Author

J. M. Muretta

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· 3

Signature Assays, Organisms & Methods

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Approach:biophysical modeling· 2 Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Approach:mechanistic / dynamical model· 1 Assay:proteomics· 1 Assay:structural biology· 1

Frequent Co-Authors

D. D. Thomas· 3 shared N. M. Levinson· 2 shared A. R. Thompson· 1 shared A. Thompson· 1 shared D. M. Rasmussen· 1 shared E. F. Ruff· 1 shared E. W. Lake· 1 shared J. A. Rohde· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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3 shared papersBiophysics

D. D. Thomas

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3 papers

Recent·Most cited

Allosteric coupling asymmetry mediates paradoxical activation of BRAF by type II inhibitors

D. M. Rasmussen, M. M. Semonis, J. T. Greene, J. M. Muretta, A. R. Thompson, S. T. Ramos, D. D. Thomas, W. C. K. Pomerantz, T. S. Freedman, N. M. Levinson

The paper explains how type II RAF inhibitors paradoxically activate BRAF by inducing asymmetric dimerization, using biophysical and structural methods.

bioRxiv · Apr 18, 2023Biophysics

Mavacamten stabilizes the auto-inhibited state of two-headed cardiac myosin

J. A. Rohde, D. D. Thomas, J. M. Muretta

This paper investigates how mavacamten stabilizes the auto-inhibited state of two-headed cardiac myosin through biochemical and structural kinetics.

bioRxiv · Mar 23, 2018Biophysics

A dynamic mechanism for allosteric activation of Aurora kinase A by activation loop phosphorylation

E. F. Ruff, J. M. Muretta, A. Thompson, E. W. Lake, S. Cyphers, S. K. Albanese, S. M. Hanson, J. M. Behr, D. D. Thomas, J. D. Chodera, N. M. Levinson

This study shows that phosphorylation of Aurora A's activation loop activates the kinase without shifting the DFG-In state population, and that a DFG-Out subpopulation is important for optimized substrate binding kinetics.

bioRxiv · Oct 18, 2017Biophysics