메뉴 건너뛰기




Volumn 22, Issue 1, 2016, Pages 53-67

The 'Omics' of Amyotrophic Lateral Sclerosis

Author keywords

Amyotrophic lateral sclerosis (ALS); Drug development; Genomics; Motor neuron diseases; Neurodegeneration

Indexed keywords

MICRORNA;

EID: 84952865082     PISSN: 14714914     EISSN: 1471499X     Source Type: Journal    
DOI: 10.1016/j.molmed.2015.11.001     Document Type: Review
Times cited : (34)

References (139)
  • 2
    • 79955824241 scopus 로고    scopus 로고
    • The 'dying-back' phenomenon of motor neurons in ALS
    • Dadon-Nachum M., et al. The 'dying-back' phenomenon of motor neurons in ALS. J. Mol. Neurosci. 2011, 43:470-477.
    • (2011) J. Mol. Neurosci. , vol.43 , pp. 470-477
    • Dadon-Nachum, M.1
  • 3
    • 84866343409 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Ludolph A.C., et al. Amyotrophic lateral sclerosis. Curr. Opin. Neurol. 2012, 25:530-535.
    • (2012) Curr. Opin. Neurol. , vol.25 , pp. 530-535
    • Ludolph, A.C.1
  • 5
    • 84865071988 scopus 로고    scopus 로고
    • Evidence for an oligogenic basis of amyotrophic lateral sclerosis
    • van Blitterswijk M., et al. Evidence for an oligogenic basis of amyotrophic lateral sclerosis. Hum. Mol. Genet. 2012, 21:3776-3784.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 3776-3784
    • van Blitterswijk, M.1
  • 6
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D.R., et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993, 362:59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1
  • 7
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski T.J., et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 2009, 323:1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, T.J.1
  • 8
    • 2442658908 scopus 로고    scopus 로고
    • DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4)
    • Chen Y.Z., et al. DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4). Am. J. Hum. Genet. 2004, 74:1128-1135.
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 1128-1135
    • Chen, Y.Z.1
  • 9
    • 84865235172 scopus 로고    scopus 로고
    • Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis
    • Wu C.H., et al. Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis. Nature 2012, 488:499-503.
    • (2012) Nature , vol.488 , pp. 499-503
    • Wu, C.H.1
  • 10
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • Deng H.X., et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 2011, 477:211-215.
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1
  • 11
    • 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 2013, 495:467-473.
    • (2013) Nature , vol.495 , pp. 467-473
    • Kim, H.J.1
  • 12
    • 85058205678 scopus 로고    scopus 로고
    • HnRNPA2B1 and hnRNPA1 mutations are rare in patients with 'multisystem proteinopathy' and frontotemporal lobar degeneration phenotypes
    • Le Ber I., et al. hnRNPA2B1 and hnRNPA1 mutations are rare in patients with 'multisystem proteinopathy' and frontotemporal lobar degeneration phenotypes. Neurobiol. Aging 2014, 35:934.
    • (2014) Neurobiol. Aging , vol.35 , pp. 934
    • Le Ber, I.1
  • 13
    • 84945749129 scopus 로고    scopus 로고
    • Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways
    • Cirulli E.T., et al. Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways. Science 2015, 347:1436-1441.
    • (2015) Science , vol.347 , pp. 1436-1441
    • Cirulli, E.T.1
  • 14
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T., et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 2006, 351:602-611.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 602-611
    • Arai, T.1
  • 15
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E., et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat. Genet. 2008, 40:572-574.
    • (2008) Nat. Genet. , vol.40 , pp. 572-574
    • Kabashi, E.1
  • 16
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J., et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008, 319:1668-1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1
  • 17
    • 84859512071 scopus 로고    scopus 로고
    • Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis
    • Pokrishevsky E., et al. Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis. PLoS ONE 2012, 7:e35050.
    • (2012) PLoS ONE , vol.7 , pp. e35050
    • Pokrishevsky, E.1
  • 18
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez M., et al. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 2011, 72:245-256.
    • (2011) Neuron , vol.72 , pp. 245-256
    • DeJesus-Hernandez, M.1
  • 19
    • 80054837386 scopus 로고    scopus 로고
    • A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD
    • Renton A.E., et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 2011, 72:257-268.
    • (2011) Neuron , vol.72 , pp. 257-268
    • Renton, A.E.1
  • 20
    • 80054842185 scopus 로고    scopus 로고
    • FTD and ALS: genetic ties that bind
    • Orr H.T. FTD and ALS: genetic ties that bind. Neuron 2011, 72:189-190.
    • (2011) Neuron , vol.72 , pp. 189-190
    • Orr, H.T.1
  • 21
    • 84885808774 scopus 로고    scopus 로고
    • RNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention
    • Donnelly C.J., et al. RNA toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention. Neuron 2013, 80:415-428.
    • (2013) Neuron , vol.80 , pp. 415-428
    • Donnelly, C.J.1
  • 22
    • 84907188956 scopus 로고    scopus 로고
    • C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins
    • Mizielinska S., et al. C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins. Science 2014, 345:1192-1194.
    • (2014) Science , vol.345 , pp. 1192-1194
    • Mizielinska, S.1
  • 23
    • 84907221451 scopus 로고    scopus 로고
    • Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells
    • Kwon I., et al. Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells. Science 2014, 345:1139-1145.
    • (2014) Science , vol.345 , pp. 1139-1145
    • Kwon, I.1
  • 24
    • 84874962380 scopus 로고    scopus 로고
    • The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS
    • Mori K., et al. The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS. Science 2013, 339:1335-1338.
    • (2013) Science , vol.339 , pp. 1335-1338
    • Mori, K.1
  • 25
    • 84920405079 scopus 로고    scopus 로고
    • C9ORF72 hexanucleotide repeat expansions are a frequent cause of Huntington disease phenocopies in the Greek population
    • Koutsis G., et al. C9ORF72 hexanucleotide repeat expansions are a frequent cause of Huntington disease phenocopies in the Greek population. Neurobiol. Aging 2015, 36:547.
    • (2015) Neurobiol. Aging , vol.36 , pp. 547
    • Koutsis, G.1
  • 26
    • 84961289268 scopus 로고    scopus 로고
    • Global investigation and meta-analysis of the C9orf72 (G4C2)n repeat in Parkinson disease
    • Theuns J., et al. Global investigation and meta-analysis of the C9orf72 (G4C2)n repeat in Parkinson disease. Neurology 2014, 83:1906-1913.
    • (2014) Neurology , vol.83 , pp. 1906-1913
    • Theuns, J.1
  • 27
    • 84862909349 scopus 로고    scopus 로고
    • Five years of GWAS discovery
    • Visscher P.M., et al. Five years of GWAS discovery. Am. J. Hum. Genet. 2012, 90:7-24.
    • (2012) Am. J. Hum. Genet. , vol.90 , pp. 7-24
    • Visscher, P.M.1
  • 28
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C., et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 2009, 323:1208-1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1
  • 29
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurin in amyotrophic lateral sclerosis
    • Maruyama H., et al. Mutations of optineurin in amyotrophic lateral sclerosis. Nature 2010, 465:223-226.
