The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA (Q37029849): Difference between revisions

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reference URL: https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2610503/fullTextXML
based on heuristic: inferred from PubMed Central ID database lookup
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Latest revision as of 00:51, 15 June 2022

scientific article

Language	Label	Description	Also known as
English	The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA	scientific article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

The roles of individual domains of RNase R in substrate binding and exoribonuclease activity. The nuclease domain is sufficient for digestion of structured RNA (English)

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

author name string

Helen A Vincent

1

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

Murray P Deutscher

2

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

language of work or name

0 references

publication date

11 November 2008

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

284

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

1

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

486-494

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

describes a project that uses

1 reference

Europe PubMed Central

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2610503/fullTextXML

based on heuristic

inferred from PubMed Central ID database lookup

Structural basis for processivity and single-strand specificity of RNase II.

1 reference

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29 September 2017

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1 reference

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1 reference

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Nucleic acid melting by Escherichia coli CspE.

1 reference

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1 reference

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An important role for RNase R in mRNA decay

1 reference

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Quality control of ribosomal RNA mediated by polynucleotide phosphorylase and RNase R

1 reference

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The phylogenetic distribution of bacterial ribonucleases.

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RNA quality control: degradation of defective transfer RNA

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Exoribonuclease superfamilies: structural analysis and phylogenetic distribution

1 reference

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Escherichia coli CspA-family RNA chaperones are transcription antiterminators

1 reference

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Action of RNase II and polynucleotide phosphorylase against RNAs containing stem-loops of defined structure

1 reference

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1 reference

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Cold-shock response and cold-shock proteins

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1 reference

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1 reference

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1 reference

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A general two-metal-ion mechanism for catalytic RNA

1 reference

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Crystal structure of CspA, the major cold shock protein of Escherichia coli

1 reference

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The processive reaction mechanism of ribonuclease II.

1 reference

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Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.

1 reference

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29 September 2017

Structure and functions of ribosomal protein S1.

1 reference

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Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12.

1 reference

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Alteration of polynucleotide secondary structure by ribosomal protein S1

1 reference

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1 reference

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Structure of single-stranded nucleic acids in the presence of ribosomal protein S1

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Three amino acids in Escherichia coli CspE surface-exposed aromatic patch are critical for nucleic acid melting activity leading to transcription antitermination and cold acclimation of cells.

1 reference

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The role of the S1 domain in exoribonucleolytic activity: substrate specificity and multimerization

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1 reference

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Substrate recognition and catalysis by the exoribonuclease RNase R.

1 reference

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4 September 2018

Characterization of the functional domains of Escherichia coli RNase II.

1 reference

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4 September 2018

The RNA degradosome and poly(A) polymerase of Escherichia coli are required in vivo for the degradation of small mRNA decay intermediates containing REP-stabilizers.

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4 September 2018

Genomic analysis in Escherichia coli demonstrates differential roles for polynucleotide phosphorylase and RNase II in mRNA abundance and decay

1 reference

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4 September 2018

Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II.

1 reference

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4 September 2018

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1 reference

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4 September 2018

CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone.

1 reference

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4 September 2018

Overexpression, purification, and properties of Escherichia coli ribonuclease II

1 reference

https://pubmed.ncbi.nlm.nih.gov/19004832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

New Insights into the Mechanism of RNA Degradation by Ribonuclease II

1 reference

https://pubmed.ncbi.nlm.nih.gov/19004832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Destabilization of the secondary structure of RNA by ribosomal protein S1 from Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/19004832

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M806468200

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

17 August 2017

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