Recognition of misfolded proteins by Lon, a AAA(+) protease - Wikidata - awgldk - TriplyDB

Recognition of misfolded proteins by Lon, a AAA(+) protease

Recognition of misfolded proteins by Lon, a AAA(+) protease

http://www.wikidata.org/entity/Q34809787

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Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid β-oxidation in peroxisomal matrix Tuning the dials of Synthetic Biology Evolution of the ssrA degradation tag in Mycoplasma: specificity switch to a different protease Multitasking in the mitochondrion by the ATP-dependent Lon protease Evolution and significance of the Lon gene family in Arabidopsis organelle biogenesis and energy metabolism Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Structure of the N-terminal fragment ofEscherichia coliLon protease Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors The N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperones Mitochondrial protein quality control: the mechanisms guarding mitochondrial health Molecular mechanisms of ethanol-induced pathogenesis revealed by RNA-sequencing Stepwise unfolding of a β barrel protein by the AAA+ ClpXP protease.Insights into the gene expression profile of uncultivable hemotrophic Mycoplasma suis during acute infection, obtained using proteome analysis.Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane.Intrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA.Co-evolution of multipartite interactions between an extended tmRNA tag and a robust Lon protease in Mycoplasma.The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpP Multifunctional Mitochondrial AAA Proteases Differential protein acetylation assists import of excess SOD2 into mitochondria and mediates SOD2 aggregation associated with cardiac hypertrophy in the murine SOD2-tg heart.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Chloroplastic Hsp100 chaperones ClpC2 and ClpD interact in vitro with a transit peptide only when it is located at the N-terminus of a protein.Mechanochemical basis of protein degradation by a double-ring AAA+ machine A Lon-like protease with no ATP-powered unfolding activity The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease Distinct quaternary structures of the AAA+ Lon protease control substrate degradation.Adaptor-mediated Lon proteolysis restricts Bacillus subtilis hyperflagellation.Complete Genome Sequence of Thermus aquaticus Y51MC23.Protein Homeostasis Imposes a Barrier on Functional Integration of Horizontally Transferred Genes in Bacteria Protein unfolding and degradation by the AAA+ Lon protease.YoeB toxin is activated during thermal stress.Characterization of the ATP-Dependent Lon-Like Protease in Methanobrevibacter smithii.Oxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerR.Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.Engineering fluorescent protein substrates for the AAA+ Lon protease.Oxygen-sensitive mitochondrial accumulation of cystathionine β-synthase mediated by Lon protease.Proteotoxic stress induces a cell-cycle arrest by stimulating Lon to degrade the replication initiator DnaA Proteins altered by elevated levels of palmitate or glucose implicated in impaired glucose-stimulated insulin secretion.Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine.A mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substrates.

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P2860

Recognition of misfolded proteins by Lon, a AAA(+) protease

http://www.wikidata.org/entity/Q34809787

description

2008 nî lūn-bûn

@nan

2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Recognition of misfolded proteins by Lon, a AAA(+) protease

@ast

Recognition of misfolded proteins by Lon, a AAA(+) protease

@en

Recognition of misfolded proteins by Lon, a AAA(+) protease

@nl

type

label

Recognition of misfolded proteins by Lon, a AAA(+) protease

@ast

Recognition of misfolded proteins by Lon, a AAA(+) protease

@en

Recognition of misfolded proteins by Lon, a AAA(+) protease

@nl

prefLabel

Recognition of misfolded proteins by Lon, a AAA(+) protease

@ast

Recognition of misfolded proteins by Lon, a AAA(+) protease

@en

Recognition of misfolded proteins by Lon, a AAA(+) protease

@nl

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Genes & Development

P1476

Recognition of misfolded proteins by Lon, a AAA(+) protease

@en

P2093

Eyal Gur

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

Robert T Sauer

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

P2860

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

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity

Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine

Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

Molecular chaperones and protein quality control

Sequence requirements for Lon-dependent degradation of the Escherichia coli transcription activator SoxS: identification of the SoxS residues critical to proteolysis and specific inhibition of in vitro degradation by a peptide comprised of the N-ter

Mechanical and chemical unfolding of a single protein: a comparison.

Binding specificity of Escherichia coli trigger factor.

A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity.

ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence.

P304

2267-2277

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scholarly article

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10.1101/GAD.1670908

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16

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22

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2008-08-01T00:00:00Z

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23176030

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18708584

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2518814

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