Publications

Found 505 results
Filters: First Letter Of Last Name is E  [Clear All Filters]
2012
Ketkar, A., Zafar, M. K., Banerjee, S., Marquez, V. E., Egli, M., and Eoff, R. L. (2012) Differential furanose selection in the active sites of archaeal DNA polymerases probed by fixed-conformation nucleotide analogues. Biochemistry. 51, 9234-44
Krauthammer, M., Kong, Y., Ha, B. Hak, Evans, P., Bacchiocchi, A., McCusker, J. P., Cheng, E., Davis, M. J., Goh, G., Choi, M., Ariyan, S., Narayan, D., Dutton-Regester, K., Capatana, A., Holman, E. C., Bosenberg, M., Sznol, M., Kluger, H. M., Brash, D. E., Stern, D. F., Materin, M. A., Lo, R. S., Mane, S., Ma, S., Kidd, K. K., Hayward, N. K., Lifton, R. P., Schlessinger, J., Boggon, T. J., and Halaban, R. (2012) Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma. Nat Genet. 44, 1006-14
Itsathitphaisarn, O., Wing, R. A., Eliason, W. K., Wang, J., and Steitz, T. A. (2012) The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell. 151, 267-77
Dhatwalia, R., Singh, H., Solano, L. M., Oppenheimer, M., Robinson, R. M., Ellerbrock, J. F., Sobrado, P., and Tanner, J. J. (2012) Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase. J Am Chem Soc. 134, 18132-8
Ausin, I., Greenberg, M. V. C., Simanshu, D. K., Hale, C. J., Vashisht, A. A., Simon, S. A., Lee, T. -fen, Feng, S., Española, S. D., Meyers, B. C., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2012) INVOLVED IN DE NOVO 2-containing complex involved in RNA-directed DNA methylation in Arabidopsis. Proc Natl Acad Sci U S A. 109, 8374-81
Ketkar, A., Zafar, M. K., Banerjee, S., Marquez, V. E., Egli, M., and Eoff, R. L. (2012) A nucleotide-analogue-induced gain of function corrects the error-prone nature of human DNA polymerase iota. J Am Chem Soc. 134, 10698-705
Ketkar, A., Zafar, M. K., Banerjee, S., Marquez, V. E., Egli, M., and Eoff, R. L. (2012) A nucleotide-analogue-induced gain of function corrects the error-prone nature of human DNA polymerase iota. J Am Chem Soc. 134, 10698-705
Liu, C., Zhao, M., Jiang, L., Cheng, P. - N., Park, J., Sawaya, M. R., Pensalfini, A., Gou, D., Berk, A. J., Glabe, C. G., Nowick, J., and Eisenberg, D. (2012) Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates.. Proc Natl Acad Sci U S A. 109, 20913-8
Hitosugi, T., Zhou, L., Elf, S., Fan, J., Kang, H. - B., Seo, J. Ho, Shan, C., Dai, Q., Zhang, L., Xie, J., Gu, T. - L., Jin, P., Alečković, M., LeRoy, G., Kang, Y., Sudderth, J. A., DeBerardinis, R. J., Luan, C. - H., Chen, G. Z., Muller, S., Shin, D. M., Owonikoko, T. K., Lonial, S., Arellano, M. L., Khoury, H. J., Khuri, F. R., Lee, B. H., Ye, K., Boggon, T. J., Kang, S., He, C., and Chen, J. (2012) Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth. Cancer Cell. 22, 585-600
Huang, S., Mahanta, N., Begley, T. P., and Ealick, S. E. (2012) Pseudouridine monophosphate glycosidase: a new glycosidase mechanism. Biochemistry. 51, 9245-55
Teng, P. K., Anderson, N. J., Goldschmidt, L., Sawaya, M. R., Sambashivan, S., and Eisenberg, D. (2012) Ribonuclease A suggests how proteins self-chaperone against amyloid fiber formation. Protein Sci. 21, 26-37
Kruidenier, L., Chung, C. -wa, Cheng, Z., Liddle, J., Che, K. H., Joberty, G., Bantscheff, M., Bountra, C., Bridges, A., Diallo, H., Eberhard, D., Hutchinson, S., Jones, E., Katso, R., Leveridge, M., Mander, P. K., Mosley, J., Ramirez-Molina, C., Rowland, P., Schofield, C. J., Sheppard, R. J., Smith, J. E., Swales, C., Tanner, R., Thomas, P., Tumber, A., Drewes, G., Oppermann, U., Patel, D. J., Lee, K., and Wilson, D. M. (2012) A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. Nature. 488, 404-8
Englert, M., Xia, S., Okada, C., Nakamura, A., Tanavde, V., Yao, M., Eom, S. Hyun, Konigsberg, W. H., Söll, D., and Wang, J. (2012) Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3'-terminal phosphate and 5'-OH. Proc Natl Acad Sci U S A. 109, 15235-40
Englert, M., Xia, S., Okada, C., Nakamura, A., Tanavde, V., Yao, M., Eom, S. Hyun, Konigsberg, W. H., Söll, D., and Wang, J. (2012) Structural and mechanistic insights into guanylylation of RNA-splicing ligase RtcB joining RNA between 3'-terminal phosphate and 5'-OH. Proc Natl Acad Sci U S A. 109, 15235-40
Xia, S., Eom, S. Hyun, Konigsberg, W. H., and Wang, J. (2012) Structural basis for differential insertion kinetics of dNMPs opposite a difluorotoluene nucleotide residue. Biochemistry. 51, 1476-85
Dessanti, P., Zhang, Y., Allegrini, S., Tozzi, M. Grazia, Sgarrella, F., and Ealick, S. E. (2012) Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase. Acta Crystallogr D Biol Crystallogr. 68, 239-48
Levin, E. J., Cao, Y., Enkavi, G., Quick, M., Pan, Y., Tajkhorshid, E., and Zhou, M. (2012) Structure and permeation mechanism of a mammalian urea transporter. Proc Natl Acad Sci U S A. 109, 11194-9
Eek, P., Järving, R., Järving, I., Gilbert, N. C., Newcomer, M. E., and Samel, N. (2012) Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+ regulation. J Biol Chem. 287, 22377-86
Tu, D., Graziano, B. R., Park, E., Zheng, W., Li, Y., Goode, B. L., and Eck, M. J. (2012) Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6. Proc Natl Acad Sci U S A. 109, E3424-33
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
Lai, R. - Y., Huang, S., Fenwick, M. K., Hazra, A., Zhang, Y., Rajashankar, K., Philmus, B., Kinsland, C., Sanders, J. Mansell, Ealick, S. E., and Begley, T. P. (2012) Thiamin pyrimidine biosynthesis in Candida albicans : a remarkable reaction between histidine and pyridoxal phosphate. J Am Chem Soc. 134, 9157-9
Goldman, P. J., Ryan, K. S., Hamill, M. J., Howard-Jones, A. R., Walsh, C. T., Elliott, S. J., and Drennan, C. L. (2012) An unusual role for a mobile flavin in StaC-like indolocarbazole biosynthetic enzymes. Chem Biol. 19, 855-65

Pages