Publications

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2016
Tabackman, A. A., Frankson, R., Marsan, E. S., Perry, K., and Cole, K. E. (2016) Structure of 'linkerless' hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket. J Struct Biol. 195, 373-378
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
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nature Microbiology. 10.1038/nmicrobiol.2016.154
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol. 1, 16154
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
Jain, R., Coloma, J., García-Sastre, A., and Aggarwal, A. K. (2016) Structure of the NS3 helicase from Zika virus. Nat Struct Mol Biol. 23, 752-4
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Ye, Q., Ur, S. N., Su, T. Y., and Corbett, K. D. (2016) Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator. EMBO J. 35, 2139-2151
Callahan, S. J., Luyten, Y. A., Gupta, Y. K., Wilson, G. G., Roberts, R. J., Morgan, R. D., and Aggarwal, A. K. (2016) Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities. PLoS Biol. 14, e1002442
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
Liu, B., Zuo, Y., and Steitz, T. A. (2016) Structures of E. coli σS-transcription initiation complexes provide new insights into polymerase mechanism.. Proc Natl Acad Sci U S A. 113, 4051-6
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
Matthews, M. M., Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., and Beal, P. A. (2016) Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. Nat Struct Mol Biol. 23, 426-33
Coloma, J., Jain, R., Rajashankar, K. R., García-Sastre, A., and Aggarwal, A. K. (2016) Structures of NS5 Methyltransferase from Zika Virus. Cell Rep. 16, 3097-102
Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., and Steitz, T. A. (2016) Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Res. 44, 2439-50
Chen, X., Randles, L., Shi, K., Tarasov, S. G., Aihara, H., and Walters, K. J. (2016) Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome. Structure. 24, 1257-70
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
Taabazuing, C. Y., Fermann, J., Garman, S., and Knapp, M. J. (2016) Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.. Biochemistry. 55, 277-86
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
Ma, W., and Goldberg, J. (2016) TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats. Proc Natl Acad Sci U S A. 113, 10061-6
Chen, M. (2016) Terpene Synthases: One Fold, Many Products. Ph.D. thesis, University of Pennsylvania, Philadelphia, Pennsylvania
Chatterjee, D., Sanchez, A. M., Goldgur, Y., Shuman, S., and Schwer, B. (2016) Transcription of lncRNA prt, clustered prt RNA sites for Mmi1 binding, and RNA polymerase II CTD phospho-sites govern the repression of pho1 gene expression under phosphate-replete conditions in fission yeast. RNA. 22, 1011-25
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
Gao, P., Yang, H., Rajashankar, K. R., Huang, Z., and Patel, D. J. (2016) Type V CRISPR-Cas Cpf1 endonuclease employs a unique mechanism for crRNA-mediated target DNA recognition. Cell Res. 26, 901-13

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