메뉴 건너뛰기




Volumn 1648, Issue , 2016, Pages 633-649

Protein folding alterations in amyotrophic lateral sclerosis

Author keywords

Amyotrophic lateral sclerosis; C9ORF72; Disulphide bonds; ER stress; FUS; Protein disulphide isomerase (PDI); Protein misfolding; Superoxide dismutase 1 (SOD1); TDP 43

Indexed keywords

CELL PROTEIN; CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; FUSED IN SARCOMA PROTEIN; PROTEASOME; PROTEIN CHROMOSOME 9 OPEN READING FRAME 72; TAR DNA BINDING PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; FUS PROTEIN, HUMAN; GUANINE NUCLEOTIDE EXCHANGE C9ORF72; RNA BINDING PROTEIN FUS; SOD1 PROTEIN, HUMAN; TDP-43 PROTEIN, HUMAN;

EID: 84975746049     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2016.04.010     Document Type: Review
Times cited : (81)

References (357)
  • 2
    • 77955203926 scopus 로고    scopus 로고
    • Quantifying colocalization by correlation: the Pearson correlation coefficient is superior to the Mander's overlap coefficient
    • Adler, J., Parmryd, I., Quantifying colocalization by correlation: the Pearson correlation coefficient is superior to the Mander's overlap coefficient. Cytom. Part A 77 (2010), 733–742.
    • (2010) Cytom. Part A , vol.77 , pp. 733-742
    • Adler, J.1    Parmryd, I.2
  • 3
    • 70349705441 scopus 로고    scopus 로고
    • Prions: protein aggregation and infectious diseases
    • Aguzzi, A., Calella, A.M., Prions: protein aggregation and infectious diseases. Physiol. Rev. 89 (2009), 1105–1152.
    • (2009) Physiol. Rev. , vol.89 , pp. 1105-1152
    • Aguzzi, A.1    Calella, A.M.2
  • 4
    • 84959421968 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and cell death in neurodegenerative diseases through nitroxidative stress
    • Akbar, M., et al. Mitochondrial dysfunction and cell death in neurodegenerative diseases through nitroxidative stress. Brain Res. 1637 (2016), 34–55.
    • (2016) Brain Res. , vol.1637 , pp. 34-55
    • Akbar, M.1
  • 5
    • 84865843186 scopus 로고    scopus 로고
    • The genetics and neuropathology of amyotrophic lateral sclerosis
    • Al-Chalabi, A., et al. The genetics and neuropathology of amyotrophic lateral sclerosis. Acta Neuropathol. 124 (2012), 339–352.
    • (2012) Acta Neuropathol. , vol.124 , pp. 339-352
    • Al-Chalabi, A.1
  • 6
    • 82355180826 scopus 로고    scopus 로고
    • p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS
    • Al-Sarraj, S., et al. p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS. Acta Neuropathol. 122 (2011), 691–702.
    • (2011) Acta Neuropathol. , vol.122 , pp. 691-702
    • Al-Sarraj, S.1
  • 7
    • 84890204277 scopus 로고    scopus 로고
    • Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system
    • Amm, I., Sommer, T., Wolf, D.H., Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system. Biochim. Et Biophys. Acta (BBA) – Mol. Cell Res. 1843 (2014), 182–196.
    • (2014) Biochim. Et Biophys. Acta (BBA) – Mol. Cell Res. , vol.1843 , pp. 182-196
    • Amm, I.1    Sommer, T.2    Wolf, D.H.3
  • 8
    • 77957806157 scopus 로고    scopus 로고
    • Disulphide production by Ero1α–PDI relay is rapid and effectively regulated
    • Appenzeller-Herzog, C., et al. Disulphide production by Ero1α–PDI relay is rapid and effectively regulated. EMBO J. 29 (2010), 3318–3329.
    • (2010) EMBO J. , vol.29 , pp. 3318-3329
    • Appenzeller-Herzog, C.1
  • 9
    • 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. 351 (2006), 602–611.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 602-611
    • Arai, T.1
  • 10
    • 84874272095 scopus 로고    scopus 로고
    • Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS
    • Ash, P.E., et al. Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS. Neuron 77 (2013), 639–646.
    • (2013) Neuron , vol.77 , pp. 639-646
    • Ash, P.E.1
  • 11
    • 33749563294 scopus 로고    scopus 로고
    • Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1
    • Atkin, J.D., et al. Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J. Biol. Chem. 281 (2006), 30152–30165.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30152-30165
    • Atkin, J.D.1
  • 12
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • Atkin, J.D., Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol. Dis. 30 (2008), 400–407.
    • (2008) Neurobiol. Dis. , vol.30 , pp. 400-407
    • Atkin, J.D.1
  • 13
    • 84897112194 scopus 로고    scopus 로고
    • Mutant SOD1 inhibits ER-Golgi transport in amyotrophic lateral sclerosis
    • Atkin, J.D., Mutant SOD1 inhibits ER-Golgi transport in amyotrophic lateral sclerosis. J. Neurochem. 129 (2014), 190–204.
    • (2014) J. Neurochem. , vol.129 , pp. 190-204
    • Atkin, J.D.1
  • 14
    • 84921935837 scopus 로고    scopus 로고
    • Experimental transmissibility of mutant SOD1 motor neuron disease
    • Ayers, J.I., et al. Experimental transmissibility of mutant SOD1 motor neuron disease. Acta Neuropathol. 128 (2014), 791–803.
    • (2014) Acta Neuropathol. , vol.128 , pp. 791-803
    • Ayers, J.I.1
  • 15
    • 75149155060 scopus 로고    scopus 로고
    • Oxidative stress in ALS: key role in motor neuron injury and therapeutic target
    • Barber, S.C., Shaw, P.J., Oxidative stress in ALS: key role in motor neuron injury and therapeutic target. Free Rad. Biol. Med. 48 (2010), 629–641.
    • (2010) Free Rad. Biol. Med. , vol.48 , pp. 629-641
    • Barber, S.C.1    Shaw, P.J.2
  • 17
    • 0028233498 scopus 로고
    • COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • Barlowe, C., et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77 (1994), 895–907.
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1
  • 18
    • 84876387069 scopus 로고    scopus 로고
    • Secretory protein biogenesis and traffic in the early secretory pathway
    • Barlowe, C.K., Miller, E.A., Secretory protein biogenesis and traffic in the early secretory pathway. Genetics 193 (2013), 383–410.
    • (2013) Genetics , vol.193 , pp. 383-410
    • Barlowe, C.K.1    Miller, E.A.2
  • 19
    • 84904729990 scopus 로고    scopus 로고
    • Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models
    • Barmada, S.J., et al. Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models. Nat. Chem. Biol. 10 (2014), 677–685.
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 677-685
    • Barmada, S.J.1
  • 21
    • 84955444375 scopus 로고    scopus 로고
    • Methylation of C9orf72 expansion reduces RNA foci formation and dipeptide-repeat proteins expression in cells
    • Bauer, P.O., Methylation of C9orf72 expansion reduces RNA foci formation and dipeptide-repeat proteins expression in cells. Neurosci. Lett. 612 (2016), 204–209.
    • (2016) Neurosci. Lett. , vol.612 , pp. 204-209
    • Bauer, P.O.1
  • 22
    • 84892596606 scopus 로고    scopus 로고
    • Reduced C9orf72 gene expression in c9FTD/ALS is caused by histone trimethylation, an epigenetic event detectable in blood
    • Belzil, V.V., et al. Reduced C9orf72 gene expression in c9FTD/ALS is caused by histone trimethylation, an epigenetic event detectable in blood. Acta Neuropathol. 126 (2013), 895–905.
    • (2013) Acta Neuropathol. , vol.126 , pp. 895-905
    • Belzil, V.V.1
  • 23
    • 84859328507 scopus 로고    scopus 로고
    • Reduced calreticulin levels link endoplasmic reticulum stress and Fas-triggered cell death in motoneurons vulnerable to ALS
    • Bernard-Marissal, N., et al. Reduced calreticulin levels link endoplasmic reticulum stress and Fas-triggered cell death in motoneurons vulnerable to ALS. J. Neurosci. 32 (2012), 4901–4912.
    • (2012) J. Neurosci. , vol.32 , pp. 4901-4912
    • Bernard-Marissal, N.1
  • 24
    • 84908544396 scopus 로고    scopus 로고
    • Calreticulin levels determine onset of early muscle denervation by fast motoneurons of ALS model mice
    • Bernard-Marissal, N., et al. Calreticulin levels determine onset of early muscle denervation by fast motoneurons of ALS model mice. Neurobiol. Dis. 73 (2015), 130–136.
    • (2015) Neurobiol. Dis. , vol.73 , pp. 130-136
    • Bernard-Marissal, N.1
  • 25
    • 84879718279 scopus 로고    scopus 로고
    • Reticulon1-C modulates protein disulphide isomerase function
    • Bernardoni, P., et al. Reticulon1-C modulates protein disulphide isomerase function. Cell Death Dis., 4, 2013, e581.
    • (2013) Cell Death Dis. , vol.4 , pp. e581
    • Bernardoni, P.1
  • 26
    • 84861898911 scopus 로고    scopus 로고
    • Dietary restriction but not rapamycin extends disease onset and survival of the H46R/H48Q mouse model of ALS
    • Bhattacharya, A., et al. Dietary restriction but not rapamycin extends disease onset and survival of the H46R/H48Q mouse model of ALS. Neurobiol. Aging 33 (2012), 1829–1832.
    • (2012) Neurobiol. Aging , vol.33 , pp. 1829-1832
    • Bhattacharya, A.1
  • 27
    • 84953391561 scopus 로고    scopus 로고
    • Protein structure and function: looking through the network of side-chain interactions
    • Bhattacharyya, M., Ghosh, S., Vishveshwara, S., Protein structure and function: looking through the network of side-chain interactions. Curr. Protein Pept. Sci. 17 (2016), 4–25.
    • (2016) Curr. Protein Pept. Sci. , vol.17 , pp. 4-25
    • Bhattacharyya, M.1    Ghosh, S.2    Vishveshwara, S.3
  • 28
    • 0038509194 scopus 로고    scopus 로고
    • Frontotemporal and motor neurone degeneration with neurofilament inclusion bodies: additional evidence for overlap between FTD and ALS
    • Bigio, E., et al. Frontotemporal and motor neurone degeneration with neurofilament inclusion bodies: additional evidence for overlap between FTD and ALS. Neuropathol. Appl. Neurobiol. 29 (2003), 239–253.
    • (2003) Neuropathol. Appl. Neurobiol. , vol.29 , pp. 239-253
    • Bigio, E.1
  • 29
    • 78650545423 scopus 로고    scopus 로고
    • Deficits in axonal transport precede ALS symptoms in vivo
    • Bilsland, L.G., et al. Deficits in axonal transport precede ALS symptoms in vivo. Proc. Natl. Acad. Sci. 107 (2010), 20523–20528.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 20523-20528
    • Bilsland, L.G.1
  • 30
    • 84878556716 scopus 로고    scopus 로고
    • Protein aggregation in amyotrophic lateral sclerosis
    • Blokhuis, A.M., et al. Protein aggregation in amyotrophic lateral sclerosis. Acta Neuropathol. 125 (2013), 777–794.
    • (2013) Acta Neuropathol. , vol.125 , pp. 777-794
    • Blokhuis, A.M.1
  • 31
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco, D.A., et al. Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum. Mol. Genet. 19 (2010), 4160–4175.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4160-4175
    • Bosco, D.A.1
  • 32
    • 77958519939 scopus 로고    scopus 로고
    • Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
    • Bosco, D.A., et al. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Nat. Neurosci. 13 (2010), 1396–1403.
    • (2010) Nat. Neurosci. , vol.13 , pp. 1396-1403
    • Bosco, D.A.1
  • 33
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP‐43 aggregation by phosphorylation and p62/SQSTM1
    • Brady, O.A., et al. Regulation of TDP‐43 aggregation by phosphorylation and p62/SQSTM1. J. Neurochem. 116 (2011), 248–259.
    • (2011) J. Neurochem. , vol.116 , pp. 248-259
    • Brady, O.A.1
  • 34
    • 33645800776 scopus 로고    scopus 로고
    • Axonal damage markers in cerebrospinal fluid are increased in ALS
    • Brettschneider, J., et al. Axonal damage markers in cerebrospinal fluid are increased in ALS. Neurology 66 (2006), 852–856.
    • (2006) Neurology , vol.66 , pp. 852-856
    • Brettschneider, J.1
  • 35
    • 84862756869 scopus 로고    scopus 로고
    • Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion
    • Brettschneider, J., et al. Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion. Acta Neuropathol. 123 (2012), 825–839.
    • (2012) Acta Neuropathol. , vol.123 , pp. 825-839
    • Brettschneider, J.1
  • 36
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn, L.I., et al. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281 (1998), 1851–1854.
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1
  • 37
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
    • Buchberger, A., Bukau, B., Sommer, T., Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell 40 (2010), 238–252.
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 38
  • 39
    • 84942609596 scopus 로고    scopus 로고
    • SOD1 function and its implications for amyotrophic lateral sclerosis pathology new and renascent themes
    • 1073858414561795
    • Bunton-Stasyshyn, R.K., et al. SOD1 function and its implications for amyotrophic lateral sclerosis pathology new and renascent themes. Neuroscientist 21 (2014), 519–529 1073858414561795.
    • (2014) Neuroscientist , vol.21 , pp. 519-529
    • Bunton-Stasyshyn, R.K.1
  • 40
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti, E., et al. TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J. Biol. Chem. 280 (2005), 37572–37584.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37572-37584
    • Buratti, E.1
  • 41
    • 80052924149 scopus 로고    scopus 로고
    • Motor neuron dysfunction in frontotemporal dementia
    • awr195
    • Burrell, J.R., et al. Motor neuron dysfunction in frontotemporal dementia. Brain, 2011 awr195.
    • (2011) Brain
    • Burrell, J.R.1
  • 42
    • 84952865082 scopus 로고    scopus 로고
    • The ‘omics’ of amyotrophic lateral sclerosis
    • Caballero-Hernandez, D., et al. The ‘omics’ of amyotrophic lateral sclerosis. Trends Mol. Med. 22 (2016), 53–67.
    • (2016) Trends Mol. Med. , vol.22 , pp. 53-67
    • Caballero-Hernandez, D.1
  • 43
    • 85016754861 scopus 로고    scopus 로고
    • Early and gender-specific differences in spinal cord mitochondrial function and oxidative stress markers in a mouse model of ALS
    • Cacabelos, D., et al. Early and gender-specific differences in spinal cord mitochondrial function and oxidative stress markers in a mouse model of ALS. Acta Neuropathol. Commun., 4, 2016, 1.
