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July 1, 1982Proceedings of the National Academy of SciencesOpen Access

Proteolytic processing of poliovirus polypeptides: antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs.

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Population

Cell-free translation extract prepared from poliovirus-infected HeLa cells

Comparison

Antibodies directed against the viral proteins… vs Preimmune antibodies

Design

Preclinical

Authors

RHRonnie HanecakIonis Pharmaceuticals (United States)BSB L SemlerUniversity of California, IrvineCACarl W. AndersonSignum Computer (Germany)

Discussion

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Overview

Localizes poliovirus Gln-Gly protease activity to P3-7c; leaves open whether this informs human antiviral development.

Structured PICO

P
Population
Cell-free translation extract prepared from poliovirus-infected HeLa cells
I
Intervention
Antibodies directed against the viral proteins P3-7c and P2-X
C
Comparator
Preimmune antibodies
O
Outcome
Inhibition of in vitro processing at Gln-Gly pairs

The activity responsible for processing poliovirus polypeptides at Gln-Gly pairs resides in the primary structure of P3-7c (or P3-2 and P3-6a) and not in P2-X.

Cite This Study

Hanecak et al. (1982) studied this question.

synapsesocial.com/papers/6a708f6c8031ec7bb1dc6d5ehttps://doi.org/10.1073/pnas.79.13.3973
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Also Consider

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

  1. 1Cleavage sites within the poliovirus capsid protein precursors1982 · 63 citations
  2. 2The 5'-terminal structures of poliovirion RNA and poliovirus mRNA differ only in the genome-linked protein VPg.1977 · 182 citations
  3. 3The fate of VPg during in vitro translation of poliovirus RNA1981 · 29 citations
  4. 4Protease required for processing picornaviral coat protein resides in the viral replicase gene1979 · 142 citations
  5. 5Translation of Encephalomyocarditis Virus RNA <i>in vitro</i> Yields an Active Proteolytic Processing Enzyme1978 · 153 citations