmith, L. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med., 2004, 10, 402-405.
    • (2004) Nat. Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 50
    • 34250177650 scopus 로고    scopus 로고
    • Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation
    • Ezzi, S.A.; Urushitani, M.; Julien, J.P. Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation. J. Neurochem., 2007, 102, 170-178.
    • (2007) J. Neurochem , vol.102 , pp. 170-178
    • Ezzi, S.A.1    Urushitani, M.2    Julien, J.P.3
  • 56
    • 48249083430 scopus 로고    scopus 로고
    • The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response
    • Andersson, M.K.; Stahlberg, A.; Arvidsson, Y.; Olofsson, A.; Semb, H.; Stenman, G.; Nilsson, O.; Aman, P. The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response. BMC Cell Biol., 2008, 9, 37.
    • (2008) BMC Cell Biol , vol.9 , pp. 37
    • Andersson, M.K.1    Stahlberg, A.2    Arvidsson, Y.3    Olofsson, A.4    Semb, H.5    Stenman, G.6    Nilsson, O.7    Aman, P.8
  • 58
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: The FUS about TDP-43
    • Lagier-Tourenne, C.; Cleveland, D.W. Rethinking ALS: the FUS about TDP-43. Cell, 2009, 136, 1001-1004.
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 59
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti, E.; Baralle, F.E. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front. Biosci., 2008, 13, 867-878.
    • (2008) Front. Biosci , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 61
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti, E.; Dork, T.; Zuccato, E.; Pagani, F.; Romano, M.; Baralle, F.E. Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J., 2001, 20, 1774-1784.
    • (2001) EMBO J , vol.20 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5    Baralle, F.E.6
  • 62
    • 0034053964 scopus 로고    scopus 로고
    • TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins
    • Yang, L.; Embree, L.J.; Hickstein, D.D. TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-arginine proteins. Mol. Cell Biol., 2000, 20, 3345-3354.
    • (2000) Mol. Cell Biol , vol.20 , pp. 3345-3354
    • Yang, L.1    Embree, L.J.2    Hickstein, D.D.3
  • 63
    • 0030746523 scopus 로고    scopus 로고
    • TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling
    • Zinszner, H.; Sok, J.; Immanuel, D.; Yin, Y.; Ron, D. TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling. J. Cell Sci., 1997, 110(Pt 15), 1741-1750.
    • (1997) J. Cell Sci , vol.110 , Issue.Pt 15 , pp. 1741-1750
    • Zinszner, H.1    Sok, J.2    Immanuel, D.3    Yin, Y.4    Ron, D.5
  • 76
    • 34247606414 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation
    • Tan, C.F.; Eguchi, H.; Tagawa, A.; Onodera, O.; Iwasaki, T.; Tsujino, A.; Nishizawa, M.; Kakita, A.; Takahashi, H. TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol., 2007, 113, 535-542.
    • (2007) Acta Neuropathol , vol.113 , pp. 535-542
    • Tan, C.F.1    Eguchi, H.2    Tagawa, A.3    Onodera, O.4    Iwasaki, T.5    Tsujino, A.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 77
    • 77649252528 scopus 로고    scopus 로고
    • Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
    • Pesiridis, G.S.; Lee, V.M.; Trojanowski, J.Q. Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis. Hum. Mol. Genet., 2009, 18, R156-R162.
    • (2009) Hum. Mol. Genet , vol.18
    • Pesiridis, G.S.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 78
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska, I.; Bell, S.; Cairns, N.J.; Miller, T.M.; Baloh, R.H. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl. Acad. Sci. USA, 2009, 106, 18809-18814.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 79
    • 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.; Skibinski, G.; Korb, E.; Rao, E.J.; Wu, J.Y.; Finkbeiner, S. Cytoplasmic, mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J. Neurosci., 2010, 30, 639-649.
    • (2010) J. Neurosci , vol.30 , pp. 639-649
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5    Finkbeiner, S.6
  • 80
    • 33748786259 scopus 로고    scopus 로고
    • Identification and characterization of the nuclear localization/retention signal in the
    • Zakaryan, R.P.; Gehring, H. Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein. J. Mol. Biol., 2006, 363, 27-38.