    • (2016) Acta Neuropathol. Commun. , vol.4 , pp. 1
    • Cacabelos, D.1
  • 44
    • 0028131648 scopus 로고
    • Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds
    • Cai, H., Wang, C.-C., Tsou, C.-L., Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds. J. Biol. Chem. 269 (1994), 24550–24552.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24550-24552
    • Cai, H.1    Wang, C.-C.2    Tsou, C.-L.3
  • 45
    • 84923647985 scopus 로고    scopus 로고
    • Neurodegeneration: selective vulnerability
    • 123–123
    • Carr, F., Neurodegeneration: selective vulnerability. Nat. Rev. Neurosci., 16, 2015 123–123.
    • (2015) Nat. Rev. Neurosci. , vol.16
    • Carr, F.1
  • 46
    • 84923250517 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial damage: importance in non-SOD1 ALS
    • Carrì, M.T., et al. Oxidative stress and mitochondrial damage: importance in non-SOD1 ALS. Front. Cell. Neurosci., 9, 2015.
    • (2015) Front. Cell. Neurosci. , vol.9
    • Carrì, M.T.1
  • 47
    • 84884294596 scopus 로고    scopus 로고
    • Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons
    • Castillo, K., et al. Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons. Autophagy 9 (2013), 1308–1320.
    • (2013) Autophagy , vol.9 , pp. 1308-1320
    • Castillo, K.1
  • 48
    • 4544249202 scopus 로고    scopus 로고
    • Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway
    • Chakravarthi, S., Bulleid, N.J., Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. J. Biol. Chem. 279 (2004), 39872–39879.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39872-39879
    • Chakravarthi, S.1    Bulleid, N.J.2
  • 49
    • 68349104931 scopus 로고    scopus 로고
    • Optineurin and its mutants: molecules associated with some forms of glaucoma
    • Chalasani, M.L., Swarup, G., Balasubramanian, D., Optineurin and its mutants: molecules associated with some forms of glaucoma. Ophthalmic Res. 42 (2009), 176–184.
    • (2009) Ophthalmic Res. , vol.42 , pp. 176-184
    • Chalasani, M.L.1    Swarup, G.2    Balasubramanian, D.3
  • 50
    • 84908018421 scopus 로고    scopus 로고
    • Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 2. Protein misfolding and ER stress
    • Chambers, J.E., Marciniak, S.J., Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 2. Protein misfolding and ER stress. Am. J. Physiol. Cell Physiol. 307 (2014), C657–C670.
    • (2014) Am. J. Physiol. Cell Physiol. , vol.307 , pp. C657-C670
    • Chambers, J.E.1    Marciniak, S.J.2
  • 51
    • 84875228800 scopus 로고    scopus 로고
    • Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function
    • Chang, C.-k, et al. Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function. FEBS Lett. 587 (2013), 575–582.
    • (2013) FEBS Lett. , vol.587 , pp. 575-582
    • Chang, C.-K.1
  • 52
    • 57749100302 scopus 로고    scopus 로고
    • Initiation and elongation in fibrillation of ALS-linked superoxide dismutase
    • Chattopadhyay, M., et al. Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc. Natl. Acad. Sci. 105 (2008), 18663–18668.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 18663-18668
    • Chattopadhyay, M.1
  • 53
    • 84881275424 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis: an update
    • Chen, S., et al. Genetics of amyotrophic lateral sclerosis: an update. Mol Neurodegener., 8, 2013, 28.
    • (2013) Mol Neurodegener. , vol.8 , pp. 28
    • Chen, S.1
  • 54
    • 84870953719 scopus 로고    scopus 로고
    • S-nitrosylated protein disulfide isomerase contributes to mutant SOD1 aggregates in amyotrophic lateral sclerosis
    • Chen, X., et al. S-nitrosylated protein disulfide isomerase contributes to mutant SOD1 aggregates in amyotrophic lateral sclerosis. J. Neurochem. 124 (2013), 45–58.
    • (2013) J. Neurochem. , vol.124 , pp. 45-58
    • Chen, X.1
  • 55
    • 24144434736 scopus 로고    scopus 로고
    • ER-associated protein degradation is a common mechanism underpinning numerous monogenic diseases including Robinow syndrome
    • Chen, Y., et al. ER-associated protein degradation is a common mechanism underpinning numerous monogenic diseases including Robinow syndrome. Hum. Mol. Genet. 14 (2005), 2559–2569.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2559-2569
    • Chen, Y.1
  • 56
    • 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. 74 (2004), 1128–1135.
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 1128-1135
    • Chen, Y.-Z.1
  • 57
    • 34447133038 scopus 로고    scopus 로고
    • Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J
    • Chow, C.Y., et al. Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J. Nature 448 (2007), 68–72.
    • (2007) Nature , vol.448 , pp. 68-72
    • Chow, C.Y.1
  • 58
    • 58049192812 scopus 로고    scopus 로고
    • Deleterious variants of FIG4, a phosphoinositide phosphatase, in patients with ALS
    • Chow, C.Y., et al. Deleterious variants of FIG4, a phosphoinositide phosphatase, in patients with ALS. Am. J. Hum. Genet. 84 (2009), 85–88.
    • (2009) Am. J. Hum. Genet. , vol.84 , pp. 85-88
    • Chow, C.Y.1
  • 59
    • 84860225255 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover, A., Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Neurodegener. Dis. 10 (2012), 7–22.
    • (2012) Neurodegener. Dis. , vol.10 , pp. 7-22
    • Ciechanover, A.1
  • 60
    • 84989284335 scopus 로고    scopus 로고
    • Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies
    • Ciechanover, A., Kwon, Y.T., Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies. Exp. Mol. Med., 47, 2015, e147.
    • (2015) Exp. Mol. Med. , vol.47 , pp. e147
    • Ciechanover, A.1    Kwon, Y.T.2
  • 61
    • 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 347 (2015), 1436–1441.
    • (2015) Science , vol.347 , pp. 1436-1441
    • Cirulli, E.T.1
  • 62
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS
    • Cleveland, D.W., Rothstein, J.D., From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2 (2001), 806–819.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 63
    • 84861362218 scopus 로고    scopus 로고
    • Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family
    • Codding, J.A., Israel, B.A., Thorpe, C., Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family. Biochemistry 51 (2012), 4226–4235.
    • (2012) Biochemistry , vol.51 , pp. 4226-4235
    • Codding, J.A.1    Israel, B.A.2    Thorpe, C.3
  • 64
    • 84973596353 scopus 로고    scopus 로고
    • Intracellular pH modulates quinary structure
    • Cohen, R.D., Guseman, A.J., Pielak, G.J., Intracellular pH modulates quinary structure. Protein Sci. 24 (2015), 1748–1755.
    • (2015) Protein Sci. , vol.24 , pp. 1748-1755
    • Cohen, R.D.1    Guseman, A.J.2    Pielak, G.J.3
  • 65
    • 84857997227 scopus 로고    scopus 로고
    • Redox signalling directly regulates TDP‐43 via cysteine oxidation and disulphide cross-linking
    • Cohen, T.J., et al. Redox signalling directly regulates TDP‐43 via cysteine oxidation and disulphide cross-linking. EMBO J. 31 (2012), 1241–1252.
    • (2012) EMBO J. , vol.31 , pp. 1241-1252
    • Cohen, T.J.1
  • 66
    • 70350135049 scopus 로고    scopus 로고
    • TDP‐43 is recruited to stress granules in conditions of oxidative insult
    • Colombrita, C., et al. TDP‐43 is recruited to stress granules in conditions of oxidative insult. J. Neurochem. 111 (2009), 1051–1061.
    • (2009) J. Neurochem. , vol.111 , pp. 1051-1061
    • Colombrita, C.1
  • 67
    • 84969508765 scopus 로고    scopus 로고
    • S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions
    • Conway, M.E., Harris, M., S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions. Front. Chem., 3, 2015.
    • (2015) Front. Chem. , vol.3
    • Conway, M.E.1    Harris, M.2
  • 68
    • 38149115471 scopus 로고    scopus 로고
    • Cysteine 111 affects aggregation and cytotoxicity of mutant Cu, Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis
    • Cozzolino, M., et al. Cysteine 111 affects aggregation and cytotoxicity of mutant Cu, Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 283 (2008), 866–874.
    • (2008) J. Biol. Chem. , vol.283 , pp. 866-874
    • Cozzolino, M.1
  • 69
    • 84890085638 scopus 로고    scopus 로고
    • Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging
    • Cuanalo-Contreras, K., Mukherjee, A., Soto, C., Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging. Int. J. Cell Biol., 2013, 2013.
    • (2013) Int. J. Cell Biol. , vol.2013
    • Cuanalo-Contreras, K.1    Mukherjee, A.2    Soto, C.3
  • 70
    • 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 72 (2011), 245–256.
    • (2011) Neuron , vol.72 , pp. 245-256
    • DeJesus-Hernandez, M.1
  • 71
    • 65449130022 scopus 로고    scopus 로고
    • TARDBP (TDP‐43) sequence analysis in patients with familial and sporadic ALS: identification of two novel mutations
    • Del Bo, R., et al. TARDBP (TDP‐43) sequence analysis in patients with familial and sporadic ALS: identification of two novel mutations. Eur. J. Neurol. 16 (2009), 727–732.
    • (2009) Eur. J. Neurol. , vol.16 , pp. 727-732
    • Del Bo, R.1
  • 72
    • 84902291718 scopus 로고    scopus 로고
    • The role of FUS gene variants in neurodegenerative diseases
    • Deng, H., Gao, K., Jankovic, J., The role of FUS gene variants in neurodegenerative diseases. Nat. Rev. Neurol. 10 (2014), 337–348.
    • (2014) Nat. Rev. Neurol. , vol.10 , pp. 337-348
    • Deng, H.1    Gao, K.2    Jankovic, J.3
  • 73
    • 77952932485 scopus 로고    scopus 로고
    • FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis
    • Deng, H.X., et al. FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis. Ann. Neurol. 67 (2010), 739–748.
    • (2010) Ann. Neurol. , vol.67 , pp. 739-748
    • Deng, H.X.1
  • 74
    • 80051563478 scopus 로고    scopus 로고
    • Differential involvement of optineurin in amyotrophic lateral sclerosis with or without SOD1 mutations
    • Deng, H.-X., et al. Differential involvement of optineurin in amyotrophic lateral sclerosis with or without SOD1 mutations. Arch. Neurol. 68 (2011), 1057–1061.
    • (2011) Arch. Neurol. , vol.68 , pp. 1057-1061
    • Deng, H.-X.1
  • 75
    • 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 477 (2011), 211–215.
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.-X.1
  • 76
    • 0042914405 scopus 로고    scopus 로고
    • The first nonsense mutation in alsin results in a homogeneous phenotype of infantile-onset ascending spastic paralysis with bulbar involvement in two siblings
    • Devon, R., et al. The first nonsense mutation in alsin results in a homogeneous phenotype of infantile-onset ascending spastic paralysis with bulbar involvement in two siblings. Clin. Genet. 64 (2003), 210–215.
    • (2003) Clin. Genet. , vol.64 , pp. 210-215
    • Devon, R.1
  • 77
    • 84862128438 scopus 로고    scopus 로고
    • TDP-43 aggregation in neurodegeneration: are stress granules the key?
    • Dewey, C.M., et al. TDP-43 aggregation in neurodegeneration: are stress granules the key?. Brain Res. 1462 (2012), 16–25.
    • (2012) Brain Res. , vol.1462 , pp. 16-25
    • Dewey, C.M.1
  • 78
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M., Protein folding and misfolding. Nature 426 (2003), 884–890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 79
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • In: 15, ed.^eds. Elsevier
    • Dobson, C.M., 2004. Principles of protein folding, misfolding and aggregation. In: Seminars in cell and developmental biology, vol. 15, ed.^eds. Elsevier, pp. 3–16.
    • (2004) Seminars in cell and developmental biology, vol , pp. 3-16
    • Dobson, C.M.1
  • 80
    • 84892451456 scopus 로고    scopus 로고
    • Characterization of the repeat expansion size in C9orf72 in amyotrophic lateral sclerosis and frontotemporal dementia
    • Dols-Icardo, O., et al. Characterization of the repeat expansion size in C9orf72 in amyotrophic lateral sclerosis and frontotemporal dementia. Hum. Mol. Genet. 23 (2014), 749–754.
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 749-754
    • Dols-Icardo, O.1
  • 81
    • 77955792022 scopus 로고    scopus 로고
    • ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import
    • Dormann, D., et al. ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import. EMBO J. 29 (2010), 2841–2857.
    • (2010) EMBO J. , vol.29 , pp. 2841-2857
    • Dormann, D.1
  • 82
    • 11144227941 scopus 로고    scopus 로고
    • Dissociation of human copper–zinc superoxide dismutase dimers using chaotrope and reductant
    • Doucette, P.A., et al. Dissociation of human copper–zinc superoxide dismutase dimers using chaotrope and reductant. J. Biol. Chem. 279 (2004), 54558–54566.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54558-54566
    • Doucette, P.A.1
  • 83
    • 79952899796 scopus 로고    scopus 로고
    • C-terminal FUS/TLS mutations in familial and sporadic ALS in Germany
    • e1-548. e4
    • Drepper, C., et al. C-terminal FUS/TLS mutations in familial and sporadic ALS in Germany. Neurobiol. Aging, 32, 2011, 548 e1-548. e4.
    • (2011) Neurobiol. Aging , vol.32 , pp. 548
    • Drepper, C.1
  • 84
    • 77955423158 scopus 로고    scopus 로고
    • Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell
    • Duan, W., et al. Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell. Neuroscience 169 (2010), 1621–1629.
    • (2010) Neuroscience , vol.169 , pp. 1621-1629
    • Duan, W.1
  • 85
    • 84924226599 scopus 로고    scopus 로고
    • Protein transport into the human endoplasmic reticulum
    • Dudek, J., et al. Protein transport into the human endoplasmic reticulum. J. Mol. Biol. 427 (2015), 1159–1175.
    • (2015) J. Mol. Biol. , vol.427 , pp. 1159-1175
    • Dudek, J.1
  • 86
    • 73349090611 scopus 로고    scopus 로고
    • Journeys through the Golgi – taking stock in a new era
    • Emr, S., et al. Journeys through the Golgi – taking stock in a new era. J. Cell Biol. 187 (2009), 449–453.
    • (2009) J. Cell Biol. , vol.187 , pp. 449-453
    • Emr, S.1
  • 87
    • 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. 102 (2007), 170–178.
    • (2007) J. Neurochem. , vol.102 , pp. 170-178
    • Ezzi, S.A.1    Urushitani, M.2    Julien, J.P.3
  • 88
    • 84866748196 scopus 로고    scopus 로고
    • Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase
    • Farg, M.A., et al. Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase. Neurobiol. Aging 33 (2012), 2855–2868.
    • (2012) Neurobiol. Aging , vol.33 , pp. 2855-2868
    • Farg, M.A.1
  • 89
    • 84901038797 scopus 로고    scopus 로고
    • C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking
    • ddu068
    • Farg, M.A., et al. C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking. Hum. Mol. Genet. 23 (2014), 3579–3595 ddu068.
