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Alicia M. Hanson
Researcher at Concordia University Wisconsin
Publications - 20
Citations - 824
Alicia M. Hanson is an academic researcher from Concordia University Wisconsin. The author has contributed to research in topics: Helicase & NS3. The author has an hindex of 10, co-authored 20 publications receiving 680 citations. Previous affiliations of Alicia M. Hanson include New York Medical College & University of Wisconsin–Milwaukee.
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Journal ArticleDOI
Ivermectin is a potent inhibitor of flavivirus replication specifically targeting NS3 helicase activity: new prospects for an old drug
Eloise Mastrangelo,Margherita Pezzullo,Tine De Burghgraeve,Suzanne J.F. Kaptein,Boris Pastorino,Kai Dallmeier,Xavier de Lamballerie,Johan Neyts,Alicia M. Hanson,David N. Frick,Martino Bolognesi,Mario Milani +11 more
TL;DR: Ivermectin, a broadly used anti-helminthic drug, proved to be a highly potent inhibitor of YFV replication and inhibited, although less efficiently, the replication of several other flaviviruses, i.e. dengue fever, Japanese encephalitis and tick-borne encephalopathy viruses.
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Discovering New Medicines Targeting Helicases Challenges and Recent Progress
William R. Shadrick,Jean Ndjomou,Rajesh Kolli,Swagata Mukherjee,Alicia M. Hanson,David N. Frick +5 more
TL;DR: The human DEAD-box protein DDX3 is the cellular antiviral target discussed, and cellular anticancer drug targets discussed are the human RecQ-like helicases and eIF4A.
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Ebselen inhibits hepatitis C virus NS3 helicase binding to nucleic acid and prevents viral replication.
Swagata Mukherjee,Warren S. Weiner,Chad E. Schroeder,Denise S. Simpson,Alicia M. Hanson,Noreena L. Sweeney,Rachel K. Marvin,Jean Ndjomou,Rajesh Kolli,Dragan Isailovic,Frank J. Schoenen,David N. Frick +11 more
TL;DR: Although the above structure–activity relationship studies suggest that ebselen targets a specific site on NS3, it is unable to confirm binding to either the NS3 ATP binding site or nucleic acid binding cleft by examining the effects of ebselsen on NS 3 proteins lacking key cysteines.
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Optimization of potent hepatitis C virus NS3 helicase inhibitors isolated from the yellow dyes thioflavine S and primuline.
Kelin Li,Kevin J. Frankowski,Craig A. Belon,Benjamin Neuenswander,Jean Ndjomou,Alicia M. Hanson,Matthew A. Shanahan,Frank J. Schoenen,Brian S. J. Blagg,Jeffrey Aubé,David N. Frick +10 more
TL;DR: A screen for hepatitis C virus (HCV) NS3 helicase inhibitors revealed that the commercial dye thioflavine S was the most potent inhibitor of NS3-catalyzed DNA and RNA unwinding in the 827-compound National Cancer Institute Mechanistic Set.
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Identification and analysis of hepatitis C virus NS3 helicase inhibitors using nucleic acid binding assays
Swagata Mukherjee,Alicia M. Hanson,William R. Shadrick,Jean Ndjomou,Noreena L. Sweeney,John J. Hernandez,Diana Bartczak,Kelin Li,Kevin J. Frankowski,Julie A. Heck,Leggy A. Arnold,Frank Schoenen,David N. Frick +12 more
TL;DR: Typical assays used to discover and analyze small molecules that inhibit the hepatitis C virus (HCV) NS3 helicase yield few hits and are often confounded by compound interference, so oligonucleotide binding assays are examined here as an alternative.