M
Meredith N Frazier
Researcher at National Institutes of Health
Publications - 6
Citations - 77
Meredith N Frazier is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Endoribonuclease & RNase P. The author has an hindex of 3, co-authored 6 publications receiving 26 citations.
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Journal ArticleDOI
Characterization of SARS2 Nsp15 nuclease activity reveals it's mad about U.
Meredith N Frazier,Lucas B. Dillard,Juno M. Krahn,Lalith Perera,Jason Williams,Isha M Wilson,Zachary D. Stewart,Monica C. Pillon,Leesa J. Deterding,Mario J. Borgnia,Robin E. Stanley +10 more
TL;DR: In this paper, the authors used cryo-EM to capture structures of Nsp15 bound to RNA in pre-and post-cleavage states, and determined how the sequence of the RNA substrate dictates cleavage and found that outside of polyU tracts, nsp15 has a strong preference for purines 3' of the cleaved uridine.
Journal ArticleDOI
Structural overview of macromolecular machines involved in ribosome biogenesis.
TL;DR: Recent structures revealing molecular insight into higher order enzymatic assemblies are summarized with an emphasis on the interplay between discrete active sites.
Journal ArticleDOI
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics.
Monica C. Pillon,Monica C. Pillon,Meredith N Frazier,Lucas B. Dillard,Jason Williams,Seda Kocaman,Juno M. Krahn,Lalith Perera,Cassandra K. Hayne,Jacob Gordon,Zachary D. Stewart,Mack Sobhany,Leesa J. Deterding,Allen L. Hsu,Venkata P. Dandey,Mario J. Borgnia,Robin E. Stanley +16 more
TL;DR: In this paper, a series of cryo-EM reconstructions of SARS-CoV-2 Nsp15, in both apo and UTP-bound states, are presented.
Posted ContentDOI
Cryo-EM Structures of the SARS-CoV-2 Endoribonuclease Nsp15
Monica C. Pillon,Meredith N Frazier,Lucas B. Dillard,Jason Williams,Kocaman, Seda, Krahn, Juno M.,Perera, Lalith, Hayne, Cassandra K.,Gordon, Jacob, Stewart, Zachary D.,Sobhany, Mack, Deterding, Leesa J.,Allen L. Hsu,Venkata P. Dandey,Mario J. Borgnia,Robin E. Stanley +11 more
TL;DR: A series of cryo-EM reconstructions of SARS-CoV-2 Nsp15 advance understanding of how NSP15 processes viral RNA and provide a structural framework for the development of new therapeutics.
Posted ContentDOI
Characterization of SARS2 Nsp15 Nuclease Activity Reveals it's Mad About U
Meredith N Frazier,Lucas B. Dillard,Juno M. Krahn,Lalith Perera,Jason Williams,Isha M Wilson,Zachary D. Stewart,Monica C. Pillon,Leesa J. Deterding,Mario J. Borgnia,Robin E. Stanley +10 more
TL;DR: In this article, the authors used cryo-EM to capture structures of Nsp15 bound to RNA in pre-and post-cleavage states, and determined how the sequence of the RNA substrate dictates cleavage and found that outside of polyU tracts, Nsp 15 has a strong preference for purines 3 of the cleaved uridine.