Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines. - Test2 - elhamkhani - TriplyDB

Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.

Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.

http://www.wikidata.org/entity/Q38660358

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Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways Fundamental Characteristics of AAA+ Protein Family Structure and Function Structural Elements Regulating AAA+ Protein Quality Control Machines.Torsin ATPases: Harnessing Dynamic Instability for Function.Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia.Attenuation of the Type IV Pilus Retraction Motor Influences Neisseria gonorrhoeae Social and Infection Behavior.Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase An intracellular compass spatially coordinates cell cycle modules in Caulobacter crescentus.Assessing heterogeneity in oligomeric AAA+ machines.Regulated Proteolysis in Bacteria: Caulobacter.Structural basis for the disaggregase activity and regulation of Hsp104.Rubisco Activases: AAA+ Chaperones Adapted to Enzyme Repair The Interplay of Cofactor Interactions and Post-translational Modifications in the Regulation of the AAA+ ATPase p97.Selective adaptor dependent protein degradation in bacteria.The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.AAA-ATPases in Protein Degradation.Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase.Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus.The AAA protein Msp1 mediates clearance of excess tail-anchored proteins from the peroxisomal membrane.A simple DNA handle attachment method for single molecule mechanical manipulation experiments.Proteolytic control of the mitochondrial calcium uniporter complex.Cell biology: Phosphate on, rubbish out.Boc3Arg-Linked Ligands Induce Degradation by Localizing Target Proteins to the 20S Proteasome.Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing.The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets.Identification of New Degrons in Streptococcus mutans Reveals a Novel Strategy for Engineering Targeted, Controllable Proteolysis.Activation of a Cell Surface Signaling Pathway in Pseudomonas aeruginosa Requires ClpP Protease and New Sigma Factor Synthesis.Structural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner cavity properties.Regulation of Proteolysis in the Gram-Negative Bacterial Envelope.A Small Periplasmic Protein with a Hydrophobic C-Terminal Residue Enhances DegP Proteolysis as a Suicide Activator.Mutation in human CLPX elevates levels of δ-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria.Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms.Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines.Growth rate correlates negatively with protein turnover in Arabidopsis accessions.Mechanically Watching the ClpXP Proteolytic Machinery.Regulated Proteolysis in Bacteria.Strategies against methicillin-resistant Staphylococcus aureus persisters.Topologically knotted deubiquitinases exhibit unprecedented mechanostability to withstand the proteolysis by an AAA+ protease.

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Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.

http://www.wikidata.org/entity/Q38660358

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2015年学术文章

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2015年学术文章

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2015年學術文章

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2015年學術文章

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2015年學術文章

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name

Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.

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Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.

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Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.

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Nature Reviews Microbiology

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Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.

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Adrian O Olivares

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Robert T Sauer

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Tania A Baker

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P2860

Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX

Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different protease

Mitochondrial AAA proteases--towards a molecular understanding of membrane-bound proteolytic machines

Pupylation as a signal for proteasomal degradation in bacteria

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

Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism

Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.

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

Structural Basis of Mycobacterial Inhibition by Cyclomarin A

Adaptor-Dependent Degradation of a Cell-Cycle Regulator Uses a Unique Substrate Architecture

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