(Q37704699)

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Inhibition of gene expression by RNase P.

scientific article published on 06 March 2010

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22 August 2017

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Europe PubMed Central

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Inhibition of gene expression by RNase P. (English)

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Europe PubMed Central

22 August 2017

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Sidney Altman

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stated in

Europe PubMed Central

22 August 2017

Eirik Wasmuth Lundblad

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stated in

Europe PubMed Central

22 August 2017

6 March 2010

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Europe PubMed Central

22 August 2017

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Europe PubMed Central

22 August 2017

27

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Europe PubMed Central

22 August 2017

212-221

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Europe PubMed Central

22 August 2017

3

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Europe PubMed Central

22 August 2017

Inhibition of viral gene expression by the catalytic RNA subunit of RNase P from Escherichia coli.

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RNase P ribozyme inhibits cytomegalovirus replication by blocking the expression of viral capsid proteins

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Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA.

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Cleavage by RNase P of gene N mRNA reduces bacteriophage lambda burst size

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Coordinate inhibition of expression of several genes for protein subunits of human nuclear RNase P.

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Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP

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Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis

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OLE RNA, an RNA motif that is highly conserved in several extremophilic bacteria, is a substrate for and can be regulated by RNase P RNA.

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RNase P ribozymes selected in vitro to cleave a viral mRNA effectively inhibit its expression in cell culture

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External Guide Sequences for an RNA Enzyme

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Engineered RNase P ribozymes inhibit gene expression and growth of cytomegalovirus by increasing rate of cleavage and substrate binding.

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The precursor tRNA 3'-CCA interaction with Escherichia coli RNase P RNA is essential for catalysis by RNase P in vivo

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10.1016/J.NBT.2010.03.003

1 reference

stated in

Europe PubMed Central

22 August 2017

1 reference

Europe PubMed Central

PubMed ID

20211282

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22 August 2017

(Q37704699)

Inhibition of gene expression by RNase P.

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