Publications

Found 1208 results
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2016
Schureck, M. A. (2016) Structural and Functional Studies of a Toxin-Antitoxin System Involved in Translational Inhibition. Ph.D. thesis, Emory University, Atlanta, Georgia, PhD, 273
Hubin, E. A. (2016) Structural and functional studies of mycobacterial general transcription factors RbpA and CarD. Ph.D. thesis, The Rockefeller University, New York City, New York
Hayes, R. P., Xiao, Y., Ding, F., van Erp, P. B. G., Rajashankar, K., Bailey, S., Wiedenheft, B., and Ke, A. (2016) Structural basis for promiscuous PAM recognition in type I-E Cascade from E. coli. Nature. 530, 499-503
Uljon, S., Xu, X., Durzynska, I., Stein, S., Adelmant, G., Marto, J. A., Pear, W. S., and Blacklow, S. C. (2016) Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Structure. 24, 687-696
Dharmaiah, S., Bindu, L., Tran, T. H., Gillette, W. K., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2016) Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.. Proc Natl Acad Sci U S A. 113, E6766-E6775
Dhindwal, S., Gomez-Gil, L., Neau, D. B., Pham, T. Thanh My, Sylvestre, M., Eltis, L. D., Bolin, J. T., and Kumar, P. (2016) Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase. J Bacteriol. 198, 1499-512
Huang, H., Deng, Z., Vladimirova, O., Wiedmer, A., Lu, F., Lieberman, P. M., and Patel, D. J. (2016) Structural basis underlying viral hijacking of a histone chaperone complex. Nat Commun. 7, 12707
Dowling, D. P., Kung, Y., Croft, A. K., Taghizadeh, K., Kelly, W. L., Walsh, C. T., and Drennan, C. L. (2016) Structural elements of an NRPS cyclization domain and its intermodule docking domain. Proc Natl Acad Sci U S A. 113, 12432-12437
Dowling, D. P., Kung, Y., Croft, A. K., Taghizadeh, K., Kelly, W. L., Walsh, C. T., and Drennan, C. L. (2016) Structural elements of an NRPS cyclization domain and its intermodule docking domain. Proc Natl Acad Sci U S A. 113, 12432-12437
Doamekpor, S. K., Lee, J. - W., Hepowit, N. L., Wu, C., Charenton, C., Leonard, M., Bengtson, M. H., Rajashankar, K. R., Sachs, M. S., Lima, C. D., and Joazeiro, C. A. P. (2016) Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits. Proc Natl Acad Sci U S A. 113, E4151-60
Wittenborn, E. C., Jost, M., Wei, Y., Stubbe, J. A., and Drennan, C. L. (2016) Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator. J Biol Chem. 291, 25264-25277
Dimitrova, Y. N., Jenni, S., Valverde, R., Khin, Y., and Harrison, S. C. (2016) Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly. Cell. 167, 1014-1027.e12
Huff, S. (2016) Structure-guided Synthesis and Evaluation of Non-nucleoside Reversible, Competitive Inhibitors of Human Ribonucleotide Reductase as Anti-proliferative Agents. Ph.D. thesis, Case Western Reserve University, OhioLINK Electronic Theses and Dissertations Center
Petrou, V. I., Herrera, C. M., Schultz, K. M., Clarke, O. B., Vendome, J., Tomasek, D., Banerjee, S., Rajashankar, K. R., Dufrisne, M. Belcher, Kloss, B., Kloppmann, E., Rost, B., Klug, C. S., M Trent, S., Shapiro, L., and Mancia, F. (2016) Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science. 351, 608-12
F Demircioglu, E., Sosa, B. A., Ingram, J., Ploegh, H. L., and Schwartz, T. U. (2016) Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia. Elife. 10.7554/eLife.17983
Zhang, W., Wu, K. - P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., Mukherjee, M., Li, N., Doye, A., Walker, J. R., Sheng, Y., Hao, Z., Li, Y., Brown, K. R., Lemichez, E., Chen, J., Tong, Y., J Harper, W., Moffat, J., Rotin, D., Schulman, B. A., and Sidhu, S. S. (2016) System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes. Mol Cell. 62, 121-36
Golani, L. K., Wallace-Povirk, A., Deis, S. M., Wong, J., Ke, J., Gu, X., Raghavan, S., Wilson, M. R., Li, X., Polin, L., de Waal, P. W., White, K., Kushner, J., O'Connor, C., Hou, Z., H Xu, E., Melcher, K., Dann, C. E., Matherly, L. H., and Gangjee, A. (2016) Tumor Targeting with Novel 6-Substituted Pyrrolo [2,3-d] Pyrimidine Antifolates with Heteroatom Bridge Substitutions via Cellular Uptake by Folate Receptor α and the Proton-Coupled Folate Transporter and Inhibition of de Novo Purine Nucleotide Biosynthes. J Med Chem. 59, 7856-76
Golani, L. K., Wallace-Povirk, A., Deis, S. M., Wong, J., Ke, J., Gu, X., Raghavan, S., Wilson, M. R., Li, X., Polin, L., de Waal, P. W., White, K., Kushner, J., O'Connor, C., Hou, Z., H Xu, E., Melcher, K., Dann, C. E., Matherly, L. H., and Gangjee, A. (2016) Tumor Targeting with Novel 6-Substituted Pyrrolo [2,3-d] Pyrimidine Antifolates with Heteroatom Bridge Substitutions via Cellular Uptake by Folate Receptor α and the Proton-Coupled Folate Transporter and Inhibition of de Novo Purine Nucleotide Biosynthes. J Med Chem. 59, 7856-76
Golani, L. K., Wallace-Povirk, A., Deis, S. M., Wong, J., Ke, J., Gu, X., Raghavan, S., Wilson, M. R., Li, X., Polin, L., de Waal, P. W., White, K., Kushner, J., O'Connor, C., Hou, Z., H Xu, E., Melcher, K., Dann, C. E., Matherly, L. H., and Gangjee, A. (2016) Tumor Targeting with Novel 6-Substituted Pyrrolo [2,3-d] Pyrimidine Antifolates with Heteroatom Bridge Substitutions via Cellular Uptake by Folate Receptor α and the Proton-Coupled Folate Transporter and Inhibition of de Novo Purine Nucleotide Biosynthes. J Med Chem. 59, 7856-76
Leroy, E., Dusa, A., Colau, D., Motamedi, A., Cahu, X., Mouton, C., Huang, L. J., Shiau, A. K., and Constantinescu, S. N. (2016) Uncoupling JAK2 V617F activation from cytokine-induced signalling by modulation of JH2 αC helix.. Biochem J. 473, 1579-91
Pierson, W. E., Hoffer, E. D., Keedy, H. E., Simms, C. L., Dunham, C. M., and Zaher, H. S. (2016) Uniformity of Peptide Release Is Maintained by Methylation of Release Factors. Cell Rep. 17, 11-8

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