Publications

Found 2717 results
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
V
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
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
W
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, 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
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
Wang, L., Qiao, Q., Ferrao, R., Shen, C., Hatcher, J. M., Buhrlage, S. J., Gray, N. S., and Wu, H. (2017) Crystal structure of human IRAK1. Proc Natl Acad Sci U S A. 10.1073/pnas.1714386114
Wang, M., Xia, S., Blaha, G., Steitz, T. A., Konigsberg, W. H., and Wang, J. (2011) Insights into base selectivity from the 1.8 Å resolution structure of an RB69 DNA polymerase ternary complex.. Biochemistry. 50, 581-90
Wang, H., Goehring, A., Wang, K. H., Penmatsa, A., Ressler, R., and Gouaux, E. (2013) Structural basis for action by diverse antidepressants on biogenic amine transporters. Nature. 503, 141-5
Wang, L., Ferrao, R., Li, Q., Hatcher, J. M., Choi, H. Geun, Buhrlage, S. J., Gray, N. S., and Wu, H. (2019) Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4). J Biol Chem. 10.1074/jbc.RA118.005428
Wang, H., Elferich, J., and Gouaux, E. (2012) Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context. Nat Struct Mol Biol. 19, 212-9
Wang, Y., Sheng, G., Juranek, S., Tuschl, T., and Patel, D. J. (2008) Structure of the guide-strand-containing argonaute silencing complex. Nature. 456, 209-13
Wang, E. S., Verano, A. L., Nowak, R. P., J Yuan, C., Donovan, K. A., Eleuteri, N. A., Yue, H., Ngo, K. H., Lizotte, P. H., Gokhale, P. C., Gray, N. S., and Fischer, E. S. (2021) Acute pharmacological degradation of Helios destabilizes regulatory T cells. Nat Chem Biol. 17, 711-717
Wang, L., Yang, J. Kuk, Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Young, Yin, Q., Damko, E., Jang, S. Bok, Raunser, S., Robinson, C. V., Siegel, R. M., Walz, T., and Wu, H. (2010) The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat Struct Mol Biol. 17, 1324-9
Wang, F., Li, L., Dou, Y., Shi, R., Duan, X., Liu, H., Zhang, J., Liu, D. D., Wu, J., He, Y., Lan, J., Lu, B., Feng, H., and Yan, J. (2022) Etesevimab in combination with JS026 neutralizing SARS-CoV-2 and its variants. Emerg Microbes Infect. 11, 548-551
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, J., and Ealick, S. E. (2004) Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data. Acta Crystallogr D Biol Crystallogr. 60, 1579-85
Wang, Q., Navarro, M. V. A. S., Peng, G., Molinelli, E., Goh, S. Lin, Judson, B. L., Rajashankar, K. R., and Sondermann, H. (2009) Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. Proc Natl Acad Sci U S A. 106, 12700-5
Wang, W., and Hendrickson, W. A. (2021) Intermediates in allosteric equilibria of DnaK-ATP interactions with substrate peptides. Acta Crystallogr D Struct Biol. 77, 606-617

Pages