Author

R. A. Atkinson

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

Signature Assays, Organisms & Methods

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Approach:mechanistic / dynamical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1 Organism:Xenopus· 1

Frequent Co-Authors

A. F. Drake· 2 shared A. J. Mason· 2 shared C. D. Lorenz· 2 shared D. A. Phoenix· 2 shared G. Manzo· 2 shared P. M. Ferguson· 2 shared T. T. Bui· 2 shared V. B. Gustilo· 2 shared

Activity by Year

2018-2018 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 44 mutual co-author links

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2 shared papersBiophysics

A. F. Drake

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2 papers

Recent·Most cited

Minor sequence modifications in temporin B cause drastic changes in antibacterial potency and selectivity by fundamentally altering membrane activity

G. Manzo, P. M. Ferguson, V. B. Gustilo, T. T. Bui, A. F. Drake, R. A. Atkinson, G. Batoni, C. D. Lorenz, D. A. Phoenix, A. J. Mason

The paper investigates how minor sequence changes in temporin B affect its antibacterial potency and selectivity by altering its membrane interaction mechanisms.

bioRxiv · Aug 9, 2018Biophysics

Parallel evolution of frog antimicrobial peptides produces identical conformations but subtly distinct membrane and antibacterial activities

G. Manzo, P. M. Ferguson, C. Hind, M. Clifford, V. B. Gustilo, H. Ali, S. S. Bansal, T. T. Bui, A. F. Drake, R. A. Atkinson, M. J. Sutton, C. D. Lorenz, D. A. Phoenix, A. J. Mason

This study compares two frog antimicrobial peptides, temporin L and aurein 2.5, to understand their differing antibacterial activities despite similar structures.

bioRxiv · Aug 9, 2018Biophysics