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 3579-3595
    • Farg, M.A.1
  • 90
    • 84940185085 scopus 로고    scopus 로고
    • Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions
    • Farrawell, N.E., et al. Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions. Sci. Rep., 5, 2015.
    • (2015) Sci. Rep. , vol.5
    • Farrawell, N.E.1
  • 91
    • 59149097039 scopus 로고    scopus 로고
    • DCTN1 mutations in Perry syndrome
    • Farrer, M.J., et al. DCTN1 mutations in Perry syndrome. Nat. Genet. 41 (2009), 163–165.
    • (2009) Nat. Genet. , vol.41 , pp. 163-165
    • Farrer, M.J.1
  • 92
    • 77952308995 scopus 로고    scopus 로고
    • A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum
    • Fasana, E., et al. A VAPB mutant linked to amyotrophic lateral sclerosis generates a novel form of organized smooth endoplasmic reticulum. FASEB J. 24 (2010), 1419–1430.
    • (2010) FASEB J. , vol.24 , pp. 1419-1430
    • Fasana, E.1
  • 93
    • 80855150639 scopus 로고    scopus 로고
    • SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Fecto, F., et al. SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis. Arch. Neurol. 68 (2011), 1440–1446.
    • (2011) Arch. Neurol. , vol.68 , pp. 1440-1446
    • Fecto, F.1
  • 94
    • 0035675962 scopus 로고    scopus 로고
    • The action of molecular chaperones in the early secretory pathway
    • Fewell, S.W., et al. The action of molecular chaperones in the early secretory pathway. Annu. Rev. Genet. 35 (2001), 149–191.
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 149-191
    • Fewell, S.W.1
  • 95
    • 0028001606 scopus 로고
    • Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis
    • Figlewicz, D.A., et al. Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum. Mol. Genet. 3 (1994), 1757–1761.
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1757-1761
    • Figlewicz, D.A.1
  • 96
    • 0345742771 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis is a distal axonopathy: evidence in mice and man
    • Fischer, L.R., et al. Amyotrophic lateral sclerosis is a distal axonopathy: evidence in mice and man. Exp. Neurol. 185 (2004), 232–240.
    • (2004) Exp. Neurol. , vol.185 , pp. 232-240
    • Fischer, L.R.1
  • 97
    • 34248998027 scopus 로고    scopus 로고
    • Nitrosative stress in the ER: a new role for S-nitrosylation in neurodegenerative diseases
    • Forrester, M.T., Benhar, M., Stamler, J.S., Nitrosative stress in the ER: a new role for S-nitrosylation in neurodegenerative diseases. ACS Chem. Biol. 1 (2006), 355–358.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 355-358
    • Forrester, M.T.1    Benhar, M.2    Stamler, J.S.3
  • 98
    • 77955352066 scopus 로고    scopus 로고
    • Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients
    • Forsberg, K., et al. Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients. PloS One, 5, 2010, e11552.
    • (2010) PloS One , vol.5 , pp. e11552
    • Forsberg, K.1
  • 99
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand, A.R., Kaiser, C.A., The ERO1gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell 1 (1998), 161–170.
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 100
    • 84940925534 scopus 로고    scopus 로고
    • GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport
    • Freibaum, B.D., et al. GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport. Nature, 2015.
    • (2015) Nature
    • Freibaum, B.D.1
  • 101
    • 84990962844 scopus 로고    scopus 로고
    • Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia
    • Freischmidt, A., et al. Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia. Nat. Neurosci. 525 (2015), 129–133.
    • (2015) Nat. Neurosci. , vol.525 , pp. 129-133
    • Freischmidt, A.1
  • 102
    • 0034175513 scopus 로고    scopus 로고
    • Early and selective loss of neuromuscular synapse subtypes with low sprouting competence in motoneuron diseases
    • Frey, D., et al. Early and selective loss of neuromuscular synapse subtypes with low sprouting competence in motoneuron diseases. J. Neurosci. 20 (2000), 2534–2542.
    • (2000) J. Neurosci. , vol.20 , pp. 2534-2542
    • Frey, D.1
  • 103
    • 37249074786 scopus 로고    scopus 로고
    • Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase
    • Fujiwara, N., et al. Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase. J. Biol. Chem. 282 (2007), 35933–35944.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35933-35944
    • Fujiwara, N.1
  • 104
    • 33646486372 scopus 로고    scopus 로고
    • Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice
    • Furukawa, Y., et al. Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. Proc. Natl. Acad. Sci. 103 (2006), 7148–7153.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 7148-7153
    • Furukawa, Y.1
  • 105
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of sarkosyl-insoluble transactivation response element (TAR) DNA-binding Protein-43 Inclusions
    • Furukawa, Y., et al. A seeding reaction recapitulates intracellular formation of sarkosyl-insoluble transactivation response element (TAR) DNA-binding Protein-43 Inclusions. J. Biol. Chem. 286 (2011), 18664–18672.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18664-18672
    • Furukawa, Y.1
  • 106
    • 84990970437 scopus 로고    scopus 로고
    • Protein Aggregates in Pathological Inclusions of Amyotrophic Lateral Sclerosis
    • INTECH Open Access Publisher Croatia
    • Furukawa, Y., Protein Aggregates in Pathological Inclusions of Amyotrophic Lateral Sclerosis. 2012, INTECH Open Access Publisher, Croatia.
    • (2012)
    • Furukawa, Y.1
  • 107
    • 34249679116 scopus 로고    scopus 로고
    • p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis
    • Gal, J., et al. p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis. J. Biol. Chem. 282 (2007), 11068–11077.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11068-11077
    • Gal, J.1
  • 108
    • 70350131893 scopus 로고    scopus 로고
    • Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism
    • Gal, J., et al. Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism. J. Neurochem. 111 (2009), 1062–1073.
    • (2009) J. Neurochem. , vol.111 , pp. 1062-1073
    • Gal, J.1
  • 109
    • 80053646130 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • e27-2323. e40
    • Gal, J., et al. Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol. Aging, 32, 2011, 2323 e27-2323. e40.
    • (2011) Neurobiol. Aging , vol.32 , pp. 2323
    • Gal, J.1
  • 110
    • 84991003243 scopus 로고    scopus 로고
    • Proteomic analysis of dynein-interacting proteins in Amyotrophic Lateral Sclerosis synaptosomes reveals alterations in the RNA-binding Protein Staufen1
    • Gershoni-Emek, N., et al. Proteomic analysis of dynein-interacting proteins in Amyotrophic Lateral Sclerosis synaptosomes reveals alterations in the RNA-binding Protein Staufen1. Mol. Cell. Proteom. MCP, M115, 2015, 049965.
    • (2015) Mol. Cell. Proteom. MCP , vol.M115 , pp. 049965
    • Gershoni-Emek, N.1
  • 111
    • 84928503137 scopus 로고    scopus 로고
    • A chemical chaperone-based drug candidate is effective in a mouse model of amyotrophic lateral sclerosis (ALS)
    • Getter, T., et al. A chemical chaperone-based drug candidate is effective in a mouse model of amyotrophic lateral sclerosis (ALS). ChemMedChem 10 (2015), 850–861.
    • (2015) ChemMedChem , vol.10 , pp. 850-861
    • Getter, T.1
  • 112
    • 84863533791 scopus 로고    scopus 로고
    • The stress of protein misfolding: from single cells to multicellular organisms
    • Gidalevitz, T., Prahlad, V., Morimoto, R.I., The stress of protein misfolding: from single cells to multicellular organisms. Cold Spring Harb. Perspect. Biol., 3, 2011, a009704.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a009704
    • Gidalevitz, T.1    Prahlad, V.2    Morimoto, R.I.3
  • 113
    • 44349107708 scopus 로고    scopus 로고
    • VAPB interacts with and modulates the activity of ATF6
    • Gkogkas, C., et al. VAPB interacts with and modulates the activity of ATF6. Hum. Mol. Genet. 17 (2008), 1517–1526.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1517-1526
    • Gkogkas, C.1
  • 114
    • 84929945166 scopus 로고    scopus 로고
    • Identification of rare protein disulfide isomerase gene variants in amyotrophic lateral sclerosis patients
    • Gonzalez-Perez, P., et al. Identification of rare protein disulfide isomerase gene variants in amyotrophic lateral sclerosis patients. Gene 566 (2015), 158–165.
    • (2015) Gene , vol.566 , pp. 158-165
    • Gonzalez-Perez, P.1
  • 116
    • 80053652133 scopus 로고    scopus 로고
    • Intermolecular transmission of superoxide dismutase 1 misfolding in living cells
    • Grad, L.I., et al. Intermolecular transmission of superoxide dismutase 1 misfolding in living cells. Proc. Natl. Acad. Sci. 108 (2011), 16398–16403.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 16398-16403
    • Grad, L.I.1
  • 117
    • 84895796816 scopus 로고    scopus 로고
    • Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and-independent mechanisms
    • Grad, L.I., et al. Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and-independent mechanisms. Proc. Natl. Acad. Sci. 111 (2014), 3620–3625.
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , pp. 3620-3625
    • Grad, L.I.1
  • 118
    • 84896970296 scopus 로고    scopus 로고
    • Prion-like activity of Cu/Zn superoxide dismutase: implications for amyotrophic lateral sclerosis
    • Grad, L.I., Cashman, N.R., Prion-like activity of Cu/Zn superoxide dismutase: implications for amyotrophic lateral sclerosis. Prion 8 (2014), 33–41.
    • (2014) Prion , vol.8 , pp. 33-41
    • Grad, L.I.1    Cashman, N.R.2
  • 119
    • 8844263662 scopus 로고    scopus 로고
    • A novel candidate region for ALS on chromosome 14q11. 2
    • Greenway, M., et al. A novel candidate region for ALS on chromosome 14q11. 2. Neurology 63 (2004), 1936–1938.
    • (2004) Neurology , vol.63 , pp. 1936-1938
    • Greenway, M.1
  • 120
    • 33750116189 scopus 로고    scopus 로고
    • Protein misfolding and human disease
    • Gregersen, N., et al. Protein misfolding and human disease. Annu. Rev. Genom. Hum. Genet. 7 (2006), 103–124.
    • (2006) Annu. Rev. Genom. Hum. Genet. , vol.7 , pp. 103-124
    • Gregersen, N.1
  • 121
    • 8544222694 scopus 로고    scopus 로고
    • A frameshift deletion in peripherin gene associated with amyotrophic lateral sclerosis
    • Gros-Louis, F., et al. A frameshift deletion in peripherin gene associated with amyotrophic lateral sclerosis. J. Biol. Chem. 279 (2004), 45951–45956.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45951-45956
    • Gros-Louis, F.1
  • 122
    • 84875273042 scopus 로고    scopus 로고
    • Lithium in patients with amyotrophic lateral sclerosis (LiCALS): a phase 3 multicentre, randomised, double-blind, placebo-controlled trial
    • Group, U.-L.S., Lithium in patients with amyotrophic lateral sclerosis (LiCALS): a phase 3 multicentre, randomised, double-blind, placebo-controlled trial. Lancet Neurol. 12 (2013), 339–345.
    • (2013) Lancet Neurol. , vol.12 , pp. 339-345
    • Group, U.-L.S.1
  • 123
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune, T., et al. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem. Biophys. Res. Commun. 305 (2003), 709–718.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 709-718
    • Grune, T.1
  • 124
    • 77956392115 scopus 로고    scopus 로고
    • Ultrastructural diversity of inclusions and aggregations in the lumbar spinal cord of SOD1-G93A transgenic mice
    • Guo, Y., et al. Ultrastructural diversity of inclusions and aggregations in the lumbar spinal cord of SOD1-G93A transgenic mice. Brain Res. 1353 (2010), 234–244.
    • (2010) Brain Res. , vol.1353 , pp. 234-244
    • Guo, Y.1
  • 125
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F.U., Bracher, A., Hayer-Hartl, M., Molecular chaperones in protein folding and proteostasis. Nature 475 (2011), 324–332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 126
    • 84922448304 scopus 로고    scopus 로고
    • Local destabilization of the metal-binding region in human copper–zinc superoxide dismutase by remote mutations is a possible determinant for progression of ALS
    • Hennig, J., et al. Local destabilization of the metal-binding region in human copper–zinc superoxide dismutase by remote mutations is a possible determinant for progression of ALS. Biochemistry 54 (2015), 323–333.
    • (2015) Biochemistry , vol.54 , pp. 323-333
    • Hennig, J.1
  • 127
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • Herczenik, E., Gebbink, M.F., Molecular and cellular aspects of protein misfolding and disease. FASEB J. 22 (2008), 2115–2133.
    • (2008) FASEB J. , vol.22 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.2
  • 128
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz, C., et al. XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev. 23 (2009), 2294–2306.
    • (2009) Genes Dev. , vol.23 , pp. 2294-2306
    • Hetz, C.1
  • 129
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz, C., The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13 (2012), 89–102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 130
    • 84879417877 scopus 로고    scopus 로고
    • The biological meaning of the UPR
    • 404–404
    • Hetz, C., The biological meaning of the UPR. Nat. Rev. Mol. Cell Biol., 14, 2013 404–404.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14
    • Hetz, C.1
  • 131
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz, C., Mollereau, B., Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 15 (2014), 233–249.
    • (2014) Nat. Rev. Neurosci. , vol.15 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 132
    • 47949110973 scopus 로고    scopus 로고
    • White matter lesions in the brain with frontotemporal lobar degeneration with motor neuron disease: TDP-43-immunopositive inclusions co-localize with p62, but not ubiquitin
    • Hiji, M., et al. White matter lesions in the brain with frontotemporal lobar degeneration with motor neuron disease: TDP-43-immunopositive inclusions co-localize with p62, but not ubiquitin. Acta Neuropathol. 116 (2008), 183–191.
    • (2008) Acta Neuropathol. , vol.116 , pp. 183-191
    • Hiji, M.1
  • 133
    • 84859983420 scopus 로고    scopus 로고
    • Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease
    • Hipp, M.S., et al. Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease. J. Cell Biol. 196 (2012), 573–587.
    • (2012) J. Cell Biol. , vol.196 , pp. 573-587
    • Hipp, M.S.1
  • 134
    • 0042626056 scopus 로고    scopus 로고
    • Survival in frontotemporal dementia
    • Hodges, J., et al. Survival in frontotemporal dementia. Neurology 61 (2003), 349–354.
    • (2003) Neurology , vol.61 , pp. 349-354
    • Hodges, J.1
  • 135
    • 78649246847 scopus 로고    scopus 로고
    • Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins
    • Hoffstrom, B.G., et al. Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins. Nat. Chem. Biol. 6 (2010), 900–906.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 900-906
    • Hoffstrom, B.G.1
  • 136
    • 0027419879 scopus 로고
    • Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport
    • Hollenbeck, P.J., Products of endocytosis and autophagy are retrieved from axons by regulated retrograde organelle transport. J. Cell Biol. 121 (1993), 305–315.
