Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase.
about
V1 and V0 domains of the human H+-ATPase are linked by an interaction between the G and a subunitsStructure of the yeast vacuolar ATPaseCrystal Structure of the Cytoplasmic N-Terminal Domain of Subunit I, a Homolog of Subunit a, of V-ATPaseCrystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGChead Peripheral Stalk ComplexCysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domainStoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometryDomain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G.Structural and functional separation of the N- and C-terminal domains of the yeast V-ATPase subunit H.Molecular characterization and serological reactivity of a vacuolar ATP synthase subunit ε-like protein from Clonorchis sinensis.Exercise intolerance and developmental delay associated with a novel mitochondrial ND5 mutation.Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase.The emerging structure of vacuolar ATPases.Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F.Glu-44 in the amino-terminal α-helix of yeast vacuolar ATPase E subunit (Vma4p) has a role for VoV1 assemblyStructural divergence of the rotary ATPases.An update in the structure, function, and regulation of V-ATPases: the role of the C subunit.Critical roles of subunit NuoH (ND1) in the assembly of peripheral subunits with the membrane domain of Escherichia coli NDH-1Interaction and stoichiometry of the peripheral stalk subunits NtpE and NtpF and the N-terminal hydrophilic domain of NtpI of Enterococcus hirae V-ATPase.A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator.Spectroscopical identification of residues of subunit G of the yeast V-ATPase in its connection with subunit E
P2860
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P2860
Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
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2005年學術文章
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name
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@en
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@en-gb
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@nl
type
label
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@en
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@en-gb
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@nl
prefLabel
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@en
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@en-gb
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@nl
P2093
P356
P1433
P1476
Defined sites of interaction b ...... ure of the vacuolar H+-ATPase.
@en
P2093
John B C Findlay
Lyndsey J Durose
Richard P O Jones
P304
P356
10.1021/BI048402X
P407
P577
2005-03-01T00:00:00Z