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Lisa Gawriyski

Researcher at University of Helsinki

Publications -  12
Citations -  141

Lisa Gawriyski is an academic researcher from University of Helsinki. The author has contributed to research in topics: Biology & Interactome. The author has an hindex of 2, co-authored 7 publications receiving 12 citations.

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Combined proximity labeling and affinity purification−mass spectrometry workflow for mapping and visualizing protein interaction networks

TL;DR: The Multiple Approaches Combined (MAC)-tag workflow is developed, which allows for both AP–MS and BioID analysis with a single construct and with almost identical protein purification and mass spectrometry (MS) identification procedures.
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SARS-CoV-2-host proteome interactions for antiviral drug discovery.

TL;DR: In this paper, the authors applied both affinity purification mass spectrometry (AP-MS) and the complementary proximity-based labeling method (BioID-MS), to map the interactions relevant to viral processing.
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DUX4 is a multifunctional factor priming human embryonic genome activation

TL;DR: In this article , double homeobox 4 (DUX4) is expressed at the early pre-implantation stage in human embryos and it is shown that induced human DUX4 expression substantially alters the chromatin accessibility of non-coding DNA and activates thousands of newly identified transcribed enhancer-like regions, preferentially located within ERVL-MaLR repeat elements.
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Molecular pathogenesis of rhegmatogenous retinal detachment

TL;DR: In this paper, the authors performed a molecular level system pathology analysis of the vitreous from 127 patients with Rhegmatogenous Retinal detachment using state-of-the art quantitative mass spectrometry to identify the individual key proteins, as well as the biochemical pathways contributing to the development of the disease.
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The comprehensive interactomes of human adenosine RNA methyltransferases and demethylases reveal distinct functional and regulatory features.

TL;DR: In this paper, the authors present a comprehensive analysis of the interactomes of N6-methyladenosine (m6A) and N6,2'-O-dimethylADenosine(m6Am) enzymes, pointing to specific molecular mechanisms of their regulation.