    • (1993) J. Cell Biol. , vol.121 , pp. 305-315
    • Hollenbeck, P.J.1
  • 137
    • 84868452494 scopus 로고    scopus 로고
    • Full-length TDP-43 and its C-terminal fragments activate mitophagy in NSC34 cell line
    • Hong, K., et al. Full-length TDP-43 and its C-terminal fragments activate mitophagy in NSC34 cell line. Neurosci. Lett. 530 (2012), 144–149.
    • (2012) Neurosci. Lett. , vol.530 , pp. 144-149
    • Hong, K.1
  • 138
    • 80055031464 scopus 로고    scopus 로고
    • Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis
    • Honjo, Y., et al. Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis. Amyotroph. Lateral Scler. 12 (2011), 444–450.
    • (2011) Amyotroph. Lateral Scler. , vol.12 , pp. 444-450
    • Honjo, Y.1
  • 139
    • 11144357460 scopus 로고    scopus 로고
    • Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants
    • Hough, M.A., et al. Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants. Proc. Natl. Acad. Sci. USA 101 (2004), 5976–5981.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5976-5981
    • Hough, M.A.1
  • 140
    • 84924179685 scopus 로고    scopus 로고
    • Oxidative protein folding: from thiol–disulfide exchange reactions to the redox poise of the endoplasmic reticulum
    • Hudson, D.A., Gannon, S.A., Thorpe, C., Oxidative protein folding: from thiol–disulfide exchange reactions to the redox poise of the endoplasmic reticulum. Free Radic. Biol. Med. 80 (2015), 171–182.
    • (2015) Free Radic. Biol. Med. , vol.80 , pp. 171-182
    • Hudson, D.A.1    Gannon, S.A.2    Thorpe, C.3
  • 141
    • 46749138739 scopus 로고    scopus 로고
    • Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Igaz, L.M., et al. Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Am. J. Pathol. 173 (2008), 182–194.
    • (2008) Am. J. Pathol. , vol.173 , pp. 182-194
    • Igaz, L.M.1
  • 142
    • 84856574050 scopus 로고    scopus 로고
    • Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies
    • Iguchi, Y., et al. Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies. Neurobiol. Dis. 45 (2012), 862–870.
    • (2012) Neurobiol. Dis. , vol.45 , pp. 862-870
    • Iguchi, Y.1
  • 143
    • 84915823076 scopus 로고    scopus 로고
    • Basophilic inclusions and neuronal intermediate filament inclusions in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • Ito, H., Basophilic inclusions and neuronal intermediate filament inclusions in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. Neuropathology 34 (2014), 589–595.
    • (2014) Neuropathology , vol.34 , pp. 589-595
    • Ito, H.1
  • 144
    • 70350340050 scopus 로고    scopus 로고
    • Involvement of CHOP, an ER-stress apoptotic mediator, in both human sporadic ALS and ALS model mice
    • Ito, Y., et al. Involvement of CHOP, an ER-stress apoptotic mediator, in both human sporadic ALS and ALS model mice. Neurobiol. Dis. 36 (2009), 470–476.
    • (2009) Neurobiol. Dis. , vol.36 , pp. 470-476
    • Ito, Y.1
  • 145
    • 84896498656 scopus 로고    scopus 로고
    • Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis
    • Jeon, G.S., et al. Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis. Mol. Neurobiol. 49 (2014), 796–807.
    • (2014) Mol. Neurobiol. , vol.49 , pp. 796-807
    • Jeon, G.S.1
  • 146
    • 84904860146 scopus 로고    scopus 로고
    • Guanabenz delays the onset of disease symptoms, extends lifespan, improves motor performance and attenuates motor neuron loss in the SOD1 G93A mouse model of amyotrophic lateral sclerosis
    • Jiang, H.-Q., et al. Guanabenz delays the onset of disease symptoms, extends lifespan, improves motor performance and attenuates motor neuron loss in the SOD1 G93A mouse model of amyotrophic lateral sclerosis. Neuroscience 277 (2014), 132–138.
    • (2014) Neuroscience , vol.277 , pp. 132-138
    • Jiang, H.-Q.1
  • 147
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • Johnson, B.S., et al. A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc. Natl. Acad. Sci. 105 (2008), 6439–6444.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 6439-6444
    • Johnson, B.S.1
  • 148
    • 78649941297 scopus 로고    scopus 로고
    • Exome sequencing reveals VCP mutations as a cause of familial ALS
    • Johnson, J.O., et al. Exome sequencing reveals VCP mutations as a cause of familial ALS. Neuron 68 (2010), 857–864.
    • (2010) Neuron , vol.68 , pp. 857-864
    • Johnson, J.O.1
  • 149
    • 84899644069 scopus 로고    scopus 로고
    • Mutations in the Matrin 3 gene cause familial amyotrophic lateral sclerosis
    • Johnson, J.O., et al. Mutations in the Matrin 3 gene cause familial amyotrophic lateral sclerosis. Nat. Neurosci. 17 (2014), 664–666.
    • (2014) Nat. Neurosci. , vol.17 , pp. 664-666
    • Johnson, J.O.1
  • 150
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston, J.A., Ward, C.L., Kopito, R.R., Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143 (1998), 1883–1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 151
    • 44849090909 scopus 로고    scopus 로고
    • Inclusions of amyotrophic lateral sclerosis – linked superoxide dismutase in ventral horns, liver, and kidney
    • Jonsson, P.A., et al. Inclusions of amyotrophic lateral sclerosis – linked superoxide dismutase in ventral horns, liver, and kidney. Ann. Neurol. 63 (2008), 671–675.
    • (2008) Ann. Neurol. , vol.63 , pp. 671-675
    • Jonsson, P.A.1
  • 152
    • 84940426318 scopus 로고    scopus 로고
    • Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS
    • Jovičić, A., et al. Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS. Nat. Neurosci. 18 (2015), 1226–1229.
    • (2015) Nat. Neurosci. , vol.18 , pp. 1226-1229
    • Jovičić, A.1
  • 153
    • 74049124412 scopus 로고    scopus 로고
    • Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
    • Ju, J.-S., et al. Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease. J. Cell Biol. 187 (2009), 875–888.
    • (2009) J. Cell Biol. , vol.187 , pp. 875-888
    • Ju, J.-S.1
  • 154
    • 67651033222 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-linked mutant SOD1 aberrantly interacts with tubulin
    • Kabuta, T., et al. Familial amyotrophic lateral sclerosis-linked mutant SOD1 aberrantly interacts with tubulin. Biochem. Biophys. Res. Commun. 387 (2009), 121–126.
    • (2009) Biochem. Biophys. Res. Commun. , vol.387 , pp. 121-126
    • Kabuta, T.1
  • 155
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich, D., Kopito, R., Frydman, J., Misfolded proteins partition between two distinct quality control compartments. Nature 454 (2008), 1088–1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 156
    • 33749554133 scopus 로고    scopus 로고
    • Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8)
    • Kanekura, K., et al. Characterization of amyotrophic lateral sclerosis-linked P56S mutation of vesicle-associated membrane protein-associated protein B (VAPB/ALS8). J. Biol. Chem. 281 (2006), 30223–30233.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30223-30233
    • Kanekura, K.1
  • 157
    • 84942985343 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and proteasomal system in amyotrophic lateral sclerosis
    • Karademir, B., Corek, C., Ozer, N.K., Endoplasmic reticulum stress and proteasomal system in amyotrophic lateral sclerosis. Free Radic. Biol. Med. 88 (2015), 42–50.
    • (2015) Free Radic. Biol. Med. , vol.88 , pp. 42-50
    • Karademir, B.1    Corek, C.2    Ozer, N.K.3
  • 158
    • 66049156169 scopus 로고    scopus 로고
    • Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
    • Karch, C.M., et al. Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc. Natl. Acad. Sci. 106 (2009), 7774–7779.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 7774-7779
    • Karch, C.M.1
  • 159
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels
    • Kato, M., et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell 149 (2012), 753–767.
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1
  • 160
    • 84954129051 scopus 로고    scopus 로고
    • p62/SQSTM1 functions as a signaling hub and an autophagy adaptor
    • Katsuragi, Y., Ichimura, Y., Komatsu, M., p62/SQSTM1 functions as a signaling hub and an autophagy adaptor. FEBS J. 282 (2015), 4672–4678.
    • (2015) FEBS J. , vol.282 , pp. 4672-4678
    • Katsuragi, Y.1    Ichimura, Y.2    Komatsu, M.3
  • 161
    • 84947552088 scopus 로고    scopus 로고
    • ALS patient stem cells for unveiling disease signatures of motoneuron susceptibility: perspectives on the deadly mitochondria, ER stress and calcium triad
    • Kaus, A., Sareen, D., ALS patient stem cells for unveiling disease signatures of motoneuron susceptibility: perspectives on the deadly mitochondria, ER stress and calcium triad. Front. Cell. Neurosci., 9, 2015.
    • (2015) Front. Cell. Neurosci. , vol.9
    • Kaus, A.1    Sareen, D.2
  • 162
    • 77951765013 scopus 로고    scopus 로고
    • Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species
    • Kayatekin, C., Zitzewitz, J.A., Matthews, C.R., Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species. J. Mol. Biol. 398 (2010), 320–331.
    • (2010) J. Mol. Biol. , vol.398 , pp. 320-331
    • Kayatekin, C.1    Zitzewitz, J.A.2    Matthews, C.R.3
  • 163
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran, D., et al. Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med. 10 (2004), 402–405.
    • (2004) Nat. Med. , vol.10 , pp. 402-405
    • Kieran, D.1
  • 164
    • 84875605133 scopus 로고    scopus 로고
    • Prion-like domain mutations in hnRNPs cause multisystem proteinopathy and ALS
    • Kim, H.J., et al. Prion-like domain mutations in hnRNPs cause multisystem proteinopathy and ALS. Nature, 495, 2013, 467.
    • (2013) Nature , vol.495 , pp. 467
    • Kim, H.J.1
  • 165
    • 84875605133 scopus 로고    scopus 로고
    • Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
    • Kim, H.J., et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 495 (2013), 467–473.
    • (2013) Nature , vol.495 , pp. 467-473
    • Kim, H.J.1
  • 166
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurin in amyotrophic lateral sclerosis
    • 223226Mattiazzi
    • Kinoshita, Y., et al. Mutations of optineurin in amyotrophic lateral sclerosis. Nature, 465, 2010 223226Mattiazzi.
    • (2010) Nature , vol.465
    • Kinoshita, Y.1
  • 167
    • 2442520399 scopus 로고    scopus 로고
    • Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains
    • Ko, H.S., et al. Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains. FEBS Lett. 566 (2004), 110–114.
    • (2004) FEBS Lett. , vol.566 , pp. 110-114
    • Ko, H.S.1
  • 168
    • 79951578639 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration
    • Koga, H., Cuervo, A.M., Chaperone-mediated autophagy dysfunction in the pathogenesis of neurodegeneration. Neurobiol. Dis. 43 (2011), 29–37.
    • (2011) Neurobiol. Dis. , vol.43 , pp. 29-37
    • Koga, H.1    Cuervo, A.M.2
  • 169
    • 84902253458 scopus 로고    scopus 로고
    • Balancing oxidative protein folding: the influences of reducing pathways on disulfide bond formation
    • Kojer, K., Riemer, J., Balancing oxidative protein folding: the influences of reducing pathways on disulfide bond formation. Biochim. Et Biophys. Acta (BBA) – Proteins Proteom. 1844 (2014), 1383–1390.
    • (2014) Biochim. Et Biophys. Acta (BBA) – Proteins Proteom. , vol.1844 , pp. 1383-1390
    • Kojer, K.1    Riemer, J.2
  • 170
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R.R., Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10 (2000), 524–530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 171
    • 84939653485 scopus 로고    scopus 로고
    • C9orf72 ablation in mice does not cause motor neuron degeneration or motor deficits
    • Koppers, M., et al. C9orf72 ablation in mice does not cause motor neuron degeneration or motor deficits. Ann. Neurol. 78 (2015), 426–438.
    • (2015) Ann. Neurol. , vol.78 , pp. 426-438
    • Koppers, M.1
  • 172
    • 34447531775 scopus 로고    scopus 로고
    • The Rab5 activator ALS2/alsin acts as a novel Rac1 effector through Rac1-activated endocytosis
    • Kunita, R., et al. The Rab5 activator ALS2/alsin acts as a novel Rac1 effector through Rac1-activated endocytosis. J. Biol. Chem. 282 (2007), 16599–16611.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16599-16611
    • Kunita, R.1
  • 173
    • 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 323 (2009), 1205–1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, T.J.1
  • 174
    • 84875991370 scopus 로고    scopus 로고
    • Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis
    • Kwok, C.T., et al. Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis. Free Radic. Biol. Med. 58 (2013), 81–86.
    • (2013) Free Radic. Biol. Med. , vol.58 , pp. 81-86
    • Kwok, C.T.1
  • 175
    • 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 345 (2014), 1139–1145.
    • (2014) Science , vol.345 , pp. 1139-1145
    • Kwon, I.1
  • 176
    • 84923189622 scopus 로고    scopus 로고
    • Marinesco-Sjogren syndrome protein SIL1 regulates motor neuron subtype-selective ER stress in ALS
    • de L'Etang, A.F., et al. Marinesco-Sjogren syndrome protein SIL1 regulates motor neuron subtype-selective ER stress in ALS. Nat. Neurosci. 18 (2015), 227–238.
    • (2015) Nat. Neurosci. , vol.18 , pp. 227-238
    • de L'Etang, A.F.1
  • 177
    • 39849107361 scopus 로고    scopus 로고
    • Motor neuron disease occurring in a mutant dynactin mouse model is characterized by defects in vesicular trafficking
    • Laird, F.M., et al. Motor neuron disease occurring in a mutant dynactin mouse model is characterized by defects in vesicular trafficking. J. Neurosci. 28 (2008), 1997–2005.
    • (2008) J. Neurosci. , vol.28 , pp. 1997-2005
    • Laird, F.M.1
  • 178
    • 41649090538 scopus 로고    scopus 로고
    • New VAPB deletion variant and exclusion of VAPB mutations in familial ALS
    • Landers, J., et al. New VAPB deletion variant and exclusion of VAPB mutations in familial ALS. Neurology 70 (2008), 1179–1185.
    • (2008) Neurology , vol.70 , pp. 1179-1185
    • Landers, J.1
  • 179
    • 79955878526 scopus 로고    scopus 로고
    • Reexamination of the role of interplay between glutathione and protein disulfide isomerase
    • Lappi, A.-K., Ruddock, L.W., Reexamination of the role of interplay between glutathione and protein disulfide isomerase. J. Mol. Biol. 409 (2011), 238–249.
    • (2011) J. Mol. Biol. , vol.409 , pp. 238-249
    • Lappi, A.-K.1    Ruddock, L.W.2
  • 180
    • 84991003298 scopus 로고    scopus 로고
    • Autophagy in Neurons a Review
    • Larsen, K., Sulzer, D., Autophagy in Neurons a Review. 2002.
    • (2002)
    • Larsen, K.1    Sulzer, D.2
  • 181
    • 0036094026 scopus 로고    scopus 로고
    • Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone
    • Laurin, N., et al. Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone. Am. J. Hum. Genet. 70 (2002), 1582–1588.
