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M Puno, R., and Lima, C. D. (2018) Structural basis for MTR4-ZCCHC8 interactions that stimulate the MTR4 helicase in the nuclear exosome-targeting complex. Proc Natl Acad Sci U S A. 10.1073/pnas.1803530115
Puleo, D. E., Kucera, K., Hammarén, H. M., Ungureanu, D., Newton, A. S., Silvennoinen, O., Jorgensen, W. L., and Schlessinger, J. (2017) Identification and Characterization of JAK2 Pseudokinase Domain Small Molecule Binders. ACS Med Chem Lett. 8, 618-621
Pruitt, R. N., Chumbler, N. M., Rutherford, S. A., Farrow, M. A., Friedman, D. B., Spiller, B., and D Lacy, B. (2012) Structural determinants of Clostridium difficile toxin A glucosyltransferase activity. J Biol Chem. 287, 8013-20
Profeta, G. S., Reis, C. V. Dos, Santiago, Ada S., Godoi, P. H. C., Fala, A. M., Wells, C. I., Sartori, R., Salmazo, A. P. T., Ramos, P. Z., Massirer, K. B., Elkins, J. M., Drewry, D. H., Gileadi, O., and Couñago, R. M. (2019) Binding and structural analyses of potent inhibitors of the human Ca/calmodulin dependent protein kinase kinase 2 (CAMKK2) identified from a collection of commercially-available kinase inhibitors. Sci Rep. 9, 16452
Price, I. R., Gaballa, A., Ding, F., Helmann, J. D., and Ke, A. (2015) Mn(2+)-sensing mechanisms of yybP-ykoY orphan riboswitches. Mol Cell. 57, 1110-1123
Pradeep, L., Kurinov, I., Ealick, S. E., and Scheraga, H. A. (2007) Implementation of a k/k(0) method to identify long-range structure in transition states during conformational folding/unfolding of proteins. Structure. 15, 1178-89
Powers, R. E., Gaudet, R., and Sotomayor, M. (2017) A Partial Calcium-Free Linker Confers Flexibility to Inner-Ear Protocadherin-15. Structure. 25, 482-495
Pourfarjam, Y., Ventura, J., Kurinov, I., Cho, A., Moss, J., and Kim, I. - K. (2018) Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. J Biol Chem. 293, 12350-12359
Posternak, G., Tang, X., Maisonneuve, P., Jin, T., Lavoie, H., Daou, S., Orlicky, S., de Rugy, T. Goullet, Caldwell, L., Chan, K., Aman, A., Prakesch, M., Poda, G., Mader, P., Wong, C., Maier, S., Kitaygorodsky, J., Larsen, B., Colwill, K., Yin, Z., Ceccarelli, D. F., Batey, R. A., Taipale, M., Kurinov, I., Uehling, D., Wrana, J., Durocher, D., Gingras, A. - C., Al-awar, R., Therrien, M., and Sicheri, F. (2020) Functional characterization of a PROTAC directed against BRAF mutant V600E. Nat Chem Biol. 10.1038/s41589-020-0609-7
Pos, W., Sethi, D. K., Call, M. J., Schulze, M. - S. E. D., Anders, A. - K., Pyrdol, J., and Wucherpfennig, K. W. (2012) Crystal structure of the HLA-DM-HLA-DR1 complex defines mechanisms for rapid peptide selection. Cell. 151, 1557-68
Porter, N. J., Osko, J. D., Diedrich, D., Kurz, T., Hooker, J. M., Hansen, F. K., and Christianson, D. W. (2018) Histone Deacetylase 6-Selective Inhibitors and the Influence of Capping Groups on Hydroxamate-Zinc Denticity. J Med Chem. 10.1021/acs.jmedchem.8b01013
Porter, N. J., Christianson, N. H., Decroos, C., and Christianson, D. W. (2016) Structural and Functional Influence of the Glycine-Rich Loop G(302)GGGY on the Catalytic Tyrosine of Histone Deacetylase 8. Biochemistry. 55, 6718-6729
Porter, N. J., Shen, S., Barinka, C., Kozikowski, A. P., and Christianson, D. W. (2018) Molecular Basis for the Selective Inhibition of Histone Deacetylase 6 by a Mercaptoacetamide Inhibitor. ACS Med Chem Lett. 9, 1301-1305
Porter, N. J., Mahendran, A., Breslow, R., and Christianson, D. W. (2017) Unusual zinc-binding mode of HDAC6-selective hydroxamate inhibitors. Proc Natl Acad Sci U S A. 10.1073/pnas.1718823114
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
Poor, C. B., Andorfer, M. C., and Lewis, J. C. (2014) Improving the stability and catalyst lifetime of the halogenase RebH by directed evolution. Chembiochem. 15, 1286-9
Pomerantz, W. Charles Kr, Cui, H., Divakaran, A., Pandey, A. K., Johnson, J. A., Zahid, H., Hoell, Z. J., Ellingson, M. O., Shi, K., Aihara, H., and Harki, D. A. (2020) Selective N-terminal BRD4 bromodomain inhibitors by targeting non-conserved residues and structured water displacement. Angew Chem Int Ed Engl. 10.1002/anie.202008625
Polley, S., Bin Huang, D. -, Hauenstein, A. V., Fusco, A. J., Zhong, X., Vu, D., Schröfelbauer, B., Kim, Y., Hoffmann, A., Verma, I. M., Ghosh, G., and Huxford, T. (2013) A structural basis for IκB kinase 2 activation via oligomerization-dependent trans auto-phosphorylation.. PLoS Biol. 11, e1001581
Pollard, A. M., Bilwes, A. M., and Crane, B. R. (2009) The structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals. Biochemistry. 48, 1936-44
Polizzi, N. F., and DeGrado, W. F. (2020) A defined structural unit enables de novo design of small-molecule-binding proteins. Science. 369, 1227-1233
Polikanov, Y. S., and Moore, P. B. (2015) Acoustic vibrations contribute to the diffuse scatter produced by ribosome crystals. Acta Crystallogr D Biol Crystallogr. 71, 2021-31
Polikanov, Y. S., Steitz, T. A., and C Innis, A. (2014) A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosome. Nat Struct Mol Biol. 21, 787-93
Polikanov, Y. S., Melnikov, S. V., Söll, D., and Steitz, T. A. (2015) Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly. Nat Struct Mol Biol. 22, 342-344
Polikanov, Y. S., Osterman, I. A., Szal, T., Tashlitsky, V. N., Serebryakova, M. V., Kusochek, P., Bulkley, D., Malanicheva, I. A., Efimenko, T. A., Efremenkova, O. V., Konevega, A. L., Shaw, K. J., Bogdanov, A. A., Rodnina, M. V., Dontsova, O. A., Mankin, A. S., Steitz, T. A., and Sergiev, P. V. (2014) Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Mol Cell. 56, 531-40
Polikanov, Y. S., Blaha, G. M., and Steitz, T. A. (2012) How hibernation factors RMF, HPF, and YfiA turn off protein synthesis. Science. 336, 915-8

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