Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry - Wikidata - awgldk - TriplyDB

Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry

Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry

http://www.wikidata.org/entity/Q28259673

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Probing subunit-subunit interactions in the yeast vacuolar ATPase by peptide arrays Structure of the yeast vacuolar ATPase Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGChead Peripheral Stalk Complex The dynamic stator stalk of rotary ATPases.Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins Rotary ATPases: models, machine elements and technical specifications Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.Revealing Higher Order Protein Structure Using Mass Spectrometry.Subunit positioning and stator filament stiffness in regulation and power transmission in the V1 motor of the Manduca sexta V-ATPase.The C-H peripheral stalk base: a novel component in V1-ATPase assembly.PA1b inhibitor binding to subunits c and e of the vacuolar ATPase reveals its insecticidal mechanism Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G.RNA interference of four genes in adult Bactrocera dorsalis by feeding their dsRNAs Challenges and rewards of interaction proteomics.Decreased expression of ATP6V1H in type 2 diabetes: a pilot report on the diabetes risk study in Mexican Americans.The ingenious structure of central rotor apparatus in VoV1; key for both complex disassembly and energy coupling between V1 and Vo Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.Extra-renal locations of the a4 subunit of H(+)ATPase.Co-evolution of primordial membranes and membrane proteins Structural divergence of the rotary ATPases.Targeting reversible disassembly as a mechanism of controlling V-ATPase activity The study of vacuolar-type ATPases by single particle electron microscopy.Studying macromolecular complex stoichiometries by peptide-based mass spectrometry Comparative molecular analyses of select pH- and osmoregulatory genes in three freshwater crayfish Cherax quadricarinatus, C. destructor and C. cainii Proton Transport and pH Control in Fungi.A new V-ATPase regulatory mechanism mediated by the Rab interacting lysosomal protein (RILP).Crystal structure of yeast V1-ATPase in the autoinhibited state.Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding.Reconstitution of vacuolar-type rotary H+-ATPase/synthase from Thermus thermophilus Synthesis of biotin-tagged chemical cross-linkers and their applications for mass spectrometry.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.Domain architecture of the stator complex of the A1A0-ATP synthase from Thermoplasma acidophilum.Functional characterization of the N-terminal domain of subunit H (Vma13p) of the yeast vacuolar ATPase.Interaction 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.Biolayer interferometry of lipid nanodisc-reconstituted yeast vacuolar H+ -ATPase.

P2860

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P2860

Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry

http://www.wikidata.org/entity/Q28259673

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Stoichiometry of the periphera ...... etermined by mass spectrometry

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Stoichiometry of the periphera ...... etermined by mass spectrometry

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Stoichiometry of the periphera ...... etermined by mass spectrometry

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type

label

Stoichiometry of the periphera ...... etermined by mass spectrometry

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Stoichiometry of the periphera ...... etermined by mass spectrometry

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Stoichiometry of the periphera ...... etermined by mass spectrometry

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prefLabel

Stoichiometry of the periphera ...... etermined by mass spectrometry

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Stoichiometry of the periphera ...... etermined by mass spectrometry

@en

Stoichiometry of the periphera ...... etermined by mass spectrometry

@nl

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P1433

Journal of Biological Chemistry

P1476

Stoichiometry of the periphera ...... etermined by mass spectrometry

@en

P2093

Albert J R Heck

http://www.w3.org/2001/XMLSchema#string

Hortense Mazon

http://www.w3.org/2001/XMLSchema#string

Norton Kitagawa

http://www.w3.org/2001/XMLSchema#string

Stephan Wilkens

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P2860

Protein stoichiometry of a multiprotein complex, the human spliceosomal U1 small nuclear ribonucleoprotein: absolute quantification using isotope-coded tags and mass spectrometry

The vacuolar H+-ATPase: a universal proton pump of eukaryotes

Structure of the mitochondrial ATP synthase by electron cryomicroscopy

Calculation of protein extinction coefficients from amino acid sequence data

Probing genuine strong interactions and post-translational modifications in the heterogeneous yeast exosome protein complex.

The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex.

Quantitative analysis of complex protein mixtures using isotope-coded affinity tags

The vacuolar (H+)-ATPases--nature's most versatile proton pumps

Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits

Cysteine-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 domain

P304

3329-37

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scholarly article

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285057

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P356

10.1074/JBC.M707924200

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P433

6

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P478

283

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2008-02-08T00:00:00Z

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18055462

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