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 1582-1588
    • Laurin, N.1
  • 182
    • 84948714601 scopus 로고    scopus 로고
    • Uncoupling of protein aggregation and neurodegeneration in a mouse amyotrophic lateral sclerosis model
    • Lee, J.-Y., et al. Uncoupling of protein aggregation and neurodegeneration in a mouse amyotrophic lateral sclerosis model. Neurodegener. Dis. 15 (2015), 339–349.
    • (2015) Neurodegener. Dis. , vol.15 , pp. 339-349
    • Lee, J.-Y.1
  • 183
    • 8444242974 scopus 로고    scopus 로고
    • Bi-directional protein transport between the ER and Golgi
    • Lee, M.C., et al. Bi-directional protein transport between the ER and Golgi. Annu. Rev. Cell Dev. Biol. 20 (2004), 87–123.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 87-123
    • Lee, M.C.1
  • 184
    • 84890233174 scopus 로고    scopus 로고
    • Hexanucleotide repeats in ALS/FTD form length-dependent RNA foci, sequester RNA binding proteins, and are neurotoxic
    • Lee, Y.-B., et al. Hexanucleotide repeats in ALS/FTD form length-dependent RNA foci, sequester RNA binding proteins, and are neurotoxic. Cell Rep. 5 (2013), 1178–1186.
    • (2013) Cell Rep. , vol.5 , pp. 1178-1186
    • Lee, Y.-B.1
  • 185
    • 4143140690 scopus 로고    scopus 로고
    • A pathogenic peripherin gene mutation in a patient with amyotrophic lateral sclerosis
    • Leung, C.L., et al. A pathogenic peripherin gene mutation in a patient with amyotrophic lateral sclerosis. Brain Pathol. 14 (2004), 290–296.
    • (2004) Brain Pathol. , vol.14 , pp. 290-296
    • Leung, C.L.1
  • 186
    • 84874246696 scopus 로고    scopus 로고
    • The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs
    • Levine, T.P., et al. The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs. Bioinformatics 29 (2013), 499–503.
    • (2013) Bioinformatics , vol.29 , pp. 499-503
    • Levine, T.P.1
  • 187
    • 84877751491 scopus 로고    scopus 로고
    • Identity of endogenous NMDAR glycine site agonist in amygdala is determined by synaptic activity level
    • Li, Y., et al. Identity of endogenous NMDAR glycine site agonist in amygdala is determined by synaptic activity level. Nat. Commun., 4, 2013, 1760.
    • (2013) Nat. Commun. , vol.4 , pp. 1760
    • Li, Y.1
  • 188
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li, Y.R., et al. Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201 (2013), 361–372.
    • (2013) J. Cell Biol. , vol.201 , pp. 361-372
    • Li, Y.R.1
  • 189
    • 17844399774 scopus 로고    scopus 로고
    • Mutant superoxide dismutase disrupts cytoplasmic dynein in motor neurons
    • Ligon, L.A., et al. Mutant superoxide dismutase disrupts cytoplasmic dynein in motor neurons. Neuroreport 16 (2005), 533–536.
    • (2005) Neuroreport , vol.16 , pp. 533-536
    • Ligon, L.A.1
  • 190
    • 84876050570 scopus 로고    scopus 로고
    • Relationship between the proteasomal system and autophagy
    • Lilienbaum, A., Relationship between the proteasomal system and autophagy. Int. J. Biochem. Mol. Biol., 4, 2013, 1.
    • (2013) Int. J. Biochem. Mol. Biol. , vol.4 , pp. 1
    • Lilienbaum, A.1
  • 191
    • 47949093588 scopus 로고    scopus 로고
    • Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases
    • Lin, W.-L., Dickson, D.W., Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases. Acta Neuropathol. 116 (2008), 205–213.
    • (2008) Acta Neuropathol. , vol.116 , pp. 205-213
    • Lin, W.-L.1    Dickson, D.W.2
  • 192
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis
    • Ling, S.-C., Polymenidou, M., Cleveland, D.W., Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 79 (2013), 416–438.
    • (2013) Neuron , vol.79 , pp. 416-438
    • Ling, S.-C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 193
    • 69249121554 scopus 로고    scopus 로고
    • Lack of evidence of monomer/misfolded superoxide dismutase‐1 in sporadic amyotrophic lateral sclerosis
    • Liu, H.N., et al. Lack of evidence of monomer/misfolded superoxide dismutase‐1 in sporadic amyotrophic lateral sclerosis. Ann. Neurol. 66 (2009), 75–80.
    • (2009) Ann. Neurol. , vol.66 , pp. 75-80
    • Liu, H.N.1
  • 194
    • 18844444198 scopus 로고    scopus 로고
    • Elevation of the Hsp70 chaperone does not effect toxicity in mouse models of familial amyotrophic lateral sclerosis
    • Liu, J., et al. Elevation of the Hsp70 chaperone does not effect toxicity in mouse models of familial amyotrophic lateral sclerosis. J. Neurochem. 93 (2005), 875–882.
    • (2005) J. Neurochem. , vol.93 , pp. 875-882
    • Liu, J.1
  • 195
    • 84896298823 scopus 로고    scopus 로고
    • ALS-linked mutations enlarge TDP-43-enriched neuronal RNA granules in the dendritic arbor
    • Liu-Yesucevitz, L., et al. ALS-linked mutations enlarge TDP-43-enriched neuronal RNA granules in the dendritic arbor. J. Neurosci. 34 (2014), 4167–4174.
    • (2014) J. Neurosci. , vol.34 , pp. 4167-4174
    • Liu-Yesucevitz, L.1
  • 196
    • 0037044240 scopus 로고    scopus 로고
    • The overlap of amyotrophic lateral sclerosis and frontotemporal dementia
    • Lomen-Hoerth, C., Anderson, T., Miller, B., The overlap of amyotrophic lateral sclerosis and frontotemporal dementia. Neurology 59 (2002), 1077–1079.
    • (2002) Neurology , vol.59 , pp. 1077-1079
    • Lomen-Hoerth, C.1    Anderson, T.2    Miller, B.3
  • 197
    • 4143084861 scopus 로고    scopus 로고
    • Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS
    • Münch, C., et al. Point mutations of the p150 subunit of dynactin (DCTN1) gene in ALS. Neurology 63 (2004), 724–726.
    • (2004) Neurology , vol.63 , pp. 724-726
    • Münch, C.1
  • 198
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Münch, C., O'Brien, J., Bertolotti, A., Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc. Natl. Acad. Sci. 108 (2011), 3548–3553.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 3548-3553
    • Münch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 199
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie, I.R., et al. Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann. Neurol. 61 (2007), 427–434.
    • (2007) Ann. Neurol. , vol.61 , pp. 427-434
    • Mackenzie, I.R.1
  • 200
    • 79959615773 scopus 로고    scopus 로고
    • Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation
    • Mackenzie, I.R., et al. Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation. Acta Neuropathol. 122 (2011), 87–98.
    • (2011) Acta Neuropathol. , vol.122 , pp. 87-98
    • Mackenzie, I.R.1
  • 201
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie, I.R., Rademakers, R., Neumann, M., TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol. 9 (2010), 995–1007.
    • (2010) Lancet Neurol. , vol.9 , pp. 995-1007
    • Mackenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 202
    • 70449698510 scopus 로고    scopus 로고
    • TDP‐43 is consistently co-localized with ubiquitinated inclusions in sporadic and Guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations
    • Maekawa, S., et al. TDP‐43 is consistently co-localized with ubiquitinated inclusions in sporadic and Guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations. Neuropathology 29 (2009), 672–683.
    • (2009) Neuropathology , vol.29 , pp. 672-683
    • Maekawa, S.1
  • 203
    • 84960540425 scopus 로고    scopus 로고
    • ER strikes again: proteostasis dysfunction in ALS
    • Maharjan, N., Saxena, S., ER strikes again: proteostasis dysfunction in ALS. EMBO J., 2016, e201694117.
    • (2016) EMBO J. , pp. e201694117
    • Maharjan, N.1    Saxena, S.2
  • 204
    • 84911191807 scopus 로고    scopus 로고
    • Molecular chaperone dysfunction in neurodegenerative diseases and effects of curcumin
    • Maiti, P., et al. Molecular chaperone dysfunction in neurodegenerative diseases and effects of curcumin. BioMed Res. Int., 2014, 2014.
    • (2014) BioMed Res. Int. , vol.2014
    • Maiti, P.1
  • 205
    • 84858622829 scopus 로고    scopus 로고
    • Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study
    • Majounie, E., et al. Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study. Lancet Neurol. 11 (2012), 323–330.
    • (2012) Lancet Neurol. , vol.11 , pp. 323-330
    • Majounie, E.1
  • 206
    • 84990915099 scopus 로고    scopus 로고
    • Mitochondria and endoplasmic reticulum crosstalk in amyotrophic lateral sclerosis
    • Manfredi, G., Kawamata, H., Mitochondria and endoplasmic reticulum crosstalk in amyotrophic lateral sclerosis. Neurobiol. Dis., 2015.
    • (2015) Neurobiol. Dis.
    • Manfredi, G.1    Kawamata, H.2
  • 207
    • 84938740314 scopus 로고    scopus 로고
    • From Nucleation to Widespread Propagation: A Prion-like Concept for ALS
    • Virus Research
    • Maniecka, Z., Polymenidou, M., 2015. From Nucleation to Widespread Propagation: A Prion-like Concept for ALS. Virus Research.
    • (2015)
    • Maniecka, Z.1    Polymenidou, M.2
  • 208
    • 52549093192 scopus 로고    scopus 로고
    • Take the 'A' train: on fast tracks to the cell surface
    • Marie, M., et al. Take the 'A' train: on fast tracks to the cell surface. Cell. Mol. Life Sci.: CMLS 65 (2008), 2859–2874.
    • (2008) Cell. Mol. Life Sci.: CMLS , vol.65 , pp. 2859-2874
    • Marie, M.1
  • 209
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurin in amyotrophic lateral sclerosis
    • Maruyama, H., et al. Mutations of optineurin in amyotrophic lateral sclerosis. Nature 465 (2010), 223–226.
    • (2010) Nature , vol.465 , pp. 223-226
    • Maruyama, H.1
  • 210
    • 84890018230 scopus 로고    scopus 로고
    • ER dysfunction and protein folding stress in ALS
    • Matus, S., et al. ER dysfunction and protein folding stress in ALS. Int. J. Cell Biol., 2013, 2013.
    • (2013) Int. J. Cell Biol. , vol.2013
    • Matus, S.1
  • 211
    • 84930000577 scopus 로고    scopus 로고
    • C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration
    • May, S., et al. C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration. Acta Neuropathol. 128 (2014), 485–503.
    • (2014) Acta Neuropathol. , vol.128 , pp. 485-503
    • May, S.1
  • 212
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J.M., Fridovich, I., Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biolo. Chem. 244 (1969), 6049–6055.
    • (1969) J. Biolo. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 214
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer, H., Bug, M., Bremer, S., Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat. Cell Biol. 14 (2012), 117–123.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 215
    • 77952194773 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase
    • Mitchell, J., et al. Familial amyotrophic lateral sclerosis is associated with a mutation in D-amino acid oxidase. Proc. Natl. Acad. Sci. 107 (2010), 7556–7561.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 7556-7561
    • Mitchell, J.1
  • 216
    • 33749661651 scopus 로고    scopus 로고
    • Immunoreactivities of p62, an ubiqutin-binding protein, in the spinal anterior horn cells of patients with amyotrophic lateral sclerosis
    • Mizuno, Y., et al. Immunoreactivities of p62, an ubiqutin-binding protein, in the spinal anterior horn cells of patients with amyotrophic lateral sclerosis. J. Neurol. Sci. 249 (2006), 13–18.
    • (2006) J. Neurol. Sci. , vol.249 , pp. 13-18
    • Mizuno, Y.1
  • 217
    • 0024428392 scopus 로고
    • Focal accumulation of phosphorylated neurofilaments within anterior horn cell in familial amyotrophic lateral sclerosis
    • Mizusawa, H., et al. Focal accumulation of phosphorylated neurofilaments within anterior horn cell in familial amyotrophic lateral sclerosis. Acta Neuropathol. 79 (1989), 37–43.
    • (1989) Acta Neuropathol. , vol.79 , pp. 37-43
    • Mizusawa, H.1
  • 218
    • 84922632709 scopus 로고    scopus 로고
    • Quinary structure modulates protein stability in cells
    • Monteith, W.B., et al. Quinary structure modulates protein stability in cells. Proc. Natl. Acad. Sci. 112 (2015), 1739–1742.
    • (2015) Proc. Natl. Acad. Sci. , vol.112 , pp. 1739-1742
    • Monteith, W.B.1
  • 219
    • 84878900746 scopus 로고    scopus 로고
    • Inhibition of fast axonal transport by pathogenic SOD1 involves activation of p38 MAP kinase
    • Morfini, G.A., et al. Inhibition of fast axonal transport by pathogenic SOD1 involves activation of p38 MAP kinase. PloS One, 8, 2013, e65235.
    • (2013) PloS One , vol.8 , pp. e65235
    • Morfini, G.A.1
  • 221
    • 0034712857 scopus 로고    scopus 로고
    • D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor
    • Mothet, J.-P., et al. D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor. Proc. Natl. Acad. Sci. 97 (2000), 4926–4931.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 4926-4931
    • Mothet, J.-P.1
  • 222
    • 27644558934 scopus 로고    scopus 로고
    • Heterozygous R1101K mutation of the DCTN1 gene in a family with ALS and FTD
    • Munch, C., et al. Heterozygous R1101K mutation of the DCTN1 gene in a family with ALS and FTD. Ann. Neurol. 58 (2005), 777–780.
    • (2005) Ann. Neurol. , vol.58 , pp. 777-780
    • Munch, C.1
  • 223
    • 77249158951 scopus 로고    scopus 로고
    • Regulation of endocytic trafficking of transferrin receptor by optineurin and its impairment by a glaucoma-associated mutant
    • Nagabhushana, A., et al. Regulation of endocytic trafficking of transferrin receptor by optineurin and its impairment by a glaucoma-associated mutant. BMC Cell Biol., 11, 2010, 4.
    • (2010) BMC Cell Biol. , vol.11 , pp. 4
    • Nagabhushana, A.1
  • 224
    • 84925725817 scopus 로고    scopus 로고
    • Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases
    • Nakamura, T., et al. Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases. Neurobiol. Dis. 84 (2015), 99–108.
    • (2015) Neurobiol. Dis. , vol.84 , pp. 99-108
    • Nakamura, T.1
  • 225
    • 84953347508 scopus 로고    scopus 로고
    • Crosstalk between endoplasmic reticulum stress, oxidative stress, and autophagy: potential therapeutic targets for acute CNS injuries
    • Nakka, V.P., Prakash-babu, P., Vemuganti, R., Crosstalk between endoplasmic reticulum stress, oxidative stress, and autophagy: potential therapeutic targets for acute CNS injuries. Mol. Neurobiol. 53 (2016), 532–544.
