Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus
about
Integral and associated lysosomal membrane proteinsThe d subunit plays a central role in human vacuolar H(+)-ATPasesRotating with the brakes on and other unresolved features of the vacuolar ATPaseInter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPaseThe structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthaseCrystal structure of the central axis DF complex of the prokaryotic V-ATPaseCrystal and NMR Structures Give Insights into the Role and Dynamics of Subunit F of the Eukaryotic V-ATPase from Saccharomyces cerevisiaeCommon evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatusThe C-H peripheral stalk base: a novel component in V1-ATPase assembly.Regulation and isoform function of the V-ATPases.Expression and activity of V-H+ -ATPase in gill and kidney of marbled eel Anguilla marmorata in response to salinity challenge.Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F.Function, structure and regulation of the vacuolar (H+)-ATPases.Mechanism of inhibition of the V-type molecular motor by tributyltin chloride.Rotation of artificial rotor axles in rotary molecular motors.The tether connecting cytosolic (N terminus) and membrane (C terminus) domains of yeast V-ATPase subunit a (Vph1) is required for assembly of V0 subunit d.V for victory--a V1-ATPase structure revealed.Structural divergence of the rotary ATPases.Reconstitution of vacuolar-type rotary H+-ATPase/synthase from Thermus thermophilusStructure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insightsSingle-molecule analysis of inhibitory pausing states of V1-ATPase.Cloning and overexpression of an important functional gene ATP6V1F encoding a component of vacuolar ATPase from the Giant Panda (Ailuropoda melanoleuca).Interaction of the Thermoplasma acidophilum A1A0-ATP synthase peripheral stalk with the catalytic domain.Subunit interactions and requirements for inhibition of the yeast V1-ATPase.Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus.Conformational dynamics of the rotary subunit F in the A3 B3 DF complex of Methanosarcina mazei Gö1 A-ATP synthase monitored by single-molecule FRET.Anchoring and scaffolding: V(1)-ATPase interactions with widespread implications.
P2860
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P2860
Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus
description
2005 nî lūn-bûn
@nan
2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Structure of a central stalk s ...... hase from Thermus thermophilus
@ast
Structure of a central stalk s ...... hase from Thermus thermophilus
@en
type
label
Structure of a central stalk s ...... hase from Thermus thermophilus
@ast
Structure of a central stalk s ...... hase from Thermus thermophilus
@en
prefLabel
Structure of a central stalk s ...... hase from Thermus thermophilus
@ast
Structure of a central stalk s ...... hase from Thermus thermophilus
@en
P2093
P2860
P50
P356
P1433
P1476
Structure of a central stalk s ...... hase from Thermus thermophilus
@en
P2093
Chiyo Ikeda
Daniela Stock
Ken Yokoyama
Masasuke Yoshida
Masatada Tamakoshi
Momi Iwata
Ricardo A Bernal
P2860
P304
P356
10.1038/SJ.EMBOJ.7600859
P407
P577
2005-11-10T00:00:00Z