Interrupted catalysis: the EF4 (LepA) effect on back-translocation. - Test2 - elhamkhani - TriplyDB

Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

http://www.wikidata.org/entity/Q30502530

about

Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome Probing translation with small-molecule inhibitors EF-G and EF4: translocation and back-translocation on the bacterial ribosome.CpLEPA is critical for chloroplast protein synthesis under suboptimal conditions in Arabidopsis thaliana.The bacterial translation stress response.The conserved GTPase LepA contributes mainly to translation initiation in Escherichia coli.Elongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations.Dynamics of forward and backward translocation of mRNA in the ribosome.Differential effects of thiopeptide and orthosomycin antibiotics on translational GTPases.Ribosomal elongation factor 4 promotes cell death associated with lethal stress The conserved protein EF4 (LepA) modulates the elongation cycle of protein synthesis Allosteric vs. spontaneous exit-site (E-site) tRNA dissociation early in protein synthesis Real-time assay for testing components of protein synthesis.Dynamics of translation by single ribosomes through mRNA secondary structures.Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome.Elongation factor 4 remodels the A-site tRNA on the ribosome Monitoring translation with modified mRNAs strategically labeled with isomorphic fluorescent guanosine mimetics.Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function The paradox of elongation factor 4: highly conserved, yet of no physiological significance?Conserved GTPase LepA (Elongation Factor 4) functions in biogenesis of the 30S subunit of the 70S ribosome.Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function.Mammalian elongation factor 4 regulates mitochondrial translation essential for spermatogenesis.EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon-anticodon duplex.Roles of elusive translational GTPases come to light and inform on the process of ribosome biogenesis in bacteria.

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P2860

Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

http://www.wikidata.org/entity/Q30502530

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

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Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

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Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

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Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

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Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

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Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

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J.JMB.2009.12.043

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Journal of Molecular Biology

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Interrupted catalysis: the EF4 (LepA) effect on back-translocation.

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P2093

Barry S Cooperman

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

Dongli Pan

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

Markus Pech

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P2860

GTP-binding membrane protein of Escherichia coli with sequence homology to initiation factor 2 and elongation factors Tu and G

The structure of LepA, the ribosomal back translocase

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit

Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3.

Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors

A Steric Block in Translation Caused by the Antibiotic Spectinomycin

A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation

The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome

Translation factor LepA contributes to tellurite resistance in Escherichia coli but plays no apparent role in the fidelity of protein synthesis.

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10.1016/J.JMB.2009.12.043

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