Macrolide antibiotics allosterically predispose the ribosome for translation arrest. - Test2 - elhamkhani - TriplyDB

Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

http://www.wikidata.org/entity/Q30584257

about

Ribosomal Antibiotics: Contemporary Challenges Antibiotics: where to throw the spanner in the ribosomal machinery?Sequence selectivity of macrolide-induced translational attenuation The general mode of translation inhibition by macrolide antibiotics Enhanced sampling techniques in molecular dynamics simulations of biological systems.High-resolution structure of the Escherichia coli ribosome.The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center.Molecular dynamics simulations of large macromolecular complexes.Resistance to ketolide antibiotics by coordinated expression of rRNA methyltransferases in a bacterial producer of natural ketolides.Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition.Amino acid sequence repertoire of the bacterial proteome and the occurrence of untranslatable sequences.Binding of Macrolide Antibiotics Leads to Ribosomal Selection against Specific Substrates Based on Their Charge and Size.The Expression of Antibiotic Resistance Methyltransferase Correlates with mRNA Stability Independently of Ribosome Stalling.Toward the rational design of macrolide antibiotics to combat resistance.Macrolide resistance mechanisms in Enterobacteriaceae: Focus on azithromycin.Resistance to Macrolide Antibiotics in Public Health Pathogens.Solithromycin: A Novel Fluoroketolide for the Treatment of Community-Acquired Bacterial Pneumonia.The macrolide antibiotic renaissance.A combined cryo-EM and molecular dynamics approach reveals the mechanism of ErmBL-mediated translation arrest.Structural insights into substrate selectivity of ribosomal RNA methyltransferase RlmCD.Parametrization of macrolide antibiotics using the force field toolkit.Nascent peptide assists the ribosome in recognizing chemically distinct small molecules.RNA Structural Dynamics As Captured by Molecular Simulations: A Comprehensive Overview.Ribosome protection by antibiotic resistance ATP-binding cassette protein.Erythromycin leads to differential protein expression through differences in electrostatic and dispersion interactions with nascent proteins.Structural basis for antibiotic resistance mediated by the ABCF ATPase VmlR Ribosomal stalling landscapes revealed by high-throughput inverse toeprinting of mRNA libraries

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P2860

Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

http://www.wikidata.org/entity/Q30584257

description

2014 nî lūn-bûn

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2014 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2014 թվականի հունիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

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Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

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type

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Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

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Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

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prefLabel

Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

@ast

Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

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

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Macrolide antibiotics allosterically predispose the ribosome for translation arrest.

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Age Brauer

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Alexander S Mankin

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Bo Liu

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Dorota Klepacki

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Haripriya Ramu

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

Nora Vázquez-Laslop

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

Shanmugapriya Sothiselvam

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Wei Han

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

P2860

Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome.

Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria

Structural insight into nascent polypeptide chain-mediated translational stalling.

Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action

Revisiting the structures of several antibiotics bound to the bacterial ribosome

Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide

Structures of the bacterial ribosome at 3.5 A resolution

RNA structure analysis at single nucleotide resolution by selective 2'-hydroxyl acylation and primer extension (SHAPE)

The role of L1 stalk-tRNA interaction in the ribosome elongation cycle

Nascent peptide-mediated translation elongation arrest coupled with mRNA degradation in the CGS1 gene of Arabidopsis

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