    • (2010) Nature , vol.465 , pp. 223-226
    • Maruyama, H.1
  • 30
    • 84859612326 scopus 로고    scopus 로고
    • Mapping of gene expression reveals CYP27A1 as a susceptibility gene for sporadic ALS
    • Diekstra F.P., et al. Mapping of gene expression reveals CYP27A1 as a susceptibility gene for sporadic ALS. PLoS ONE 2012, 7:e35333.
    • (2012) PLoS ONE , vol.7 , pp. e35333
    • Diekstra, F.P.1
  • 31
    • 80052253329 scopus 로고    scopus 로고
    • A functional variant in ZNF512B is associated with susceptibility to amyotrophic lateral sclerosis in Japanese
    • Iida A., et al. A functional variant in ZNF512B is associated with susceptibility to amyotrophic lateral sclerosis in Japanese. Hum. Mol. Genet. 2011, 20:3684-3692.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 3684-3692
    • Iida, A.1
  • 32
    • 84870881192 scopus 로고    scopus 로고
    • ZNF512B gene is a prognostic factor in patients with amyotrophic lateral sclerosis
    • Tetsuka S., et al. ZNF512B gene is a prognostic factor in patients with amyotrophic lateral sclerosis. J. Neurol. Sci. 2013, 324:163-166.
    • (2013) J. Neurol. Sci. , vol.324 , pp. 163-166
    • Tetsuka, S.1
  • 33
    • 77957739219 scopus 로고    scopus 로고
    • A large genome scan for rare CNVs in amyotrophic lateral sclerosis
    • Blauw H.M., et al. A large genome scan for rare CNVs in amyotrophic lateral sclerosis. Hum. Mol. Genet. 2010, 19:4091-4099.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4091-4099
    • Blauw, H.M.1
  • 34
    • 77949529252 scopus 로고    scopus 로고
    • The role of copy number variation in susceptibility to amyotrophic lateral sclerosis: genome-wide association study and comparison with published loci
    • Wain L.V., et al. The role of copy number variation in susceptibility to amyotrophic lateral sclerosis: genome-wide association study and comparison with published loci. PLoS ONE 2009, 4:e8175.
    • (2009) PLoS ONE , vol.4 , pp. e8175
    • Wain, L.V.1
  • 35
    • 80052886551 scopus 로고    scopus 로고
    • Looking for differences in copy number between blood and brain in sporadic amyotrophic lateral sclerosis
    • Pamphlett R., et al. Looking for differences in copy number between blood and brain in sporadic amyotrophic lateral sclerosis. Muscle Nerve 2011, 44:492-498.
    • (2011) Muscle Nerve , vol.44 , pp. 492-498
    • Pamphlett, R.1
  • 36
    • 78649632679 scopus 로고    scopus 로고
    • An estimate of amyotrophic lateral sclerosis heritability using twin data
    • Al-Chalabi A., et al. An estimate of amyotrophic lateral sclerosis heritability using twin data. J. Neurol. Neurosurg. Psychiatry 2010, 81:1324-1326.
    • (2010) J. Neurol. Neurosurg. Psychiatry , vol.81 , pp. 1324-1326
    • Al-Chalabi, A.1
  • 37
    • 79960983213 scopus 로고    scopus 로고
    • Copy number imbalances in blood and hair in monozygotic twins discordant for amyotrophic lateral sclerosis
    • Pamphlett R., Morahan J.M. Copy number imbalances in blood and hair in monozygotic twins discordant for amyotrophic lateral sclerosis. J. Clin. Neurosci. 2011, 18:1231-1234.
    • (2011) J. Clin. Neurosci. , vol.18 , pp. 1231-1234
    • Pamphlett, R.1    Morahan, J.M.2
  • 38
    • 81255143014 scopus 로고    scopus 로고
    • Epigenetic regulation of motor neuron cell death through DNA methylation
    • Chestnut B.A., et al. Epigenetic regulation of motor neuron cell death through DNA methylation. J. Neurosci. 2011, 31:16619-16636.
    • (2011) J. Neurosci. , vol.31 , pp. 16619-16636
    • Chestnut, B.A.1
  • 39
    • 84891533924 scopus 로고    scopus 로고
    • Mitochondrial DNMT3A and DNA methylation in skeletal muscle and CNS of transgenic mouse models of ALS
    • Wong M., et al. Mitochondrial DNMT3A and DNA methylation in skeletal muscle and CNS of transgenic mouse models of ALS. Front. Cell. Neurosci. 2013, 7:279.
    • (2013) Front. Cell. Neurosci. , vol.7 , pp. 279
    • Wong, M.1
  • 40
    • 78650176242 scopus 로고    scopus 로고
    • The association of exposure to lead, mercury, and selenium and the development of amyotrophic lateral sclerosis and the epigenetic implications
    • Callaghan B., et al. The association of exposure to lead, mercury, and selenium and the development of amyotrophic lateral sclerosis and the epigenetic implications. Neurodegener. Dis. 2011, 8:1-8.
    • (2011) Neurodegener. Dis. , vol.8 , pp. 1-8
    • Callaghan, B.1
  • 41
    • 84871536769 scopus 로고    scopus 로고
    • Identification of epigenetically altered genes in sporadic amyotrophic lateral sclerosis
    • Figueroa-Romero C., et al. Identification of epigenetically altered genes in sporadic amyotrophic lateral sclerosis. PLoS ONE 2012, 7:e52672.
    • (2012) PLoS ONE , vol.7 , pp. e52672
    • Figueroa-Romero, C.1
  • 42
    • 84870667053 scopus 로고    scopus 로고
    • Epigenetic histone acetylation and deacetylation mechanisms in experimental models of neurodegenerative disorders
    • Konsoula Z., Barile F.A. Epigenetic histone acetylation and deacetylation mechanisms in experimental models of neurodegenerative disorders. J. Pharmacol. Toxicol. Methods 2012, 66:215-220.
    • (2012) J. Pharmacol. Toxicol. Methods , vol.66 , pp. 215-220
    • Konsoula, Z.1    Barile, F.A.2
  • 43
    • 84890872365 scopus 로고    scopus 로고
    • Investigating cell death mechanisms in amyotrophic lateral sclerosis using transcriptomics
    • Heath P.R., et al. Investigating cell death mechanisms in amyotrophic lateral sclerosis using transcriptomics. Front. Cell. Neurosci. 2013, 7:259.
    • (2013) Front. Cell. Neurosci. , vol.7 , pp. 259
    • Heath, P.R.1
  • 44
    • 84875737451 scopus 로고    scopus 로고
    • Gene expression profile of SOD1-G93A mouse spinal cord, blood and muscle
    • Saris C.G., et al. Gene expression profile of SOD1-G93A mouse spinal cord, blood and muscle. Amyotroph. Lateral Scler. Frontotemporal Degener. 2013, 14:190-198.