    • (2016) Mol. Neurobiol. , vol.53 , pp. 532-544
    • Nakka, V.P.1    Prakash-babu, P.2    Vemuganti, R.3
  • 226
    • 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, 6, 2011, e25545.
    • (2011) PloS One , vol.6 , pp. e25545
    • Nardo, G.1
  • 227
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann, M., et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314 (2006), 130–133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1
  • 228
    • 79551689187 scopus 로고    scopus 로고
    • Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation
    • Nguyen, V.D., et al. Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation. J. Mol. Biol. 406 (2011), 503–515.
    • (2011) J. Mol. Biol. , vol.406 , pp. 503-515
    • Nguyen, V.D.1
  • 229
    • 6344257200 scopus 로고    scopus 로고
    • A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis
    • Nishimura, A.L., et al. A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am. J. Hum. Genet. 75 (2004), 822–831.
    • (2004) Am. J. Hum. Genet. , vol.75 , pp. 822-831
    • Nishimura, A.L.1
  • 230
    • 44849124411 scopus 로고    scopus 로고
    • ALS-linked mutant SOD1 induces ER stress-and ASK1-dependent motor neuron death by targeting Derlin-1
    • Nishitoh, H., et al. ALS-linked mutant SOD1 induces ER stress-and ASK1-dependent motor neuron death by targeting Derlin-1. Genes Dev. 22 (2008), 1451–1464.
    • (2008) Genes Dev. , vol.22 , pp. 1451-1464
    • Nishitoh, H.1
  • 231
    • 34948850962 scopus 로고    scopus 로고
    • Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1
    • Niwa, J.-I., et al. Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. J. Biol. Chem. 282 (2007), 28087–28095.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28087-28095
    • Niwa, J.-I.1
  • 232
    • 84885484356 scopus 로고    scopus 로고
    • Prion-like properties of pathological TDP-43 aggregates from diseased brains
    • Nonaka, T., et al. Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell Rep. 4 (2013), 124–134.
    • (2013) Cell Rep. , vol.4 , pp. 124-134
    • Nonaka, T.1
  • 233
    • 84883403943 scopus 로고    scopus 로고
    • Molecular chaperone mediated late-stage neuroprotection in the SOD1 (G93A) mouse model of amyotrophic lateral sclerosis
    • Novoselov, S.S., et al. Molecular chaperone mediated late-stage neuroprotection in the SOD1 (G93A) mouse model of amyotrophic lateral sclerosis. PloS One, 8, 2013, e73944.
    • (2013) PloS One , vol.8 , pp. e73944
    • Novoselov, S.S.1
  • 234
    • 33747371085 scopus 로고    scopus 로고
    • Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates
    • Nowis, D., McConnell, E., Wójcik, C., Destabilization of the VCP-Ufd1-Npl4 complex is associated with decreased levels of ERAD substrates. Exp. Cell Res. 312 (2006), 2921–2932.
    • (2006) Exp. Cell Res. , vol.312 , pp. 2921-2932
    • Nowis, D.1    McConnell, E.2    Wójcik, C.3
  • 236
    • 77249126425 scopus 로고    scopus 로고
    • SPATACSIN mutations cause autosomal recessive juvenile amyotrophic lateral sclerosis
    • awp325
    • Orlacchio, A., et al. SPATACSIN mutations cause autosomal recessive juvenile amyotrophic lateral sclerosis. Brain, 2010 awp325.
    • (2010) Brain
    • Orlacchio, A.1
  • 237
    • 0041308082 scopus 로고    scopus 로고
    • ALS2, a novel guanine nucleotide exchange factor for the small GTPase Rab5, is implicated in endosomal dynamics
    • Otomo, A., et al. ALS2, a novel guanine nucleotide exchange factor for the small GTPase Rab5, is implicated in endosomal dynamics. Hum. Mol. Genet. 12 (2003), 1671–1687.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1671-1687
    • Otomo, A.1
  • 238
    • 84929264163 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: mechanisms and therapeutics in the epigenomic era
    • Paez-Colasante, X., et al. Amyotrophic lateral sclerosis: mechanisms and therapeutics in the epigenomic era. Nat. Rev. Neurol. 11 (2015), 266–279.
    • (2015) Nat. Rev. Neurol. , vol.11 , pp. 266-279
    • Paez-Colasante, X.1
  • 239
    • 33646522699 scopus 로고    scopus 로고
    • Glia-derived D-serine controls NMDA receptor activity and synaptic memory
    • Panatier, A., et al. Glia-derived D-serine controls NMDA receptor activity and synaptic memory. Cell 125 (2006), 775–784.
    • (2006) Cell , vol.125 , pp. 775-784
    • Panatier, A.1
  • 240
    • 33745713871 scopus 로고    scopus 로고
    • The first ALS2 missense mutation associated with JPLS reveals new aspects of alsin biological function
    • Panzeri, C., et al. The first ALS2 missense mutation associated with JPLS reveals new aspects of alsin biological function. Brain 129 (2006), 1710–1719.
    • (2006) Brain , vol.129 , pp. 1710-1719
    • Panzeri, C.1
  • 241
    • 84875505629 scopus 로고    scopus 로고
    • Redox regulation in amyotrophic lateral sclerosis
    • Parakh, S., et al. Redox regulation in amyotrophic lateral sclerosis. Oxidative Med. Cell. Longev., 2013, 2013, 408681.
    • (2013) Oxidative Med. Cell. Longev. , vol.2013 , pp. 408681
    • Parakh, S.1
  • 242
    • 84983338291 scopus 로고    scopus 로고
    • Novel roles for protein disulphide isomerase in disease states: a double edged sword?
    • Parakh, S., Atkin, J., Novel roles for protein disulphide isomerase in disease states: a double edged sword?. Front. Cell Dev. Biol., 3, 2015.
    • (2015) Front. Cell Dev. Biol. , vol.3
    • Parakh, S.1    Atkin, J.2
  • 243
    • 84908032996 scopus 로고    scopus 로고
    • The heat-shock response co-inducer arimoclomol protects against retinal degeneration in rhodopsin retinitis pigmentosa
    • Parfitt, D., et al. The heat-shock response co-inducer arimoclomol protects against retinal degeneration in rhodopsin retinitis pigmentosa. Cell Death Dis., 5, 2014, e1236.
    • (2014) Cell Death Dis. , vol.5 , pp. e1236
    • Parfitt, D.1
  • 244
    • 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. 7 (2006), 710–723.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 245
    • 84945471407 scopus 로고    scopus 로고
    • Experimental approaches for elucidating co-agonist regulation of NMDA receptor in motor neurons: therapeutic implications for amyotrophic lateral sclerosis (ALS)
    • Paul, P., de Belleroche, J., Experimental approaches for elucidating co-agonist regulation of NMDA receptor in motor neurons: therapeutic implications for amyotrophic lateral sclerosis (ALS). J. Pharm. Biomed. Anal. 116 (2015), 2–6.
    • (2015) J. Pharm. Biomed. Anal. , vol.116 , pp. 2-6
    • Paul, P.1    de Belleroche, J.2
  • 246
    • 55549111249 scopus 로고    scopus 로고
    • Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport
    • Peretti, D., et al. Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport. Mol. Biol. cell 19 (2008), 3871–3884.
    • (2008) Mol. Biol. cell , vol.19 , pp. 3871-3884
    • Peretti, D.1
  • 247
    • 84963673231 scopus 로고    scopus 로고
    • The unfolded protein response and the role of protein disulphide isomerase in neurodegeneration
    • Perri, E., et al. The unfolded protein response and the role of protein disulphide isomerase in neurodegeneration. Front. Cell Dev. Biol., 3, 2015, 80.
    • (2015) Front. Cell Dev. Biol. , vol.3 , pp. 80
    • Perri, E.1
  • 248
    • 84949228570 scopus 로고    scopus 로고
    • Rodent models of amyotrophic lateral sclerosis
    • 67. 21
    • Philips, T., Rothstein, J.D., Rodent models of amyotrophic lateral sclerosis. Curr. Protoc. Pharmacol. 5:67 (2015), 1–5 67. 21.
    • (2015) Curr. Protoc. Pharmacol. , vol.5 , Issue.67 , pp. 1-5
    • Philips, T.1    Rothstein, J.D.2
  • 249
    • 0037251889 scopus 로고    scopus 로고
    • Neuropathology with clinical correlations of sporadic amyotrophic lateral sclerosis: 102 autopsy cases examined between 1962 and 2000
    • Piao, Y.S., et al. Neuropathology with clinical correlations of sporadic amyotrophic lateral sclerosis: 102 autopsy cases examined between 1962 and 2000. Brain Pathol. 13 (2003), 10–22.
    • (2003) Brain Pathol. , vol.13 , pp. 10-22
    • Piao, Y.S.1
  • 250
    • 84865357562 scopus 로고    scopus 로고
    • TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation
    • Pilli, M., et al. TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation. Immunity 37 (2012), 223–234.
    • (2012) Immunity , vol.37 , pp. 223-234
    • Pilli, M.1
  • 251
    • 68149100027 scopus 로고    scopus 로고
    • Treatment with lithium carbonate does not improve disease progression in two different strains of SOD1 mutant mice
    • Pizzasegola, C., et al. Treatment with lithium carbonate does not improve disease progression in two different strains of SOD1 mutant mice. Amyotroph. Lateral Scler. 10 (2009), 221–228.
    • (2009) Amyotroph. Lateral Scler. , vol.10 , pp. 221-228
    • Pizzasegola, C.1
  • 252
    • 84859512071 scopus 로고    scopus 로고
    • Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis
    • e35050–e35050
    • Pokrishevsky, E., et al. Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis. PloS One, 7, 2012 e35050–e35050.
    • (2012) PloS One , vol.7
    • Pokrishevsky, E.1
  • 253
    • 84863808563 scopus 로고    scopus 로고
    • Prion-like spread of protein aggregates in neurodegeneration
    • Polymenidou, M., Cleveland, D.W., Prion-like spread of protein aggregates in neurodegeneration. J. Exp. Med. 209 (2012), 889–893.
    • (2012) J. Exp. Med. , vol.209 , pp. 889-893
    • Polymenidou, M.1    Cleveland, D.W.2
  • 254
    • 84857953079 scopus 로고    scopus 로고
    • The unfolded protein response in models of human mutant G93A amyotrophic lateral sclerosis
    • Prell, T., et al. The unfolded protein response in models of human mutant G93A amyotrophic lateral sclerosis. Eur. J. Neurosci. 35 (2012), 652–660.
    • (2012) Eur. J. Neurosci. , vol.35 , pp. 652-660
    • Prell, T.1
  • 255
    • 0037382240 scopus 로고    scopus 로고
    • Mutant dynactin in motor neuron disease
    • Puls, I., et al. Mutant dynactin in motor neuron disease. Nat. Genet. 33 (2003), 455–456.
    • (2003) Nat. Genet. , vol.33 , pp. 455-456
    • Puls, I.1
  • 256
    • 20944448536 scopus 로고    scopus 로고
    • Distal spinal and bulbar muscular atrophy caused by dynactin mutation
    • Puls, I., et al. Distal spinal and bulbar muscular atrophy caused by dynactin mutation. Ann. Neurol. 57 (2005), 687–694.
    • (2005) Ann. Neurol. , vol.57 , pp. 687-694
    • Puls, I.1
  • 257
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
    • Quan, H., Fan, G., Wang, C.-C., Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J. Biol. Chem. 270 (1995), 17078–17080.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17078-17080
    • Quan, H.1    Fan, G.2    Wang, C.-C.3
  • 258
    • 84991000537 scopus 로고    scopus 로고
    • Protein misfolding and aggregation in neurodegenerative disorders: focus on chaperone-mediated protein folding machinery
    • Raj, K., Chanu, S.I., Sarkar, S., Protein misfolding and aggregation in neurodegenerative disorders: focus on chaperone-mediated protein folding machinery. Int. J. Neurol. Res. 1 (2015), 72–78.
    • (2015) Int. J. Neurol. Res. , vol.1 , pp. 72-78
    • Raj, K.1    Chanu, S.I.2    Sarkar, S.3
  • 259
    • 0037461350 scopus 로고    scopus 로고
    • Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation
    • Raje, S., Thorpe, C., Inter-domain redox communication in flavoenzymes of the quiescin/sulfhydryl oxidase family: role of a thioredoxin domain in disulfide bond formation. Biochemistry 42 (2003), 4560–4568.
    • (2003) Biochemistry , vol.42 , pp. 4560-4568
    • Raje, S.1    Thorpe, C.2
  • 260
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM)
    • Raturi, A., Simmen, T., Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM). Biochim. Et Biophys. Acta (BBA) – Mol. Cell Res. 1833 (2013), 213–224.
    • (2013) Biochim. Et Biophys. Acta (BBA) – Mol. Cell Res. , vol.1833 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 261
    • 84877871521 scopus 로고    scopus 로고
    • Deciphering amyotrophic lateral sclerosis: what phenotype, neuropathology and genetics are telling us about pathogenesis
    • Ravits, J., et al. Deciphering amyotrophic lateral sclerosis: what phenotype, neuropathology and genetics are telling us about pathogenesis. Amyotroph. Lateral Scler. Front. Degener. 14 (2013), 5–18.
    • (2013) Amyotroph. Lateral Scler. Front. Degener. , vol.14 , pp. 5-18
    • Ravits, J.1
  • 262
    • 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 72 (2011), 257–268.
    • (2011) Neuron , vol.72 , pp. 257-268
    • Renton, A.E.1
  • 263
    • 84865079772 scopus 로고    scopus 로고
    • Protein misfolding and degenerative diseases
    • Reynaud, E., Protein misfolding and degenerative diseases. Nat. Educ., 3, 2010, 28.
    • (2010) Nat. Educ. , vol.3 , pp. 28
    • Reynaud, E.1
  • 264
    • 84875441083 scopus 로고    scopus 로고
    • The changing scene of amyotrophic lateral sclerosis
    • Robberecht, W., Philips, T., The changing scene of amyotrophic lateral sclerosis. Nat. Rev. Neurosc. 14 (2013), 248–264.
    • (2013) Nat. Rev. Neurosc. , vol.14 , pp. 248-264
    • Robberecht, W.1    Philips, T.2
  • 265
    • 84875441083 scopus 로고    scopus 로고
    • The changing scene of amyotrophic lateral sclerosis
    • Robberecht, W., Philips, T., The changing scene of amyotrophic lateral sclerosis. Nat. Rev. Neurosci. 14 (2013), 248–264.
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 248-264
    • Robberecht, W.1    Philips, T.2
  • 266
    • 84991000532 scopus 로고    scopus 로고
    • Role of Disulfide Cross-linking Of Mutant SOD1 in the Formation of Inclusion-Body-Like Structures
    • Roberts, B.L., et al. Role of Disulfide Cross-linking Of Mutant SOD1 in the Formation of Inclusion-Body-Like Structures. 2012.