    • (2006) EWS Proto-Oncoprotein. J. Mol. Biol , vol.363 , pp. 27-38
    • Zakaryan, R.P.1    Gehring, H.2
  • 84
    • 13244264730 scopus 로고    scopus 로고
    • Endogenous angiogenin in endothelial cells is a general requirement for cell proliferation and angiogenesis
    • Kishimoto, K.; Liu, S.; Tsuji, T.; Olson, K.A.; Hu, G.F. Endogenous angiogenin in endothelial cells is a general requirement for cell proliferation and angiogenesis. Oncogene, 2005, 24, 445-456.
    • (2005) Oncogene , vol.24 , pp. 445-456
    • Kishimoto, K.1    Liu, S.2    Tsuji, T.3    Olson, K.A.4    Hu, G.F.5
  • 88
  • 93
    • 37549019664 scopus 로고    scopus 로고
    • Human angiogenin is a neuroprotective factor and amyotrophic lateral sclerosis associated angiogenin variants affect neurite extension/pathfinding and survival of motor neurons
    • Subramanian, V.; Crabtree, B.; Acharya, K.R. Human angiogenin is a neuroprotective factor and amyotrophic lateral sclerosis associated angiogenin variants affect neurite extension/pathfinding and survival of motor neurons. Hum. Mol. Genet., 2008, 17, 130-149.
    • (2008) Hum. Mol. Genet , vol.17 , pp. 130-149
    • Subramanian, V.1    Crabtree, B.2    Acharya, K.R.3
  • 94
    • 0028032835 scopus 로고
    • The widespread expression of angiogenin in different human cells suggests a biological function not only related to angiogenesis
    • Moenner, M.; Gusse, M.; Hatzi, E.; Badet, J. The widespread expression of angiogenin in different human cells suggests a biological function not only related to angiogenesis. Eur. J. Biochem., 1994, 226, 483-490.
    • (1994) Eur. J. Biochem , vol.226 , pp. 483-490
    • Moenner, M.1    Gusse, M.2    Hatzi, E.3    Badet, J.4
  • 95
    • 70350708176 scopus 로고    scopus 로고
    • Human mast cells synthesize and release angiogenin, a member of the ribonuclease A (RNase A) superfamily
    • Kulka, M.; Fukuishi, N.; Metcalfe, D.D. Human mast cells synthesize and release angiogenin, a member of the ribonuclease A (RNase A) superfamily. J. Leukoc. Biol., 2009, 85, 1217-1226.
    • (2009) J. Leukoc. Biol , vol.85 , pp. 1217-1226
    • Kulka, M.1    Fukuishi, N.2    Metcalfe, D.D.3
  • 96
    • 69549114285 scopus 로고    scopus 로고
    • Dominant expression of angiogenin in NeuN positive cells in the focal ischemic rat brain
    • Huang, L.; Huang, Y.; Guo, H. Dominant expression of angiogenin in NeuN positive cells in the focal ischemic rat brain. J. Neurol. Sci., 2009, 285, 220-223.
    • (2009) J. Neurol. Sci , vol.285 , pp. 220-223
    • Huang, L.1    Huang, Y.2    Guo, H.3
  • 97
    • 0027941844 scopus 로고
    • Identification of the nucleolar targeting signal of human angiogenin
    • Moroianu, J.; Riordan, J.F. Identification of the nucleolar targeting signal of human angiogenin. Biochem. Biophys. Res. Commun., 1994, 203, 1765-1772.
    • (1994) Biochem. Biophys. Res. Commun , vol.203 , pp. 1765-1772
    • Moroianu, J.1    Riordan, J.F.2
  • 98
    • 0028262977 scopus 로고
    • Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity
    • Moroianu, J.; Riordan, J.F. Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. Proc. Natl. Acad. Sci. USA, 1994, 91, 1677-1681.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1677-1681
    • Moroianu, J.1    Riordan, J.F.2
  • 99
    • 0032510699 scopus 로고    scopus 로고
    • Structural features that determine the enzymatic potency and specificity of human angiogenin: Threonine-80 and residues 58-70 and 116-123
    • Shapiro, R. Structural features that determine the enzymatic potency and specificity of human angiogenin: threonine-80 and residues 58-70 and 116-123. Biochemistry, 1998, 37, 6847-6856.
