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November 1, 1987Proceedings of the National Academy of SciencesOpen Access

Capsid protein VP4 of poliovirus is N-myristoylated.

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Population

Poliovirus

Design

Preclinical

Authors

APAniko V. PaulState University of New YorkASA M SchultzThe University of SydneySPS PincusElusys Therapeutics (United States)

Discussion

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Member takes

Implication

Confirms N-myristoylation of poliovirus VP4; leaves open its viability as an antiviral target pending human studies.

Structured PICO

P
Population
Poliovirus
I
Intervention
[3H]myristic acid labeling
O
Outcome
N-myristoylation of capsid protein VP4surrogate

The study demonstrates that the capsid protein VP4 of poliovirus is N-myristoylated at its N-terminal glycine residue.

Cite This Study

Paul et al. (1987) studied this question.

synapsesocial.com/papers/6a20b46bf778797513eb8a15https://doi.org/10.1073/pnas.84.22.7827
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Also Consider

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

  1. 1Identification of the initiation site of poliovirus polyprotein synthesis1982 · 89 citations
  2. 2Implications of the picornavirus capsid structure for polyprotein processing.1987 · 188 citations
  3. 3Bivalent attachment of antibody onto poliovirus leads to conformational alteration and neutralization1983 · 84 citations
  4. 4Guanidine-selected mutants of poliovirus: mapping of point mutations to polypeptide 2C1986 · 177 citations
  5. 5A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation.1984 · 444 citations