1972
DOI: 10.1016/0042-6822(72)90571-5
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The mechanisms of reovirus uncoating and gene activation in vivo

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Cited by 163 publications
(150 citation statements)
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“…Densities of bands corresponding to 3 were divided by those corresponding to 2 as a control for loading. Core protein 2 is not degraded during protease treatment of virions to generate ISVPs (11,14,16,(43)(44)(45). To statistically compare 3/2 ratios between two different conditions, one-tailed, two-sample t tests assuming unequal variance were calculated using Excel 97 (Microsoft, Redmond, WA).…”
Section: Sds-page Of Reovirus Structuralmentioning
confidence: 99%
“…Densities of bands corresponding to 3 were divided by those corresponding to 2 as a control for loading. Core protein 2 is not degraded during protease treatment of virions to generate ISVPs (11,14,16,(43)(44)(45). To statistically compare 3/2 ratios between two different conditions, one-tailed, two-sample t tests assuming unequal variance were calculated using Excel 97 (Microsoft, Redmond, WA).…”
Section: Sds-page Of Reovirus Structuralmentioning
confidence: 99%
“…Following attachment to cell surface receptors sialic acid (9,10) and junctional adhesion molecule 1 (11), reovirus virions are internalized into cells by receptormediated endocytosis (12)(13)(14)(15). Within the endocytic pathway, host proteases catalyze the conversion of virions to infectious subvirion particles (ISVPs) by cleavage of viral outer-capsid proteins (13,(15)(16)(17). In murine fibroblasts, either of the endocytic proteases cathepsin B or cathepsin L are required for viral disassembly (3).…”
Section: Cathepsin B-green Fluorescent Protein (Gfp) Fusion Protein Ementioning
confidence: 99%
“…When virions are used to infect cells in culture, the a3 and ,ulC proteins of infecting virions are cleaved in similar ways as during generation of ISVPs in vitro (33, [38][39][40]. These cleavages may be initiated by proteases inside endosomes or lysosomes, which virions enter after attachment and endocytosis (33).…”
mentioning
confidence: 99%