메뉴 건너뛰기




Volumn 51, Issue 1, 2003, Pages 68-73

Local protein unfolding and pathogenesis of polyglutamine-expansion diseases

Author keywords

Ataxin; CAG trinucleotide repeat; Huntingtin; Huntington's disease; Neurodegeneration; Spinocerebellar ataxia

Indexed keywords

GLUTAMINE; HUNTINGTIN; POLYGLUTAMINE;

EID: 0037375786     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10325     Document Type: Article
Times cited : (12)

References (20)
  • 1
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz MF. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem Sci 1999;24:58-63.
    • (1999) Trends Biochem Sci , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 2
    • 0034329159 scopus 로고    scopus 로고
    • Molecular genetics: Unmasking polyglutamine triggers in neurodegenerative disease
    • Gusella JF, MacDonald ME. Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease. Nat Rev Neurosci 2000;1:109-115.
    • (2000) Nat Rev Neurosci , vol.1 , pp. 109-115
    • Gusella, J.F.1    MacDonald, M.E.2
  • 4
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J Mol Biol 1999;293:321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 6
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky VN. What does it mean to be natively unfolded? Eur J Biochem 2002;269:2-12.
    • (2002) Eur J Biochem , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 7
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000;41:415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 8
    • 0012306630 scopus 로고    scopus 로고
    • http://www.ebi.ac.uk/swissprot
  • 10
    • 0012228205 scopus 로고    scopus 로고
    • http://www.expasy.org
  • 11
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982;157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 12
  • 13
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils
    • Bevivino AE, Loll PJ. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils. Proc Natl Acad Sci USA 2001;98:11955-11960.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 15
    • 0035976971 scopus 로고    scopus 로고
    • Intraand intermolecular β-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases
    • Tanaka M, Morishima I, Akagi T, Hashikawa T, Nukina N. Intraand intermolecular β-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases. J Biol Chem 2001;276:45470-45475.
    • (2001) J Biol Chem , vol.276 , pp. 45470-45475
    • Tanaka, M.1    Morishima, I.2    Akagi, T.3    Hashikawa, T.4    Nukina, N.5
  • 16
    • 0035869544 scopus 로고    scopus 로고
    • Tissue-specific proteolysis of Huntingtin (htt) in human brain: Evidence of enhanced levels of N- and C-terminal htt fragments in Huntington's disease striatum
    • Mende-Mueller LM, Toneff T, Hwang S-R, Chesselet M-F, Hook VYH. Tissue-specific proteolysis of Huntingtin (htt) in human brain: evidence of enhanced levels of N- and C-terminal htt fragments in Huntington's disease striatum. J Neurosci 2001;21:1830-1837.
    • (2001) J Neurosci , vol.21 , pp. 1830-1837
    • Mende-Mueller, L.M.1    Toneff, T.2    Hwang, S.-R.3    Chesselet, M.-F.4    Hook, V.Y.H.5
  • 17
    • 0012280685 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation influence of structure-stabilishing solutes and protein interactions
    • Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation influence of structure-stabilishing solutes and protein interactions. J Biol Chem 2002;14:14.
    • (2002) J Biol Chem , vol.14 , pp. 14
    • Reid, J.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 18
    • 0012339275 scopus 로고    scopus 로고
    • http://www.sanger.ac.uk/Software/Pfam
  • 19
    • 0029401042 scopus 로고
    • Glutamine repeats as polar zippers: Their role in inherited neurodegenerative disease
    • Perutz MF. Glutamine repeats as polar zippers: their role in inherited neurodegenerative disease. Mol Med 1995;1:718-721.
    • (1995) Mol Med , vol.1 , pp. 718-721
    • Perutz, M.F.1
  • 20
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • Liu Y, Gotte G, Libonati M, Eisenberg D. A domain-swapped RNase A dimer with implications for amyloid formation. Nat Struct Biol 2001;8:211-214.
    • (2001) Nat Struct Biol , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.