Ribosomal protein S1 influences trans-translation in vitro and in vivo - Wikidata - awgldk - TriplyDB

Ribosomal protein S1 influences trans-translation in vitro and in vivo

Ribosomal protein S1 influences trans-translation in vitro and in vivo

http://www.wikidata.org/entity/Q42779785

about

Pyrazinamide inhibits trans-translation in Mycobacterium tuberculosis The role of upstream sequences in selecting the reading frame on tmRNA.Direct interaction of the N-terminal domain of ribosomal protein S1 with protein S2 in Escherichia coli.Requirements for resuming translation in chimeric transfer-messenger RNAs of Escherichia coli and Mycobacterium tuberculosis The deleterious effect of an insertion sequence removing the last twenty percent of the essential Escherichia coli rpsA gene is due to mRNA destabilization, not protein truncation Ribosomal protein S1 unwinds double-stranded RNA in multiple steps.SmpB contributes to reading frame selection in the translation of transfer-messenger RNA tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation Molecular biology of drug resistance in Mycobacterium tuberculosis Mechanism of trans-translation revealed by in vitro studies.Trends in discovery of new drugs for tuberculosis therapy.Antibiotic resistance mechanisms in M. tuberculosis: an update.Role of the C-terminal tail of SmpB in the early stage of trans-translation.A multiple genome analysis of Mycobacterium tuberculosis reveals specific novel genes and mutations associated with pyrazinamide resistance.Polynucleotide phosphorylase hinders mRNA degradation upon ribosomal protein S1 overexpression in Escherichia coli.Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM.An A/U-Rich Enhancer Region Is Required for High-Level Protein Secretion through the HlyA Type I Secretion System.(1)H, (15)N, (13)C resonance assignments for pyrazinoic acid binding domain of ribosomal protein S1 from Mycobacterium tuberculosis.

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P2860

Ribosomal protein S1 influences trans-translation in vitro and in vivo

http://www.wikidata.org/entity/Q42779785

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

@zh-cn

name

Ribosomal protein S1 influences trans-translation in vitro and in vivo

@en

Ribosomal protein S1 influences trans-translation in vitro and in vivo

@nl

type

label

Ribosomal protein S1 influences trans-translation in vitro and in vivo

@en

Ribosomal protein S1 influences trans-translation in vitro and in vivo

@nl

prefLabel

Ribosomal protein S1 influences trans-translation in vitro and in vivo

@en

Ribosomal protein S1 influences trans-translation in vitro and in vivo

@nl

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P1433

Nucleic Acids Research

P1476

Ribosomal protein S1 influences trans-translation in vitro and in vivo

@en

P2093

Brice Felden

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

Matthieu Saguy

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

Patricia Skorski

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

Reynald Gillet

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

Sylvie Hermann-Le Denmat

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P2860

A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli

Scaffolding as an Organizing Principle in Trans-translation: THE ROLES OF SMALL PROTEIN B AND RIBOSOMAL PROTEIN S1

Visualizing tmRNA entry into a stalled ribosome

The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold

Function of the SmpB tail in transfer-messenger RNA translation revealed by a nucleus-encoded form.

The last RNA-binding repeat of the Escherichia coli ribosomal protein S1 is specifically involved in autogenous control

Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA.

Binding and cross-linking of tmRNA to ribosomal protein S1, on and off the Escherichia coli ribosome.

Protein factors associated with the SsrA.SmpB tagging and ribosome rescue complex.

tmRNA and associated ligands: a puzzling relationship.

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2368-2376

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scholarly article

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10.1093/NAR/GKM100

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7

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35

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2007-03-28T00:00:00Z

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51376788

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17392345

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1874662

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