Author

N. R. Silvaggi

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 4

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Approach:statistical model· 2 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Organism:E. coli· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

N. Vuksanovic· 4 shared D. A. Serrano· 2 shared D. Frick· 2 shared R. S. Virdi· 2 shared A. W. Schwabacher· 1 shared B. R. Patterson· 1 shared N. C. Hopper· 1 shared N. Dahal· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

4 shared papersBiochemistry

N. Vuksanovic

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structural and Preliminary Biochemical Characterization of MppQ, a PLP-Dependent Aminotransferase from Streptomyces hygroscopicus

N. Vuksanovic, D. A. Serrano, A. W. Schwabacher, N. R. Silvaggi

This study characterizes MppQ, a PLP-dependent aminotransferase from Streptomyces hygroscopicus, revealing its structure and function in L-enduracididine biosynthesis.

bioRxiv · Apr 3, 2022 · PreprintBiochemistry

Engineering a more specific E. coli glyoxylate/hydroxypyruvate reductase for coupled steady state kinetics assays

N. Vuksanovic, D. A. Serrano, B. R. Patterson, N. R. Silvaggi

The paper engineers a more specific variant of E. coli glyoxylate/hydroxypyruvate reductase (EcGhrA) to improve its use as a coupling enzyme for monitoring aminotransferase activity.

bioRxiv · Apr 2, 2022 · PreprintBiochemistry

Discovery of Drug-like Ligands for the Mac1 Domain of SARS-CoV-2 Nsp3

R. S. Virdi, R. V. Bavisotto, N. C. Hopper, N. Vuksanovic, T. R. Melkonian, N. R. Silvaggi, D. Frick

The paper identifies potential ligands for the SARS-CoV-2 Nsp3 Mac1 domain using a high-throughput DSF assay and validates them with molecular docking and structural analysis.

bioRxiv · Jul 6, 2020Biochemistry

Molecular Basis for ADP-ribose Binding to the Macro-X Domain of SARS-CoV-2 Nsp3

D. Frick, R. S. Virdi, N. Vuksanovic, N. Dahal, N. R. Silvaggi

This study investigates the ADP-ribose binding capability of the SARS-CoV-2 nsp3 macrodomain, revealing its structural conservation despite sequence divergence from other coronaviruses.

bioRxiv · Mar 31, 2020Biochemistry