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Volumn 546, Issue , 2013, Pages 67-70

α-Synuclein mutations cluster around a putative protein loop

Author keywords

Synuclein; Genetics; Parkinson's disease; SNCA

Indexed keywords

ALPHA SYNUCLEIN; AMINO ACID; TETRAMER;

EID: 84878910950     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2013.04.058     Document Type: Article
Times cited : (38)

References (43)
  • 2
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T., Choi J.G., Selkoe D.J. alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 2011, 477:107-110.
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 4
    • 84866671599 scopus 로고    scopus 로고
    • Bacterial in-cell NMR of human alpha-synuclein: a disordered monomer by nature?
    • Binolfi A., Theillet F.X., Selenko P. Bacterial in-cell NMR of human alpha-synuclein: a disordered monomer by nature?. Biochem. Soc. Trans. 2012, 40:950-954.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 950-954
    • Binolfi, A.1    Theillet, F.X.2    Selenko, P.3
  • 9
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo A.M., Stefanis L., Fredenburg R., Lansbury P.T., Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305:1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 10
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 1998, 273:9443-9449.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 11
    • 83455213859 scopus 로고    scopus 로고
    • Contribution of individual histidines to prion protein copper binding
    • Davies P., McHugh P.C., Hammond V.J., Marken F., Brown D.R. Contribution of individual histidines to prion protein copper binding. Biochemistry 2011, 50:10781-10791.
    • (2011) Biochemistry , vol.50 , pp. 10781-10791
    • Davies, P.1    McHugh, P.C.2    Hammond, V.J.3    Marken, F.4    Brown, D.R.5
  • 13
    • 84874769548 scopus 로고    scopus 로고
    • In vivo crosslinking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells
    • Dettmer U., Newman A.J., Luth E.S., Bartels T., Selkoe D. In vivo crosslinking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells. J. Biol. Chem. 2013, 288(9):6371-6385.
    • (2013) J. Biol. Chem. , vol.288 , Issue.9 , pp. 6371-6385
    • Dettmer, U.1    Newman, A.J.2    Luth, E.S.3    Bartels, T.4    Selkoe, D.5
  • 16
    • 79952780867 scopus 로고    scopus 로고
    • Coordination features and affinity of the Cu(2)+ site in the alpha-synuclein protein of Parkinson's disease
    • Dudzik C.G., Walter E.D., Millhauser G.L. Coordination features and affinity of the Cu(2)+ site in the alpha-synuclein protein of Parkinson's disease. Biochemistry 2011, 50:1771-1777.
    • (2011) Biochemistry , vol.50 , pp. 1771-1777
    • Dudzik, C.G.1    Walter, E.D.2    Millhauser, G.L.3
  • 23
    • 23844446448 scopus 로고    scopus 로고
    • Expression of normal sequence pathogenic proteins for neurodegenerative disease contributes to disease risk: 'permissive templating' as a general mechanism underlying neurodegeneration
    • Hardy J. Expression of normal sequence pathogenic proteins for neurodegenerative disease contributes to disease risk: 'permissive templating' as a general mechanism underlying neurodegeneration. Biochem. Soc. Trans. 2005, 33:578-581.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 578-581
    • Hardy, J.1
  • 24
    • 0026894414 scopus 로고
    • Framing beta-amyloid
    • Hardy J. Framing beta-amyloid. Nat. Genet. 1992, 1:233-234.
    • (1992) Nat. Genet. , vol.1 , pp. 233-234
    • Hardy, J.1
  • 25
    • 0035968117 scopus 로고    scopus 로고
    • Presenilin mutations line up along transmembrane alpha-helices
    • Hardy J., Crook R. Presenilin mutations line up along transmembrane alpha-helices. Neurosci. Lett. 2001, 306:203-205.
    • (2001) Neurosci. Lett. , vol.306 , pp. 203-205
    • Hardy, J.1    Crook, R.2
  • 26
    • 84861671617 scopus 로고    scopus 로고
    • The spread of neurodegenerative disease
    • Hardy J., Revesz T. The spread of neurodegenerative disease. N. Engl. J. Med. 2012, 366:2126-2128.
    • (2012) N. Engl. J. Med. , vol.366 , pp. 2126-2128
    • Hardy, J.1    Revesz, T.2
  • 28
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower J.H., Chu Y., Hauser R.A., Freeman T.B., Olanow C.W. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 2008, 14:504-506.
    • (2008) Nat. Med. , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 33
    • 0031933012 scopus 로고    scopus 로고
    • Familial Parkinsonism and dementia with ballooned neurons, argyrophilic neuronal inclusions, atypical neurofibrillary tangles, tau-negative astrocytic fibrillary tangles, and Lewy bodies
    • Mizutani T., Inose T., Nakajima S., Kakimi S., Uchigata M., Ikeda K., Gambetti P., Takasu T. Familial Parkinsonism and dementia with ballooned neurons, argyrophilic neuronal inclusions, atypical neurofibrillary tangles, tau-negative astrocytic fibrillary tangles, and Lewy bodies. Acta Neuropathol. 1998, 95:15-27.
    • (1998) Acta Neuropathol. , vol.95 , pp. 15-27
    • Mizutani, T.1    Inose, T.2    Nakajima, S.3    Kakimi, S.4    Uchigata, M.5    Ikeda, K.6    Gambetti, P.7    Takasu, T.8
  • 38
    • 84860172516 scopus 로고    scopus 로고
    • N-terminal acetylation is critical for forming alpha-helical oligomer of alpha-synuclein
    • Trexler A.J., Rhoades E. N-terminal acetylation is critical for forming alpha-helical oligomer of alpha-synuclein. Protein Sci. 2012, 21:601-605.
    • (2012) Protein Sci. , vol.21 , pp. 601-605
    • Trexler, A.J.1    Rhoades, E.2
  • 39
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • Ulmer T.S., Bax A., Cole N.B., Nussbaum R.L. Structure and dynamics of micelle-bound human alpha-synuclein. J. Biol. Chem. 2005, 280:9595-9603. 10.2210/pdb1xq8/pdb.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 42
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri M., Vogiatzi T., Vekrellis K., Park D., Stefanis L. Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS ONE 2009, 4:e5515.
    • (2009) PLoS ONE , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.