    • (2013) Amyotroph. Lateral Scler. Frontotemporal Degener. , vol.14 , pp. 190-198
    • Saris, C.G.1
  • 45
    • 84875740460 scopus 로고    scopus 로고
    • Meta-analysis of gene expression profiling in amyotrophic lateral sclerosis: a comparison between transgenic mouse models and human patients
    • Saris C.G., et al. Meta-analysis of gene expression profiling in amyotrophic lateral sclerosis: a comparison between transgenic mouse models and human patients. Amyotroph. Lateral Scler. Frontotemporal Degener. 2013, 14:177-189.
    • (2013) Amyotroph. Lateral Scler. Frontotemporal Degener. , vol.14 , pp. 177-189
    • Saris, C.G.1
  • 46
    • 84862115153 scopus 로고    scopus 로고
    • Misregulated RNA processing in amyotrophic lateral sclerosis
    • Polymenidou M., et al. Misregulated RNA processing in amyotrophic lateral sclerosis. Brain Res. 2012, 1462:3-15.
    • (2012) Brain Res. , vol.1462 , pp. 3-15
    • Polymenidou, M.1
  • 47
    • 77951766920 scopus 로고    scopus 로고
    • From transcriptome analysis to therapeutic anti-CD40L treatment in the SOD1 model of amyotrophic lateral sclerosis
    • Lincecum J.M., et al. From transcriptome analysis to therapeutic anti-CD40L treatment in the SOD1 model of amyotrophic lateral sclerosis. Nat. Genet. 2010, 42:392-399.
    • (2010) Nat. Genet. , vol.42 , pp. 392-399
    • Lincecum, J.M.1
  • 48
    • 21944454604 scopus 로고    scopus 로고
    • Mutant SOD1 alters the motor neuronal transcriptome: implications for familial ALS
    • Kirby J., et al. Mutant SOD1 alters the motor neuronal transcriptome: implications for familial ALS. Brain 2005, 128:1686-1706.
    • (2005) Brain , vol.128 , pp. 1686-1706
    • Kirby, J.1
  • 49
    • 58149232639 scopus 로고    scopus 로고
    • Nuclear erythroid 2-related factor 2-antioxidative response element signaling pathway in motor cortex and spinal cord in amyotrophic lateral sclerosis
    • Sarlette A., et al. Nuclear erythroid 2-related factor 2-antioxidative response element signaling pathway in motor cortex and spinal cord in amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 2008, 67:1055-1062.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 1055-1062
    • Sarlette, A.1
  • 50
    • 58149379610 scopus 로고    scopus 로고
    • Nrf2 activation in astrocytes protects against neurodegeneration in mouse models of familial amyotrophic lateral sclerosis
    • Vargas M.R., et al. Nrf2 activation in astrocytes protects against neurodegeneration in mouse models of familial amyotrophic lateral sclerosis. J. Neurosci. 2008, 28:13574-13581.
    • (2008) J. Neurosci. , vol.28 , pp. 13574-13581
    • Vargas, M.R.1
  • 51
    • 84900390805 scopus 로고    scopus 로고
    • A novel acylaminoimidazole derivative, WN1316, alleviates disease progression via suppression of glial inflammation in ALS mouse model
    • Tanaka K., et al. A novel acylaminoimidazole derivative, WN1316, alleviates disease progression via suppression of glial inflammation in ALS mouse model. PLoS ONE 2014, 9:e87728.
    • (2014) PLoS ONE , vol.9 , pp. e87728
    • Tanaka, K.1
  • 52
    • 84903948781 scopus 로고    scopus 로고
    • Fishing for causes and cures of motor neuron disorders
    • Patten S.A., et al. Fishing for causes and cures of motor neuron disorders. Dis. Models Mech. 2014, 7:799-809.
    • (2014) Dis. Models Mech. , vol.7 , pp. 799-809
    • Patten, S.A.1
  • 53
    • 84926226703 scopus 로고    scopus 로고
    • A fruitful endeavor: modeling ALS in the fruit fly
    • Casci I., Pandey U.B. A fruitful endeavor: modeling ALS in the fruit fly. Brain Res. 2015, 1607:47-74.
    • (2015) Brain Res. , vol.1607 , pp. 47-74
    • Casci, I.1    Pandey, U.B.2
  • 54
    • 84937139749 scopus 로고    scopus 로고
    • U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish
    • Yu Y., et al. U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish. Nucleic Acids Res. 2015, 43:3208-3218.
    • (2015) Nucleic Acids Res. , vol.43 , pp. 3208-3218
    • Yu, Y.1
  • 55
    • 84952862498 scopus 로고    scopus 로고
    • Fragile X protein mitigates TDP-43 toxicity by remodeling RNA granules and restoring translation
    • Coyne A.N., et al. Fragile X protein mitigates TDP-43 toxicity by remodeling RNA granules and restoring translation. Hum. Mol. Genet. 2015, 24:6886-6898.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 6886-6898
    • Coyne, A.N.1
  • 56
    • 77952336221 scopus 로고    scopus 로고
    • Aberrant microRNA expression in the brains of neurodegenerative diseases: miR-29a decreased in Alzheimer disease brains targets neurone navigator
    • Shioya M., et al. Aberrant microRNA expression in the brains of neurodegenerative diseases: miR-29a decreased in Alzheimer disease brains targets neurone navigator. Neuropathol. Appl. Neurobiol. 2010, 36:320-330.
    • (2010) Neuropathol. Appl. Neurobiol. , vol.36 , pp. 320-330
    • Shioya, M.1
  • 57
    • 84865536102 scopus 로고    scopus 로고
    • A miRNA signature in leukocytes from sporadic amyotrophic lateral sclerosis
    • De Felice B., et al. A miRNA signature in leukocytes from sporadic amyotrophic lateral sclerosis. Gene 2012, 508:35-40.
    • (2012) Gene , vol.508 , pp. 35-40
    • De Felice, B.1
  • 58
    • 84919475780 scopus 로고    scopus 로고
    • MiR-338-3p is over-expressed in blood, CFS, serum and spinal cord from sporadic amyotrophic lateral sclerosis patients
    • De Felice B., et al. miR-338-3p is over-expressed in blood, CFS, serum and spinal cord from sporadic amyotrophic lateral sclerosis patients. Neurogenetics 2014, 15:243-253.
    • (2014) Neurogenetics , vol.15 , pp. 243-253
    • De Felice, B.1
  • 59
    • 84927566123 scopus 로고    scopus 로고
    • Serum microRNAs in patients with genetic amyotrophic lateral sclerosis and pre-manifest mutation carriers
    • Freischmidt A., et al. Serum microRNAs in patients with genetic amyotrophic lateral sclerosis and pre-manifest mutation carriers. Brain 2014, 137:2938-2950.
