Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. - Wikidata - awgldk - TriplyDB

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

http://www.wikidata.org/entity/Q31063061

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A common origin for the bacterial toxin-antitoxin systems parD and ccd, suggested by analyses of toxin/target and toxin/antitoxin interactions Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems The solution structure of ParD, the antidote of the ParDE toxin-antitoxin module, provides the structural basis for DNA and toxin binding Doc of Prophage P1 Is Inhibited by Its Antitoxin Partner Phd through Fold Complementation A Conserved Mode of Protein Recognition and Binding in a ParD−ParE Toxin−Antitoxin Complex Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module Structure of the Escherichia coli Antitoxin MqsA (YgiT/b3021) Bound to Its Gene Promoter Reveals Extensive Domain Rearrangements and the Specificity of Transcriptional Regulation Structure and Function of AvtR, a Novel Transcriptional Regulator from a Hyperthermophilic Archaeal Lipothrixvirus Structural Studies of E73 from a Hyperthermophilic Archaeal Virus Identify the “RH3” Domain, an Elaborated Ribbon–Helix–Helix Motif Involved in DNA Recognition The Transcription Factor AmrZ Utilizes Multiple DNA Binding Modes to Recognize Activator and Repressor Sequences of Pseudomonas aeruginosa Virulence Genes Alternative interactions define gyrase specificity in the CcdB family Structural Basis of mRNA Recognition and Cleavage by Toxin MazF and Its Regulation by Antitoxin MazE in Bacillus subtilis Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy A Structure-free Method for Quantifying Conformational Flexibility in proteins.Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state.Molecular mechanism governing ratio-dependent transcription regulation in the ccdAB operon.RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB.parD toxin-antitoxin system of plasmid R1--basic contributions, biotechnological applications and relationships with closely-related toxin-antitoxin systems.Exploiting bacterial DNA gyrase as a drug target: current state and perspectives.Vibrio cholerae ParE2 poisons DNA gyrase via a mechanism distinct from other gyrase inhibitors Recent advancements in toxin and antitoxin systems involved in bacterial programmed cell death.Helicobacter pylori NikR protein exhibits distinct conformations when bound to different promoters.A general model for toxin-antitoxin module dynamics can explain persister cell formation in E. coli.Plasmids of carotenoid-producing Paracoccus spp. (Alphaproteobacteria) - structure, diversity and evolution.Developing Universal Genetic Tools for Rapid and Efficient Deletion Mutation in Vibrio Species Based on Suicide T-Vectors Carrying a Novel Counterselectable Marker, vmi480 Additional role for the ccd operon of F-plasmid as a transmissible persistence factor.Maintenance forced by a restriction-modification system can be modulated by a region in its modification enzyme not essential for methyltransferase activity.The Escherichia coli toxin MqsR destabilizes the transcriptional repression complex formed between the antitoxin MqsA and the mqsRA operon promoter.Stabilization of the Virulence Plasmid pSLT of Salmonella Typhimurium by Three Maintenance Systems and Its Evaluation by Using a New Stability Test.MqsR, a crucial regulator for quorum sensing and biofilm formation, is a GCU-specific mRNA interferase in Escherichia coli.Toxin-antitoxin systems as multilevel interaction systems.Regulating toxin-antitoxin expression: controlled detonation of intracellular molecular timebombs Toxins-antitoxins: diversity, evolution and function.The Pseudomonas aeruginosa AmrZ C-terminal domain mediates tetramerization and is required for its activator and repressor functions Toxin-antitoxin systems in bacterial growth arrest and persistence.VapC6, a ribonucleolytic toxin regulates thermophilicity in the crenarchaeote Sulfolobus solfataricus Stability of the GraA Antitoxin Depends on Growth Phase, ATP Level, and Global Regulator MexT Unrelated toxin-antitoxin systems cooperate to induce persistence.Interactions of Kid-Kis toxin-antitoxin complexes with the parD operator-promoter region of plasmid R1 are piloted by the Kis antitoxin and tuned by the stoichiometry of Kid-Kis oligomers.Linkage, mobility, and selfishness in the MazF family of bacterial toxins: a snapshot of bacterial evolution

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P2860

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

http://www.wikidata.org/entity/Q31063061

description

2006 nî lūn-bûn

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2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

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Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

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type

label

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

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Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

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prefLabel

Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

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Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

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Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA.

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Laurence Van Melderen

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Leila Khatai

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Michal Respondek

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Natacha Mine

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