Author

J. Clayton

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

Biophysics· 3 Biochemistry· 2 Ecology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:protein structure· 3 Approach:statistical model· 3 Approach:biophysical modeling· 2 Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Organism:virus· 2 Approach:Bayesian inference· 1

Frequent Co-Authors

J. Shen· 3 shared J. Wereszczynski· 2 shared R. Hilgenfeld· 2 shared V. M. de Oliveira· 2 shared X. Sun· 2 shared A. D. Yoder· 1 shared A. Romany· 1 shared B. J. Bradley· 1 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 11 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

3 shared papersBiochemistry

J. Shen

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Why is the Omicron main protease of SARS-CoV-2 less stable than its wild-type counterpart? A crystallographic, biophysical, and theoretical study of the free enzyme and its complex with inhibitor 13b-K

M. Ibrahim, X. Sun, V. M. de Oliveira, R. Liu, J. Clayton, H. El Kilani, J. Shen, R. Hilgenfeld

This study investigates why the Omicron variant's main protease is less stable than the wild-type by analyzing its structure, enzymatic activity, and biophysical properties.

bioRxiv · Mar 4, 2024Biochemistry

Mechanism of Dimer Selectivity and Binding Cooperativity of BRAF inhibitors

J. Clayton, A. Romany, E. Matenoglou, E. Gavathiotis, P. I. Poulikakos, J. Shen

This study uses molecular dynamics simulations to uncover the mechanism of dimer selectivity and binding cooperativity of BRAF inhibitors, revealing structural changes and hydrogen bonding that influence inhibitor binding preferences.

bioRxiv · Dec 12, 2023Biophysics

An Integrative Approach to Dissect the Drug Resistance Mechanism of the H172Y Mutation of SARS-CoV-2 Main Protease

J. Clayton, V. M. de Oliveira, M. F. Ibrahim, X. Sun, P. Mahinthichaichan, M. Shen, R. Hilgenfeld, J. Shen

This study investigates how the H172Y mutation in SARS-CoV-2 Mpro reduces nirmatrelvir efficacy using simulations, AI, and experiments, revealing structural and functional changes in the enzyme.

bioRxiv · Jul 31, 2022Biochemistry

Directed inter-domain motions enable the IsdH Staphylococcus aureus receptor to rapidly extract heme from human hemoglobin

J. Clayton, K. Ellis-Guardiola, B. Mahoney, J. Soule, R. T. Clubb, J. Wereszczynski

This study shows directed inter-domain motions in the IsdH receptor enable efficient heme extraction from human hemoglobin by distorting the heme pocket.

bioRxiv · Dec 28, 2021Biophysics

Molecular adaptation to folivory and the conservation implications for Madagascar's lemurs

E. E. Guevara, L. K. Greene, M. B. Blanco, C. Farmer, J. Ranaivonasy, J. Ratsirarson, K. Mahefarisoa, T. Rajaonarivelo, H. Rakotondrainibe, R. Junge, C. Williams, E. Rambeloson, H. Rasoanaivo, V. Rahalinarivo, L. Andrianandrianina, , A. D. Yoder

This study examines genetic adaptation in RNASE1 across folivorous lemurs to understand dietary specialization and its conservation implications.

bioRxiv · Jul 6, 2021 · PreprintEcology

BEES: Bayesian Ensemble Estimation from SAS

S. Bowerman, J. E. Curtis, J. Clayton, E. H. Brookes, J. Wereszczynski

BEES is a Bayesian tool for fitting ensemble models to SAS data, allowing users to sample and compare models while incorporating additional data.

bioRxiv · Feb 9, 2019Biophysics