about
Addressing preferred specimen orientation in single-particle cryo-EM through tilting.Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase.Recruitment dynamics of ESCRT-III and Vps4 to endosomes and implications for reverse membrane budding.The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets.Katanin spiral and ring structures shed light on power stroke for microtubule severing.Dividing the Archaeal Way: The Ancient Cdv Cell-Division Machinery.
P2860
description
2017 nî lūn-bûn
@nan
2017 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2017 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2017年の論文
@ja
2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
name
Mechanism of Vps4 hexamer function revealed by cryo-EM
@ast
Mechanism of Vps4 hexamer function revealed by cryo-EM
@en
type
label
Mechanism of Vps4 hexamer function revealed by cryo-EM
@ast
Mechanism of Vps4 hexamer function revealed by cryo-EM
@en
prefLabel
Mechanism of Vps4 hexamer function revealed by cryo-EM
@ast
Mechanism of Vps4 hexamer function revealed by cryo-EM
@en
P2093
P2860
P50
P356
P1433
P1476
Mechanism of Vps4 hexamer function revealed by cryo-EM
@en
P2093
Jeffrey T Tarrasch
Xinqiang Ding
P2860
P304
P356
10.1126/SCIADV.1700325
P577
2017-04-14T00:00:00Z