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Richard F. Allison

Researcher at North Carolina State University

Publications -  4
Citations -  628

Richard F. Allison is an academic researcher from North Carolina State University. The author has contributed to research in topics: Nucleic acid sequence & Peptide sequence. The author has an hindex of 4, co-authored 4 publications receiving 625 citations.

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The nucleotide sequence of the coding region of tobacco etch virus genomic RNA: Evidence for the synthesis of a single polyprotein☆

TL;DR: The complete nucleotide sequence of the tobacco etch virus (TEV) RNA genome has been determined excepting only the nucleotide(s) present at the extreme 5' terminus, and a function for the large nuclear inclusion protein is suggested by a comparison of the deduced amino acid sequence with a protein data bank.
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Biochemical analysis of the capsid protein gene and capsid protein of tobacco etch virus: N-terminal amino acids are located on the virion's surface.

TL;DR: The sequence of the 1491 nucleotides found at the 3' end of the genome of the highly aphid-transmissible (HAT) isolate of tobacco etch virus (TEV) has been determined and the deduced amino acid sequences of the two TEV capsid proteins displayed 98% homology and a 66% Homology with PeMV capside protein.
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Nucleotide sequence at the 3' terminus of pepper mottle virus genomic RNA: evidence for an alternative mode of potyvirus capsid protein gene organization

TL;DR: Combined nucleotide and amino acid sequence data suggest that the PeMV capsid protein is encoded by the 3'-most cistron on the genomic RNA and that it may be expressed as a precursor that is proteolytically processed to produce the mature capsidprotein.
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Sequence determination of the capsid protein gene and flanking regions of tobacco etch virus: Evidence for synthesis and processing of a polyprotein in potyvirus genome expression.

TL;DR: Data indicated that maturation of the capsid protein required a post-translational cleavage of a larger protein precursor, with a probable cleavage site between the amino acids glutamine and glycine.