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January 16, 2005Journal of Biological ChemistryOpen Access

Crystal Structure of Foot-and-Mouth Disease Virus 3C Protease

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Population

Recombinant form of Foot-and-Mouth Disease Virus (FMDV) 3C protease

Design

Preclinical

Authors

JBJames R. BirtleyHammersmith HospitalSKStephen R. KnoxImperial College LondonAJAgnès M. JaulentEspeRare Foundation

Discussion

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Overview

Provides framework for FMDV 3Cpro inhibitor design; leaves open efficacy in cellular or animal models.

Structured PICO

P
Population
Recombinant form of Foot-and-Mouth Disease Virus (FMDV) 3C protease
I
Intervention
X-ray crystallography and peptide cleavage assays
O
Outcome
Crystal structure resolution and cleavage specificitysurrogate

The determination of the FMDV 3C protease crystal structure and its cleavage specificity provides a structural framework for developing targeted antiviral inhibitors.

Cite This Study

Birtley et al. (2005) studied this question.

synapsesocial.com/papers/6a7fa517feefc34aa44222b0https://doi.org/10.1074/jbc.m413254200
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Also Consider

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  1. 1The complete nucleotide sequence of a common cold virus: human rhinovlrus 141984 · 256 citations
  2. 2Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes1999 · 322 citations
  3. 3Cleavage site analysis in picornaviral polyproteins: Discovering cellular targets by neural networks1996 · 231 citations