Author

J. K. Peters

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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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein structure prediction· 3 Organism:virus· 3 Assay:structural biology· 2 Assay:cryo-EM· 1 Approach:deep learning· 1 Approach:statistical model· 1

Frequent Co-Authors

G. E. Merz· 2 shared H. T. Kratochvil· 2 shared I. D. Young· 2 shared M. Moritz· 2 shared N. Herrera· 2 shared T. W. Owens· 2 shared U. Schulze-Gahmen· 2 shared A. Aimon· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 43 mutual co-author links

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2 shared papersBiophysics

G. E. Merz

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Author profile →

3 papers

Recent·Most cited

Structure of the poxvirus decapping enzyme D9 reveals its mechanism of cap recognition and catalysis

J. K. Peters, R. W. Tibble, M. Warminski, J. Jemielity, J. D. Gross

The paper determines the structure of the poxvirus decapping enzyme D9, revealing its mechanism for recognizing and catalyzing the removal of the 5' cap from mRNA.

bioRxiv · Oct 4, 2021Biophysics

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

M. Gupta, C. M. Azumaya, M. Moritz, S. Pourmal, A. Diallo, G. E. Merz, G. M. Jang, M. Bouhaddou, A. Fossati, A. F. Brilot, D. Diwanji, E. Hernandez, N. Herrera, H. T. Kratochvil, V. L. Lam, , K. I Pawar

The paper uses cryo-EM and AlphaFold2 to determine the structure of SARS-CoV-2 Nsp2, revealing its zinc-binding site and potential interactions with host proteins.

bioRxiv · May 10, 2021 · PreprintBiophysics

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