Category: Bowman Publications

Dr. Bowman’s Publications

Cooperative Changes in Solvent Exposure Identify Cryptic Pockets, Switches, and Allosteric Coupling.

Porter J.R., Moeder K.E., Sibbald C.A., Zimmerman M.I., Hart K.M., Greenberg M.J., & Bowman G.R. (2019). “Cooperative Changes in Solvent Exposure Identify Cryptic Pockets, Switches, and Allosteric Coupling.” Biophys J. 2019 Mar 5;116(5):818-830. doi: 10.1016/j.bpj.2018.11.3144. Epub 2019 Jan 25. (Abstract)

Advanced Methods for Accessing Protein Shape-Shifting Present New Therapeutic Opportunities.

Knoverek C.R., Amarasinghe G.K., & Bowman G.R. (2018). “Advanced Methods for Accessing Protein Shape-Shifting Present New Therapeutic Opportunities.” Trends Biochem Sci. 2018 Dec 13. pii: S0968-0004(18)30248-2. doi: 10.1016/j.tibs.2018.11.007. [Epub ahead of print] (Abstract)

Choice of Adaptive Sampling Strategy Impacts State Discovery, Transition Probabilities, and the Apparent Mechanism of Conformational Changes.

Zimmerman M.I., Porter J.R., Sun X., Silva R.R., & Bowman G.R. (2018). “Choice of Adaptive Sampling Strategy Impacts State Discovery, Transition Probabilities, and the Apparent Mechanism of Conformational Changes.” J Chem Theory Comput. 2018 Nov 13;14(11):5459-5475. doi: 10.1021/acs.jctc.8b00500. Epub 2018 Oct 23. (Abstract)

Cooperative changes in solvent exposure identify cryptic pockets, conformational switches, and allosteric coupling

Justin R Porter, Katelyn E Moeder, Carrie A Sibbald, Maxwell I Zimmerman, Kathryn M Hart, Michael J Greenberg, & Gregory R Bowman (2018). “Cooperative changes in solvent exposure identify cryptic pockets, conformational switches, and allosteric coupling” bioRxiv. September 18, 2018. doi.org/10.1101/323568. (Abstract)

Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly.

Su Z., Wu C., Shi L., Luthra P., Pintilie G.D., Johnson B., Porter J.R., Ge P., Chen M., Liu G., Frederick T.E., Binning J.M., Bowman G.R., Zhou Z.H., Basler C.F., Gross M.L., Leung D.W., Chiu W., & Amarasinghe G.K. (2018). “Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly.” Cell. 2018 Feb 22;172(5):966-978.e12. doi: 10.1016/j.cell.2018.02.009. (Abstract)

Prediction of New Stabilizing Mutations Based on Mechanistic Insights from Markov State Models.

Zimmerman M.I., Hart K.M., Sibbald C.A., Frederick T.E., Jimah J.R., Knoverek C.R., Tolia N.H., & Bowman G.R. (2017). “Prediction of New Stabilizing Mutations Based on Mechanistic Insights from Markov State Models.” ACS Cent Sci. 2017 Dec 27;3(12):1311-1321. doi: 10.1021/acscentsci.7b00465. Epub 2017 Nov 21. (Abstract)

Bladder-cancer-associated mutations in RXRA activate peroxisome proliferator-activated receptors to drive urothelial proliferation.

Halstead A.M., Kapadia C.D., Bolzenius J., Chu C.E., Schriefer A., Wartman L.D., Bowman G.R., & Arora V.K. (2017). “Bladder-cancer-associated mutations in RXRA activate peroxisome proliferator-activated receptors to drive urothelial proliferation.” Elife. 2017 Nov 16;6. pii: e30862. doi: 10.7554/eLife.30862. (Abstract)

Endogenous retinoid X receptor ligands in mouse hematopoietic cells.

Niu H., Fujiwara H., di Martino O., Hadwiger G., Frederick T.E., Menéndez-Gutiérrez M.P., Ricote M., Bowman G.R., & Welch J.S. (2017). “Endogenous retinoid X receptor ligands in mouse hematopoietic cells.” Sci Signal. 2017 Oct 31;10(503). pii: eaan1011. doi: 10.1126/scisignal.aan1011. (Abstract)