D
David L. Evers
Researcher at Veterans Health Administration
Publications - 16
Citations - 619
David L. Evers is an academic researcher from Veterans Health Administration. The author has contributed to research in topics: Human cytomegalovirus & Transactivation. The author has an hindex of 11, co-authored 16 publications receiving 538 citations. Previous affiliations of David L. Evers include University of North Carolina at Chapel Hill & United States Department of Veterans Affairs.
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Human cytomegalovirus-inhibitory flavonoids: studies on antiviral activity and mechanism of action.
TL;DR: The data suggested that the primary mechanism of action for baicalein may be to block HCMV infection at entry while the primary Mechanism of Action for genistein may is to blockHCMV immediate-early protein functioning.
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The effect of formaldehyde fixation on RNA: optimization of formaldehyde adduct removal.
David L. Evers,Carol B. Fowler,Carol B. Fowler,Brady R. Cunningham,Jeffrey T. Mason,Timothy J. O'Leary +5 more
TL;DR: Formaldehyde-fixed RNA was more labile than native RNA to treatment with heat and buffer, suggesting that antigen retrieval methods for proteins may impede RNA hybridization or RNA extraction.
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3,4',5-Trihydroxy-trans-stilbene (resveratrol) inhibits human cytomegalovirus replication and virus-induced cellular signaling.
TL;DR: Mechanism of action studies determined that resveratrol blocked virus-induced activation of the epidermal growth factor receptor (EGFR) and phosphatidylinositol-3-kinase signal transduction as well as NF-kappaB and Sp1 transcription factor activation shortly following infection.
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Antigen Retrieval Causes Protein Unfolding: Evidence for a Linear Epitope Model of Recovered Immunoreactivity
Carol B. Fowler,David L. Evers,David L. Evers,Timothy J. O'Leary,Timothy J. O'Leary,Jeffrey T. Mason,Jeffrey T. Mason +6 more
TL;DR: Results revealed that for some proteins, formal in treatment left the native protein conformation unaltered, whereas for others, formalin denatured tertiary structure led to irreversible protein unfolding, which supports a linear epitope model of recovered protein immunoreactivity.
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Inhibition of human cytomegalovirus signaling and replication by the immunosuppressant FK778.
TL;DR: The clinical possibility of a single drug treatment to achieve immunosuppression and inhibit opportunistic herpesvirus infections is substantiated and DHODH may be an effective cellular antiviral target.