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Rechkoblit, O., Choudhury, J. Roy, Buku, A., Prakash, L., Prakash, S., and Aggarwal, A. K. (2018) Structural basis for polymerase η-promoted resistance to the anticancer nucleoside analog cytarabine.. Sci Rep. 8, 12702
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
Rechkoblit, O., Johnson, R. E., Buku, A., Prakash, L., Prakash, S., and Aggarwal, A. K. (2019) Structural insights into mutagenicity of anticancer nucleoside analog cytarabine during replication by DNA polymerase η.. Sci Rep. 9, 16400
Ramagopal, U. A., Liu, W., Garrett-Thomson, S. C., Bonanno, J. B., Yan, Q., Srinivasan, M., Wong, S. C., Bell, A., Mankikar, S., Rangan, V. S., Deshpande, S., Korman, A. J., and Almo, S. C. (2017) Structural basis for cancer immunotherapy by the first-in-class checkpoint inhibitor ipilimumab. Proc Natl Acad Sci U S A. 114, E4223-E4232
Rajagopalan, S., Teter, S. J., Zwart, P. H., Brennan, R. G., Phillips, K. J., and Kiley, P. J. (2013) Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity. Nat Struct Mol Biol. 20, 740-7
Radakovic, A., Lewicka, A., Todisco, M., Aitken, H. R. M., Weiss, Z., Kim, S., Bannan, A., Piccirilli, J. A., and Szostak, J. W. (2024) Structure-guided aminoacylation and assembly of chimeric RNAs. bioRxiv. 10.1101/2024.03.02.583109
Q
Qi, Y., Nam, K., Spong, M. C., Banerjee, A., Sung, R. - J., Zhang, M., Karplus, M., and Verdine, G. L. (2012) Strandwise translocation of a DNA glycosylase on undamaged DNA. Proc Natl Acad Sci U S A. 109, 1086-91
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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
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
Priest, J. M., Nichols, E. L., Smock, R. G., Hopkins, J. B., Mendoza, J. L., Meijers, R., Shen, K., and zkan, E. Ö. (2024) Structural insights into the formation of repulsive netrin guidance complexes. Sci Adv. 10, eadj8083
Prew, M. S., Camara, C. M., Botzanowski, T., Moroco, J. A., Bloch, N. B., Levy, H. R., Seo, H. - S., Dhe-Paganon, S., Bird, G. H., Herce, H. D., Gygi, M. A., Escudero, S., Wales, T. E., Engen, J. R., and Walensky, L. D. (2022) Structural basis for defective membrane targeting of mutant enzyme in human VLCAD deficiency. Nat Commun. 13, 3669
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
Pourfarjam, Y., Ma, Z., Kurinov, I., Moss, J., and Kim, I. - K. (2021) Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 (ARH3) reveals the basis of metal selectivity and different roles for the two Mg ions. J Biol Chem. 10.1016/j.jbc.2021.100692
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
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
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
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
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
Pidathala, S., Mallela, A. Kumar, Joseph, D., and Penmatsa, A. (2021) Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters. Nat Commun. 12, 2199
Pickens, L. B., Sawaya, M. R., Rasool, H., Pashkov, I., Yeates, T. O., and Tang, Y. (2011) Structural and biochemical characterization of the salicylyl-acyltranferase SsfX3 from a tetracycline biosynthetic pathway. J Biol Chem. 286, 41539-51
Phillips, C. M., Schreiter, E. R., Guo, Y., Wang, S. C., Zamble, D. B., and Drennan, C. L. (2008) Structural basis of the metal specificity for nickel regulatory protein NikR. Biochemistry. 47, 1938-46
Phelps, C. B., Huang, R. J., Lishko, P. V., Wang, R. R., and Gaudet, R. (2008) Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels. Biochemistry. 47, 2476-84
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
Peng, G., Yang, Y., Pasquarella, J. R., Xu, L., Qian, Z., Holmes, K. V., and Li, F. (2017) Structural and Molecular Evidence Suggesting Coronavirus-driven Evolution of Mouse Receptor. J Biol Chem. 292, 2174-2181

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