Publications

Found 1129 results
Filters: First Letter Of Last Name is D  [Clear All Filters]
2014
Huang, H., Zeqiraj, E., Dong, B., Jha, B. Kant, Duffy, N. M., Orlicky, S., Thevakumaran, N., Talukdar, M., Pillon, M. C., Ceccarelli, D. F., Wan, L. C. K., Juang, Y. - C., Mao, D. Y. L., Gaughan, C., Brinton, M. A., Perelygin, A. A., Kourinov, I., Guarné, A., Silverman, R. H., and Sicheri, F. (2014) Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity. Mol Cell. 53, 221-34
Do, T. D., LaPointe, N. E., Sangwan, S., Teplow, D. B., Feinstein, S. C., Sawaya, M. R., Eisenberg, D. S., and Bowers, M. T. (2014) Factors that drive peptide assembly from native to amyloid structures: experimental and theoretical analysis of [leu-5]-enkephalin mutants. J Phys Chem B. 118, 7247-56
Doamekpor, S. K., Sanchez, A. M., Schwer, B., Shuman, S., and Lima, C. D. (2014) How an mRNA capping enzyme reads distinct RNA polymerase II and Spt5 CTD phosphorylation codes. Genes Dev. 28, 1323-36
Sosa, B. A., F Demircioglu, E., Chen, J. Z., Ingram, J., Ploegh, H. L., and Schwartz, T. U. (2014) How lamina-associated polypeptide 1 (LAP1) activates Torsin. Elife. 3, e03239
Deinema, M. S., Perry, K., Kearns, S. P., D’Antonio, E. L., and D’Antonio, J. (2014) Inhibition of Trypanosoma cruzi Glucokinase with 2,6-Dideoxy-2,6-Diamino-D-Glucose. 66th Southeastern Regional Meeting of the American Chemical Society, October 16-19, 2014
Deinema, M. S., Perry, K., Kearns, S. P., D’Antonio, E. L., and D’Antonio, J. (2014) Inhibition of Trypanosoma cruzi Glucokinase with 2,6-Dideoxy-2,6-Diamino-D-Glucose. 66th Southeastern Regional Meeting of the American Chemical Society, October 16-19, 2014
Deinema, M. S., Perry, K., Kearns, S. P., D’Antonio, E. L., and D’Antonio, J. (2014) Inhibition of Trypanosoma cruzi Glucokinase with 2,6-Dideoxy-2,6-Diamino-D-Glucose. 66th Southeastern Regional Meeting of the American Chemical Society, October 16-19, 2014
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
Du, J., Johnson, L. M., Groth, M., Feng, S., Hale, C. J., Li, S., Vashisht, A. A., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2014) Mechanism of DNA methylation-directed histone methylation by KRYPTONITE. Mol Cell. 55, 495-504
Brown, N. G., Watson, E. R., Weissmann, F., Jarvis, M. A., VanderLinden, R., Grace, C. R. R., Frye, J. J., Qiao, R., Dube, P., Petzold, G., Cho, S. Ei, Alsharif, O., Bao, J., Davidson, I. F., Zheng, J. J., Nourse, A., Kurinov, I., Peters, J. - M., Stark, H., and Schulman, B. A. (2014) Mechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly. Mol Cell. 56, 246-260
Brown, N. G., Watson, E. R., Weissmann, F., Jarvis, M. A., VanderLinden, R., Grace, C. R. R., Frye, J. J., Qiao, R., Dube, P., Petzold, G., Cho, S. Ei, Alsharif, O., Bao, J., Davidson, I. F., Zheng, J. J., Nourse, A., Kurinov, I., Peters, J. - M., Stark, H., and Schulman, B. A. (2014) Mechanism of polyubiquitination by human anaphase-promoting complex: RING repurposing for ubiquitin chain assembly. Mol Cell. 56, 246-260
Ruangprasert, A., Maehigashi, T., Miles, S. J., Giridharan, N., Liu, J. X., and Dunham, C. M. (2014) Mechanisms of toxin inhibition and transcriptional repression by Escherichia coli DinJ-YafQ. J Biol Chem. 289, 20559-69
Lee, K., Zhong, X., Gu, S., Kruel, A. Magdalena, Dorner, M. B., Perry, K., Rummel, A., Dong, M., and Jin, R. (2014) Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex. Science. 344, 1405-10
