Author

A. A. Vinogradov

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· 3 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:deep learning· 2 Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:plant (other)· 1

Frequent Co-Authors

H. Suga· 4 shared H. Onaka· 3 shared Y. Goto· 3 shared M. Shimomura· 2 shared D. B. Ascher· 1 shared G. Kelly· 1 shared H. R. King· 1 shared J. S. Chang· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 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

H. Suga

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Targeting the Plasmodium falciparum UCHL3 ubiquitin hydrolase using chemically constrained peptides

H. R. King, M. Bycroft, T.-B. Nguyen, G. Kelly, A. A. Vinogradov, P. J. Rowling, K. Stott, D. B. Ascher, H. Suga, L. S. Itzhaki, K. Artavanis-Tsakonas

This study identifies chemically constrained peptides that inhibit PfUCHL3, a critical deubiquitinating enzyme in Plasmodium falciparum, by blocking substrate binding rather than active site interaction.

bioRxiv · Jan 11, 2024 · PreprintBiophysics

Accurate models of substrate preferences of post-translational modification enzymes from a combination of mRNA display and deep learning

A. A. Vinogradov, J. S. Chang, H. Onaka, Y. Goto, H. Suga

The paper develops a platform combining mRNA display and deep learning to accurately model substrate preferences of PTM enzymes, showing high accuracy and complexity in enzyme specificity.

bioRxiv · Feb 14, 2022Biochemistry

Promiscuous enzymes cooperate at the substrate level en route to lactazole A

A. A. Vinogradov, M. Shimomura, N. Kano, Y. Goto, H. Onaka, H. Suga

This study investigates the biosynthesis of lactazole A, revealing dynamic enzyme cooperation and kinetic control in thiopeptide assembly using an in vitro system.

bioRxiv · May 12, 2020Biochemistry

Minimal lactazole scaffold for in vitro production of pseudo-natural thiopeptides

A. A. Vinogradov, M. Shimomura, Y. Goto, T. Ozaki, S. Asamizu, Y. Sugai, H. Suga, H. Onaka

This paper develops a platform for in vitro biosynthesis of lactazole A, enabling the creation of diverse thiopeptide analogs with modified structures.

bioRxiv · Oct 16, 2019 · PreprintBiochemistry