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Daria V. Rakitina

Researcher at Federal Biomedical Agency

Publications -  25
Citations -  1143

Daria V. Rakitina is an academic researcher from Federal Biomedical Agency. The author has contributed to research in topics: RNA & Cajal body. The author has an hindex of 15, co-authored 25 publications receiving 1001 citations. Previous affiliations of Daria V. Rakitina include Scottish Crop Research Institute & Moscow State University.

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Journal ArticleDOI

Cucumber Mosaic Virus 2b Protein Subcellular Targets and Interactions: Their Significance to RNA Silencing Suppressor Activity

TL;DR: It is shown that the putative nuclear localization signals and phosphorylation motif of the 2b protein are not required for self-interaction or for interaction with AGO proteins, which appears to be indispensable for silencing suppressing activity.
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Cell-to-cell movement of potato potexvirus X is dependent on suppression of RNA silencing.

TL;DR: It is concluded that suppression ofsilencing is not sufficient to allow virus movement between cells: there must be a second P25 function that is independent of silencing but also required for cell-to-cell movement.
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Interaction of a plant virus-encoded protein with the major nucleolar protein fibrillarin is required for systemic virus infection

TL;DR: Previously undescribed functions for fibrillarin are demonstrated as an essential component of translocatable viral RNPs and may have implications for other plant and animal viruses that interact with the nucleolus.
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Cajal bodies and the nucleolus are required for a plant virus systemic infection

TL;DR: The ability of the groundnut rosette virus open reading frame (ORF) 3 protein to move viral RNA long distances through the phloem strictly depends on its interaction with CBs and the nucleolus.
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RNA Helicase Activity of the Plant Virus Movement Proteins Encoded by the First Gene of the Triple Gene Block

TL;DR: A recombinant His-tagged form of TGBp1 of two hordeiviruses and potato virus X, a potexvirus, produced in Escherichia coli had unwinding activity on a partially duplexed RNA, but not DNA substrate.