Lee, K., Zhong, X., Gu, S., Kruel, A. Magdalena, Dorner, M. B., Perry, K., Rummel, A., Dong, M., and Jin, R. (2014) Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex. Science. 344, 1405-10
Albright, R. A., Ornstein, D. L., Cao, W., Chang, W. C., Robert, D., Tehan, M., Hoyer, D., Liu, L., Stabach, P., Yang, G., De La Cruz, E. M., and Braddock, D. T. (2014) Molecular basis of purinergic signal metabolism by ectonucleotide pyrophosphatase/phosphodiesterases 4 and 1 and implications in stroke. J Biol Chem. 289, 3294-306
Poor, C. B., Wegner, S. V., Li, H., Dlouhy, A. C., Schuermann, J. P., Sanishvili, R., Hinshaw, J. R., Riggs-Gelasco, P. J., Outten, C. E., and He, C. (2014) Molecular mechanism and structure of the Saccharomyces cerevisiae iron regulator Aft2. Proc Natl Acad Sci U S A. 111, 4043-8
Zhong, X., Du, J., Hale, C. J., Gallego-Bartolome, J., Feng, S., Vashisht, A. A., Chory, J., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2014) Molecular mechanism of action of plant DRM de novo DNA methyltransferases. Cell. 157, 1050-60
Dunkle, J. A., Vinal, K., Desai, P. M., Zelinskaya, N., Savic, M., West, D. M., Conn, G. L., and Dunham, C. M. (2014) Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA. Proc Natl Acad Sci U S A. 111, 6275-80
Dunkle, J. A., Vinal, K., Desai, P. M., Zelinskaya, N., Savic, M., West, D. M., Conn, G. L., and Dunham, C. M. (2014) Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA. Proc Natl Acad Sci U S A. 111, 6275-80
Dunkle, J. A., Vinal, K., Desai, P. M., Zelinskaya, N., Savic, M., West, D. M., Conn, G. L., and Dunham, C. M. (2014) Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA. Proc Natl Acad Sci U S A. 111, 6275-80
Lee, K. Sing Steph, Liu, J. - Y., Wagner, K. M., Pakhomova, S., Dong, H., Morisseau, C., Fu, S. H., Yang, J., Wang, P., Ulu, A., Mate, C. A., Nguyen, L. V., Hwang, S. Hee, Edin, M. L., Mara, A. A., Wulff, H., Newcomer, M. E., Zeldin, D. C., and Hammock, B. D. (2014) Optimized inhibitors of soluble epoxide hydrolase improve in vitro target residence time and in vivo efficacy. J Med Chem. 57, 7016-30
Luo, Z., Dauter, M., and Dauter, Z. (2014) Phosphates in the Z-DNA dodecamer are flexible, but their P-SAD signal is sufficient for structure solution. Acta Crystallogr D Biol Crystallogr. 70, 1790-800
Luo, Z., Dauter, M., and Dauter, Z. (2014) Phosphates in the Z-DNA dodecamer are flexible, but their P-SAD signal is sufficient for structure solution. Acta Crystallogr D Biol Crystallogr. 70, 1790-800
Sawaya, M. R., Cascio, D., Gingery, M., Rodriguez, J., Goldschmidt, L., Colletier, J. - P., Messerschmidt, M. M., Boutet, S., Koglin, J. E., Williams, G. J., Brewster, A. S., Nass, K., Hattne, J., Botha, S., R Doak, B., Shoeman, R. L., DePonte, D. P., Park, H. - W., Federici, B. A., Sauter, N. K., Schlichting, I., and Eisenberg, D. S. (2014) Protein crystal structure obtained at 2.9 Å resolution from injecting bacterial cells into an X-ray free-electron laser beam.. Proc Natl Acad Sci U S A. 111, 12769-74
Sawaya, M. R., Cascio, D., Gingery, M., Rodriguez, J., Goldschmidt, L., Colletier, J. - P., Messerschmidt, M. M., Boutet, S., Koglin, J. E., Williams, G. J., Brewster, A. S., Nass, K., Hattne, J., Botha, S., R Doak, B., Shoeman, R. L., DePonte, D. P., Park, H. - W., Federici, B. A., Sauter, N. K., Schlichting, I., and Eisenberg, D. S. (2014) Protein crystal structure obtained at 2.9 Å resolution from injecting bacterial cells into an X-ray free-electron laser beam.. Proc Natl Acad Sci U S A. 111, 12769-74

Pages