Danger - misfolding proteins

被引:117
作者
Ellis, RJ [1 ]
Pinheiro, TJT [1 ]
机构
[1] Univ Warwick, Dept Biol Sci, Coventry CV4 7AL, W Midlands, England
关键词
D O I
10.1038/416483a
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Protein folding is vital to living organisms because it adds functional flesh to the bare bones of genes. But errors in this process generate misfolded structures that can be lethal.
引用
收藏
页码:483 / 484
页数:2
相关论文
共 10 条
[1]   Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases [J].
Bucciantini, M ;
Giannoni, E ;
Chiti, F ;
Baroni, F ;
Formigli, L ;
Zurdo, JS ;
Taddei, N ;
Ramponi, G ;
Dobson, CM ;
Stefani, M .
NATURE, 2002, 416 (6880) :507-511
[2]   Role of Escherichia coli curli operons in directing amyloid fiber formation [J].
Chapman, MR ;
Robinson, LS ;
Pinkner, JS ;
Roth, R ;
Heuser, J ;
Hammar, M ;
Normark, S ;
Hultgren, SJ .
SCIENCE, 2002, 295 (5556) :851-855
[3]   Protein misfolding, evolution and disease [J].
Dobson, CM .
TRENDS IN BIOCHEMICAL SCIENCES, 1999, 24 (09) :329-332
[4]   Protein misfolding and disease - Preface [J].
Dobson, CM ;
Ellis, RJ ;
Fersht, AR .
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 2001, 356 (1406) :129-131
[5]   Macromolecular crowding: obvious but underappreciated [J].
Ellis, RJ .
TRENDS IN BIOCHEMICAL SCIENCES, 2001, 26 (10) :597-604
[6]   Amyloid fibrils from muscle myoglobin -: Even an ordinary globular protein can assume a rogue guise if conditions are right. [J].
Fändrich, M ;
Fletcher, MA ;
Dobson, CM .
NATURE, 2001, 410 (6825) :165-166
[7]  
Kim JH, 2001, J NEUROSCI, V21, P1327
[8]   Implications of macromolecular crowding for protein assembly [J].
Minton, AP .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2000, 10 (01) :34-39
[9]   Alzheimer's disease: Genes, proteins, and therapy [J].
Selkoe, DJ .
PHYSIOLOGICAL REVIEWS, 2001, 81 (02) :741-766
[10]   Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo [J].
Walsh, DM ;
Klyubin, I ;
Fadeeva, JV ;
Cullen, WK ;
Anwyl, R ;
Wolfe, MS ;
Rowan, MJ ;
Selkoe, DJ .
NATURE, 2002, 416 (6880) :535-539