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Volumn 72, Issue 5, 2012, Pages 739-749

A novel monoclonal antibody reveals a conformational alteration shared by amyotrophic lateral sclerosis-linked SOD1 mutants

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY MS785; UNCLASSIFIED DRUG;

EID: 84871961507     PISSN: 03645134     EISSN: 15318249     Source Type: Journal    
DOI: 10.1002/ana.23668     Document Type: Article
Times cited : (64)

References (35)
  • 1
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • DOI 10.1038/nrn1971, PII NRN1971
    • Pasinelli P, Brown RH,. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci 2006; 7: 710-723. (Pubitemid 44267495)
    • (2006) Nature Reviews Neuroscience , vol.7 , Issue.9 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 2
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • DOI 10.1146/annurev.biochem.72.121801.161647
    • Valentine JS, Doucette PA, Zittin Potter S,. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu Rev Biochem 2005; 74: 563-593. (Pubitemid 40995518)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Potter, S.Z.3
  • 6
    • 42249102078 scopus 로고    scopus 로고
    • Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS
    • Turner BJ, Talbot K,. Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS. Prog Neurobiol 2008; 85: 94-134.
    • (2008) Prog Neurobiol , vol.85 , pp. 94-134
    • Turner, B.J.1    Talbot, K.2
  • 7
    • 0035936804 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded
    • Julien JP,. Amyotrophic lateral sclerosis. Unfolding the toxicity of the misfolded. Cell 2001; 104: 581-591.
    • (2001) Cell , vol.104 , pp. 581-591
    • Julien, J.P.1
  • 8
    • 77958519939 scopus 로고    scopus 로고
    • Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
    • Bosco DA, Morfini G, Karabacak NM, et al. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Nat Neurosci 2010; 13: 1396-1403.
    • (2010) Nat Neurosci , vol.13 , pp. 1396-1403
    • Bosco, D.A.1    Morfini, G.2    Karabacak, N.M.3
  • 9
    • 0039251419 scopus 로고    scopus 로고
    • Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase
    • Estevez AG, Crow JP, Sampson JB, et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 1999; 286: 2498-2500.
    • (1999) Science , vol.286 , pp. 2498-2500
    • Estevez, A.G.1    Crow, J.P.2    Sampson, J.B.3
  • 10
    • 77955352066 scopus 로고    scopus 로고
    • Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients
    • Forsberg K, Jonsson PA, Andersen PM, et al. Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients. PLoS One 2010; 5: e11552.
    • (2010) PLoS One , vol.5
    • Forsberg, K.1    Jonsson, P.A.2    Andersen, P.M.3
  • 11
    • 80052783545 scopus 로고    scopus 로고
    • Astrocytes from familial and sporadic ALS patients are toxic to motor neurons
    • Haidet-Phillips AM, Hester ME, Miranda CJ, et al. Astrocytes from familial and sporadic ALS patients are toxic to motor neurons. Nat Biotechnol 2011; 29: 824-828.
    • (2011) Nat Biotechnol , vol.29 , pp. 824-828
    • Haidet-Phillips, A.M.1    Hester, M.E.2    Miranda, C.J.3
  • 12
    • 77953028624 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form
    • Kerman A, Liu HN, Croul S, et al. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. Acta Neuropathol 2010; 119: 335-344.
    • (2010) Acta Neuropathol , vol.119 , pp. 335-344
    • Kerman, A.1    Liu, H.N.2    Croul, S.3
  • 15
    • 80053252011 scopus 로고    scopus 로고
    • Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders
    • Doyle KM, Kennedy D, Gorman AM, et al. Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders. J Cell Mol Med 2011; 15: 2025-2039.
    • (2011) J Cell Mol Med , vol.15 , pp. 2025-2039
    • Doyle, K.M.1    Kennedy, D.2    Gorman, A.M.3
  • 17
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • DOI 10.1038/nature02592
    • Lilley BN, Ploegh HL,. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004; 429: 834-840. (Pubitemid 38843291)
    • (2004) Nature , vol.429 , Issue.6994 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 18
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • DOI 10.1038/nature02656
