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Volumn 9, Issue 10, 2017, Pages

Prion properties of SOD1 in amyotrophic lateral sclerosis and potential therapy

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; SOD1 PROTEIN, HUMAN;

EID: 85030715828     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a024141     Document Type: Article
Times cited : (28)

References (60)
  • 2
    • 84936751681 scopus 로고    scopus 로고
    • Exome sequencing uncovers hidden pathways in familial and sporadic ALS
    • Bettencourt C, Houlden H. 2015. Exome sequencing uncovers hidden pathways in familial and sporadic ALS. Nat Neurosci 18: 611–613.
    • (2015) Nat Neurosci , vol.18 , pp. 611-613
    • Bettencourt, C.1    Houlden, H.2
  • 10
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by α -synuclein oligomers provides evidence for spreading of α -synuclein pathology
    • Danzer KM, Krebs SK, Wolff M, Birk G, Hengerer B. 2009. Seeding induced by α -synuclein oligomers provides evidence for spreading of α -synuclein pathology. J Neurochem 111: 192–203.
    • (2009) J Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 13
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M. 2012. The amyloid state of proteins in human diseases. Cell 148: 1188–1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 14
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost B, Jacks RL, Diamond MI. 2009. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 284: 12845–12852.
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 19
    • 0022257968 scopus 로고
    • Guanabenz overdose
    • Hall AH. 1985. Guanabenz overdose. Ann Intern Med 102: 787–788.
    • (1985) Ann Intern Med , vol.102 , pp. 787-788
    • Hall, A.H.1
  • 20
    • 0020545855 scopus 로고
    • Guanabenz. A review of its pharmacodynamic properties and therapeutic efficacy in hypertension
    • Holmes B, Brogden RN, Heel RC, Speight TM, Avery GS. 1983. Guanabenz. A review of its pharmacodynamic properties and therapeutic efficacy in hypertension. Drugs 26: 212–229.
    • (1983) Drugs , vol.26 , pp. 212-229
    • Holmes, B.1    Brogden, R.N.2    Heel, R.C.3    Speight, T.M.4    Avery, G.S.5
  • 22
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston JA, Dalton MJ, Gurney ME, Kopito RR. 2000. Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci 97: 12571–12576.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 23
    • 0345599024 scopus 로고    scopus 로고
    • Inhibition of a constitutive translation initiation factor 2α phosphatase,CReP, promotes survival of stressed cells
    • Jousse C, Oyadomari S, Novoa I, Lu P, Zhang Y, Harding HP, Ron D. 2003. Inhibition of a constitutive translation initiation factor 2α phosphatase,CReP, promotes survival of stressed cells. J Cell Biol 163: 767–775.
    • (2003) J Cell Biol , vol.163 , pp. 767-775
    • Jousse, C.1    Oyadomari, S.2    Novoa, I.3    Lu, P.4    Zhang, Y.5    Harding, H.P.6    Ron, D.7
  • 24
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker M, Walker LC. 2011. Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann Neurol 70: 532–540.
    • (2011) Ann Neurol , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 25
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor proteintransgenic mice
    • Kane MD, Lipinski WJ, Callahan MJ, Bian F, Durham RA, Schwarz RD, Roher AE, Walker LC. 2000. Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor proteintransgenic mice. J Neurosci 20: 3606–3611.
    • (2000) J Neurosci , vol.20 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3    Bian, F.4    Durham, R.A.5    Schwarz, R.D.6    Roher, A.E.7    Walker, L.C.8
  • 27
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: Elucidation by GADD34-deficient mice
    • Kojima E, Takeuchi A, Haneda M, Yagi A, Hasegawa T, Yamaki K, Takeda K, Akira S, Shimokata K, Isobe K. 2003. The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: Elucidation by GADD34-deficient mice. FASEB J 17: 1573–1575.
    • (2003) FASEB J , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3    Yagi, A.4    Hasegawa, T.5    Yamaki, K.6    Takeda, K.7    Akira, S.8    Shimokata, K.9    Isobe, K.10
  • 29
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk KC, Kehm V, Carroll J, Zhang B, O’Brien P, Trojanowski JQ, Lee VM. 2012. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338: 949–953.
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O’Brien, P.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 31
    • 84901047429 scopus 로고    scopus 로고
    • Proteostasis and the aging proteome in health and disease
