Author

P. C. Aoto

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Organism:human· 2 Assay:proteomics· 2 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Organism:mouse· 1 Approach:simulation· 1

Frequent Co-Authors

S. S. Taylor· 3 shared F. W. Herberg· 2 shared J.-H. Weng· 2 shared S. H. Schmidt· 2 shared S. Knapp· 2 shared S. Mathea· 2 shared A. M. Wolff· 1 shared D. Boassa· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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3 shared papersBiochemistry

S. S. Taylor

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Author profile →

3 papers

Recent·Most cited

Molecular-Dynamics Simulation Methods for Macromolecular Crystallography

D. C. Wych, P. C. Aoto, L. Vu, A. M. Wolff, D. L. Mobley, J. S. Fraser, S. S. Taylor, M. E. Wall

The paper applies molecular-dynamics simulations to macromolecular crystallography to refine protein structures and improve interpretation of electron density.

bioRxiv · Apr 4, 2022Biophysics

Two helices control the dynamic crosstalk between the catalytic domains of LRRK2

J.-H. Weng, P. C. Aoto, R. Lorenz, J. Wu, S. H. Schmidt, J. T. Manschwetus, P. Kaila-Sharma, S. Mathea, S. Knapp, F. W. Herberg, S. S. Taylor

The paper identifies two helices that regulate the conformation and function of the kinase domain in LRRK2 through dynamic crosstalk.

bioRxiv · Sep 29, 2021 · PreprintBiochemistry

Conformation and dynamics of the kinase domain drive subcellular location and activation of LRRK2

S. H. Schmidt, J.-H. Weng, P. C. Aoto, D. Boassa, S. Mathea, S. Silletti, J. Hu, M. Wallbott, E. A. Komives, S. Knapp, F. W. Herberg, S. S. Taylor

This study investigates how Parkinson's Disease mutations affect LRRK2 activation and subcellular localization through conformational changes and domain interactions.

bioRxiv · Jul 13, 2020Biochemistry