    • (2014) Brain , vol.137 , pp. 2938-2950
    • Freischmidt, A.1
  • 60
    • 84866491615 scopus 로고    scopus 로고
    • Disruption of skeletal muscle mitochondrial network genes and miRNAs in amyotrophic lateral sclerosis
    • Russell A.P., et al. Disruption of skeletal muscle mitochondrial network genes and miRNAs in amyotrophic lateral sclerosis. Neurobiol. Dis. 2012, 49:107-117.
    • (2012) Neurobiol. Dis. , vol.49 , pp. 107-117
    • Russell, A.P.1
  • 61
    • 84898606538 scopus 로고    scopus 로고
    • Analysis of novel NEFL mRNA targeting microRNAs in amyotrophic lateral sclerosis
    • Ishtiaq M., et al. Analysis of novel NEFL mRNA targeting microRNAs in amyotrophic lateral sclerosis. PLoS ONE 2014, 9:e85653.
    • (2014) PLoS ONE , vol.9 , pp. e85653
    • Ishtiaq, M.1
  • 62
    • 72149131804 scopus 로고    scopus 로고
    • MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice
    • Williams A.H., et al. MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice. Science 2009, 326:1549-1554.
    • (2009) Science , vol.326 , pp. 1549-1554
    • Williams, A.H.1
  • 63
    • 77951700391 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 can affect selected microRNA levels
    • Buratti E., et al. Nuclear factor TDP-43 can affect selected microRNA levels. FEBS J. 2010, 277:2268-2281.
    • (2010) FEBS J. , vol.277 , pp. 2268-2281
    • Buratti, E.1
  • 64
    • 84857772495 scopus 로고    scopus 로고
    • TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes
    • Kawahara Y., Mieda-Sato A. TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:3347-3352.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 3347-3352
    • Kawahara, Y.1    Mieda-Sato, A.2
  • 65
    • 84901006597 scopus 로고    scopus 로고
    • The RNA-binding protein TDP-43 selectively disrupts microRNA-1/206 incorporation into the RNA-induced silencing complex
    • King I.N., et al. The RNA-binding protein TDP-43 selectively disrupts microRNA-1/206 incorporation into the RNA-induced silencing complex. J. Biol. Chem. 2014, 289:14263-14271.
    • (2014) J. Biol. Chem. , vol.289 , pp. 14263-14271
    • King, I.N.1
  • 66
    • 84871002507 scopus 로고    scopus 로고
    • FUS stimulates microRNA biogenesis by facilitating co-transcriptional Drosha recruitment
    • Morlando M., et al. FUS stimulates microRNA biogenesis by facilitating co-transcriptional Drosha recruitment. EMBO J. 2012, 31:4502-4510.
    • (2012) EMBO J. , vol.31 , pp. 4502-4510
    • Morlando, M.1
  • 67
    • 84904195219 scopus 로고    scopus 로고
    • An ALS-associated mutation in the FUS 3'-UTR disrupts a microRNA-FUS regulatory circuitry
    • Dini Modigliani S., et al. An ALS-associated mutation in the FUS 3'-UTR disrupts a microRNA-FUS regulatory circuitry. Nat. Commun. 2014, 5:4335.
    • (2014) Nat. Commun. , vol.5 , pp. 4335
    • Dini Modigliani, S.1
  • 68
    • 84947284577 scopus 로고    scopus 로고
    • Plasma exosomal miRNAs in persons with and without Alzheimer disease: altered expression and prospects for biomarkers
    • Lugli G., et al. Plasma exosomal miRNAs in persons with and without Alzheimer disease: altered expression and prospects for biomarkers. PLoS ONE 2015, 10:e0139233.
    • (2015) PLoS ONE , vol.10 , pp. e0139233
    • Lugli, G.1
  • 69
    • 84867582241 scopus 로고    scopus 로고
    • Interrogation of brain miRNA and mRNA expression profiles reveals a molecular regulatory network that is perturbed by mutant huntingtin
    • Jin J., et al. Interrogation of brain miRNA and mRNA expression profiles reveals a molecular regulatory network that is perturbed by mutant huntingtin. J. Neurochem. 2012, 123:477-490.
    • (2012) J. Neurochem. , vol.123 , pp. 477-490
    • Jin, J.1
  • 70
    • 84901490002 scopus 로고    scopus 로고
    • Alterations in muscle proteome of patients diagnosed with amyotrophic lateral sclerosis
    • Elf K., et al. Alterations in muscle proteome of patients diagnosed with amyotrophic lateral sclerosis. J. Proteomics 2014, 108:55-64.
    • (2014) J. Proteomics , vol.108 , pp. 55-64
    • Elf, K.1
  • 71
    • 84898716762 scopus 로고    scopus 로고
    • Human SOD1-G93A specific distribution evidenced in murine brain of a transgenic model for amyotrophic lateral sclerosis by MALDI imaging mass spectrometry
    • Acquadro E., et al. Human SOD1-G93A specific distribution evidenced in murine brain of a transgenic model for amyotrophic lateral sclerosis by MALDI imaging mass spectrometry. J. Proteome Res. 2014, 13:1800-1809.
    • (2014) J. Proteome Res. , vol.13 , pp. 1800-1809
    • Acquadro, E.1
  • 72
    • 33845979055 scopus 로고    scopus 로고
    • Proteomic analysis of spinal cord of presymptomatic amyotrophic lateral sclerosis G93A SOD1 mouse
    • Massignan T., et al. Proteomic analysis of spinal cord of presymptomatic amyotrophic lateral sclerosis G93A SOD1 mouse. Biochem. Biophys. Res. Commun. 2007, 353:719-725.
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 719-725
    • Massignan, T.1
  • 73
    • 80053209608 scopus 로고    scopus 로고
    • Apoptosis-inducing factor and cyclophilin A cotranslocate to the motor neuronal nuclei in amyotrophic lateral sclerosis model mice
    • Tanaka H., et al. Apoptosis-inducing factor and cyclophilin A cotranslocate to the motor neuronal nuclei in amyotrophic lateral sclerosis model mice. CNS Neurosci. Ther. 2011, 17:294-304.
    • (2011) CNS Neurosci. Ther. , vol.17 , pp. 294-304
    • Tanaka, H.1
  • 74
    • 80053615914 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis multiprotein biomarkers in peripheral blood mononuclear cells
    • Nardo G., et al. Amyotrophic lateral sclerosis multiprotein biomarkers in peripheral blood mononuclear cells. PLoS ONE 2011, 6:e25545.
    • (2011) PLoS ONE , vol.6 , pp. e25545
    • Nardo, G.1
  • 75
    • 84925307620 scopus 로고    scopus 로고
    • Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport
    • Stalekar M., et al. Proteomic analyses reveal that loss of TDP-43 affects RNA processing and intracellular transport. Neuroscience 2015, 293:157-170.
    • (2015) Neuroscience , vol.293 , pp. 157-170
    • Stalekar, M.1
  • 76
    • 38749113921 scopus 로고    scopus 로고
    • Gene profiling of skeletal muscle in an amyotrophic lateral sclerosis mouse model
    • Gonzalez de Aguilar J.L., et al. Gene profiling of skeletal muscle in an amyotrophic lateral sclerosis mouse model. Physiol. Genomics 2008, 32:207-218.
