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Sean P. J. Whelan
Researcher at Washington University in St. Louis
Publications - 194
Citations - 22049
Sean P. J. Whelan is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Vesicular stomatitis virus & Virus. The author has an hindex of 58, co-authored 171 publications receiving 15387 citations. Previous affiliations of Sean P. J. Whelan include University of Pittsburgh & University of Alabama.
Papers
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Journal ArticleDOI
Erratum: Anterograde or retrograde transsynaptic labeling of CNS neurons with vesicular stomatitis virus vectors (Proceedings of the National Academy of Sciences (2011) 108, 37 (15414-15419) DOI: 10.1073/pnas.1110854108)
Kevin T. Beier,Arpiar Saunders,Ian A. Oldenburg,Kazunari Miyamichi,Nazia Akhtar,Liqun Luo,Sean P. J. Whelan,Bernardo L. Sabatini,Constance L. Cepko +8 more
Posted ContentDOI
FXa cleaves the SARS-CoV-2 spike protein and blocks cell entry to protect against infection with inferior effects in B.1.1.7 variant
Jianhua Yu,Wenjuan Dong,Jing Wang,Lei Tian,Jianying Zhang,Heather L. Mead,Sierra A. Jaramillo,Aimin Li,Ross E. Zumwalt,Sean P. J. Whelan,Erik W. Settles,Paul Keim,Bridget M. Barker,Michael A. Caligiuri +13 more
TL;DR: The authors showed that FXa, a serine protease for blood coagulation, is upregulated in COVID-19 patients compared to non-COVID-2019 donors and exerts anti-viral activity.
Posted ContentDOI
Cellular endosomal potassium ion flux regulates arenavirus uncoating during virus entry
Amelia Shaw,Hiu Nam Tse,Grace Plahe,Alex Moon-Walker,Erica Ollmann-Saphire,Sean P. J. Whelan,Jamel Mankouri,Juan Fontana,John N. Barr +8 more
TL;DR: In this article , an siRNA screen identified K+ channels as important for LCMV infection, and pharmacological inhibition confirmed K+ involvement during entry, suggesting repurposing licensed K+ channel inhibitors represents a potential anti-arenaviral strategy.
Patent
Methods and compositions relating to high resolution structure of non-segmented negative strand virus l proteins
TL;DR: In this paper, methods and compositions relating to the high resolution 3D structure determination for non-segmented negative strand (NNS) virus multifunction L proteins are described, which permits the application of a range of rational drug design and screening approaches to the identification of inhibitors of any of the varying functions of the NNS virus L proteins.