    • Morimoto RI, Cuervo AM. 2014. Proteostasis and the aging proteome in health and disease. J Gerontol A Biol Sci Med Sci 69: S33–S38.
    • (2014) J Gerontol a Biol Sci Med Sci , vol.69 , pp. S33-S38
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 33
    • 79957910396 scopus 로고    scopus 로고
    • Self-propagation and transmission of misfolded mutant SOD1: Prion or prion-like phenomenon?
    • Münch C, Bertolotti A. 2011. Self-propagation and transmission of misfolded mutant SOD1: Prion or prion-like phenomenon? Cell Cycle 10: 1711.
    • (2011) Cell Cycle , vol.10 , pp. 1711
    • Münch, C.1    Bertolotti, A.2
  • 35
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Munch C, O’Brien J, Bertolotti A. 2011. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci 108: 3548-3553.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 3548-3553
    • Munch, C.1    O’Brien, J.2    Bertolotti, A.3
  • 37
    • 74649086999 scopus 로고    scopus 로고
    • SOD 1-associated ALS: A promising system for elucidating the origin of protein-misfolding disease
    • Nordlund A, Oliveberg M. 2008. SOD 1-associated ALS: A promising system for elucidating the origin of protein-misfolding disease. HFSP J 2: 354-364.
    • (2008) HFSP J , vol.2 , pp. 354-364
    • Nordlund, A.1    Oliveberg, M.2
  • 38
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α. J
    • Novoa I, Zeng H, Harding HP, Ron D. 2001. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α. j Cell Biol 153: 1011-1022.
    • (2001) Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 40
    • 84862620376 scopus 로고    scopus 로고
    • Cell biology. A unifying role for prions in neurodegenerative diseases
    • Prusiner SB. 2012. Cell biology. A unifying role for prions in neurodegenerative diseases. Science 336: 1511-1513.
    • (2012) Science , vol.336 , pp. 1511-1513
    • Prusiner, S.B.1
  • 42
    • 70349581626 scopus 로고    scopus 로고
    • ALS motor phenotype heterogeneity, focality, and spread: Deconstructing motor neuron degeneration
    • Ravits JM, La Spada AR. 2009. ALS motor phenotype heterogeneity, focality, and spread: Deconstructing motor neuron degeneration. Neurology 73: 805-811.
    • (2009) Neurology , vol.73 , pp. 805-811
    • Ravits, J.M.1    La Spada, A.R.2
  • 44
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren PH, Lauckner JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR. 2009. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 11: 219-225.
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 50
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • Shaw BF, Valentine JS. 2007. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem Sci 32: 78-85.
    • (2007) Trends Biochem Sci , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 51
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler R Harding HP, Ron D, Bertolotti A. 2011. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 332: 91-94.
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler R Harding, H.P.1    Ron, D.2    Bertolotti, A.3
  • 52
    • 22244479388 scopus 로고    scopus 로고
    • Copperzinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine JS, Doucette PA, Zittin Potter S. 2005. Copperzinc superoxide dismutase and amyotrophic lateral sclerosis. Annu Rev Biochem 74: 563-593.
    • (2005) Annu Rev Biochem , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 53
    • 84922606978 scopus 로고    scopus 로고
    • The role of protein clearance mechanisms in organismal ageing and age-related diseases
    • Vilchez D, Saez I, Dillin A. 2014. The role of protein clearance mechanisms in organismal ageing and age-related diseases. Nat Commun 5: 5659.
    • (2014) Nat Commun , vol.5 , pp. 5659
    • Vilchez, D.1    Saez, I.2    Dillin, A.3
  • 55
    • 79551584057 scopus 로고    scopus 로고
    • The unfolded protein response in familial amyotrophic lateral sclerosis
    • Wang L, Popko B, Roos RP. 2011. The unfolded protein response in familial amyotrophic lateral sclerosis. Hum Mol Genet 20: 1008-1015.
    • (2011) Hum Mol Genet , vol.20 , pp. 1008-1015
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 56
    • 84898817967 scopus 로고    scopus 로고
    • An enhanced integrated stress response ameliorates mutant SOD 1-induced ALS
    • Wang L, Popko B, Roos RP. 2014. An enhanced integrated stress response ameliorates mutant SOD 1-induced ALS. Hum Mol Genet 23: 2629-2638.
    • (2014) Hum Mol Genet , vol.23 , pp. 2629-2638
    • Wang, L.1    Popko, B.2    Roos, R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.