Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine - Wikidata - thesis-toulmin - TriplyDB

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

http://www.wikidata.org/entity/Q27677748

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Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation Functions and mechanics of dynein motor proteins Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane.Mechanical operation and intersubunit coordination of ring-shaped molecular motors: insights from single-molecule studies Mechanochemical basis of protein degradation by a double-ring AAA+ machine AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication.Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching Structure and mechanism of the ATPase that powers viral genome packaging.Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy.Transition metal ion FRET uncovers K(+) regulation of a neurotransmitter/sodium symporter.Structural insights into proteasome activation by the 19S regulatory particle.Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase Marching to the beat of the ring: polypeptide translocation by AAA+ proteases.Dynamic look at DNA unwinding by a replicative helicase.Bacterial protein networks: properties and functions.Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins.ESCRT-III and Vps4: a dynamic multipurpose tool for membrane budding and scission.Mini review: ATP-dependent proteases in bacteria.Assessing heterogeneity in oligomeric AAA+ machines.The development of small-molecule modulators for ClpP protease activity.High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx.Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.AAA-ATPases in Protein Degradation.ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function.ClpP-independent function of ClpX interferes with telithromycin resistance conferred by Msr(A) in Staphylococcus aureus.Discovery of a novel ligand that modulates the protein-protein interactions of the AAA+ superfamily oncoprotein reptin.Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle.Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine.The ClpXP protease unfolds substrates using a constant rate of pulling but different gears.Stochastic but highly coordinated protein unfolding and translocation by the ClpXP proteolytic machine.

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Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

http://www.wikidata.org/entity/Q27677748

description

2013 nî lūn-bûn

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2013 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2013 թվականի ապրիլին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@ast

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@en

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@nl

type

label

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@ast

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@en

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@nl

prefLabel

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@ast

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

@en

Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine

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J.CELL.2013.03.029

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Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine

@en

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Andrew R Nager

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

Benjamin M Stinson

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

Karl R Schmitz

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

Tania A Baker

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

P2860

Structural model of F1-ATPase and the implications for rotary catalysis

Mapping the structure and conformational movements of proteins with transition metal ion FRET

Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.

Complete subunit architecture of the proteasome regulatory particle

AAA+ proteins: have engine, will work

Stepwise unfolding of a β barrel protein by the AAA+ ClpXP protease.

Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.

A rotary molecular motor that can work at near 100% efficiency

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

ClpXP, an ATP-powered unfolding and protein-degradation machine

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628-639

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scholarly article

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2779794

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10.1016/J.CELL.2013.03.029

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3

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