L.P.F. Balapiti-Modarage
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Biography and Research Information
OverviewAI-generated summary
L.P.F. Balapiti-Modarage studies the structural basis of enzyme inhibition, with recent work focusing on SARS-CoV-2 Nsp3 macrodomain targeting. This research leverages insights from human poly(ADP-ribose) glycohydrolase (PARG) structures and inhibitors. Balapiti-Modarage has authored 5 publications with 189 citations and an h-index of 2. Key collaborators include Shobanbabu Bommagani and Darin E. Jones, both from the University of Arkansas for Medical Sciences, with whom Balapiti-Modarage shares one publication each. The researcher's work is situated within the broader fields of molecular biology and pharmacology, contributing to the understanding of enzyme function and potential therapeutic targets.
Metrics
- h-index: 2
- Publications: 5
- Citations: 201
Selected Publications
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Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors (2021)
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Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death (2019)
Collaboration Network
Top Collaborators
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
- Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
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