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December 1, 1992Journal of VirologyOpen Access

Antiviral effects of a thiol protease inhibitor on foot-and-mouth disease virus

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Population

In vitro translation assay programmed with virion RNA and FMDV-infected cells

Design

Preclinical

Authors

LKLynn G. KleinaMGMarvin J. Grubman

Discussion

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Overview

E-64 compounds merit preclinical antiviral development for FMDV; leaves open translation to natural hosts or clinical use.

Structured PICO

P
Population
In vitro translation assay programmed with virion RNA and FMDV-infected cells
I
Intervention
Thiol protease inhibitor E-64 or its membrane-permeable analog E-64d
O
Outcome
Autocatalytic activity of the leader protease and cleavage of the structural protein precursorsurrogate

E-64-based compounds demonstrate antiviral effects against foot-and-mouth disease virus by inhibiting viral protease activity and reducing virus yield in vitro.

Cite This Study

Kleina et al. (1992) studied this question.

synapsesocial.com/papers/6a7152b0febe604dd70a01ddhttps://doi.org/10.1128/jvi.66.12.7168-7175.1992
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts1987 · 106 citations
  2. 2Poliovirus proteinase 2A induces cleavage of eucaryotic initiation factor 4F polypeptide p2201987 · 321 citations
  3. 3Inhibition of translation in cells infected with a poliovirus 2Apro mutant correlates with phosphorylation of the alpha subunit of eucaryotic initiation factor 21989 · 82 citations
  4. 4Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex.1982 · 589 citations
  5. 5A Gly1 to Ala substitution in poliovirus capsid protein VP0 blocks its myristoylation and prevents viral assembly1991 · 35 citations