Dagan C. Marx
Affiliations: | Weill Cornell Medical College, New York, NY, United States |
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Parents
Sign in to add mentor| Madeline A. Shea | research assistant | 2010-2014 | University of Iowa Carver College of Medicine |
| Karen Gibson Fleming | grad student | 2014-2021 | Johns Hopkins |
| David Eliezer | post-doc | 2021- | Weill Cornell Medical College |
| Joshua Levitz | post-doc | 2021- | Weill Cornell Medical College (Neurotree) |
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Publications
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| Lee J, Gonzalez-Hernandez AJ, Kristt M, et al. (2023) Distinct beta-arrestin coupling and intracellular trafficking of metabotropic glutamate receptor homo- and heterodimers. Science Advances. 9: eadi8076 |
| Mancinelli C, Marx DC, Gonzalez-Hernandez AJ, et al. (2023) Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains. Biorxiv : the Preprint Server For Biology |
| Strauss A, Gonzalez-Hernandez AJ, Lee J, et al. (2023) Structural basis of allosteric modulation of metabotropic glutamate receptor activation and desensitization. Biorxiv : the Preprint Server For Biology |
| Devlin T, Marx DC, Roskopf MA, et al. (2023) FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface. Protein Science : a Publication of the Protein Society. e4592 |
| Marx DC, Fleming KG. (2021) Membrane proteins enter the fold. Current Opinion in Structural Biology. 69: 124-130 |
| Mahling R, Hovey L, Isbell HM, et al. (2021) Na1.2 EFL domain allosterically enhances Ca binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD. Structure (London, England : 1993) |
| Vorobieva AA, White P, Liang B, et al. (2021) De novo design of transmembrane β barrels. Science (New York, N.Y.). 371 |
| Marx DC, Fleming KG. (2021) Local Bilayer Hydrophobicity Modulates Membrane Protein Stability. Journal of the American Chemical Society. 143: 764-772 |
| Huysmans GHM, Marx DC, Radford SE, et al. (2020) Determining the Free Energies of Outer Membrane Proteins in Lipid Bilayers. Methods in Molecular Biology (Clifton, N.J.). 2168: 217-232 |
| Marx DC, Plummer AM, Faustino AM, et al. (2020) SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins. Proceedings of the National Academy of Sciences of the United States of America |