p97 Composition Changes Caused by Allosteric Inhibition Are Suppressed by an On-Target Mechanism that Increases the Enzyme's ATPase Activity.
about
A threonine turnstile defines a dynamic amphiphilic binding motif in the AAA ATPase p97 allosteric binding site.Valosin-containing protein (VCP)-Adaptor Interactions are Exceptionally Dynamic and Subject to Differential Modulation by a VCP Inhibitor.Specific mutations in the D1-D2 linker region of VCP/p97 enhance ATPase activity and confer resistance to VCP inhibitors.
P2860
p97 Composition Changes Caused by Allosteric Inhibition Are Suppressed by an On-Target Mechanism that Increases the Enzyme's ATPase Activity.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
p97 Composition Changes Caused ...... the Enzyme's ATPase Activity.
@en
type
label
p97 Composition Changes Caused ...... the Enzyme's ATPase Activity.
@en
prefLabel
p97 Composition Changes Caused ...... the Enzyme's ATPase Activity.
@en
P2093
P2860
P1476
p97 Composition Changes Caused ...... the Enzyme's ATPase Activity.
@en
P2093
Chen-Ting Ma
Eduard Sergienko
Julia I Toth
Khatereh Motamedchaboki
Matthew D Petroski
Nam-Gu Her
P2860
P304
P356
10.1016/J.CHEMBIOL.2016.03.012
P577
2016-04-01T00:00:00Z