ArticleProceedings of the National Academy of Sciences of the United States of America2001
RNase P-mediated inhibition of cytomegalovirus protease expression and viral DNA encapsidation by oligonucleotide external guide sequences.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Antibody reveals conformational latch regulating dimerization in β- and γ-herpesvirus proteases.Nature communications · 2026Article
- Antibody Reveals Conformational Latch Controlling Herpesvirus Proteases.bioRxiv : the preprint server for biology · 2025Article
- Inhibiting a dynamic viral protease by targeting a non-catalytic cysteine.Cell chemical biology · 2022Article
- RNase P-Mediated Sequence-Specific Cleavage of RNA by Engineered External Guide Sequences.Biomolecules · 2015Review
- Role of Oxidative RNA Damage in Chronic-Degenerative Diseases.Oxidative medicine and cellular longevity · 2015Review
- Modulation of the cellular distribution of human cytomegalovirus helicase by cellular factor Snapin.Journal of virology · 2013Article
- Human cytomegalovirus primase UL70 specifically interacts with cellular factor Snapin.Journal of virology · 2011Article
- Cytomegalovirus antivirals and development of improved animal models.Expert opinion on drug metabolism & toxicology · 2011Review
- Yeast two hybrid analyses reveal novel binary interactions between human cytomegalovirus-encoded virion proteins.PloS one · 2011Article
- Hitting bacteria at the heart of the central dogma: sequence-specific inhibition.Microbial cell factories · 2007Article
- Infection of human cytomegalovirus in cultured human gingival tissue.Virology journal · 2006Article
- Article
- Functional profiling of a human cytomegalovirus genome.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Cytomegalovirus assemblin (pUL80a): cleavage at internal site not essential for virus growth; proteinase absent from virions.Journal of virology · 2002Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
External guide sequences (EGSs) are oligonucleotides that consist of a sequence complementary to a target mRNA and recruit intracellular RNase P for specific degradation of the target RNA. In this study, DNA-based EGS molecules were chemically synthesized to target the mRNA coding for the protease of human cytomegalovirus (HCMV). The EGS molecules efficiently directed human RNase P to cleave the target mRNA sequence in vitro. When EGSs were exogenously administered into HCMV-infected human foreskin fibroblasts, a reduction of about 80-90% in the expression level of the protease and a reduction of about 300-fold in HCMV growth were observed in the cells that were treated with a functional EGS, but not in cells that were not treated with the EGS or with a "disabled" EGS carrying nucleotide mutations that precluded RNase P recognition. Moreover, packaging of the viral DNA genome into the capsid was blocked in the cells treated with the functional EGS. These results indicate that HCMV protease is essential for viral DNA encapsidation. Moreover, our study provides direct evidence that exogenous administration of a DNA-based EGS can be used as a therapeutic approach for inhibiting gene expression and replication of a human virus.
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