The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease. - Wikidata - wikimedia - TriplyDB

The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.

The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.

http://www.wikidata.org/entity/Q34615400

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Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and Disease Microbial biofilm formation: a need to act Acyldepsipeptide antibiotics induce the formation of a structured axial channel in ClpP: A model for the ClpX/ClpA-bound state of ClpP.Structural Basis of Mycobacterial Inhibition by Cyclomarin A Lassomycin, a Ribosomally Synthesized Cyclic Peptide, Kills Mycobacterium tuberculosis by Targeting the ATP-Dependent Protease ClpC1P1P2 Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection A Conformationally Constrained Cyclic Acyldepsipeptide Is Highly Effective in Mice Infected with Methicillin-Susceptible and -Resistant Staphylococcus aureus Segregation of molecules at cell division reveals native protein localization.Activated ClpP kills persisters and eradicates a chronic biofilm infection ClpXP, an ATP-powered unfolding and protein-degradation machine Antibiotic acyldepsipeptides activate ClpP peptidase to degrade the cell division protein FtsZ Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP.Mycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.The cyclic peptide ecumicin targeting ClpC1 is active against Mycobacterium tuberculosis in vivo.The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1 Target mechanism-based whole-cell screening identifies bortezomib as an inhibitor of caseinolytic protease in mycobacteria The tuberculosis drug discovery and development pipeline and emerging drug targets.Structure and Functional Properties of the Active Form of the Proteolytic Complex, ClpP1P2, from Mycobacterium tuberculosis.Roles of adaptor proteins in regulation of bacterial proteolysis Sclerotiamide: The First Non-Peptide-Based Natural Product Activator of Bacterial Caseinolytic Protease P.Examination of a Structural Model of Peptidomimicry by Cyclic Acyldepsipeptide Antibiotics in Their Interaction with the ClpP Peptidase Regulated proteolysis in bacterial development.How to cope with the quest for new antibiotics.Proteomic signatures in antibiotic research.Proteases in Mycobacterium tuberculosis pathogenesis: potential as drug targets.mazEF-mediated programmed cell death in bacteria: "what is this?".Tuberculosis drug discovery and emerging targets.Staphylococcus aureus chronic and relapsing infections: Evidence of a role for persister cells: An investigation of persister cells, their formation and their role in S. aureus disease.Functional Diversity of AAA+ Protease Complexes in Bacillus subtilis.Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines.Mini review: ATP-dependent proteases in bacteria.Acyldepsipeptide antibiotics as a potential therapeutic agent against Clostridium difficile recurrent infections.The development of small-molecule modulators for ClpP protease activity.Bacterial proteases, untapped antimicrobial drug targets.Restriction of the conformational dynamics of the cyclic acyldepsipeptide antibiotics improves their antibacterial activity.Antibiotics and iron-limiting conditions and their effect on the production and composition of outer membrane vesicles secreted from clinical isolates of extraintestinal pathogenic E. coli.Antibiotics: Precious Goods in Changing Times.The Cell Wall Polymer Lipoteichoic Acid Becomes Nonessential in Staphylococcus aureus Cells Lacking the ClpX Chaperone.

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P2860

The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.

http://www.wikidata.org/entity/Q34615400

description

2009 nî lūn-bûn

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2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2009 թվականի ապրիլին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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type

label

The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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prefLabel

The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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EMBO Molecular Medicine

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The antibiotic ADEP reprogramm ...... d to an uncontrolled protease.

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Anja Hoffmann

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Hauke Lilie

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Heike Brötz-Oesterhelt

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Helga Rübsamen-Waigmann

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Janine Kirstein

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Kürşad Turgay

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Ronny Schmidt

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P2860

Bleach activates a redox-regulated chaperone by oxidative protein unfolding

The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

Molecular chaperones in the cytosol: from nascent chain to folded protein

A common mechanism of cellular death induced by bactericidal antibiotics

Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli

MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis

Adaptor protein controlled oligomerization activates the AAA+ protein ClpC

The antibiotic resistome: the nexus of chemical and genetic diversity

Molecular chaperones and protein quality control

Antibacterial resistance worldwide: causes, challenges and responses

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10.1002/EMMM.200900002

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1

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1

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