The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function.
The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function.
复制标题
N-乙基马来酰亚胺敏感因子的六聚结构域:伴侣功能的结构线索。
DOI:
10.1016/s0969-2126(99)80015-x
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发表时间:
1999
期刊:
影响因子:
--
通讯作者:
Neuwald,AF
中科院分区:
文献类型:
--
作者:
Neuwald,AF
The hexameric structure of the D2 ATP-binding module of N-ethylmaleimide-sensitive factor (NSF), a chaperone involved in SNARE complex disassembly, was recently determined. This structure and the previously determined structure of the DNA polymerase IIIδ′ subunit have far-reaching biological significance because these modules are related to diverse ATPases that promote the assembly, disassembly and operation of various protein complexes.
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影响因子:
7
作者:
A. F. Neuwald;L. Aravind;J. Spouge;E. Koonin
通讯作者:
A. F. Neuwald;L. Aravind;J. Spouge;E. Koonin
DOI:
--
发表时间:
1997
期刊:
TIBS -Trends in Biochemical Sciences. Regular ed
影响因子:
--
作者:
C. Suzuki;M. Rep;J. V. van Dijl;K. Suda;L. Grivell;G. Schatz
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G. Schatz
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3.5
作者:
Khattar, Medhat M.
通讯作者:
Khattar, Medhat M.
DOI:
--
发表时间:
1997
影响因子:
11.1
作者:
M. Pak;S. Wickner
通讯作者:
S. Wickner
影响因子:
14.9
作者:
G. Weeda;M. Rossignol;R. Fraser;G. Winkler;W. Vermeulen;L. J. Veer;Libin Ma;J. Hoeijmakers;J. Egly
通讯作者:
J. Egly