    • (2008) Physiol. Genomics , vol.32 , pp. 207-218
    • Gonzalez de Aguilar, J.L.1
  • 77
    • 77957372670 scopus 로고    scopus 로고
    • Galectin-3 is a candidate biomarker for amyotrophic lateral sclerosis: discovery by a proteomics approach
    • Zhou J.Y., et al. Galectin-3 is a candidate biomarker for amyotrophic lateral sclerosis: discovery by a proteomics approach. J. Proteome Res. 2010, 9:5133-5141.
    • (2010) J. Proteome Res. , vol.9 , pp. 5133-5141
    • Zhou, J.Y.1
  • 78
    • 84888399981 scopus 로고    scopus 로고
    • Deletion of galectin-3 exacerbates microglial activation and accelerates disease progression and demise in a SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Lerman B.J., et al. Deletion of galectin-3 exacerbates microglial activation and accelerates disease progression and demise in a SOD1(G93A) mouse model of amyotrophic lateral sclerosis. Brain Behav. 2012, 2:563-575.
    • (2012) Brain Behav. , vol.2 , pp. 563-575
    • Lerman, B.J.1
  • 79
    • 84861603970 scopus 로고    scopus 로고
    • Glycans in sera of amyotrophic lateral sclerosis patients and their role in killing neuronal cells
    • Edri-Brami M., et al. Glycans in sera of amyotrophic lateral sclerosis patients and their role in killing neuronal cells. PLoS ONE 2012, 7:e35772.
    • (2012) PLoS ONE , vol.7 , pp. e35772
    • Edri-Brami, M.1
  • 80
    • 84929577531 scopus 로고    scopus 로고
    • Plasma profiling reveals three proteins associated to amyotrophic lateral sclerosis
    • Haggmark A., et al. Plasma profiling reveals three proteins associated to amyotrophic lateral sclerosis. Ann. Clin. Transl. Neurol. 2014, 1:544-553.
    • (2014) Ann. Clin. Transl. Neurol. , vol.1 , pp. 544-553
    • Haggmark, A.1
  • 81
    • 84908125781 scopus 로고    scopus 로고
    • Phosphoneurofilament heavy chain and N-glycomics from the cerebrospinal fluid in amyotrophic lateral sclerosis
    • Goncalves M., et al. Phosphoneurofilament heavy chain and N-glycomics from the cerebrospinal fluid in amyotrophic lateral sclerosis. Clin. Chim. Acta 2015, 438:342-349.
    • (2015) Clin. Chim. Acta , vol.438 , pp. 342-349
    • Goncalves, M.1
  • 82
    • 0029006191 scopus 로고
    • Preliminary results of proton magnetic resonance spectroscopy in motor neurone disease (amytrophic lateral sclerosis)
    • Jones A.P., et al. Preliminary results of proton magnetic resonance spectroscopy in motor neurone disease (amytrophic lateral sclerosis). J. Neurol. Sci. 1995, 129:85-89.
    • (1995) J. Neurol. Sci. , vol.129 , pp. 85-89
    • Jones, A.P.1
  • 83
    • 0031003973 scopus 로고    scopus 로고
    • Quantification of brain metabolites in amyotrophic lateral sclerosis by localized proton magnetic resonance spectroscopy
    • Gredal O., et al. Quantification of brain metabolites in amyotrophic lateral sclerosis by localized proton magnetic resonance spectroscopy. Neurol. 1997, 48:878-881.
    • (1997) Neurol. , vol.48 , pp. 878-881
    • Gredal, O.1
  • 84
    • 0031930760 scopus 로고    scopus 로고
    • Estimation of brainstem neuronal loss in amyotrophic lateral sclerosis with in vivo proton magnetic resonance spectroscopy
    • Cwik V.A., et al. Estimation of brainstem neuronal loss in amyotrophic lateral sclerosis with in vivo proton magnetic resonance spectroscopy. Neurology 1998, 50:72-77.
    • (1998) Neurology , vol.50 , pp. 72-77
    • Cwik, V.A.1
  • 85
    • 0031992489 scopus 로고    scopus 로고
    • Quantification of brain metabolites in ALS by localized proton magnetic spectroscopy
    • Ikeda K., et al. Quantification of brain metabolites in ALS by localized proton magnetic spectroscopy. Neurology 1998, 50:576-577.
    • (1998) Neurology , vol.50 , pp. 576-577
    • Ikeda, K.1
  • 86
    • 79955769734 scopus 로고    scopus 로고
    • Magnetic resonance spectroscopy of the cervical cord in amyotrophic lateral sclerosis
    • Carew J.D., et al. Magnetic resonance spectroscopy of the cervical cord in amyotrophic lateral sclerosis. Amyotroph. Lateral Scler. 2011, 12:185-191.
    • (2011) Amyotroph. Lateral Scler. , vol.12 , pp. 185-191
    • Carew, J.D.1
  • 87
    • 84871278626 scopus 로고    scopus 로고
    • 1H-magnetic resonance spectroscopy and clinoco-electromyographic profile in amyotrophic lateral sclerosis
    • 1H-magnetic resonance spectroscopy and clinoco-electromyographic profile in amyotrophic lateral sclerosis. Muscle Nerve 2013, 47:61-67.
    • (2013) Muscle Nerve , vol.47 , pp. 61-67
    • Ikeda, K.1
  • 88
    • 82255179751 scopus 로고    scopus 로고
    • Presymptomatic spinal cord neurometabolic findings in SOD1-positive people at risk for familial ALS
    • Carew J.D., et al. Presymptomatic spinal cord neurometabolic findings in SOD1-positive people at risk for familial ALS. Neurology 2011, 77:1370-1375.
    • (2011) Neurology , vol.77 , pp. 1370-1375
    • Carew, J.D.1
  • 89
    • 0035871761 scopus 로고    scopus 로고
    • Magnetic resonance spectroscopy of the human brain
    • Ross B., Bluml S. Magnetic resonance spectroscopy of the human brain. Anat. Rec. 2001, 265:54-84.
    • (2001) Anat. Rec. , vol.265 , pp. 54-84
    • Ross, B.1    Bluml, S.2
  • 90
    • 20344385568 scopus 로고    scopus 로고
    • Metabolomic analysis and signatures in motor neuron disease
    • Rozen S., et al. Metabolomic analysis and signatures in motor neuron disease. Metabolomics 2005, 1:101-108.
    • (2005) Metabolomics , vol.1 , pp. 101-108
    • Rozen, S.1
  • 91
    • 84855398606 scopus 로고    scopus 로고
    • Biochemical alterations associated with ALS
    • Lawton K.A., et al. Biochemical alterations associated with ALS. Amyotroph. Lateral Scler. 2012, 13:110-118.
    • (2012) Amyotroph. Lateral Scler. , vol.13 , pp. 110-118
    • Lawton, K.A.1
  • 92
    • 38149038841 scopus 로고    scopus 로고
    • Elevated plasma homocysteine levels in patients with amyotrophic lateral sclerosis
    • Zoccolella S., et al. Elevated plasma homocysteine levels in patients with amyotrophic lateral sclerosis. Neurol. 2008, 70:222-225.
