Author

T. W. Owens

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 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Organism:virus· 2 Organism:bacteria (other)· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

G. E. Merz· 2 shared H. T. Kratochvil· 2 shared I. D. Young· 2 shared J. K. Peters· 2 shared M. Moritz· 2 shared N. Herrera· 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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Curved chords = mutual co-authorship

2 shared papersBiophysics

G. E. Merz

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiophysicsbioRxivPreprintMay 10, 2021

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…·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.

DOI 10.1101/2021.05.10.443524

viruscryo-EM

𝕏 PostBluesky

BiochemistryScience AdvancesPeer-reviewedApr 16, 2021

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

M. Schuller, G. J. Correy, S. Gahbauer…·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.

DOI 10.1126/sciadv.abf8711

virusstructural biology

𝕏 PostBluesky

MicrobiologybioRxivMay 21, 2020

Structure and reconstitution of a hydrolase complex that releases peptidoglycan from the membrane after polymerization

K. Schaefer, T. W. Owens, J. E. Page…·S. Walker

This paper identifies a hydrolase complex in Staphylococcus aureus that releases peptidoglycan from the membrane by cleaving nascent polymers, enabling their integration into the cell wall matrix.

DOI 10.1038/s41564-020-00808-5

bacteria (other)structural biology

𝕏 PostBluesky