Match tier
Listed
Presence
Current · Arkansas
Last published
2022
Sources
OpenAlex · ORCID
Refreshed
2026-08-18
E
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Edward J. Selvik's research investigates DNA repair mechanisms, with a specific focus on uracil-DNA glycosylase (UNG) inhibitors. His work has explored targeting the open pre-catalytic active site conformation of human UNG to develop effective inhibitors. Selvik has also contributed to the analysis of plant-plant interactions, identifying potent antileukemic compounds derived from plants. His scholarly output includes three publications, accumulating 26 citations, and he holds an h-index of 1. Selvik collaborates with researchers at the University of Arkansas for Medical Sciences, including Darin E. Jones, David E. Mery, and Philip J. Breen, with whom he has co-authored multiple publications.
Metrics
- h-index: 1
- Publications: 3
- Citations: 29
Selected Publications
-
Analysis of Plant–Plant Interactions Reveals the Presence of Potent Antileukemic Compounds (2022)
-
An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation (2021)
Collaboration Network
Top Collaborators
Darin E. Jones
University of Arkansas for Medical Sciences
2 shared publications
In database
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
- Analysis of Plant–Plant Interactions Reveals the Presence of Potent Antileukemic Compounds
My T. Nguyen
Case Western Reserve University (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Davide Moiani
The University of Texas MD Anderson Cancer Center (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Zamal Ahmed
The University of Texas MD Anderson Cancer Center (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Andy Arvai
Scripps Research Institute (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Sarita Namjoshi
The University of Texas MD Anderson Cancer Center (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Dave S. Shin
Lawrence Berkeley National Laboratory (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Yuriy Fedorov
Case Western Reserve University (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
John J. Pink
Case Western Reserve University (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Yan Yan
Case Western Reserve University (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Daniel J. Laverty
Harvard University (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Zachary D. Nagel
Harvard University (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
John A. Tainer
Lawrence Berkeley National Laboratory (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
Stanton L. Gerson
Case Western Reserve University (US)
1 shared publication
- An effective human uracil-DNA glycosylase inhibitor targets the open pre-catalytic active site conformation
David E. Mery
University of Arkansas for Medical Sciences
1 shared publication
In database
- Analysis of Plant–Plant Interactions Reveals the Presence of Potent Antileukemic Compounds
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