Matthew R. Whorton, Ph.D.
Affiliations: | 2008 | University of Michigan, Ann Arbor, Ann Arbor, MI |
Area:
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"Matthew Whorton"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| Roger K. Sunahara | grad student | 2008 | University of Michigan | |
| (The functional significance of G protein -coupled receptor dimerization.) | ||||
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| Martin GM, Yoshioka C, Rex EA, et al. (2017) Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. Elife. 6 |
| Whorton M. (2014) Structural biology: Calcium-activated proteins visualized. Nature. 516: 176-8 |
| Wang W, Whorton MR, MacKinnon R. (2014) Quantitative analysis of mammalian GIRK2 channel regulation by G proteins, the signaling lipid PIP2 and Na+ in a reconstituted system. Elife. 3: e03671 |
| Wang W, Whorton MR, MacKinnon R. (2014) Author response: Quantitative analysis of mammalian GIRK2 channel regulation by G proteins, the signaling lipid PIP2 and Na+ in a reconstituted system Elife |
| Whorton MR, MacKinnon R. (2013) X-ray structure of the mammalian GIRK2-βγ G-protein complex. Nature. 498: 190-7 |
| Whorton MR, MacKinnon R. (2011) Crystal structure of the mammalian GIRK2 K+ channel and gating regulation by G proteins, PIP2, and sodium. Cell. 147: 199-208 |
| Yao XJ, Vélez Ruiz G, Whorton MR, et al. (2009) The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex. Proceedings of the National Academy of Sciences of the United States of America. 106: 9501-6 |
| Whorton MR, Jastrzebska B, Park PS, et al. (2008) Efficient coupling of transducin to monomeric rhodopsin in a phospholipid bilayer. The Journal of Biological Chemistry. 283: 4387-94 |
| Cunliffe JM, Whorton MR, Sunahara RK, et al. (2007) A CE assay for the detection of agonist-stimulated adenylyl cyclase activity. Electrophoresis. 28: 1913-20 |
| Whorton MR, Bokoch MP, Rasmussen SG, et al. (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proceedings of the National Academy of Sciences of the United States of America. 104: 7682-7 |