Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA
about
The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation.A single ClpS monomer is sufficient to direct the activity of the ClpA hexamerLocal and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotations.The nuclear envelope localization of DYT1 dystonia torsinA-ΔE requires the SUN1 LINC complex component.Activation of human VPS4A by ESCRT-III proteins reveals ability of substrates to relieve enzyme autoinhibition.
P2860
Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Role of a conserved pore resid ...... ate in the AAA+ chaperone ClpA
@ast
Role of a conserved pore resid ...... ate in the AAA+ chaperone ClpA
@en
type
label
Role of a conserved pore resid ...... ate in the AAA+ chaperone ClpA
@ast
Role of a conserved pore resid ...... ate in the AAA+ chaperone ClpA
@en
prefLabel
Role of a conserved pore resid ...... ate in the AAA+ chaperone ClpA
@ast
Role of a conserved pore resid ...... ate in the AAA+ chaperone ClpA
@en
P2860
P356
P1433
P1476
Role of a conserved pore resid ...... ate in the AAA+ chaperone ClpA
@en
P2093
Mary E Farbman
Stuart Licht
P2860
P304
13497-13505
P356
10.1021/BI801140Y
P407
P577
2008-12-01T00:00:00Z