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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

http://www.wikidata.org/entity/Q27668103

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Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT)Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections Mycobacterium tuberculosis Eis protein initiates suppression of host immune responses by acetylation of DUSP16/MKP-7 Chemical and Structural Insights into the Regioversatility of the Aminoglycoside Acetyltransferase Eis Potent Inhibitors of Acetyltransferase Eis Overcome Kanamycin Resistance in Mycobacterium tuberculosis Octanoylation of early intermediates of mycobacterial methylglucose lipopolysaccharides A random sequential mechanism of aminoglycoside acetylation by Mycobacterium tuberculosis Eis protein Molecular characterization of amikacin, kanamycin and capreomycin resistance in M/XDR-TB strains isolated in Thailand.New trends in aminoglycosides use.Thermostable hexameric form of Eis (Rv2416c) protein of M. tuberculosis plays an important role for enhanced intracellular survival within macrophages Structure of Mycobacterium smegmatis Eis in complex with paromomycin Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.Rapid synthesis, RNA binding, and antibacterial screening of a peptidic-aminosugar (PA) library Influence of linker length and composition on enzymatic activity and ribosomal binding of neomycin dimers.Inhibition of aminoglycoside acetyltransferase resistance enzymes by metal salts.Amphiphilic Tobramycin Analogues as Antibacterial and Antifungal Agents.Microevolution of extensively drug-resistant tuberculosis in Russia.Identification and characterization of inhibitors of the aminoglycoside resistance acetyltransferase Eis from Mycobacterium tuberculosis Aminoglycoside multiacetylating activity of the enhanced intracellular survival protein from Mycobacterium smegmatis and its inhibition.Synthesis and Biological Activity of Mono- and Di-N-acylated Aminoglycosides.Biochemical and structural analysis of an Eis family aminoglycoside acetyltransferase from bacillus anthracis.Cosubstrate tolerance of the aminoglycoside resistance enzyme Eis from Mycobacterium tuberculosis Biochemical and structural analysis of aminoglycoside acetyltransferase Eis from Anabaena variabilis Arginine-linked neomycin B dimers: synthesis, rRNA binding, and resistance enzyme activity.Mechanisms of Resistance to Aminoglycoside Antibiotics: Overview and Perspectives Unexpected N-acetylation of capreomycin by mycobacterial Eis enzymes.A review of patents (2011-2015) towards combating resistance to and toxicity of aminoglycosides Rise and dissemination of aminoglycoside resistance: the aac(6')-Ib paradigm.Redesign of substrate specificity and identification of the aminoglycoside binding residues of Eis from Mycobacterium tuberculosis.Overexpression of the Rv0805 phosphodiesterase elicits a cAMP-independent transcriptional response Transcriptional Profiling of Mycobacterium tuberculosis Exposed to In Vitro Lysosomal Stress.Synthesis and evaluation of hetero- and homodimers of ribosome-targeting antibiotics: antimicrobial activity, in vitro inhibition of translation, and drug resistance.Comparative Study of Eis-like Enzymes from Pathogenic and Nonpathogenic Bacteria.Synthesis and Bioactivities of Kanamycin B-Derived Cationic Amphiphiles.Understanding and overcoming aminoglycoside resistance caused by N-6'-acetyltransferase.WhiB7, a transcriptional activator that coordinates physiology with intrinsic drug resistance in Mycobacterium tuberculosis.Advances In Mycobacterium Tuberculosis Therapeutics Discovery Utlizing Structural Biology.Molecular biology of drug resistance in Mycobacterium tuberculosis Resistance in tuberculosis: what do we know and where can we go?First Insight Into the Fluoroquinolone and Aminoglycoside Resistance of Multidrug-Resistant Mycobacterium tuberculosis in Saudi Arabia.

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

http://www.wikidata.org/entity/Q27668103

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2011 nî lūn-bûn

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2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2011 թվականի հունիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Proceedings of the National Academy of Sciences of the United States of America

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Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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Oleg V Tsodikov

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Tapan Biswas

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Vanessa R Porter

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Wenjing Chen

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P2860

Eis (enhanced intracellular survival) protein of Mycobacterium tuberculosis disturbs the cross regulation of T-cells

Structure of sterol carrier protein 2 at 1.8 A resolution reveals a hydrophobic tunnel suitable for lipid binding

Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics

Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates

The structural determination of an insect sterol carrier protein-2 with a ligand-bound C16 fatty acid at 1.35-A resolution

Enzyme structural plasticity and the emergence of broad-spectrum antibiotic resistance

The structure of myristoyl-CoA:protein N-myristoyltransferase.

Overexpression and mechanistic analysis of chromosomally encoded aminoglycoside 2'-N-acetyltransferase (AAC(2')-Ic) from Mycobacterium tuberculosis

Mycobacterium tuberculosis eis regulates autophagy, inflammation, and cell death through redox-dependent signaling

Activation of the eis gene in a W-Beijing strain of Mycobacterium tuberculosis correlates with increased SigA levels and enhanced intracellular growth

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10.1073/PNAS.1105379108

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24

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108

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Sylvie Garneau-Tsodikova

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2011-06-14T00:00:00Z

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51180403

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21628583

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