(Q40650358)

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Expression of an RNase P ribozyme against the mRNA encoding human cytomegalovirus protease inhibits viral capsid protein processing and growth

scientific article published on May 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

22 September 2017

Expression of an RNase P ribozyme against the mRNA encoding human cytomegalovirus protease inhibits viral capsid protein processing and growth (English)

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

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author name string

Phong Trang

1

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Kihoon Kim

2

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Jiaming Zhu

3

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Fenyong Liu

4

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Europe PubMed Central

PubMed publication ID

22 September 2017

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publication date

1 May 2003

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Europe PubMed Central

PubMed publication ID

22 September 2017

Journal of Molecular Biology

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Europe PubMed Central

PubMed publication ID

22 September 2017

328

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Europe PubMed Central

PubMed publication ID

22 September 2017

5

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Europe PubMed Central

PubMed publication ID

22 September 2017

1123-1135

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

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Group II introns designed to insert into therapeutically relevant DNA target sites in human cells

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Ribonuclease P: unity and diversity in a tRNA processing ribozyme

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The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme

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External Guide Sequences for an RNA Enzyme

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Rational design of self-cleaving pre-tRNA-ribonuclease P RNA conjugates

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

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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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UV cross-link mapping of the substrate-binding site of an RNase P ribozyme to a target mRNA sequence

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Differential effects of the protein cofactor on the interactions between an RNase P ribozyme and its target mRNA substrate

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Nuclease footprint analyses of the interactions between RNase P ribozyme and a model mRNA substrate

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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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Effective inhibition of human cytomegalovirus gene expression and replication by a ribozyme derived from the catalytic RNA subunit of RNase P from Escherichia coli

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A herpesvirus maturational proteinase, assemblin: identification of its gene, putative active site domain, and cleavage site

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Processing of the herpes simplex virus assembly protein ICP35 near its carboxy terminal end requires the product of the whole of the UL26 reading frame

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Requirements for cleavage by a modified RNase P of a small model substrate

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Targeted cleavage of mRNA by human RNase P

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Inhibition of viral gene expression by human ribonuclease P.

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Expression of small, therapeutic RNAs in human cell nuclei.

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A ribozyme derived from the catalytic subunit of RNase P from Escherichia coli is highly effective in inhibiting replication of herpes simplex virus 1.

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Effective inhibition of herpes simplex virus 1 gene expression and growth by engineered RNase P ribozyme

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Facilitation of hammerhead ribozyme catalysis by the nucleocapsid protein of HIV-1 and the heterogeneous nuclear ribonucleoprotein A1

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Escherichia coli proteins, including ribosomal protein S12, facilitate in vitro splicing of phage T4 introns by acting as RNA chaperones

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Protein enhancement of hammerhead ribozyme catalysis

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Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena

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based on heuristic

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Phenotype of the herpes simplex virus type 1 protease substrate ICP35 mutant virus.

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based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0022-2836(03)00398-X

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

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