    • (2012)
    • Roberts, B.L.1
  • 267
    • 84991013337 scopus 로고    scopus 로고
    • The endoplasmic reticulum unfolded protein response and neurodegeneration
    • In: vol., ed.^eds. Springer
    • Ron, D., 2013. The endoplasmic reticulum unfolded protein response and neurodegeneration. In: Protein Quality Control in Neurodegenerative Diseases, vol., ed.^eds. Springer, pp. 19–35.
    • (2013) Protein Quality Control in Neurodegenerative Diseases , pp. 19-35
    • Ron, D.1
  • 268
    • 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 362 (1993), 59–62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1
  • 269
    • 84890890208 scopus 로고    scopus 로고
    • An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis
    • Rotunno, M.S., Bosco, D.A., An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis. Front. Cell. Neurosci., 7, 2013.
    • (2013) Front. Cell. Neurosci. , vol.7
    • Rotunno, M.S.1    Bosco, D.A.2
  • 270
    • 84859226465 scopus 로고    scopus 로고
    • Low-molecular-weight oxidants involved in disulfide bond formation
    • Ruddock, L.W., Low-molecular-weight oxidants involved in disulfide bond formation. Antioxid. Redox Signal. 16 (2012), 1129–1138.
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 1129-1138
    • Ruddock, L.W.1
  • 271
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford, N.J., et al. Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet., 4, 2008, e1000193.
    • (2008) PLoS Genet. , vol.4 , pp. e1000193
    • Rutherford, N.J.1
  • 272
    • 84911386329 scopus 로고    scopus 로고
    • Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons
    • Ryu, H.-H., et al. Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons. Neurobiol. Aging 35 (2014), 2822–2831.
    • (2014) Neurobiol. Aging , vol.35 , pp. 2822-2831
    • Ryu, H.-H.1
  • 273
    • 84880956773 scopus 로고    scopus 로고
    • Is SOD1 loss of function involved in amyotrophic lateral sclerosis?
    • awt097
    • Saccon, R.A., et al. Is SOD1 loss of function involved in amyotrophic lateral sclerosis?. Brain 136 (2013), 2342–2358 awt097.
    • (2013) Brain , vol.136 , pp. 2342-2358
    • Saccon, R.A.1
  • 274
    • 79960167259 scopus 로고    scopus 로고
    • Selective neuronal vulnerability in neurodegenerative diseases: from stressor thresholds to degeneration
    • Saxena, S., Caroni, P., Selective neuronal vulnerability in neurodegenerative diseases: from stressor thresholds to degeneration. Neuron 71 (2011), 35–48.
    • (2011) Neuron , vol.71 , pp. 35-48
    • Saxena, S.1    Caroni, P.2
  • 275
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype–selective ER stress in disease manifestations of FALS mice
    • Saxena, S., Cabuy, E., Caroni, P., A role for motoneuron subtype–selective ER stress in disease manifestations of FALS mice. Nat. Neurosci. 12 (2009), 627–636.
    • (2009) Nat. Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 276
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U., et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404 (2000), 770–774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1
  • 277
    • 0004153150 scopus 로고    scopus 로고
    • Principles of Protein Structure
    • Springer Science & Business Media Germany
    • Schulz, G.E., Schirmer, R.H., Principles of Protein Structure. 2013, Springer Science & Business Media, Germany.
    • (2013)
    • Schulz, G.E.1    Schirmer, R.H.2
  • 278
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener, M.L., et al. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol. 24 (2004), 8055–8068.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1
  • 279
    • 84944175522 scopus 로고    scopus 로고
    • Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes
    • Sin, O., Nollen, E.A.A., Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes. Cell. Mol. Life Sci. 72 (2015), 4027–4047.
    • (2015) Cell. Mol. Life Sci. , vol.72 , pp. 4027-4047
    • Sin, O.1    Nollen, E.A.A.2
  • 280
    • 23044471011 scopus 로고    scopus 로고
    • Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia
    • Skibinski, G., et al. Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia. Nat. Genet. 37 (2005), 806–808.
    • (2005) Nat. Genet. , vol.37 , pp. 806-808
    • Skibinski, G.1
  • 281
    • 0033964710 scopus 로고    scopus 로고
    • From genes to protein structure and function: novel applications of computational approaches in the genomic era
    • Skolnick, J., Fetrow, J.S., From genes to protein structure and function: novel applications of computational approaches in the genomic era. Trends Biotechnol. 18 (2000), 34–39.
    • (2000) Trends Biotechnol. , vol.18 , pp. 34-39
    • Skolnick, J.1    Fetrow, J.S.2
  • 282
    • 0037423187 scopus 로고    scopus 로고
    • ATPase activity of p97-valosin-containing protein (VCP) D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
    • Song, C., Wang, Q., Li, C.-C.H., ATPase activity of p97-valosin-containing protein (VCP) D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity. J. Biol. Chem. 278 (2003), 3648–3655.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3648-3655
    • Song, C.1    Wang, Q.2    Li, C.-C.H.3
  • 283
    • 84975275228 scopus 로고    scopus 로고
    • Autophagy dysregulation by mutant fused in sarcoma—implications for amyotrophic lateral sclerosis
    • Soo, K., Atkin, J., Autophagy dysregulation by mutant fused in sarcoma—implications for amyotrophic lateral sclerosis. Cell Death Dis., 6, 2015, e1945.
    • (2015) Cell Death Dis. , vol.6 , pp. e1945
    • Soo, K.1    Atkin, J.2
  • 284
    • 84859867839 scopus 로고    scopus 로고
    • Bim links ER stress and apoptosis in cells expressing mutant SOD1 associated with amyotrophic lateral sclerosis
    • Soo, K.Y., et al. Bim links ER stress and apoptosis in cells expressing mutant SOD1 associated with amyotrophic lateral sclerosis. PLoS One, 7, 2012, e35413.
    • (2012) PLoS One , vol.7 , pp. e35413
    • Soo, K.Y.1
  • 285
    • 84945492093 scopus 로고    scopus 로고
    • Rab1-dependent ER–Golgi transport dysfunction is a common pathogenic mechanism in SOD1, TDP-43 and FUS-associated ALS
    • Soo, K.Y., et al. Rab1-dependent ER–Golgi transport dysfunction is a common pathogenic mechanism in SOD1, TDP-43 and FUS-associated ALS. Acta Neuropathol., 2015, 1–19.
    • (2015) Acta Neuropathol. , pp. 1-19
    • Soo, K.Y.1
  • 286
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C., Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4 (2003), 49–60.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 287
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurodegeneration
    • Soto, C., Estrada, L.D., Protein misfolding and neurodegeneration. Arch. Neurol. 65 (2008), 184–189.
    • (2008) Arch. Neurol. , vol.65 , pp. 184-189
    • Soto, C.1    Estrada, L.D.2
  • 288
    • 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 319 (2008), 1668–1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1
  • 289
    • 33847298447 scopus 로고    scopus 로고
    • Mutations in SPG11, encoding spatacsin, are a major cause of spastic paraplegia with thin corpus callosum
    • Stevanin, G., et al. Mutations in SPG11, encoding spatacsin, are a major cause of spastic paraplegia with thin corpus callosum. Nat. Genet. 39 (2007), 366–372.
    • (2007) Nat. Genet. , vol.39 , pp. 366-372
    • Stevanin, G.1
  • 290
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Sun, Z., et al. Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol., 9, 2011, e1000614.
    • (2011) PLoS Biol. , vol.9 , pp. e1000614
    • Sun, Z.1
  • 291
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Sun, Z., et al. Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol., 9, 2011, e1000614.
    • (2011) PLoS Biol. , vol.9 , pp. e1000614
    • Sun, Z.1
  • 292
    • 84887069357 scopus 로고    scopus 로고
    • Extracellular wildtype and mutant SOD1 induces ER–Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells
    • Sundaramoorthy, V., et al. Extracellular wildtype and mutant SOD1 induces ER–Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells. Cell. Mol. Life Sci. 70 (2013), 4181–4195.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 4181-4195
    • Sundaramoorthy, V.1
  • 293
    • 84936752124 scopus 로고    scopus 로고
    • Defects in optineurin and myosin VI mediated cellular trafficking in amyotrophic lateral sclerosis
    • ddv126
    • Sundaramoorthy, V., et al. Defects in optineurin and myosin VI mediated cellular trafficking in amyotrophic lateral sclerosis. Hum. Mol. Genet. 24 (2015), 3830–3846 ddv126.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 3830-3846
    • Sundaramoorthy, V.1
  • 294
    • 84946574062 scopus 로고    scopus 로고
    • Golgi fragmentation in amyotrophic lateral sclerosis, an overview of possible triggers and consequences
    • Sundaramoorthy, V., Sultana, J.M., Atkin, J.D., Golgi fragmentation in amyotrophic lateral sclerosis, an overview of possible triggers and consequences. Front. Neurosci., 9, 2015.
    • (2015) Front. Neurosci. , vol.9
    • Sundaramoorthy, V.1    Sultana, J.M.2    Atkin, J.D.3
  • 295
    • 84980052506 scopus 로고    scopus 로고
    • Protein aggregation and degradation mechanisms in neurodegenerative diseases
    • Takalo, M., et al. Protein aggregation and degradation mechanisms in neurodegenerative diseases. Am. J. Neurodegener. Dis., 2, 2013, 1.
    • (2013) Am. J. Neurodegener. Dis. , vol.2 , pp. 1
    • Takalo, M.1
  • 296
    • 60549104791 scopus 로고    scopus 로고
    • Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3
    • Tateno, M., et al. Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3. Hum. Mol. Genet. 18 (2009), 942–955.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 942-955
    • Tateno, M.1
  • 297
    • 34848904785 scopus 로고    scopus 로고
    • Motor neuron disease-associated mutant vesicle-associated membrane protein-associated protein (VAP) B recruits wild-type VAPs into endoplasmic reticulum-derived tubular aggregates
    • Teuling, E., et al. Motor neuron disease-associated mutant vesicle-associated membrane protein-associated protein (VAP) B recruits wild-type VAPs into endoplasmic reticulum-derived tubular aggregates. J. Neurosci. 27 (2007), 9801–9815.
    • (2007) J. Neurosci. , vol.27 , pp. 9801-9815
    • Teuling, E.1
  • 298
    • 84876533723 scopus 로고    scopus 로고
    • Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology
    • Teyssou, E., et al. Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology. Acta Neuropathol. 125 (2013), 511–522.
    • (2013) Acta Neuropathol. , vol.125 , pp. 511-522
    • Teyssou, E.1
  • 299
    • 79952585425 scopus 로고    scopus 로고
    • Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis
    • Ticozzi, N., et al. Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis. Am. J. Med. Genet. Part B: Neuropsychiatr. Genet. 156 (2011), 285–290.
    • (2011) Am. J. Med. Genet. Part B: Neuropsychiatr. Genet. , vol.156 , pp. 285-290
    • Ticozzi, N.1
  • 300
    • 43449099127 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors
    • Tsuda, H., et al. The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell 133 (2008), 963–977.
    • (2008) Cell , vol.133 , pp. 963-977
    • Tsuda, H.1
  • 301
    • 43449099127 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors
    • Tsuda, H., et al. The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell 133 (2008), 963–977.
    • (2008) Cell , vol.133 , pp. 963-977
    • Tsuda, H.1
  • 302
    • 33646176558 scopus 로고    scopus 로고
    • ER stress and UPR in familial amyotrophic lateral sclerosis
    • Turner, B.J., Atkin, J.D., ER stress and UPR in familial amyotrophic lateral sclerosis. Curr. Mol. Med. 6 (2006), 79–86.
    • (2006) Curr. Mol. Med. , vol.6 , pp. 79-86
    • Turner, B.J.1    Atkin, J.D.2
  • 303
    • 33745315287 scopus 로고    scopus 로고
    • S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara, T., et al. S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 441 (2006), 513–517.
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1
  • 306
    • 84877075803 scopus 로고    scopus 로고
    • Pharmacological reduction of ER stress protects against TDP-43 neuronal toxicity in vivo
    • Vaccaro, A., et al. Pharmacological reduction of ER stress protects against TDP-43 neuronal toxicity in vivo. Neurobiol. Dis. 55 (2013), 64–75.
    • (2013) Neurobiol. Dis. , vol.55 , pp. 64-75
    • Vaccaro, A.1
  • 307
    • 84892408458 scopus 로고    scopus 로고
    • Mechanisms of protein-folding diseases at a glance
    • Valastyan, J.S., Lindquist, S., Mechanisms of protein-folding diseases at a glance. Dis. Model. Mech. 7 (2014), 9–14.
    • (2014) Dis. Model. Mech. , vol.7 , pp. 9-14
    • Valastyan, J.S.1    Lindquist, S.2
  • 308
    • 22244479388 scopus 로고    scopus 로고
    • Copper–zinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine, J.S., Doucette, P.A., Zittin Potter, S., Copper–zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem. 74 (2005), 563–593.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 309
    • 41949100148 scopus 로고    scopus 로고
    • TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis
    • Van Deerlin, V.M., et al. TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis. Lancet Neurol. 7 (2008), 409–416.
    • (2008) Lancet Neurol. , vol.7 , pp. 409-416
    • Van Deerlin, V.M.1
  • 310
    • 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 323 (2009), 1208–1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1
  • 311
    • 79960276613 scopus 로고    scopus 로고
    • Decreased glutathione accelerates neurological deficit and mitochondrial pathology in familial ALS-linked hSOD1 G93A mice model
    • Vargas, M.R., Johnson, D.A., Johnson, J.A., Decreased glutathione accelerates neurological deficit and mitochondrial pathology in familial ALS-linked hSOD1 G93A mice model. Neurobiol. Dis. 43 (2011), 543–551.
    • (2011) Neurobiol. Dis. , vol.43 , pp. 543-551
    • Vargas, M.R.1    Johnson, D.A.2    Johnson, J.A.3
  • 312
    • 84859718510 scopus 로고    scopus 로고
    • Lithium lacks effect on survival in amyotrophic lateral sclerosis: a phase IIb randomised sequential trial
    • Verstraete, E., et al. Lithium lacks effect on survival in amyotrophic lateral sclerosis: a phase IIb randomised sequential trial. J. Neurol., Neurosurg. Psychiatry 83 (2012), 557–564.
    • (2012) J. Neurol., Neurosurg. Psychiatry , vol.83 , pp. 557-564
    • Verstraete, E.1
  • 313
    • 57149130824 scopus 로고    scopus 로고
    • AAA ATPase p97/VCP: cellular functions, disease and therapeutic potential
    • Vij, N., AAA ATPase p97/VCP: cellular functions, disease and therapeutic potential. J. Cell. Mol. Med. 12 (2008), 2511–2518.
    • (2008) J. Cell. Mol. Med. , vol.12 , pp. 2511-2518
    • Vij, N.1
  • 314
    • 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. 1305 (2009), 168–182.
