AAA proteins: in search of a common molecular basisInternational meeting on cellular functions of AAA proteins

被引：47

作者：

Michael R Maurizi ^{[1
]}

Chou‐Chi H Li ^{[2
]}

机构：

[1] Laboratory of Cell Biology,

[2] National Cancer Institute,undefined

[3] Basic Research Laboratory,undefined

[4] National Cancer Institute at Frederick,undefined

[5] Intramural Research Support Program,undefined

[6] SAIC Frederick,undefined

来源：

关键词：

D O I：

10.1093/embo-reports/kve229

中图分类号：

学科分类号：

摘要：

引用

页码：980 / 985

页数：5

共 47 条

[1] Bochtler M.(1997)Crystal structure of heat shock locus V (HslV) from Proc. Natl Acad. Sci. USA 94 6070-6074
[2] Ditzel L.(1998)A subcomplex of the proteasome regulatory particle required for ubiquitin‐conjugate degradation and related to the COP9‐signalosome and eIF3 Cell 94 615-623
[3] Groll M.(1998)Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins Cell 94 73-82
[4] Huber R.(1997)Crystal structure of the δ′ subunit of the clamp‐loader complex of Cell 91 335-345
[5] Glickman M.H.(1999) DNA polymerase III Proc. Natl Acad. Sci. USA 96 11033-11040
[6] Rubin D.M.(2000)Chaperone rings in protein folding and degradation Trends Biochem. Sci. 25 247-251
[7] Coux O.(1998)AAA proteases: cellular machines for degrading membrane proteins Cell 94 525-536
[8] Wefes I.(1995)Crystal structure of the hexamerization domain of Genes Dev. 9 2399-2408
[9] Pfeifer G.(2001)‐ethylmaleimide‐sensitive fusion protein J. Biol. Chem. 276 21991-21994
[10] Cjeka Z.(1999)Disassembly of the Mu transposase tetramer by the ClpX chaperone Genome Res. 9 27-43