ATP-dependent proteases differ substantially in their ability to unfold globular proteins - Wikidata - wikimedia - TriplyDB

ATP-dependent proteases differ substantially in their ability to unfold globular proteins

ATP-dependent proteases differ substantially in their ability to unfold globular proteins

http://www.wikidata.org/entity/Q37254059

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The ClpS Adaptor Mediates Staged Delivery of N-End Rule Substrates to the AAA+ ClpAP Protease An intersubunit signaling network coordinates ATP hydrolysis by m-AAA proteases Targeting proteins for degradation Disordered proteinaceous machines Stepwise unfolding of a β barrel protein by the AAA+ ClpXP protease.Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane.Rad23 escapes degradation because it lacks a proteasome initiation region Mechanochemical basis of protein degradation by a double-ring AAA+ machine Slipping up: partial substrate degradation by ATP-dependent proteases.Dependence of proteasome processing rate on substrate unfolding Regulated protein turnover: snapshots of the proteasome in action.Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization.Assaying the kinetics of protein denaturation catalyzed by AAA+ unfolding machines and proteases Protein unfolding and degradation by the AAA+ Lon protease.Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.Sequence- and species-dependence of proteasomal processivity.Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37 homologs.Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation Engineering fluorescent protein substrates for the AAA+ Lon protease.Quality control of mitochondrial proteostasis.Regulated proteolysis in Gram-negative bacteria--how and when?Comparison of differential gene expression to water stress among bacteria with relevant pollutant-degradation properties.Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Mini review: ATP-dependent proteases in bacteria.Posttranslational control of the scaffold for Fe-S cluster biogenesis as a compensatory regulatory mechanism.Nonspecific yet decisive: Ubiquitination can affect the native-state dynamics of the modified protein.An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria.Multiple sequence signals direct recognition and degradation of protein substrates by the AAA+ protease HslUV.Slippery substrates impair ATP-dependent protease function by slowing unfolding.A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis.Dissection of Axial-Pore Loop Function during Unfolding and Translocation by a AAA+ Proteolytic Machine.The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradation The ubiquitin ligase Hul5 promotes proteasomal processivity.Identification of New Degrons in Streptococcus mutans Reveals a Novel Strategy for Engineering Targeted, Controllable Proteolysis.The C-terminal region of Bacillus subtilis SwrA is required for activity and adaptor-dependent LonA-proteolysis.Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines.Regulated Proteolysis in Bacteria.

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ATP-dependent proteases differ substantially in their ability to unfold globular proteins

http://www.wikidata.org/entity/Q37254059

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 21 April 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

ATP-dependent proteases differ substantially in their ability to unfold globular proteins

@en

ATP-dependent proteases differ ...... y to unfold globular proteins.

@nl

type

label

ATP-dependent proteases differ substantially in their ability to unfold globular proteins

@en

ATP-dependent proteases differ ...... y to unfold globular proteins.

@nl

prefLabel

ATP-dependent proteases differ substantially in their ability to unfold globular proteins

@en

ATP-dependent proteases differ ...... y to unfold globular proteins.

@nl

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Journal of Biological Chemistry

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ATP-dependent proteases differ substantially in their ability to unfold globular proteins

@en

P2093

Christophe Herman

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

Neil E Jaffe

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

Prakash Koodathingal

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

Susan Fishbain

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

P2860

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism

Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95

Recognition of the polyubiquitin proteolytic signal

Interaction of dihydrofolate reductase with methotrexate: ensemble and single-molecule kinetics.

The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease

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

Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

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18674-18684

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scholarly article

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10.1074/JBC.M900783200

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P433

28

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284

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Andreas Matouschek

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2009-04-21T00:00:00Z

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19383601

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2707231

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