Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase - sprookjes - yvandenbroek - TriplyDB

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

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Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases Rotating with the brakes on and other unresolved features of the vacuolar ATPase Membrane protein structures without crystals, by single particle electron cryomicroscopy Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance Regulation of Vacuolar H+-ATPase (V-ATPase) Reassembly by Glycolysis Flow in 6-Phosphofructo-1-kinase (PFK-1)-deficient Yeast Cells.Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states Single-particle cryo-EM data acquisition by using direct electron detection camera.Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.Single-particle electron microscopy in the study of membrane protein structure The changing landscape of membrane protein structural biology through developments in electron microscopy.Structure of the Lipid Nanodisc-reconstituted Vacuolar ATPase Proton Channel: DEFINITION OF THE INTERACTION OF ROTOR AND STATOR AND IMPLICATIONS FOR ENZYME REGULATION BY REVERSIBLE DISSOCIATION.cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination.Breaking up and making up: The secret life of the vacuolar H+ -ATPase.Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor.Oscillating Electric Field Measures the Rotation Rate in a Native Rotary Enzyme Continuous changes in structure mapped by manifold embedding of single-particle data in cryo-EM.Methods to account for movement and flexibility in cryo-EM data processing.Computational Methodologies for Real-Space Structural Refinement of Large Macromolecular Complexes.Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.Elasticity, friction, and pathway of γ-subunit rotation in FoF1-ATP synthase.How does transmembrane electrochemical potential drive the rotation of Fo motor in an ATP synthase?Molecular Interactions and Cellular Itinerary of the Yeast RAVE (Regulator of the H+-ATPase of Vacuolar and Endosomal Membranes) Complex Biophysical comparison of ATP-driven proton pumping mechanisms suggests a kinetic advantage for the rotary process depending on coupling ratio.Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.CryoEM at IUCrJ: a new era Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology.Sequence- and Structure-Based Functional Annotation and Assessment of Metabolic Transporters in Aspergillus oryzae: A Representative Case Study.The Function of V-ATPases in Cancer Unravelling biological macromolecules with cryo-electron microscopy.Recent Insights into the Structure, Regulation, and Function of the V-ATPases Specification of binding modes between a transmembrane peptide mimic of ATP6V0C and polytopic E5 of human papillomavirus-16.Osteoclast proton pump regulator Atp6v1c1 enhances breast cancer growth by activating the mTORC1 pathway and bone metastasis by increasing V-ATPase activity.Regulation of V-ATPase assembly and function of V-ATPases in tumor cell invasiveness.Current strategies for protein production and purification enabling membrane protein structural biology.Neurotransmitter release: vacuolar ATPase V0 sector c-subunits in possible gene or cell therapies for Parkinson's, Alzheimer's, and psychiatric diseases.While the revolution will not be crystallized, biochemistry reigns supreme.A mathematical model of osteoclast acidification during bone resorption.Crystal structure of yeast V1-ATPase in the autoinhibited state.

P2860

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P2860

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

http://www.wikidata.org/entity/Q27700838

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2015 nî lūn-bûn

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2015 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի մայիսին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

@zh-tw

2015年论文

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name

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

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Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@en

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@nl

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label

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@ast

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@en

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@nl

prefLabel

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@ast

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@en

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

@nl

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P1476

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

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P2093

Samir Benlekbir

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P2860

Crystal structure of yeast V-ATPase subunit C reveals its stator function

Accuracy of structure-derived properties in simple comparative models of protein structures

Molecular architecture of the rotary motor in ATP synthase

Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae

Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase

Asymmetric Structure of the Yeast F1 ATPase in the Absence of Bound Nucleotides

Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase

Crystal Structure of the Cytoplasmic N-Terminal Domain of Subunit I, a Homolog of Subunit a, of V-ATPase

Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGChead Peripheral Stalk Complex

Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase

P2888

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241-5

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scholarly article

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1134100

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10.1038/NATURE14365

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7551

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521

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John L. Rubinstein

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2015-05-14T00:00:00Z

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1039389149

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25971514

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