Publications

Found 2819 results
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Uervirojnangkoorn, M., Lyubimov, A. Y., Zhou, Q., Weis, W. I., and Brunger, A. T. (2019) Resolving indexing ambiguities in X-ray free-electron laser diffraction patterns. Acta Crystallogr D Struct Biol. 75, 234-241
Ujwal, R., Cascio, D., Colletier, J. - P., Faham, S., Zhang, J., Toro, L., Ping, P., and Abramson, J. (2008) The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci U S A. 105, 17742-7
Uljon, S., Xu, X., Durzynska, I., Stein, S., Adelmant, G., Marto, J. A., Pear, W. S., and Blacklow, S. C. (2016) Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Structure. 24, 687-696
Ultsch, M., Li, W., Eigenbrot, C., Di Lello, P., Lipari, M. T., Gerhardy, S., AhYoung, A. P., Quinn, J., Franke, Y., Chen, Y., M Beltran, K., Peterson, A., and Kirchhofer, D. (2019) Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. J Mol Biol. 431, 885-903
Unciuleac, M. - C., Smith, P. C., and Shuman, S. (2016) Crystal Structure and Biochemical Characterization of a Mycobacterium smegmatis AAA-Type Nucleoside Triphosphatase Phosphohydrolase (Msm0858). J Bacteriol. 198, 1521-33
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2020) Caveat mutator: alanine substitutions for conserved amino acids in RNA ligase elicit unexpected rearrangements of the active site for lysine adenylylation. Nucleic Acids Res. 10.1093/nar/gkaa238
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2015) Structure and two-metal mechanism of a eukaryal nick-sealing RNA ligase. Proc Natl Acad Sci U S A. 112, 13868-73
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2017) Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NAD(+)-dependent polynucleotide ligases. Proc Natl Acad Sci U S A. 114, 2592-2597
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2019) Structures of ATP-bound DNA ligase D in a closed domain conformation reveal a network of amino acid and metal contacts to the ATP phosphates. J Biol Chem. 10.1074/jbc.RA119.007445
Unger, E. K., Keller, J. P., Altermatt, M., Liang, R., Matsui, A., Dong, C., Hon, O. J., Yao, Z., Sun, J., Banala, S., Flanigan, M. E., Jaffe, D. A., Hartanto, S., Carlen, J., Mizuno, G. O., Borden, P. M., Shivange, A. V., Cameron, L. P., Sinning, S., Underhill, S. M., Olson, D. E., Amara, S. G., Lang, D. Temple, Rudnick, G., Marvin, J. S., Lavis, L. D., Lester, H. A., Alvarez, V. A., Fisher, A. J., Prescher, J. A., Kash, T. L., Yarov-Yarovoy, V., Gradinaru, V., Looger, L. L., and Tian, L. (2020) Directed Evolution of a Selective and Sensitive Serotonin Sensor via Machine Learning. Cell. 183, 1986-2002.e26
Uppalapati, M., Lee, D. Jun, Mandal, K., Li, H., Miranda, L. P., Lowitz, J., Kenney, J., Adams, J. J., Ault-Riché, D., Kent, S. B. H., and Sidhu, S. S. (2016) A Potent d-Protein Antagonist of VEGF-A is Nonimmunogenic, Metabolically Stable, and Longer-Circulating in Vivo. ACS Chem Biol. 11, 1058-65
Uson, M. Loressa, Carl, A., Goldgur, Y., and Shuman, S. (2018) Crystal structure and mutational analysis of Mycobacterium smegmatis FenA highlight active site amino acids and three metal ions essential for flap endonuclease and 5' exonuclease activities. Nucleic Acids Res. 10.1093/nar/gky238
Uysal, S., Cuello, L. G., D Cortes, M., Koide, S., Kossiakoff, A. A., and Perozo, E. (2011) Mechanism of activation gating in the full-length KcsA K+ channel. Proc Natl Acad Sci U S A. 108, 11896-9
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Vaccaro, F. A., Born, D. A., and Drennan, C. L. (2023) Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery. Proc Natl Acad Sci U S A. 120, e2214085120
Vaidya, A. T., Lomakin, I. B., Joseph, N. N., Dmitriev, S. E., and Steitz, T. A. (2017) Crystal Structure of the C-terminal Domain of Human eIF2D and its Implications on Eukaryotic Translation Initiation. J Mol Biol. 10.1016/j.jmb.2017.07.015
Vaidya, A. T., Chen, C. - H., Dunlap, J. C., Loros, J. J., and Crane, B. R. (2011) Structure of a light-activated LOV protein dimer that regulates transcription. Sci Signal. 4, ra50
Vaisey, G., Miller, A. N., and Long, S. B. (2016) Distinct regions that control ion selectivity and calcium-dependent activation in the bestrophin ion channel. Proc Natl Acad Sci U S A. 113, E7399-E7408
Valentino, H., Korasick, D. A., Bohac, T. J., Shapiro, J. A., Wencewicz, T. A., Tanner, J. J., and Sobrado, P. (2021) Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from . ACS Omega. 6, 18537-18547
Valentino, H., Campbell, A. C., Schuermann, J. P., Sultana, N., Nam, H. G., LeBlanc, S., Tanner, J. J., and Sobrado, P. (2020) Structure and function of a flavin-dependent S-monooxygenase from garlic (). J Biol Chem. 295, 11042-11055
Valverde, R., Ingram, J., and Harrison, S. C. (2016) Conserved Tetramer Junction in the Kinetochore Ndc80 Complex. Cell Rep. 17, 1915-1922
Van den Berg, B., Black, P. N., Clemons, W. M., and Rapoport, T. A. (2004) Crystal structure of the long-chain fatty acid transporter FadL. Science. 304, 1506-9
Van den Berg, B., Clemons, W. M., Collinson, I., Modis, Y., Hartmann, E., Harrison, S. C., and Rapoport, T. A. (2004) X-ray structure of a protein-conducting channel. Nature. 427, 36-44
van Rosenburgh, I. K. van Alde, Lu, D. M., Grant, M. J., Stayrook, S. E., Phadke, M., Walther, Z., Goldberg, S. B., Politi, K., Lemmon, M. A., Ashtekar, K. D., and Tsutsui, Y. (2022) Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations. Nat Commun. 13, 6791
Van Straaten, K. E., Hoffort, A., Palmer, D. R. J., and Sanders, D. A. R. (2008) Purification, crystallization and preliminary X-ray analysis of inositol dehydrogenase (IDH) from Bacillus subtilis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64, 98-101
Van Wagoner, R. M., and Clardy, J. (2006) FeeM, an N-acyl amino acid synthase from an uncultured soil microbe: structure, mechanism, and acyl carrier protein binding. Structure. 14, 1425-35

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