    • (2008) Neurol. , vol.70 , pp. 222-225
    • Zoccolella, S.1
  • 93
    • 80053892763 scopus 로고    scopus 로고
    • Serum N-acetylaspartate level in amyotrophic lateral sclerosis
    • Simone I.L., et al. Serum N-acetylaspartate level in amyotrophic lateral sclerosis. Arch. Neurol. 2011, 68:1308-1312.
    • (2011) Arch. Neurol. , vol.68 , pp. 1308-1312
    • Simone, I.L.1
  • 94
    • 79953781989 scopus 로고    scopus 로고
    • An exploratory study of serum urate levels in patients with amyotrophic lateral sclerosis
    • Zoccolella S., et al. An exploratory study of serum urate levels in patients with amyotrophic lateral sclerosis. J. Neurol. 2011, 258:238-243.
    • (2011) J. Neurol. , vol.258 , pp. 238-243
    • Zoccolella, S.1
  • 95
    • 84863462965 scopus 로고    scopus 로고
    • CSF markers in amyotrophic lateral sclerosis
    • Tarasiuk J., et al. CSF markers in amyotrophic lateral sclerosis. J. Neural Transm. 2012, 119:747-757.
    • (2012) J. Neural Transm. , vol.119 , pp. 747-757
    • Tarasiuk, J.1
  • 96
    • 78149444882 scopus 로고    scopus 로고
    • 1H-NMR-based metabolomic profiling of CSF in early amyotrophic lateral sclerosis
    • 1H-NMR-based metabolomic profiling of CSF in early amyotrophic lateral sclerosis. PLoS ONE 2010, 5:e13223.
    • (2010) PLoS ONE , vol.5 , pp. e13223
    • Blasco, H.1
  • 97
    • 79953717156 scopus 로고    scopus 로고
    • Disease-related changes in the cerebrospinal fluid metabolome in amyotrophic lateral sclerosis detected by GC/TOFMS
    • Wuolikainen A., et al. Disease-related changes in the cerebrospinal fluid metabolome in amyotrophic lateral sclerosis detected by GC/TOFMS. PLoS ONE 2011, 6:e17947.
    • (2011) PLoS ONE , vol.6 , pp. e17947
    • Wuolikainen, A.1
  • 98
    • 84858280794 scopus 로고    scopus 로고
    • ALS patients with mutations in the SOD1 gene have an unique metabolomic profile in the cerebrospinal fluid compared with ALS patients without mutations
    • Wuolikainen A., et al. ALS patients with mutations in the SOD1 gene have an unique metabolomic profile in the cerebrospinal fluid compared with ALS patients without mutations. Mol. Gen. Metabol. 2012, 105:472-478.
    • (2012) Mol. Gen. Metabol. , vol.105 , pp. 472-478
    • Wuolikainen, A.1
  • 99
    • 84899124212 scopus 로고    scopus 로고
    • The metabolic signature of C9ORF72-related ALS: FDG PET comparison with nonmutated patients
    • Cistaro A., et al. The metabolic signature of C9ORF72-related ALS: FDG PET comparison with nonmutated patients. Eur. J. Nucl. Med. Mol. Imaging 2014, 41:844-852.
    • (2014) Eur. J. Nucl. Med. Mol. Imaging , vol.41 , pp. 844-852
    • Cistaro, A.1
  • 100
    • 84952862320 scopus 로고    scopus 로고
    • Impact of the C9Orf72 expansion on brain glucose metabolism in ALS patients
    • Verschueren J., et al. Impact of the C9Orf72 expansion on brain glucose metabolism in ALS patients. J. Nucl. Med. 2013, 54:155.
    • (2013) J. Nucl. Med. , vol.54 , pp. 155
    • Verschueren, J.1
  • 101
    • 0035051503 scopus 로고    scopus 로고
    • Increases in cortical glutamate concentrations in transgenic amyotrophic lateral sclerosis mice are attenuated by creatine supplementation
    • Andreassen O.A., et al. Increases in cortical glutamate concentrations in transgenic amyotrophic lateral sclerosis mice are attenuated by creatine supplementation. J. Neurochem. 2001, 77:383-390.
    • (2001) J. Neurochem. , vol.77 , pp. 383-390
    • Andreassen, O.A.1
  • 102
    • 0043095290 scopus 로고    scopus 로고
    • Skeletal muscle properties in a transgenic mouse model for amyotrophic lateral sclerosis: effects of creatine treatment
    • Derave W., et al. Skeletal muscle properties in a transgenic mouse model for amyotrophic lateral sclerosis: effects of creatine treatment. Neurobiol. Dis. 2003, 13:264-272.
    • (2003) Neurobiol. Dis. , vol.13 , pp. 264-272
    • Derave, W.1
  • 103
    • 34047245280 scopus 로고    scopus 로고
    • Metabolic progression markers of neurodegeneration in the transgenic G93A-SOD1 mouse model of amyotrophic lateral sclerosis
    • Niessen H.G., et al. Metabolic progression markers of neurodegeneration in the transgenic G93A-SOD1 mouse model of amyotrophic lateral sclerosis. Eur. J. Neurosci. 2007, 25:1669-1677.
    • (2007) Eur. J. Neurosci. , vol.25 , pp. 1669-1677
    • Niessen, H.G.1
  • 104
    • 71249123229 scopus 로고    scopus 로고
    • Magnetic resonance spectroscopy of regional brain metabolite markers in FALS mice and the effects of dietary creatine supplementation
    • Choi J.K., et al. Magnetic resonance spectroscopy of regional brain metabolite markers in FALS mice and the effects of dietary creatine supplementation. Eur. J. Neurosci. 2009, 30:2143-2150.
    • (2009) Eur. J. Neurosci. , vol.30 , pp. 2143-2150
    • Choi, J.K.1
  • 105
    • 84906343045 scopus 로고    scopus 로고
    • Plasma metabolomic biomarker panel to distinguish patients with amyotrophic lateral sclerosis from disease mimics
    • Lawton K.A., et al. Plasma metabolomic biomarker panel to distinguish patients with amyotrophic lateral sclerosis from disease mimics. Amyotroph. Lateral Scler. Frontotemporal Degener. 2014, 15:362-370.
    • (2014) Amyotroph. Lateral Scler. Frontotemporal Degener. , vol.15 , pp. 362-370
    • Lawton, K.A.1
  • 106
    • 70249096265 scopus 로고    scopus 로고
    • Optimization of procedures for collecting and storing of CSF for studying the metabolome in ALS
    • Wuolikainen A., et al. Optimization of procedures for collecting and storing of CSF for studying the metabolome in ALS. Amyotroph. Lateral Scler. 2009, 10:229-236.