    • (1998) Biochemistry , vol.37 , pp. 6847-6856
    • Shapiro, R.1
  • 100
    • 0026794004 scopus 로고
    • Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily
    • Saxena, S.K.; Rybak, S.M.; Davey, R.T., Jr.; Youle, R.J.; Ackerman, E.J. Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. J. Biol. Chem., 1992, 267, 21982-21986.
    • (1992) J. Biol. Chem , vol.267 , pp. 21982-21986
    • Saxena, S.K.1    Rybak, S.M.2    Davey Jr., R.T.3    Youle, R.J.4    Ackerman, E.J.5
  • 101
    • 65249129859 scopus 로고    scopus 로고
    • Angiogenin cleaves tRNA and promotes stress-induced translational repression
    • Yamasaki, S.; Ivanov, P.; Hu, G.F.; Anderson P. Angiogenin cleaves tRNA and promotes stress-induced translational repression. J. Cell Biol., 2009, 185, 35-42.
    • (2009) J. Cell Biol , vol.185 , pp. 35-42
    • Yamasaki, S.1    Ivanov, P.2    Hu, G.F.3    Anderson, P.4
  • 102
    • 0036293389 scopus 로고    scopus 로고
    • The nuclear function of angiogenin in endothelial cells is related to rRNA production
    • Xu, Z.P.; Tsuji, T.; Riordan, J.F.; Hu, G.F. The nuclear function of angiogenin in endothelial cells is related to rRNA production. Biochem. Biophys. Res. Commun., 2002, 294, 287-292.
    • (2002) Biochem. Biophys. Res. Commun , vol.294 , pp. 287-292
    • Xu, Z.P.1    Tsuji, T.2    Riordan, J.F.3    Hu, G.F.4
  • 103
    • 0037435587 scopus 로고    scopus 로고
    • Identification and characterization of an angiogenin-binding DNA sequence that stimulates luciferase reporter gene expression
    • Xu, Z.P.; Tsuji, T.; Riordan, J.F.; Hu, G.F. Identification and characterization of an angiogenin-binding DNA sequence that stimulates luciferase reporter gene expression. Biochemistry, 2003, 42, 121-128.
    • (2003) Biochemistry , vol.42 , pp. 121-128
    • Xu, Z.P.1    Tsuji, T.2    Riordan, J.F.3    Hu, G.F.4
  • 106
    • 34447317537 scopus 로고    scopus 로고
    • A new role for angiogenin in neurite growth and pathfinding: Implications for amyotrophic lateral sclerosis
    • Subramanian, V.; Feng, Y. A new role for angiogenin in neurite growth and pathfinding: implications for amyotrophic lateral sclerosis. Hum. Mol. Genet., 2007, 16, 1445-1453.
    • (2007) Hum. Mol. Genet , vol.16 , pp. 1445-1453
    • Subramanian, V.1    Feng, Y.2
  • 110
    • 78649301205 scopus 로고
    • Baltimore: University Press: Johns Hopkins
    • Ott, J. Analysis of Human Genetics; Baltimore: University Press: Johns Hopkins, 1991.
    • (1991) Analysis of Human Genetics
    • Ott, J.1
  • 111
    • 44349132708 scopus 로고    scopus 로고
    • Common and rare variants in multifactorial susceptibility to common diseases
    • Bodmer, W.; Bonilla, C. Common and rare variants in multifactorial susceptibility to common diseases. Nat. Genet., 2008, 40, 695-701.
    • (2008) Nat. Genet , vol.40 , pp. 695-701
    • Bodmer, W.1    Bonilla, C.2
  • 112
    • 53649093358 scopus 로고    scopus 로고
    • Genome-wide association studies in neurological disorders
    • Simon-Sanchez, J.; Singleton, A. Genome-wide association studies in neurological disorders. Lancet Neurol., 2008, 7, 1067-1072.
    • (2008) Lancet Neurol , vol.7 , pp. 1067-1072
    • Simon-Sanchez, J.1    Singleton, A.2
  • 113
    • 66349121862 scopus 로고    scopus 로고
    • The HapMap and genome-wide association studies in diagnosis and therapy
    • Manolio, T.A.; Collins, F.S. The HapMap and genome-wide association studies in diagnosis and therapy. Annu. Rev. Med., 2009, 60, 443-456.
