Author
R. T. Kennedy
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
Biology Disciplines
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2019-2023 · peak 2/yrCo-Author Collaboration Network
10 top collaborators · 21 mutual co-author links6 papers
Recent·Most cited
- BiochemistrybioRxiv
Methylated guanosine and uridine modifications in S. cerevisiae mRNAs modulate translation elongation
J. D. Jones, M. K. Franco, T. J. Smith…·K. S. Koutmou
This study identifies and quantifies new mRNA modifications in S. cerevisiae and shows how they affect translation elongation.
DOI 10.1039/d2cb00229a - BioengineeringbioRxivPreprint
Mapping enzyme catalysis with metabolomic biosensing
L. Xu, K.-C. Chang, E. M. Payne…·A. R. Abate
The paper introduces a method to sense enzyme product formation using host cell metabolism and mass spectrometry to map enzyme activity and mutagenesis effects.
DOI 10.1101/2021.10.15.464597 - BiochemistrybioRxivPreprint
Viperin inhibits cholesterol biosynthesis and interacts with enzymes in the cholesterol biosynthetic pathway
T. J. Grunkemeyer, S. Ghosh, A. M. Patel…·E. N. G. Marsh
This study shows viperin reduces cholesterol levels by inhibiting key enzymes in the biosynthetic pathway, though the exact mechanism remains unclear.
DOI 10.1101/2021.02.19.431989 - BiochemistrybioRxivPreprint
The Interaction of Viperin with Hepatitis C Virus Non-Structural Protein 5A Inhibits the Catalytic Activity of Viperin
S. Ghosh, A. M. Patel, T. J. Grunkemeyer…·E. N. G. Marsh
This study shows viperin interacts with NS5A and VAP-33, reducing NS5A levels and viperin activity, suggesting NS5A evolved to inhibit ddhCTP synthesis.
DOI 10.1101/824458 - BiochemistrybioRxiv
Targeting Viperin to the Mitochondrion Inhibits the Thiolase Activity of the Trifunctional Enzyme Complex
A. B. Dumbrepatil, K. A. Zegalia, K. Sajja…·E. N. G. Marsh
This paper investigates how HCMV co-opts viperin to inhibit mitochondrial thiolase activity and alter ATP levels, revealing a novel mechanism of viral immune evasion.
DOI 10.1074/jbc.ra119.011526