    • (2009) Brain Res. , vol.1305 , pp. 168-182
    • Volkening, K.1
  • 315
    • 0028208495 scopus 로고
    • Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes
    • Volterra, A., et al. Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14 (1994), 2924–2932.
    • (1994) J. Neurosci. , vol.14 , pp. 2924-2932
    • Volterra, A.1
  • 316
    • 74249084267 scopus 로고    scopus 로고
    • Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis
    • Walker, A.K., et al. Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis. Brain 133 (2010), 105–116.
    • (2010) Brain , vol.133 , pp. 105-116
    • Walker, A.K.1
  • 317
    • 84896710448 scopus 로고    scopus 로고
    • ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation
    • Walker, A.K., et al. ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PloS One, 8, 2013, e81170.
    • (2013) PloS One , vol.8 , pp. e81170
    • Walker, A.K.1
  • 318
    • 80052081196 scopus 로고    scopus 로고
    • Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis
    • Walker, A.K., Atkin, J.D., Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis. IUBMB Life 63 (2011), 754–763.
    • (2011) IUBMB Life , vol.63 , pp. 754-763
    • Walker, A.K.1    Atkin, J.D.2
  • 319
    • 33645108336 scopus 로고    scopus 로고
    • Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra-and intermolecular disulfide bonding in aggregation
    • Wang, J., Xu, G., Borchelt, D.R., Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra-and intermolecular disulfide bonding in aggregation. J. Neurochem. 96 (2006), 1277–1288.
    • (2006) J. Neurochem. , vol.96 , pp. 1277-1288
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 320
    • 84887465759 scopus 로고    scopus 로고
    • Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding
    • Wang, L., et al. Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding. Antioxid. Redox Signal. 20 (2014), 545–556.
    • (2014) Antioxid. Redox Signal. , vol.20 , pp. 545-556
    • Wang, L.1
  • 321
    • 84929330695 scopus 로고    scopus 로고
    • Protein disulfide–isomerase, a folding catalyst and a redox-regulated chaperone
    • Wang, L., Wang, X., Wang, C.-c, Protein disulfide–isomerase, a folding catalyst and a redox-regulated chaperone. Free Radic. Biol. Med. 83 (2015), 305–313.
    • (2015) Free Radic. Biol. Med. , vol.83 , pp. 305-313
    • Wang, L.1    Wang, X.2    Wang, C.-C.3
  • 322
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe, M., et al. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol. Dis. 8 (2001), 933–941.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 933-941
    • Watanabe, M.1
  • 323
    • 20544471158 scopus 로고    scopus 로고
    • ER-to-Golgi transport: form and formation of vesicular and tubular carriers
    • Watson, P., Stephens, D.J., ER-to-Golgi transport: form and formation of vesicular and tubular carriers. Biochim. Et Biophys. Acta (BBA) – Mol. Cell Res. 1744 (2005), 304–315.
    • (2005) Biochim. Et Biophys. Acta (BBA) – Mol. Cell Res. , vol.1744 , pp. 304-315
    • Watson, P.1    Stephens, D.J.2
  • 324
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts, G.D., et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat. Genet. 36 (2004), 377–381.
    • (2004) Nat. Genet. , vol.36 , pp. 377-381
    • Watts, G.D.1
  • 325
    • 80052197913 scopus 로고    scopus 로고
    • TBK1 mediates crosstalk between the innate immune response and autophagy
    • pe39–pe39
    • Weidberg, H., Elazar, Z., TBK1 mediates crosstalk between the innate immune response and autophagy. Sci. Signal., 4, 2011 pe39–pe39.
    • (2011) Sci. Signal. , vol.4
    • Weidberg, H.1    Elazar, Z.2
  • 326
    • 84899869014 scopus 로고    scopus 로고
    • Motor cortex glutathione deficit in ALS measured in vivo with the J-editing technique
    • Weiduschat, N., et al. Motor cortex glutathione deficit in ALS measured in vivo with the J-editing technique. Neurosci. Lett. 570 (2014), 102–107.
    • (2014) Neurosci. Lett. , vol.570 , pp. 102-107
    • Weiduschat, N.1
  • 327
    • 31144470450 scopus 로고    scopus 로고
    • Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation
    • Weihl, C.C., et al. Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation. Hum. Mol. Genet. 15 (2006), 189–199.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 189-199
    • Weihl, C.C.1
  • 328
    • 84866883258 scopus 로고    scopus 로고
    • Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity
    • Weisberg, S.J., et al. Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity. Proc. Natl. Acad. Sci. 109 (2012), 15811–15816.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 15811-15816
    • Weisberg, S.J.1
  • 329
    • 84926357619 scopus 로고    scopus 로고
    • Antisense proline-arginine RAN dipeptides linked to C9ORF72-ALS/FTD form toxic nuclear aggregates that initiate in vitro and in vivo neuronal death
    • Wen, X., et al. Antisense proline-arginine RAN dipeptides linked to C9ORF72-ALS/FTD form toxic nuclear aggregates that initiate in vitro and in vivo neuronal death. Neuron 84 (2014), 1213–1225.
    • (2014) Neuron , vol.84 , pp. 1213-1225
    • Wen, X.1
  • 330
    • 84864380051 scopus 로고    scopus 로고
    • UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis
    • e3-2527. e10
    • Williams, K.L., et al. UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis. Neurobiol. Aging, 33, 2012, 2527 e3-2527. e10.
    • (2012) Neurobiol. Aging , vol.33 , pp. 2527
    • Williams, K.L.1
  • 331
    • 0033366384 scopus 로고    scopus 로고
    • Slowing of axonal transport is a very early event in the toxicity of ALS–linked SOD1 mutants to motor neurons
    • Williamson, T.L., Cleveland, D.W., Slowing of axonal transport is a very early event in the toxicity of ALS–linked SOD1 mutants to motor neurons. Nat. Neurosci. 2 (1999), 50–56.
    • (1999) Nat. Neurosci. , vol.2 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 332
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton, M.J., et al. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 283 (2008), 13302–13309.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13302-13309
    • Winton, M.J.1
  • 333
    • 84958594182 scopus 로고    scopus 로고
    • ALS-linked protein disulfide isomerase variants cause motor dysfunction
    • Woehlbier, U., et al. ALS-linked protein disulfide isomerase variants cause motor dysfunction. EMBO J., 2016, e201592224.
    • (2016) EMBO J. , pp. e201592224
    • Woehlbier, U.1
  • 334
    • 18544394748 scopus 로고    scopus 로고
    • RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis
    • Wojcik, C., Yano, M., DeMartino, G.N., RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis. J. Cell Sci. 117 (2004), 281–292.
    • (2004) J. Cell Sci. , vol.117 , pp. 281-292
    • Wojcik, C.1    Yano, M.2    DeMartino, G.N.3
  • 335
    • 48249084875 scopus 로고    scopus 로고
    • Autophagy-mediated clearance of aggresomes is not a universal phenomenon
    • Wong, E.S., et al. Autophagy-mediated clearance of aggresomes is not a universal phenomenon. Hum. Mol. Genet. 17 (2008), 2570–2582.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2570-2582
    • Wong, E.S.1
  • 337
    • 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 488 (2012), 499–503.
    • (2012) Nature , vol.488 , pp. 499-503
    • Wu, C.-H.1
  • 338
    • 84963698905 scopus 로고    scopus 로고
    • Polymorphisms in protein disulfide isomerase are associated with sporadic amyotrophic lateral sclerosis in the Chinese Han population
    • Yang, Q., Guo, Z.-b, Polymorphisms in protein disulfide isomerase are associated with sporadic amyotrophic lateral sclerosis in the Chinese Han population. Int. J. Neurosci., 2015, 1–5.
    • (2015) Int. J. Neurosci. , pp. 1-5
    • Yang, Q.1    Guo, Z.-B.2
  • 339
    • 77955093329 scopus 로고    scopus 로고
    • Fused in sarcoma/translocated in liposarcoma: a multifunctional DNA/RNA binding protein
    • Yang, S., et al. Fused in sarcoma/translocated in liposarcoma: a multifunctional DNA/RNA binding protein. Int. J. Biochem. Cell Biol. 42 (2010), 1408–1411.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 1408-1411
    • Yang, S.1
  • 340
    • 0034785509 scopus 로고    scopus 로고
    • The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis
    • Yang, Y., et al. The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis. Nat. Genet. 29 (2001), 160–165.
    • (2001) Nat. Genet. , vol.29 , pp. 160-165
    • Yang, Y.1
  • 341
    • 70449377144 scopus 로고    scopus 로고
    • Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis
    • Yang, Y.S., Harel, N.Y., Strittmatter, S.M., Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis. J. Neurosci. 29 (2009), 13850–13859.
    • (2009) J. Neurosci. , vol.29 , pp. 13850-13859
    • Yang, Y.S.1    Harel, N.Y.2    Strittmatter, S.M.3
  • 342
    • 77949455790 scopus 로고    scopus 로고
    • Posttranslational modifications, localization, and protein interactions of optineurin, the product of a glaucoma gene
    • Ying, H., et al. Posttranslational modifications, localization, and protein interactions of optineurin, the product of a glaucoma gene. PLoS One, 5, 2010, e9168.
    • (2010) PLoS One , vol.5 , pp. e9168
    • Ying, H.1
  • 343
    • 84929145298 scopus 로고    scopus 로고
    • Induction of autophagy in rats upon overexpression of wild-type and mutant optineurin gene
    • Ying, H., et al. Induction of autophagy in rats upon overexpression of wild-type and mutant optineurin gene. BMC Cell Biol., 16, 2015, 14.
    • (2015) BMC Cell Biol. , vol.16 , pp. 14
    • Ying, H.1
  • 344
    • 84951909061 scopus 로고    scopus 로고
    • Optineurin: the autophagy connection
    • Ying, H., Yue, B.Y., Optineurin: the autophagy connection. Exp. Eye Res. 144 (2016), 73–80.
    • (2016) Exp. Eye Res. , vol.144 , pp. 73-80
    • Ying, H.1    Yue, B.Y.2
  • 345
    • 84980052653 scopus 로고    scopus 로고
    • C9ORF72 hexanucleotide repeats in behavioral and motor neuron disease: clinical heterogeneity and pathological diversity
    • Yokoyama, J.S., Sirkis, D.W., Miller, B.L., C9ORF72 hexanucleotide repeats in behavioral and motor neuron disease: clinical heterogeneity and pathological diversity. Am. J. Neurodegener. Dis., 3, 2014, 1.
    • (2014) Am. J. Neurodegener. Dis. , vol.3 , pp. 1
    • Yokoyama, J.S.1    Sirkis, D.W.2    Miller, B.L.3
  • 346
    • 33748786259 scopus 로고    scopus 로고
    • Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein
    • Zakaryan, R.P., Gehring, H., Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein. J. Mol. Biol. 363 (2006), 27–38.
    • (2006) J. Mol. Biol. , vol.363 , pp. 27-38
    • Zakaryan, R.P.1    Gehring, H.2
  • 347
    • 0036667555 scopus 로고    scopus 로고
    • Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
    • Zelko, I.N., Mariani, T.J., Folz, R.J., Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 33 (2002), 337–349.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 337-349
    • Zelko, I.N.1    Mariani, T.J.2    Folz, R.J.3
  • 348
    • 84922459192 scopus 로고    scopus 로고
    • Opposing roles of p38 and JNK in a Drosophila model of TDP-43 proteinopathy reveal oxidative stress and innate immunity as pathogenic components of neurodegeneration
    • ddu493
    • Zhan, L., Xie, Q., Tibbetts, R.S., Opposing roles of p38 and JNK in a Drosophila model of TDP-43 proteinopathy reveal oxidative stress and innate immunity as pathogenic components of neurodegeneration. Hum. Mol. Genet. 24 (2014), 757–772 ddu493.
    • (2014) Hum. Mol. Genet. , vol.24 , pp. 757-772
    • Zhan, L.1    Xie, Q.2    Tibbetts, R.S.3
  • 349
    • 34447550238 scopus 로고    scopus 로고
    • Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex
    • Zhang, F., et al. Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex. J. Biol. Chem. 282 (2007), 16691–16699.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16691-16699
    • Zhang, F.1
  • 350
    • 84897863195 scopus 로고    scopus 로고
    • Ubiquilin 2: a component of the ubiquitin–proteasome system with an emerging role in neurodegeneration
    • Zhang, K.Y., et al. Ubiquilin 2: a component of the ubiquitin–proteasome system with an emerging role in neurodegeneration. Int. J. Biochem. Cell Biol. 50 (2014), 123–126.
    • (2014) Int. J. Biochem. Cell Biol. , vol.50 , pp. 123-126
    • Zhang, K.Y.1
  • 351
    • 79953647105 scopus 로고    scopus 로고
    • Rapamycin treatment augments motor neuron degeneration in SOD1G93A mouse model of amyotrophic lateral sclerosis
    • Zhang, X., et al. Rapamycin treatment augments motor neuron degeneration in SOD1G93A mouse model of amyotrophic lateral sclerosis. Autophagy 7 (2011), 412–425.
    • (2011) Autophagy , vol.7 , pp. 412-425
    • Zhang, X.1
  • 352
    • 84898465382 scopus 로고    scopus 로고
    • MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis
    • Zhang, X., et al. MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis. Autophagy 10 (2014), 588–602.
    • (2014) Autophagy , vol.10 , pp. 588-602
    • Zhang, X.1
  • 353
    • 84919912448 scopus 로고    scopus 로고
    • Aggregation-prone c9FTD/ALS poly (GA) RAN-translated proteins cause neurotoxicity by inducing ER stress
    • Zhang, Y.-J., et al. Aggregation-prone c9FTD/ALS poly (GA) RAN-translated proteins cause neurotoxicity by inducing ER stress. Acta Neuropathol. 128 (2014), 505–524.
    • (2014) Acta Neuropathol. , vol.128 , pp. 505-524
    • Zhang, Y.-J.1
  • 354
    • 84940923271 scopus 로고    scopus 로고
    • The C9orf72 repeat expansion disrupts nucleocytoplasmic transport
    • Zhang, K., The C9orf72 repeat expansion disrupts nucleocytoplasmic transport. Nature 525:7567 (2015), 56–61.
    • (2015) Nature , vol.525 , Issue.7567 , pp. 56-61
    • Zhang, K.1
  • 355
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao, L., et al. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 37 (2005), 974–979.
    • (2005) Nat. Genet. , vol.37 , pp. 974-979
    • Zhao, L.1
  • 356
    • 78649918283 scopus 로고    scopus 로고
    • Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
    • Zito, E., et al. Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol. Cell 40 (2010), 787–797.
    • (2010) Mol. Cell , vol.40 , pp. 787-797
    • Zito, E.1
  • 357
    • 84890837640 scopus 로고    scopus 로고
    • RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia
    • Zu, T., et al. RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia. Proc. Natl. Acad. Sci. 110 (2013), E4968–E4977.
    • (2013) Proc. Natl. Acad. Sci. , vol.110 , pp. E4968-E4977
    • Zu, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.