    • Ye Y, Shibata Y, Yun C, et al. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 2004; 429: 841-847. (Pubitemid 38843292)
    • (2004) Nature , vol.429 , Issue.6994 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 20
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame K, Agarwala KL, Kato H, Miyata T,. Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J Biol Chem 2000; 275: 32846-32853.
    • (2000) J Biol Chem , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 21
  • 22
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • DOI 10.1016/S0092-8674(01)00611-0
    • Yoshida H, Matsui T, Yamamoto A, et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001; 107: 881-891. (Pubitemid 34084979)
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 23
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 A structure of copper, zinc superoxide dismutase
    • DOI 10.1016/0022-2836(82)90174-7
    • Tainer JA, Getzoff ED, Beem KM, et al. Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. J Mol Biol 1982; 160: 181-217. (Pubitemid 13239300)
    • (1982) Journal of Molecular Biology , vol.160 , Issue.2 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3
  • 24
    • 0036231449 scopus 로고    scopus 로고
    • The solution structure of reduced dimeric copper zinc superoxide dismutase: The structural effects of dimerization
    • DOI 10.1046/j.1432-1327.2002.02840.x
    • Banci L, Bertini I, Cramaro F, et al. The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization. Eur J Biochem 2002; 269: 1905-1915. (Pubitemid 34429672)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.7 , pp. 1905-1915
    • Banci, L.1    Bertini, I.2    Cramaro, F.3    Del Conte, R.4    Viezzoli, M.S.5
  • 25
    • 47049120538 scopus 로고    scopus 로고
    • Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis
    • Cao X, Antonyuk SV, Seetharaman SV, et al. Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. J Biol Chem 2008; 283: 16169-16177.
    • (2008) J Biol Chem , vol.283 , pp. 16169-16177
    • Cao, X.1    Antonyuk, S.V.2    Seetharaman, S.V.3
  • 28
    • 70450286167 scopus 로고    scopus 로고
    • Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A
    • Galaleldeen A, Strange RW, Whitson LJ, et al. Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. Arch Biochem Biophys 2009; 492: 40-47.
    • (2009) Arch Biochem Biophys , vol.492 , pp. 40-47
    • Galaleldeen, A.1    Strange, R.W.2    Whitson, L.J.3
  • 29
    • 45949083132 scopus 로고    scopus 로고
    • SOD1 and amyotrophic lateral sclerosis: Mutations and oligomerization
    • Banci L, Bertini I, Boca M, et al. SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization. PLoS One 2008; 3: e1677.
    • (2008) PLoS One , vol.3
    • Banci, L.1    Bertini, I.2    Boca, M.3
  • 30
    • 0035136084 scopus 로고    scopus 로고
    • Compound heterozygous D90A and D96N SOD1 mutations in a recessive amyotrophic lateral sclerosis family
    • DOI 10.1002/1531-8249(20010201)49:2 <267::AID-ANA51>3.0.CO;2-D
    • Hand CK, Mayeux-Portas V, Khoris J, et al. Compound heterozygous D90A and D96N SOD1 mutations in a recessive amyotrophic lateral sclerosis family. Ann Neurol 2001; 49: 267-271. (Pubitemid 32158007)
    • (2001) Annals of Neurology , vol.49 , Issue.2 , pp. 267-271
    • Hand, C.K.1    Mayeux-Portas, V.2    Khoris, J.3    Briolotti, V.4    Clavelou, P.5    Camu, W.6    Rouleau, G.A.7
  • 32
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, et al. Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 2009; 323: 1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, Jr.T.J.1    Bosco, D.A.2    Leclerc, A.L.3
  • 33
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurin in amyotrophic lateral sclerosis
    • Maruyama H, Morino H, Ito H, et al. Mutations of optineurin in amyotrophic lateral sclerosis. Nature 2010; 465: 223-226.
    • (2010) Nature , vol.465 , pp. 223-226
    • Maruyama, H.1    Morino, H.2    Ito, H.3
  • 35
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortobagyi T, et al. Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 2009; 323: 1208-1211
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.