Found 2669 results
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Velilla, J. A., Volpe, M. R., Kenney, G. E., Walsh, R. M., Balskus, E. P., and Gaudet, R. (2022) Structural basis of colibactin activation by the ClbP peptidase. Nat Chem Biol. 10.1038/s41589-022-01142-z
Vemulapalli, V., Donovan, K. A., Seegar, T. C. M., Rogers, J. M., Bae, M., Lumpkin, R. J., Cao, R., Henke, M. T., Ray, S. S., Fischer, E. S., Cuny, G. D., and Blacklow, S. C. (2021) Targeted Degradation of the Oncogenic Phosphatase SHP2. Biochemistry. 60, 2593-2609
Vendeix, F. A. P., Murphy, F. V., Cantara, W. A., Leszczyńska, G., Gustilo, E. M., Sproat, B., Malkiewicz, A., and Agris, P. F. (2012) Human tRNA(Lys3)(UUU) is pre-structured by natural modifications for cognate and wobble codon binding through keto-enol tautomerism. J Mol Biol. 416, 467-85
Vigdorovich, V., Ramagopal, U. A., Lázár-Molnár, E., Sylvestre, E., Lee, J. Sik, Hofmeyer, K. A., Zang, X., Nathenson, S. G., and Almo, S. C. (2013) Structure and T cell inhibition properties of B7 family member, B7-H3. Structure. 21, 707-17
Vincent, J., Adura, C., Gao, P., Luz, A., Lama, L., Asano, Y., Okamoto, R., Imaeda, T., Aida, J., Rothamel, K., Gogakos, T., Steinberg, J., Reasoner, S., Aso, K., Tuschl, T., Patel, D. J., J Glickman, F., and Ascano, M. (2017) Small molecule inhibition of cGAS reduces interferon expression in primary macrophages from autoimmune mice. Nat Commun. 8, 750
Vinokur, J. M., Korman, T. P., Sawaya, M. R., Collazo, M., Cascio, D., and Bowie, J. U. (2015) Structural analysis of mevalonate-3-kinase provides insight into the mechanisms of isoprenoid pathway decarboxylases. Protein Sci. 24, 212-20
Viswanathan, T., Arya, S., Chan, S. - H., Qi, S., Dai, N., Misra, A., Park, J. - G., Oladunni, F., Kovalskyy, D., Hromas, R. A., Martinez-Sobrido, L., and Gupta, Y. K. (2020) Structural basis of RNA cap modification by SARS-CoV-2. Nat Commun. 11, 3718
Viswanathan, T., Misra, A., Chan, S. - H., Qi, S., Dai, N., Arya, S., Martinez-Sobrido, L., and Gupta, Y. K. (2021) A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2'-O methylation of its first nucleotide. Nat Commun. 12, 3287
Vizcarra, C. L., Kreutz, B., Rodal, A. A., Toms, A. V., Lu, J., Zheng, W., Quinlan, M. E., and Eck, M. J. (2011) Structure and function of the interacting domains of Spire and Fmn-family formins. Proc Natl Acad Sci U S A. 108, 11884-9
Vorobieva, A. A., White, P., Liang, B., Horne, J. E., Bera, A. K., Chow, C. M., Gerben, S., Marx, S., Kang, A., Stiving, A. Q., Harvey, S. R., Marx, D. C., G Khan, N., Fleming, K. G., Wysocki, V. H., Brockwell, D. J., Tamm, L. K., Radford, S. E., and Baker, D. (2021) De novo design of transmembrane β barrels.. Science. 10.1126/science.abc8182
Voronkova, M. A., Hansen, H. L., Cooper, M. P., Miller, J., Sukumar, N., Geldenhuys, W. J., Robart, A. R., and Webb, B. A. (2023) Cancer-associated somatic mutations in human phosphofructokinase-1 reveal a critical electrostatic interaction for allosteric regulation of enzyme activity. Biochem J. 480, 1411-1427
Vorontsov, I. I., Minasov, G., Brunzelle, J. S., Shuvalova, L., Kiryukhina, O., Collart, F. R., and Anderson, W. F. (2007) Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity. Protein Sci. 16, 2483-90
Vuksanovic, N., Clasman, J. R., Imperiali, B., and Allen, K. N. (2023) Specificity determinants revealed by the structure of glycosyltransferase Campylobacter concisus PglA. Protein Sci. 10.1002/pro.4848