    • (2009) Amyotroph. Lateral Scler. , vol.10 , pp. 229-236
    • Wuolikainen, A.1
  • 107
    • 79551493048 scopus 로고    scopus 로고
    • Conditioned media from cell lines: a complementary model to clinical specimens for the discovery of disease-specific biomarkers
    • Dowling P., Clynes M. Conditioned media from cell lines: a complementary model to clinical specimens for the discovery of disease-specific biomarkers. Proteomics 2011, 11:794-804.
    • (2011) Proteomics , vol.11 , pp. 794-804
    • Dowling, P.1    Clynes, M.2
  • 108
    • 33744798774 scopus 로고    scopus 로고
    • Onset and progression in inherited ALS determined by motor neurons and microglia
    • Boillee S., et al. Onset and progression in inherited ALS determined by motor neurons and microglia. Science 2006, 312:1389-1392.
    • (2006) Science , vol.312 , pp. 1389-1392
    • Boillee, S.1
  • 109
    • 74049164709 scopus 로고    scopus 로고
    • Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond
    • Ilieva H., et al. Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J. Cell Biol. 2009, 187:761-772.
    • (2009) J. Cell Biol. , vol.187 , pp. 761-772
    • Ilieva, H.1
  • 110
    • 80052783545 scopus 로고    scopus 로고
    • Astrocytes from familial and sporadic ALSpatients are toxic to motor neurons
    • Haidet-Phillips A.M., et al. Astrocytes from familial and sporadic ALSpatients are toxic to motor neurons. Nat. Biotechnol. 2011, 29:824-828.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 824-828
    • Haidet-Phillips, A.M.1
  • 111
    • 77952544821 scopus 로고    scopus 로고
    • Mutant superoxide dismutase 1 overexpression in NSC-34 cells: effect of trehalose on aggregation, TDP-43 localization and levels of co-expressed glycoproteins
    • Gomes C., et al. Mutant superoxide dismutase 1 overexpression in NSC-34 cells: effect of trehalose on aggregation, TDP-43 localization and levels of co-expressed glycoproteins. Neurosci. Lett. 2010, 475:145-149.
    • (2010) Neurosci. Lett. , vol.475 , pp. 145-149
    • Gomes, C.1
  • 112
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani M., et al. 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
  • 113
    • 84920768238 scopus 로고    scopus 로고
    • Exosome-dependent and independent mechanisms are involved in prion-like transmission of propagated Cu/Zn superoxide dismutase misfolding
    • Grad L.I., et al. Exosome-dependent and independent mechanisms are involved in prion-like transmission of propagated Cu/Zn superoxide dismutase misfolding. Prion 2014, 8:331-335.
    • (2014) Prion , vol.8 , pp. 331-335
    • Grad, L.I.1
  • 114
    • 77957285745 scopus 로고    scopus 로고
    • TDP-43 proteinopathy and motor neuron disease in chronic traumatic encephalopathy
    • McKee A.C., et al. TDP-43 proteinopathy and motor neuron disease in chronic traumatic encephalopathy. J. Neuropathol. Exp. Neurol. 2010, 69:918-929.
    • (2010) J. Neuropathol. Exp. Neurol. , vol.69 , pp. 918-929
    • McKee, A.C.1
  • 115
    • 84860381354 scopus 로고    scopus 로고
    • TDP-43 identified from a genome wide RNAi screen for SOD1 regulators
    • Somalinga B.R., et al. TDP-43 identified from a genome wide RNAi screen for SOD1 regulators. PLoS One 2012, 7:e35818.
    • (2012) PLoS One , vol.7 , pp. e35818
    • Somalinga, B.R.1
  • 116
    • 80052374038 scopus 로고    scopus 로고
    • FUS and TARDBP but not SOD1 interact in genetic models of amyotrophic lateral sclerosis
    • Kabashi E., et al. FUS and TARDBP but not SOD1 interact in genetic models of amyotrophic lateral sclerosis. PLoS genetics 2011, 7:e1002214.
    • (2011) PLoS genetics , vol.7 , pp. e1002214
    • Kabashi, E.1
  • 117
    • 73949134014 scopus 로고    scopus 로고
    • Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)
    • Volkening K., et al. Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS). Brain Res. 2009, 1305:168-182.
    • (2009) Brain Res. , vol.1305 , pp. 168-182
    • Volkening, K.1
  • 118
    • 78649629032 scopus 로고    scopus 로고
    • TDP-43 physically interacts with amyotrophic lateral sclerosis-linked mutant CuZn superoxide dismutase
    • Higashi S., et al. TDP-43 physically interacts with amyotrophic lateral sclerosis-linked mutant CuZn superoxide dismutase. Neurochem. Int. 2010, 57:906-913.
    • (2010) Neurochem. Int. , vol.57 , pp. 906-913
    • Higashi, S.1
  • 119
    • 84940006895 scopus 로고    scopus 로고
    • Protective and toxic neuroinflammation in amyotrophic lateral sclerosis
    • Hooten K.G., et al. Protective and toxic neuroinflammation in amyotrophic lateral sclerosis. Neurotherapeutics 2015, 12:364-375.
    • (2015) Neurotherapeutics , vol.12 , pp. 364-375
    • Hooten, K.G.1
  • 120
    • 33847787621 scopus 로고    scopus 로고
    • Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis
    • Urushitani M., et al. Therapeutic effects of immunization with mutant superoxide dismutase in mice models of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:2495-2500.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 2495-2500
    • Urushitani, M.1
  • 121
    • 77957946030 scopus 로고    scopus 로고
    • Induction of protective immunity by vaccination with wild-type apo superoxide dismutase 1 in mutant SOD1 transgenic mice
    • Takeuchi S., et al. Induction of protective immunity by vaccination with wild-type apo superoxide dismutase 1 in mutant SOD1 transgenic mice. J. Neuropathol. Exp. Neurol. 2010, 69:1044-1056.
    • (2010) J. Neuropathol. Exp. Neurol. , vol.69 , pp. 1044-1056
    • Takeuchi, S.1
  • 122
    • 34249980373 scopus 로고    scopus 로고
    • An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS
    • Rakhit R., et al. An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS. Nat. Med. 2007, 13:754-759.
    • (2007) Nat. Med. , vol.13 , pp. 754-759
    • Rakhit, R.1
  • 123
    • 84862854446 scopus 로고    scopus 로고
    • Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis
    • Liu H.N., et al. Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis. J. Neurosci. 2012, 32:8791-8799.
    • (2012) J. Neurosci. , vol.32 , pp. 8791-8799
    • Liu, H.N.1
  • 124
    • 77953503937 scopus 로고    scopus 로고
    • Riluzole, neuroprotection and amyotrophic lateral sclerosis
    • Cheah B.C., et al. Riluzole, neuroprotection and amyotrophic lateral sclerosis. Curr. Med. Chem. 2010, 17:1199-1942.
    • (2010) Curr. Med. Chem. , vol.17 , pp. 1199-1942
    • Cheah, B.C.1
  • 125
    • 34250208597 scopus 로고    scopus 로고
    • Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND)
    • Miller R.G., et al. Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND). Cochrane Database Syst. Rev. 2007, 1:CD001447.