    • (2009) Annu. Rev. Med , vol.60 , pp. 443-456
    • Manolio, T.A.1    Collins, F.S.2
  • 114
    • 56049116741 scopus 로고    scopus 로고
    • Common genetic variation and human disease
    • Orr, N.; Chanock, S. Common genetic variation and human disease. Adv. Genet., 2008, 62, 1-32.
    • (2008) Adv. Genet , vol.62 , pp. 1-32
    • Orr, N.1    Chanock, S.2
  • 118
    • 0344407006 scopus 로고    scopus 로고
    • Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins
    • Meissner, M.; Lopato, S.; Gotzmann, J.; Sauermann, G.; Barta, A. Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins. Exp. Cell. Res., 2003, 283, 184-195.
    • (2003) Exp. Cell. Res , vol.283 , pp. 184-195
    • Meissner, M.1    Lopato, S.2    Gotzmann, J.3    Sauermann, G.4    Barta, A.5
  • 121
    • 0035892642 scopus 로고    scopus 로고
    • Assay of superoxide dismutase: Cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide
    • Okado-Matsumoto, A.; Fridovich, I. Assay of superoxide dismutase: cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide. Anal. Biochem., 2001, 298, 337-342.
    • (2001) Anal. Biochem , vol.298 , pp. 337-342
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 124
    • 58349115384 scopus 로고    scopus 로고
    • Screening for replication of genome-wide SNP associations in sporadic ALS
    • Cronin, S.; Tomik, B.; Bradley, D.G.; Slowik, A.; Hardiman, O. Screening for replication of genome-wide SNP associations in sporadic ALS. Eur. J. Hum. Genet., 2009, 17, 213-218.
    • (2009) Eur. J. Hum. Genet , vol.17 , pp. 213-218
    • Cronin, S.1    Tomik, B.2    Bradley, D.G.3    Slowik, A.4    Hardiman, O.5
  • 126
    • 0034689028 scopus 로고    scopus 로고
    • Kinesin superfamily protein 3 (KIF3) motor transports fodrin-associating vesicles important for neurite building
    • Takeda, S.; Yamazaki, H.; Seog, D.H.; Kanai, Y.; Terada, S.; Hirokawa, N. Kinesin superfamily protein 3 (KIF3) motor transports fodrin-associating vesicles important for neurite building. J. Cell Biol., 2000, 148, 1255-1265.
    • (2000) J. Cell Biol , vol.148 , pp. 1255-1265
    • Takeda, S.1    Yamazaki, H.2    Seog, D.H.3    Kanai, Y.4    Terada, S.5    Hirokawa, N.6
  • 129
    • 33750932783 scopus 로고    scopus 로고
    • A role for kinesin-2 in COPI-dependent recycling between the ER and the Golgi complex
    • Stauber, T.; Simpson, J.C.; Pepperkok, R.; Vernos, I. A role for kinesin-2 in COPI-dependent recycling between the ER and the Golgi complex. Curr. Biol., 2006, 16, 2245-2251.
    • (2006) Curr. Biol , vol.16 , pp. 2245-2251
    • Stauber, T.1    Simpson, J.C.2    Pepperkok, R.3    Vernos, I.4
  • 130
    • 0029781733 scopus 로고    scopus 로고
    • Cloning and characterization of KAP3: A novel kinesin superfamily-associated protein of KIF3A/3B
    • Yamazaki, H.; Nakata, T.; Okada, Y.; Hirokawa, N. Cloning and characterization of KAP3: a novel kinesin superfamily-associated protein of KIF3A/3B. Proc. Natl. Acad. Sci. USA, 1996, 93, 8443-8448.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8443-8448
    • Yamazaki, H.1    Nakata, T.2    Okada, Y.3    Hirokawa, N.4
  • 131
    • 0029155982 scopus 로고
    • KIF3A/B: A heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport
    • Yamazaki, H.; Nakata, T.; Okada, Y.; Hirokawa, N. KIF3A/B: a heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport. J. Cell Biol., 1995, 130, 1387-1399.
