2012
DOI: 10.1016/j.virol.2012.05.024
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Agnoprotein of mammalian polyomaviruses

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Cited by 46 publications
(45 citation statements)
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References 114 publications
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“…Coding mRNAs for these proteins are transcribed later in the infection, initiated by the early T antigens, and like the early proteins are also produced from overlapping coding sequences that are alternatively spliced from a common mRNA. In several members of the mammalian polyomaviruses an additional ‘agnoprotein’ is also expressed, which is thought to be associated with capsid assembly and enhancing viral release [5].…”
Section: Introductionmentioning
confidence: 99%
“…Coding mRNAs for these proteins are transcribed later in the infection, initiated by the early T antigens, and like the early proteins are also produced from overlapping coding sequences that are alternatively spliced from a common mRNA. In several members of the mammalian polyomaviruses an additional ‘agnoprotein’ is also expressed, which is thought to be associated with capsid assembly and enhancing viral release [5].…”
Section: Introductionmentioning
confidence: 99%
“…T-Ag and t-Ag are transcribed early in infection. In a few mammalian polyomaviruses and some avian polyomaviruses, an additional ORF is expressed (VP4) that is thought to play a role in capsid assembly and release (Gerits & Moens, 2012).…”
mentioning
confidence: 99%
“…Conversely, even the largest ORF with 43 amino acids, is smaller than the already known agnoproteins, except for the putative Myotis polyomavirus agnoprotein, which is only 30 amino acids long [18]. Nonetheless, the basic nature and the genomic position are consistent with that of a mammalian polyomavirus agnoprotein [34]. Further research will be necessary to confirm whether one of the 3 putative agnoproteins is expressed and whether it is fully functional.…”
Section: Resultsmentioning
confidence: 99%