    • (2007) Cochrane Database Syst. Rev. , vol.1 , pp. CD001447
    • Miller, R.G.1
  • 126
    • 78649352832 scopus 로고    scopus 로고
    • Mesenchymal stem cells for the treatment of neurodegenerative disease
    • Joyce N., et al. Mesenchymal stem cells for the treatment of neurodegenerative disease. Reg. Med. 2010, 5:933-946.
    • (2010) Reg. Med. , vol.5 , pp. 933-946
    • Joyce, N.1
  • 127
    • 83755188611 scopus 로고    scopus 로고
    • Mesenchymal stromal cell transplantation in amyotrophic lateral sclerosis: a long-term safety study
    • Mazzini L., et al. Mesenchymal stromal cell transplantation in amyotrophic lateral sclerosis: a long-term safety study. Cytotherapy 2012, 14:56-60.
    • (2012) Cytotherapy , vol.14 , pp. 56-60
    • Mazzini, L.1
  • 128
    • 84868489394 scopus 로고    scopus 로고
    • Intravenous mesenchymal stem cells improve survival and motor function in experimental amyotrophic lateral sclerosis
    • Uccelli A., et al. Intravenous mesenchymal stem cells improve survival and motor function in experimental amyotrophic lateral sclerosis. Mol. Med. 2012, 18:794-804.
    • (2012) Mol. Med. , vol.18 , pp. 794-804
    • Uccelli, A.1
  • 129
    • 84862685373 scopus 로고    scopus 로고
    • Intracerebroventricular injection of encapsulated human mesenchymal cells producing glucagon-like peptide 1 prolongs survival in a mouse model of ALS
    • Knippenberg S., et al. Intracerebroventricular injection of encapsulated human mesenchymal cells producing glucagon-like peptide 1 prolongs survival in a mouse model of ALS. PLoS ONE 2012, 7:e36857.
    • (2012) PLoS ONE , vol.7 , pp. e36857
    • Knippenberg, S.1
  • 130
    • 8544249121 scopus 로고    scopus 로고
    • Diffusion tensor MRI as a diagnostic tool of upper motor neuron involvement in amyotrophic lateral sclerosis
    • Hong Y.H., et al. Diffusion tensor MRI as a diagnostic tool of upper motor neuron involvement in amyotrophic lateral sclerosis. J. Neurol. Sci. 2004, 227:73-78.
    • (2004) J. Neurol. Sci. , vol.227 , pp. 73-78
    • Hong, Y.H.1
  • 131
    • 0742323507 scopus 로고    scopus 로고
    • Diffusion tensor MRI of early upper motor neuron involvement in amyotrophic lateral sclerosis
    • Sach M., et al. Diffusion tensor MRI of early upper motor neuron involvement in amyotrophic lateral sclerosis. Brain 2004, 127:340-350.
    • (2004) Brain , vol.127 , pp. 340-350
    • Sach, M.1
  • 132
    • 8744291752 scopus 로고    scopus 로고
    • Combined MR spectroscopic imaging and diffusion tensor MRI visualizes corticospinal tract degeneration in amyotrophic lateral sclerosis
    • Yin H., et al. Combined MR spectroscopic imaging and diffusion tensor MRI visualizes corticospinal tract degeneration in amyotrophic lateral sclerosis. J. Neurol. 2004, 251:1249-1254.
    • (2004) J. Neurol. , vol.251 , pp. 1249-1254
    • Yin, H.1
  • 133
    • 58249084223 scopus 로고    scopus 로고
    • A longitudinal diffusion tensor MRI study of the cervical cord and brain in amyotrophic lateral sclerosis patients
    • Agosta F., et al. A longitudinal diffusion tensor MRI study of the cervical cord and brain in amyotrophic lateral sclerosis patients. J. Neurol. Neurosurg. Psychiatry 2009, 80:53-55.
    • (2009) J. Neurol. Neurosurg. Psychiatry , vol.80 , pp. 53-55
    • Agosta, F.1
  • 134
    • 77955715842 scopus 로고    scopus 로고
    • Utility of axial and radial diffusivity from diffusion tensor MRI as markers of neurodegeneration in amyotrophic lateral sclerosis
    • Metwalli N.S., et al. Utility of axial and radial diffusivity from diffusion tensor MRI as markers of neurodegeneration in amyotrophic lateral sclerosis. Brain Res. 2010, 1348:156-164.
    • (2010) Brain Res. , vol.1348 , pp. 156-164
    • Metwalli, N.S.1
  • 135
    • 78649239995 scopus 로고    scopus 로고
    • Advances in the application of MRI to amyotrophic lateral sclerosis
    • Turner M.R., Modo M. Advances in the application of MRI to amyotrophic lateral sclerosis. Exp. Opin. Med. Diagn. 2010, 4:483-496.
    • (2010) Exp. Opin. Med. Diagn. , vol.4 , pp. 483-496
    • Turner, M.R.1    Modo, M.2
  • 136
    • 34247181189 scopus 로고    scopus 로고
    • Diffusion anisotropy of the cervical cord is strictly associated with disability in amyotrophic lateral sclerosis
    • Valsasina P., et al. Diffusion anisotropy of the cervical cord is strictly associated with disability in amyotrophic lateral sclerosis. J. Neurol. Neurosurg. Psychiatry 2007, 78:480-484.
    • (2007) J. Neurol. Neurosurg. Psychiatry , vol.78 , pp. 480-484
    • Valsasina, P.1
  • 137
    • 84873341544 scopus 로고    scopus 로고
    • Diffusion tensor imaging of the mouse brainstem and cervical spinal cord
    • Kim J.H., Song S.K. Diffusion tensor imaging of the mouse brainstem and cervical spinal cord. Nat. Protocol. 2013, 8:409-417.
    • (2013) Nat. Protocol. , vol.8 , pp. 409-417
    • Kim, J.H.1    Song, S.K.2
  • 138
    • 77958119924 scopus 로고    scopus 로고
    • Evaluation of corticospinal tract impairment in the brain of patients with amyotrophic lateral sclerosis by using diffusion tensor imaging acquisition schemes with different numbers of diffusion-weighting directions
    • Cosottini M., et al. Evaluation of corticospinal tract impairment in the brain of patients with amyotrophic lateral sclerosis by using diffusion tensor imaging acquisition schemes with different numbers of diffusion-weighting directions. J. Comp. Assist. Tomography 2010, 34:746-750.
    • (2010) J. Comp. Assist. Tomography , vol.34 , pp. 746-750
    • Cosottini, M.1
  • 139
    • 84890079933 scopus 로고    scopus 로고
    • Brain iron MRI: a biomarker for amyotrophic lateral sclerosis
    • Ignjatovic A., et al. Brain iron MRI: a biomarker for amyotrophic lateral sclerosis. J. Magn. Res. Imaging 2013, 38:1472-1479.
    • (2013) J. Magn. Res. Imaging , vol.38 , pp. 1472-1479
    • Ignjatovic, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.