Author: Myra Hosmillo; Jia Lu; Michael R. McAllaster; James B. Eaglesham; Xinjie Wang; Edward Emmott; Patricia Domingues; Yasmin Chaudhry; Timothy J Fitzmaurice; Matthew K.H. Tung; Marc Panas; Gerald McInerney; Nicholas Locker; Craig B. Willen; Ian Goodfellow
Title: Noroviruses subvert the core stress granule component G3BP1 to promote viral VPg-dependent translation Document date: 2019_3_8
ID: d0q5lhf4_41
Snippet: Our data suggests that G3BP1 plays a key role in promoting the translation of 418 The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It . https://doi.org/10.1101/571455 doi: bioRxiv preprint 20 G3BP1 is known to associate primarily with free 40S subunits and not 80S 426 monosomes (Kedersha et al., 2016) . Our data supports a hypothesis whereby the 427 association of G3BP1 with 40S ribosomal subunits provide.....
Document: Our data suggests that G3BP1 plays a key role in promoting the translation of 418 The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. It . https://doi.org/10.1101/571455 doi: bioRxiv preprint 20 G3BP1 is known to associate primarily with free 40S subunits and not 80S 426 monosomes (Kedersha et al., 2016) . Our data supports a hypothesis whereby the 427 association of G3BP1 with 40S ribosomal subunits provides a selective advantage 428 for norovirus VPg-dependent translation, thereby uncovering a new function in virus 429 specific translation. The mechanism by which G3BP1 contributes to this process has 430 yet to be fully explored but our data supports the hypothesis that G3BP1 directly or 431
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