Publications

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Whittle, J. R. R., and Schwartz, T. U. (2009) Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element. J Biol Chem. 284, 28442-52
Whorton, M. R., and MacKinnon, R. (2011) Crystal structure of the mammalian GIRK2 K+ channel and gating regulation by G proteins, PIP2, and sodium. Cell. 147, 199-208
Wicky, B. I. M., Milles, L. F., Courbet, A., Ragotte, R. J., Dauparas, J., Kinfu, E., Tipps, S., Kibler, R. D., Baek, M., DiMaio, F., Li, X., Carter, L., Kang, A., Nguyen, H., Bera, A. K., and Baker, D. (2022) Hallucinating symmetric protein assemblies. Science. 378, 56-61
Widjaja-Adhi, M. Airanthi K., and Golczak, M. (2020) The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates. Biochim Biophys Acta Mol Cell Biol Lipids. 1865, 158571
Wiechmann, S., Maisonneuve, P., Grebbin, B. Moyo, Hoffmeister, M., Kaulich, M., Clevers, H., Rajalingam, K., Kurinov, I., Farin, H. F., Sicheri, F., and Ernst, A. (2020) Conformation-specific inhibitors of activated Ras GTPases reveal limited Ras dependency of patient-derived cancer organoids. J Biol Chem. 10.1074/jbc.RA119.011025
Wilker, E. W., Grant, R. A., Artim, S. C., and Yaffe, M. B. (2005) A structural basis for 14-3-3sigma functional specificity. J Biol Chem. 280, 18891-8
Williams, K. M., Qie, S., Atkison, J. H., Salazar-Arango, S., J Diehl, A., and Olsen, S. K. (2019) Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34. Nat Commun. 10, 3296
Williams, W. B., R Meyerhoff, R., Edwards, R. J., Li, H., Manne, K., Nicely, N. I., Henderson, R., Zhou, Y., Janowska, K., Mansouri, K., Gobeil, S., Evangelous, T., Hora, B., Berry, M., A Abuahmad, Y., Sprenz, J., Deyton, M., Stalls, V., Kopp, M., Hsu, A. L., Borgnia, M. J., Stewart-Jones, G. B. E., Lee, M. S., Bronkema, N., M Moody, A., Wiehe, K., Bradley, T., S Alam, M., Parks, R. J., Foulger, A., Oguin, T., Sempowski, G. D., Bonsignori, M., LaBranche, C. C., Montefiori, D. C., Seaman, M., Santra, S., Perfect, J., Francica, J. R., Lynn, G. M., Aussedat, B., Walkowicz, W. E., Laga, R., Kelsoe, G., Saunders, K. O., Fera, D., Kwong, P. D., Seder, R. A., Bartesaghi, A., Shaw, G. M., Acharya, P., and Haynes, B. F. (2021) Fab-dimerized glycan-reactive antibodies are a structural category of natural antibodies. Cell. 184, 2955-2972.e25
Wilson, S. C., K White, I., Zhou, Q., Pfuetzner, R. A., Choi, U. B., Südhof, T. C., and Brunger, A. T. (2019) Structures of neurexophilin-neurexin complexes reveal a regulatory mechanism of alternative splicing. EMBO J. 10.15252/embj.2019101603
Wiltzius, J. J. W., Sievers, S. A., Sawaya, M. R., and Eisenberg, D. (2009) Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process. Protein Sci. 18, 1521-30
Wiltzius, J. J. W., Landau, M., Nelson, R., Sawaya, M. R., Apostol, M. I., Goldschmidt, L., Soriaga, A. B., Cascio, D., Rajashankar, K., and Eisenberg, D. (2009) Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol. 16, 973-8
Windsor, M. A., Hermanson, D. J., Kingsley, P. J., Xu, S., Crews, B. C., Ho, W., Keenan, C. M., Banerjee, S., Sharkey, K. A., and Marnett, L. J. (2012) Substrate-Selective Inhibition of Cyclooxygenase-2: Development and Evaluation of Achiral Profen Probes. ACS Med Chem Lett. 3, 759-763
Windsor, M. A., Valk, P. L., Xu, S., Banerjee, S., and Marnett, L. J. (2013) Exploring the molecular determinants of substrate-selective inhibition of cyclooxygenase-2 by lumiracoxib. Bioorg Med Chem Lett. 23, 5860-4
Wing, R. A., Bailey, S., and Steitz, T. A. (2008) Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit. J Mol Biol. 382, 859-69
Winter, J. M., Cascio, D., Dietrich, D., Sato, M., Watanabe, K., Sawaya, M. R., Vederas, J. C., and Tang, Y. (2015) Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis. J Am Chem Soc. 137, 9885-93
Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., and Bradner, J. E. (2015) DRUG DEVELOPMENT. Phthalimide conjugation as a strategy for in vivo target protein degradation. Science. 348, 1376-81
R Wiseman, L., Zhang, Y., Lee, K. P. K., Harding, H. P., Haynes, C. M., Price, J., Sicheri, F., and Ron, D. (2010) Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol Cell. 38, 291-304
Witkowski, W. A., and Hardy, J. A. (2011) A designed redox-controlled caspase. Protein Sci. 20, 1421-31
Wittenborn, E. C., Guendon, C., Merrouch, M., Benvenuti, M., Fourmond, V., Léger, C., Drennan, C. L., and Dementin, S. (2020) The Solvent-Exposed Fe-S D-Cluster Contributes to Oxygen-Resistance in Ni-Fe Carbon Monoxide Dehydrogenase. ACS Catal. 10, 7328-7335
Wittenborn, E. C., Jost, M., Wei, Y., Stubbe, J. A., and Drennan, C. L. (2016) Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator. J Biol Chem. 291, 25264-25277
Wittenborn, E. C., Merrouch, M., Ueda, C., Fradale, L., Léger, C., Fourmond, V., Pandelia, M. - E., Dementin, S., and Drennan, C. L. (2018) Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Elife. 10.7554/eLife.39451
Wittenborn, E. C. (2017) Structural Enzymology of Bacterial Carbon Fixation and Storage. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, Massachusetts
Wittenborn, E. C., Cohen, S. E., Merrouch, M., Léger, C., Fourmond, V., Dementin, S., and Drennan, C. L. (2019) Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase. J Biol Chem. 294, 13017-13026
Wittlinger, F., Heppner, D. E., To, C., Günther, M., Shin, B. Hee, Rana, J. K., Schmoker, A. M., Beyett, T. S., Berger, L. M., Berger, B. - T., Bauer, N., Vasta, J. D., Corona, C. R., Robers, M. B., Knapp, S., Jänne, P. A., Eck, M. J., and Laufer, S. A. (2021) Design of a "Two-in-One" Mutant-Selective Epidermal Growth Factor Receptor Inhibitor That Spans the Orthosteric and Allosteric Sites. J Med Chem. 10.1021/acs.jmedchem.1c00848
Wohlever, M. L., Mateja, A., McGilvray, P. T., Day, K. J., and Keenan, R. J. (2017) Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins. Mol Cell. 67, 194-202.e6

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