Wada, M., Heux, L., Nishiyama, Y., and Langan, P. (2009) X-ray crystallographic, scanning microprobe X-ray diffraction, and cross-polarized/magic angle spinning 13C NMR studies of the structure of cellulose III(II). Biomacromolecules. 10, 302-9
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Wagner, F. F., Bishop, J. A., Gale, J. P., Shi, X., Walk, M., Ketterman, J., Patnaik, D., Barker, D., Walpita, D., Campbell, A. J., Nguyen, S., Lewis, M., Ross, L., Weïwer, M., W An, F., Germain, A. R., Nag, P. P., Metkar, S., Kaya, T., Dandapani, S., Olson, D. E., Barbe, A. - L., Lazzaro, F., Sacher, J. R., Cheah, J. H., Fei, D., Perez, J., Munoz, B., Palmer, M., Stegmaier, K., Schreiber, S. L., Scolnick, E., Zhang, Y. - L., Haggarty, S. J., Holson, E. B., and Pan, J. Q. (2016) Inhibitors of Glycogen Synthase Kinase 3 with Exquisite Kinome-Wide Selectivity and Their Functional Effects. ACS Chem Biol. 11, 1952-63
Wan, Q., Ahmad, M. Faiz, Fairman, J., Gorzelle, B., de la Fuente, M., Dealwis, C., and Maguire, M. E. (2011) X-ray crystallography and isothermal titration calorimetry studies of the Salmonella zinc transporter ZntB. Structure. 19, 700-10
Wan, B., Wu, J., Meng, X., Lei, M., and Zhao, X. (2019) Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107. Mol Cell. 75, 238-251.e5
Wan, L. C. K., Mao, D. Y. L., Neculai, D., Strecker, J., Chiovitti, D., Kurinov, I., Poda, G., Thevakumaran, N., Yuan, F., Szilard, R. K., Lissina, E., Nislow, C., Caudy, A. A., Durocher, D., and Sicheri, F. (2013) Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Res. 41, 6332-46
Wang, Z., Dang, H. V., Amaya, M., Xu, Y., Yin, R., Yan, L., Hickey, A. C., Annand, E. J., Horsburgh, B. A., Reid, P. A., Smith, I., Eden, J. - S., Xu, K., Broder, C. C., and Veesler, D. (2022) Potent monoclonal antibody-mediated neutralization of a divergent Hendra virus variant. Proc Natl Acad Sci U S A. 119, e2122769119
Wang, Y., Juranek, S., Li, H., Sheng, G., Wardle, G. S., Tuschl, T., and Patel, D. J. (2009) Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes. Nature. 461, 754-61
Wang, B., Grant, R. A., and Laub, M. T. (2020) ppGpp Coordinates Nucleotide and Amino-Acid Synthesis in E. coli During Starvation.. Mol Cell. 10.1016/j.molcel.2020.08.005
Wang, C., Chung, B. C., Yan, H., Lee, S. - Y., and Pitt, G. S. (2012) Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. Structure. 20, 1167-76
Wang, J., Erazo, T., Ferguson, F. M., Buckley, D. L., Gomez, N., Muñoz-Guardiola, P., Diéguez-Martínez, N., Deng, X., Hao, M., Massefski, W., Fedorov, O., Offei-Addo, N. Kwaku, Park, P. M., Dai, L., DiBona, A., Becht, K., Kim, N. Doo, McKeown, M. R., Roberts, J. M., Zhang, J., Sim, T., Alessi, D. R., Bradner, J. E., Lizcano, J. M., Blacklow, S. C., Qi, J., Xu, X., and Gray, N. S. (2018) Structural and Atropisomeric Factors Governing the Selectivity of Pyrimido-benzodiazipinones as Inhibitors of Kinases and Bromodomains. ACS Chem Biol. 10.1021/acschembio.7b00638
Wang, X. - H., Su, M., Gao, F., Xie, W., Zeng, Y., Li, D. - L., Liu, X. - L., Zhao, H., Qin, L., Li, F., Liu, Q., Clarke, O. B., Lam, S. Man, Shui, G. - H., Hendrickson, W. A., and Chen, Y. - H. (2019) Structural basis for activity of TRIC counter-ion channels in calcium release. Proc Natl Acad Sci U S A. 10.1073/pnas.1817271116