    • (1995) J. Cell Biol , vol.130 , pp. 1387-1399
    • Yamazaki, H.1    Nakata, T.2    Okada, Y.3    Hirokawa, N.4
  • 132
    • 0033826065 scopus 로고    scopus 로고
    • Differential screening of mutated SOD1 transgenic mice reveals early up-regulation of a fast axonal transport component in spinal cord motor neurons
    • Dupuis, L.; de Tapia, M.; Rene, F.; Lutz-Bucher, B.; Gordon, J.W.; Mercken, L.; Pradier, L.; Loeffler, J.P. Differential screening of mutated SOD1 transgenic mice reveals early up-regulation of a fast axonal transport component in spinal cord motor neurons. Neurobiol. Dis., 2000, 7, 274-285.
    • (2000) Neurobiol. Dis , vol.7 , pp. 274-285
    • Dupuis, L.1    de Tapia, M.2    Rene, F.3    Lutz-Bucher, B.4    Gordon, J.W.5    Mercken, L.6    Pradier, L.7    Loeffler, J.P.8
  • 133
    • 33745945163 scopus 로고    scopus 로고
    • TLS EWS and TAF15: A model for transcriptional integration of gene expression
    • Law, W.J.; Cann, K.L.; Hicks, G.G. TLS, EWS and TAF15: a model for transcriptional integration of gene expression. Brief Funct. Genomic Proteomics, 2006, 5, 8-14.
    • (2006) Brief Funct. Genomic Proteomics , vol.5 , pp. 8-14
    • Law, W.J.1    Cann, K.L.2    Hicks, G.G.3
  • 137
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R.B.; Fasshauer, D.; Jahn, R.; Brunger, A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature, 1998, 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 138
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof, T.C. The synaptic vesicle cycle. Annu. Rev. Neurosci., 2004, 27, 509-547.
    • (2004) Annu. Rev. Neurosci , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 139
  • 140
    • 0037172972 scopus 로고    scopus 로고
    • Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming
    • Varoqueaux, F.; Sigler, A.; Rhee, J.S.; Brose, N.; Enk, C.; Reim, K.; Rosenmund, C. Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming. Proc. Natl. Acad. Sci. USA, 2002, 99, 9037-9042.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9037-9042
    • Varoqueaux, F.1    Sigler, A.2    Rhee, J.S.3    Brose, N.4    Enk, C.5    Reim, K.6    Rosenmund, C.7
  • 141
    • 0033615054 scopus 로고    scopus 로고
    • Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles
    • Augustin, I.; Rosenmund, C.; Sudhof, T.C.; Brose, N. Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles. Nature, 1999, 400, 457-461.
    • (1999) Nature , vol.400 , pp. 457-461
    • Augustin, I.1    Rosenmund, C.2    Sudhof, T.C.3    Brose, N.4
  • 143
    • 0033349884 scopus 로고    scopus 로고
    • UNC-13 is required for synaptic vesicle fusion in C. elegans
    • Richmond, J.E.; Davis, W.S.; Jorgensen, E.M. UNC-13 is required for synaptic vesicle fusion in C. elegans. Nat. Neurosci., 1999, 2, 959-964.
    • (1999) Nat. Neurosci , vol.2 , pp. 959-964
    • Richmond, J.E.1    Davis, W.S.2    Jorgensen, E.M.3
  • 144
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • Richmond, J.E.; Weimer, R.M.; Jorgensen, E.M. An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Nature, 2001, 412, 338-341.
    • (2001) Nature , vol.412 , pp. 338-341
    • Richmond, J.E.1    Weimer, R.M.2    Jorgensen, E.M.3
  • 152
    • 0028001606 scopus 로고
    • Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis
    • Figlewicz, D.A.; Krizus, A.; Martinoli, M.G.; Meininger, V.; Dib, M.; Rouleau, G.A.; Julien, J.P. Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum. Mol. Genet., 1994, 3, 1757-1761.
    • (1994) Hum. Mol. Genet , vol.3 , pp. 1757-1761
    • Figlewicz, D.A.1    Krizus, A.2    Martinoli, M.G.3    Meininger, V.4    Dib, M.5    Rouleau, G.A.6    Julien, J.P.7


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