Author

A. Galera-Prat

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

Biology Disciplines

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Biochemistry· 7 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:drug response / drug discovery· 6 Organism:human· 4 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:E. coli· 1

Frequent Co-Authors

L. Lehtiö· 5 shared M. M. Maksimainen· 5 shared S. T. Sowa· 4 shared H. I. Alanen· 2 shared J. Alaviuhkola· 2 shared J. P. Heiskanen· 2 shared L. Lehtio· 2 shared S. Murthy· 2 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

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5 shared papersBiochemistry

L. Lehtiö

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

High-throughput screening assay for PARP-HPF1 interaction inhibitors to affect DNA damage repair

S. S. Dhakar, A. Galera-Prat, L. Lehtiö

This study develops a FRET-based high-throughput screening assay to identify inhibitors of PARP1/2-HPF1 interaction, discovering two compounds with μM potency.

bioRxiv · Nov 14, 2023Biochemistry

Discovery of 2-amide-3-methylester thiophenes that target SARS-CoV-2 Mac1 and repress coronavirus replication, validating Mac1 as an anti-viral target

S. Wazir, T. A. O. Parviainen, M. M. Maksimainen, M. T. H. Duong, J. J. Pfannenstiel, D. Cluff, S. T. Sowa, A. Galera-Prat, D. V. Ferraris, A. Fehr, J. P. Heiskanen, L. Lehtiö

This paper identifies small molecule inhibitors of SARS-CoV-2 Mac1 that inhibit coronavirus replication, validating Mac1 as an anti-viral target.

bioRxiv · Aug 28, 2023 · PreprintBiochemistry

benzothiazole scaffold as versatile nicotinamide mimic allowing nanomolar inhibition of different PARP enzymes

S. Murthy, M. G. Nizi, M. M. Maksimainen, S. Massari, J. Alaviuhkola, B. E. Lippok, C. Vagaggini, S. T. Sowa, A. Galera-Prat, Y. Ashok, H. Venkannagari, R. Prunskaite-Hyyryläinen, E. Dreassi, B. Lüscher, P. Korn, , L. Lehtiö

The paper identifies a benzothiazole scaffold that inhibits multiple PARP enzymes with nanomolar potency, showing selectivity for mono-ARTs and poly-ARTs.

bioRxiv · Aug 29, 2022Biochemistry

Protein engineering approach to enhance activity assays of mono-ADP-ribosyltransferases through proximity

A. Galera-Prat, J. Alaviuhkola, H. I. Alanen, L. Lehtiö

The paper enhances PARP enzyme activity assays using a scaffold-based system, improving sensitivity and enabling more potent compound discovery.

bioRxiv · Apr 11, 2022Biochemistry

Analogs of TIQ-A as inhibitors of human mono-ADP-ribosylating PARPs

M. M. Maksimainen, S. Murthy, S. T. Sowa, A. Galera-Prat, E. Rolina, J. P. Heiskanen, L. Lehtiö

The paper develops TIQ-A analogs that selectively inhibit mono-ADP-ribosyltransferases PARP10 and PARP15 over poly-ADP-ribosyltransferases, achieving 10-20-fold selectivity while maintaining micromolar potency.

bioRxiv · Aug 30, 2021Biochemistry

A molecular toolbox for ADP-ribosyl binding proteins

S. T. Sowa, A. Galera-Prat, S. Wazir, H. I. Alanen, M. M. Maksimainen, L. Lehtio

The paper develops a molecular toolbox for studying ADP-ribosyl binding proteins, including a fusion tag and high-affinity binders, and identifies suramin as an inhibitor of SARS-CoV-2 nsp3 macrodomain.

bioRxiv · May 31, 2021Biochemistry

Activation of ARTD2/PARP2 by DNA damage induces conformational changes relieving enzyme autoinhibition

E. Obaji, M. M. Maksimainen, A. Galera-Prat, L. Lehtio

The paper describes how DNA damage activates ARTD2/PARP2 through conformational changes that relieve autoinhibition and enable catalytic activity.

bioRxiv · Nov 24, 2020Biochemistry

Cohesin-dockerin code in cellulosomal dual binding modes and its allosteric regulation by proline isomerization

A. M. Vera, A. Galera-Prat, M. Wojciechowski, B. Rozycki, D. V. Laurents, M. Carrion-Vazquez, M. Cieplak, P. Tinnefeld

The paper investigates cohesin-dockerin interactions in cellulosomes, revealing two binding modes and an allosteric regulation mechanism via proline isomerization.

bioRxiv · Dec 19, 2019Biophysics