Biomedicine - One misfolded protein allows others to sneak by

被引：10

作者：

Bates, GP ^{[1
]}

机构：

[1] Kings Coll London, Sch Med, London SE1 9RT, England

来源：

SCIENCE | 2006年 / 311卷 / 5766期

关键词：

D O I：

10.1126/science.1125246

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：

Proteins prone to aggregate in cells have been linked to neurodegenerative diseases. As cells try to eliminate such aggregates, other misfolded proteins may go undetected, making the cell susceptible to their toxic effects.

引用

页码：1385 / 1386

页数：2

共 6 条

[1]

BRIGNULL HR, COMMUNICATION

[2] Progressive disruption of cellular protein folding in models of polyglutamine diseases [J].

Gidalevitz, T ;

Ben-Zvi, A ;

Ho, KH ;

Brignull, HR ;

Morimoto, RI .

SCIENCE, 2006, 311 (5766) :1471-1474

[3] The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans [J].

Morley, JF ;

Brignull, HR ;

Weyers, JJ ;

Morimoto, RI .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (16) :10417-10422

[4] Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation [J].

Nollen, EAA ;

Garcia, SM ;

van Haaften, G ;

Kim, S ;

Chavez, A ;

Morimoto, RI ;

Plasterk, RHA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (17) :6403-6408

[5] Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology [J].

Scherzinger, E ;

Sittler, A ;

Schweiger, K ;

Heiser, V ;

Lurz, R ;

Hasenbank, R ;

Bates, GP ;

Lehrach, H ;

Wanker, EE .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (08) :4604-4609

[6]

Wexler NS, 2004, P NATL ACAD SCI USA, V101, P3498, DOI 10.1073/pnas.0308479101

← 1 →