Publications

Found 2920 results
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Vasan, N., Hutagalung, A., Novick, P., and Reinisch, K. M. (2010) Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes. Proc Natl Acad Sci U S A. 107, 14176-81
Varlakhanova, N. V., Alvarez, F. J. D., Brady, T. M., Tornabene, B. A., Hosford, C. J., Chappie, J. S., Zhang, P., and Ford, M. G. J. (2018) Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture. J Cell Biol. 10.1083/jcb.201712021
Vangaveti, S., Cantara, W. A., Spears, J. L., Demirci, H., Murphy, F. V., Ranganathan, S. V., Sarachan, K. L., and Agris, P. F. (2020) A structural basis for restricted codon recognition mediated by 2-thiocytidine in tRNA containing a wobble position inosine. J Mol Biol. 10.1016/j.jmb.2019.12.016
Vance, T. D. R., Yip, P., Jiménez, E., Li, S., Gawol, D., Byrnes, J., Usón, I., Ziyyat, A., and Lee, J. E. (2022) SPACA6 ectodomain structure reveals a conserved superfamily of gamete fusion-associated proteins. Commun Biol. 5, 984
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
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 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 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
Valverde, R., Ingram, J., and Harrison, S. C. (2016) Conserved Tetramer Junction in the Kinetochore Ndc80 Complex. Cell Rep. 17, 1915-1922
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
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
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
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
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
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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
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
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
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
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. (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. (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
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. (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

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