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pro vyhledávání: '"Hannah L. Townsend"'
Publikováno v:
RNA Biology. 5:263-272
A phylogenetically conserved RNA structure within the open reading frame of poliovirus and other group C enteroviruses functions as a competitive inhibitor of the antiviral endoribonuclease RNase L. Hence, we call this viral RNA the RNase L competiti
Autor:
N. Karl Maluf, Jian Qiu Han, Babal K. Jha, Robert H. Silverman, David J. Barton, Hannah L. Townsend
Publikováno v:
RNA. 14:1026-1036
Ribonuclease L (RNase L) is a latent endoribonuclease in an evolutionarily ancient interferon-regulated dsRNA-activated antiviral pathway. 2′–5′ oligoadenylate (2–5A), the product of dsRNA-activated oligoadenylate synthetases (OASes), binds t
Autor:
Robert H. Silverman, David J. Barton, Jayashree M. Paranjape, Babal K. Jha, Hannah L. Townsend, Jian Qiu Han
Publikováno v:
Journal of Virology. 81:5561-5572
RNase L is an antiviral endoribonuclease that cleaves viral mRNAs after single-stranded UA and UU dinucleotides. Poliovirus (PV) mRNA is surprisingly resistant to cleavage by RNase L due to an RNA structure in the 3C Pro open reading frame (ORF). The
Autor:
Paul F. Agris, Hannah L. Townsend, Elzbieta Sochacka, Connie Yarian, Agnieszka Miskiewicz, Wojciech Czestkowski, Richard H. Guenther, Andrzej Malkiewicz
Publikováno v:
Journal of Biological Chemistry. 277:16391-16395
Transfer RNA molecules translate the genetic code by recognizing cognate mRNA codons during protein synthesis. The anticodon wobble at position 34 and the nucleotide immediately 3' to the anticodon triplet at position 37 display a large diversity of
Autor:
Guihua Liu, Paul F. Agris, Winnell Newman, Richard H. Guenther, Michael A. Dolan, Hanna S. Gracz, Hannah L. Townsend, Tim L. Sit, Steven A. Lommel
The 34-nucleotide trans-activator (TA) located within the RNA-2 of Red clover necrotic mosaic virus folds into a simple hairpin. The eight-nucleotide TA loop base pairs with eight complementary nucleotides in the TA binding sequence (TABS) of the cap
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac72d8bd32ce5aa62ef7aa266f8a4cb5
https://europepmc.org/articles/PMC419593/
https://europepmc.org/articles/PMC419593/