Author

J. G. M. Rack

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· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

M. Schuller· 2 shared A. Aimon· 1 shared A. C. Thwin· 1 shared A. Dias· 1 shared A. Douangamath· 1 shared A. E. Cohen· 1 shared A. J. Powell· 1 shared C. Chatrin· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersCell Biology

M. Schuller

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Author profile →

2 papers

Recent·Most cited

PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities

N. Đukic, O. Stromland, D. Munnur, K. Zhu, M. Schuller, C. Chatrin, P. Kar, J. G. M. Rack, D. Baretic, H. Schüler, S. Wijngaarden, D. V. Filippov, S. Sanyal, R. Smith, D. Ahel, I. Ahel

This study identifies PARP14 as a dual-function enzyme with ADP-ribosyl transferase and hydrolase activities, revealing its role in antiviral responses and substrate specificity.

bioRxiv · Jun 25, 2023Cell Biology

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry