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Wang, H., and Gouaux, E. (2012) Substrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologue. EMBO Rep. 13, 861-6
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J. - L., Patel, D. J., and C Allis, D. (2009) Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature. 459, 847-51
Wang, H., Cheng, C., Dal Santo, J. L., Shen, C. - H., Bylund, T., Henry, A. R., Howe, C. A., Hwang, J., Morano, N. C., Morris, D. J., Pletnev, S., Roark, R. S., Zhou, T., Hansen, B. T., Hoyt, F. H., Johnston, T. S., Wang, S., Zhang, B., Ambrozak, D. R., Becker, J. E., Bender, M. F., Changela, A., Chaudhary, R., Corcoran, M., Corrigan, A. R., Foulds, K. E., Guo, Y., Lee, M., Li, Y., Lin, B. C., Liu, T., Louder, M. K., Mandolesi, M., Mason, R. D., McKee, K., Nair, V., O'Dell, S., Olia, A. S., Ou, L., Pegu, A., Raju, N., Rawi, R., Roberts-Torres, J., Sarfo, E. K., Sastry, M., Schaub, A. J., Schmidt, S. D., Schramm, C. A., Schwartz, C. L., Smith, S. C., Stephens, T., Stuckey, J., Teng, I. - T., Todd, J. - P., Tsybovsky, Y., Van Wazer, D. J., Wang, S., Doria-Rose, N. A., Fischer, E. R., Georgiev, I. S., Hedestam, G. B. Karlsson, Sheng, Z., Woodward, R. A., Douek, D. C., Koup, R. A., Pierson, T. C., Shapiro, L., Shaw, G. M., Mascola, J. R., and Kwong, P. D. (2024) Potent and broad HIV-1 neutralization in fusion peptide-primed SHIV-infected macaques. Cell. 187, 7214-7231.e23
Wang, J., Sachpatzidis, A., Christian, T. D., Lomakin, I. B., Garen, A., and Konigsberg, W. H. (2022) Insight into the Tumor Suppression Mechanism from the Structure of Human Polypyrimidine Splicing Factor (PSF/SFPQ) Complexed with a 30mer RNA from Murine Virus-like 30S Transcript-1. Biochemistry. 61, 1723-1734
Wang, L., Nam, Y., Lee, A. K., Yu, C., Roth, K., Chen, C., Ransey, E. M., and Sliz, P. (2017) LIN28 Zinc Knuckle Domain Is Required and Sufficient to Induce let-7 Oligouridylation. Cell Rep. 18, 2664-2675
Wang, R., Persky, N. S., Yoo, B., Ouerfelli, O., Smogorzewska, A., Elledge, S. J., and Pavletich, N. P. (2014) DNA repair. Mechanism of DNA interstrand cross-link processing by repair nuclease FAN1. Science. 346, 1127-30
Wang, P., Bashiri, G., Gao, X., Sawaya, M. R., and Tang, Y. (2013) Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis. J Am Chem Soc. 135, 7138-41
Warner, K. Deigan, Homan, P., Weeks, K. M., Smith, A. G., Abell, C., and Ferré-D'Amaré, A. R. (2014) Validating fragment-based drug discovery for biological RNAs: lead fragments bind and remodel the TPP riboswitch specifically. Chem Biol. 21, 591-5
Warner, K. Deigan, and Ferré-D'Amaré, A. R. (2014) Crystallographic analysis of TPP riboswitch binding by small-molecule ligands discovered through fragment-based drug discovery approaches. Methods Enzymol. 549, 221-33
Warner, K. Deigan, Chen, M. C., Song, W., Strack, R. L., Thorn, A., Jaffrey, S. R., and Ferré-D'Amaré, A. R. (2014) Structural basis for activity of highly efficient RNA mimics of green fluorescent protein. Nat Struct Mol Biol. 21, 658-63
Warner, K. Deigan, Sjekloća, L., Song, W., Filonov, G. S., Jaffrey, S. R., and Ferré-D'Amaré, A. R. (2017) A homodimer interface without base pairs in an RNA mimic of red fluorescent protein. Nat Chem Biol. 13, 1195-1201
Warren, G. M., and Shuman, S. (2024) Structure and psoralen DNA crosslink repair activity of mycobacterial Nei2. mBio. 15, e0124824
Waschbüsch, D., Purlyte, E., and Khan, A. R. (2021) Dual arginine recognition of LRRK2 phosphorylated Rab GTPases. Biophys J. 10.1016/j.bpj.2021.03.030
Waschbüsch, D., Purlyte, E., Pal, P., McGrath, E., Alessi, D. R., and Khan, A. R. (2020) Structural Basis for Rab8a Recruitment of RILPL2 via LRRK2 Phosphorylation of Switch 2. Structure. 10.1016/j.str.2020.01.005
Waschbüsch, D., Berndsen, K., Lis, P., Knebel, A., Lam, Y. Py, Alessi, D. R., and Khan, A. R. (2021) Structural basis for the specificity of PPM1H phosphatase for Rab GTPases. EMBO Rep. 10.15252/embr.202152675
Washington, A. Z., Benicewicz, D. B., Canzoneri, J. C., Fagan, C. E., Mwakwari, S. C., Maehigashi, T., Dunham, C. M., and Oyelere, A. K. (2014) Macrolide-peptide conjugates as probes of the path of travel of the nascent peptides through the ribosome. ACS Chem Biol. 9, 2621-31
Wasmuth, E. V., Zinder, J. C., Zattas, D., Das, M., and Lima, C. D. (2017) Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase. Elife. 10.7554/eLife.29062
Wasmuth, E. V., Januszyk, K., and Lima, C. D. (2014) Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA. Nature. 511, 435-9
Watanabe, A., McCarthy, K. R., Kuraoka, M., Schmidt, A. G., Adachi, Y., Onodera, T., Tonouchi, K., Caradonna, T. M., Bajic, G., Song, S., McGee, C. E., Sempowski, G. D., Feng, F., Urick, P., Kepler, T. B., Takahashi, Y., Harrison, S. C., and Kelsoe, G. (2019) Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism. Cell. 177, 1124-1135.e16
Watson, E. R., Grace, C. R. R., Zhang, W., Miller, D. J., Davidson, I. F., J Prabu, R., Yu, S., Bolhuis, D. L., Kulko, E. T., Vollrath, R., Haselbach, D., Stark, H., Peters, J. - M., Brown, N. G., Sidhu, S. S., and Schulman, B. A. (2019) Protein engineering of a ubiquitin-variant inhibitor of APC/C identifies a cryptic K48 ubiquitin chain binding site. Proc Natl Acad Sci U S A. 116, 17280-17289
Watson, P. R., and Christianson, D. W. (2023) Structure and Function of Kdac1, a Class II Deacetylase from the Multidrug-Resistant Pathogen . Biochemistry. 62, 2689-2699
Watson, P. R., Bai, P., Wang, C., Cragin, A. D., Hooker, J. M., and Christianson, D. W. (2022) Aromatic Ring Fluorination Patterns Modulate Inhibitory Potency of Fluorophenylhydroxamates Complexed with Histone Deacetylase 6. Biochemistry. 10.1021/acs.biochem.2c00332
Wei, H., Ruthenburg, A. J., Bechis, S. K., and Verdine, G. L. (2005) Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase. J Biol Chem. 280, 37041-7
Wei, J., and Tong, L. (2015) Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer. Nature. 526, 723-7
Wei, J., Zhang, Y., Yu, T. - Y., Sadre-Bazzaz, K., Rudolph, M. J., Amodeo, G. A., Symington, L. S., Walz, T., and Tong, L. (2016) A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation. Cell Discov. 2, 16044

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