Publications

Found 1131 results
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2016
Neumann, W., Xu, S., Sárosi, M. B., Scholz, M. S., Crews, B. C., Ghebreselasie, K., Banerjee, S., Marnett, L. J., and Hey-Hawkins, E. (2016) nido-Dicarbaborate Induces Potent and Selective Inhibition of Cyclooxygenase-2. ChemMedChem. 11, 175-8
Gibson, M. I., Chen, P. Yang- Ting, Johnson, A. C., Pierce, E., Can, M., Ragsdale, S. W., and Drennan, C. L. (2016) One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography. Proc Natl Acad Sci U S A. 113, 320-5
Yang, H., Gao, P., Rajashankar, K. R., and Patel, D. J. (2016) PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease. Cell. 167, 1814-1828.e12
Schormann, N., Zhukovskaya, N., Bedwell, G., Nuth, M., Gillilan, R., Prevelige, P. E., Ricciardi, R. P., Banerjee, S., and Chattopadhyay, D. (2016) Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases. Protein Sci. 25, 2113-2131
Kim, K. - H., Ko, D. - K., Kim, Y. - T., Kim, N. Hyeong, Paul, J., Zhang, S. - Q., Murray, C. B., Acharya, R., DeGrado, W. F., Kim, Y. Ho, and Grigoryan, G. (2016) Protein-directed self-assembly of a fullerene crystal. Nat Commun. 7, 11429
Hicks, K. A., Yuen, M. E., Zhen, W. Feng, Gerwig, T. J., Story, R. W., Kopp, M. C., and Snider, M. J. (2016) Structural and Biochemical Characterization of 6-Hydroxynicotinic Acid 3-Monooxygenase, A Novel Decarboxylative Hydroxylase Involved in Aerobic Nicotinate Degradation. Biochemistry. 55, 3432-46
Polley, S., Passos, D. Oliveira, Bin Huang, D. -, Mulero, M. Carmen, Mazumder, A., Biswas, T., Verma, I. M., Lyumkis, D., and Ghosh, G. (2016) Structural Basis for the Activation of IKK1/α.. Cell Rep. 17, 1907-1914
Stein, B. J., Grant, R. A., Sauer, R. T., and Baker, T. A. (2016) Structural Basis of an N-Degron Adaptor with More Stringent Specificity. Structure. 24, 232-42
Goodman, K. Marie, Rubinstein, R., Thu, C. Aye, Bahna, F., Mannepalli, S., Ahlsen, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins.. Neuron. 90, 709-23
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
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
Geng, Y., Mosyak, L., Kurinov, I., Zuo, H., Sturchler, E., Cheng, T. Cheung, Subramanyam, P., Brown, A. P., Brennan, S. C., Mun, H. - C., Bush, M., Chen, Y., Nguyen, T. X., Cao, B., Chang, D. D., Quick, M., Conigrave, A. D., Colecraft, H. M., McDonald, P., and Fan, Q. R. (2016) Structural mechanism of ligand activation in human calcium-sensing receptor. Elife. 10.7554/eLife.13662
Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Rechkoblit, O., Gupta, Y. K., Malik, R., Rajashankar, K. R., Johnson, R. E., Prakash, L., Prakash, S., and Aggarwal, A. K. (2016) Structure and mechanism of human PrimPol, a DNA polymerase with primase activity. Sci Adv. 2, e1601317
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
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
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
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
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
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
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

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