Evidence for rotation of V1-ATPase. - Wikidata - wikimedia - TriplyDB

Evidence for rotation of V1-ATPase.

Evidence for rotation of V1-ATPase.

http://www.wikidata.org/entity/Q34804967

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The d subunit plays a central role in human vacuolar H(+)-ATPases Crystal structure of yeast V-ATPase subunit C reveals its stator function Structure of the yeast vacuolar ATPase Flexibility within the rotor and stators of the vacuolar H+-ATPase Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilus Topological characterization of the c, c', and c" subunits of the vacuolar ATPase from the yeast Saccharomyces cerevisiae.Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum 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 Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus F1 rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft Molecular structure and rotary dynamics of Enterococcus hirae V₁-ATPase.Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus Rotation scheme of V1-motor is different from that of F1-motor.Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor.The stator complex of the A1A0-ATP synthase--structural characterization of the E and H subunits.Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements.Inhibition of osteoclast bone resorption by disrupting vacuolar H+-ATPase a3-B2 subunit interaction.PA1b inhibitor binding to subunits c and e of the vacuolar ATPase reveals its insecticidal mechanism Regulation and isoform function of the V-ATPases.The F subunit of Thermus thermophilus V1-ATPase promotes ATPase activity but is not necessary for rotation.Seventeen a-subunit isoforms of paramecium V-ATPase provide high specialization in localization and function.Structural and functional separation of the N- and C-terminal domains of the yeast V-ATPase subunit H.Renal vacuolar H+-ATPase.Torque generation of Enterococcus hirae V-ATPase.Resolving stepping rotation in Thermus thermophilus H(+)-ATPase/synthase with an essentially drag-free probe.Definition of membrane topology and identification of residues important for transport in subunit a of the vacuolar ATPase.ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus A nanobuffer reporter library for fine-scale imaging and perturbation of endocytic organelles Purification, crystallization and preliminary crystallographic analysis of the vacuole-type ATPase subunit E from Pyrococcus horikoshii OT3 Investigation of endosome and lysosome biology by ultra pH-sensitive nanoprobes.Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide.Dodecamer rotor ring defines H+/ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus.The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase.Regulation of transport in the connecting tubule and cortical collecting duct Biological Nanomotors with a Revolution, Linear, or Rotation Motion Mechanism Arrangement of subunits in the proteolipid ring of the V-ATPase.Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity.Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F.

P2860

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P2860

Evidence for rotation of V1-ATPase.

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2003 nî lūn-bûn

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2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Evidence for rotation of V1-ATPase.

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Proceedings of the National Academy of Sciences of the United States of America

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Evidence for rotation of V1-ATPase

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P2093

Eiro Muneyuki

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

Hiroyuki Noji

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

Ken Yokoyama

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

Masahiro Nakano

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

Masasuke Yoshida

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

Shoji Ohkuma

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P2860

Structure, function and regulation of the vacuolar (H+)-ATPase

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

The binding change mechanism for ATP synthase--some probabilities and possibilities

Direct observation of the rotation of F1-ATPase

Catalytic site forms and controls in ATP synthase catalysis.

Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.

Pause and rotation of F(1)-ATPase during catalysis

ATP synthase--a marvellous rotary engine of the cell.

Thermus thermophilus membrane-associated ATPase. Indication of a eubacterial V-type ATPase.

Isolation of prokaryotic V0V1-ATPase from a thermophilic eubacterium Thermus thermophilus.

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