Found 71 results
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Conference Proceedings
Murphy, F. (2018) Rapd - Automated processing/structure determination. Best Practices for the Collection, Processing, Analysis, Transfer and Storage of Data from the New SER-CAT Eiger 16M Detector, April 12, 2018
Neau, D. (2014) Recent Developments at NE-CAT, a Macromolecular Crystallography Synchrotron Facility. Indo-US International Conference/Workshop on Recent Advances in Structural Biology and Drug Discovery, October 9-11, 2014
Journal Article
Davis, M. J., Ha, B. Hak, Holman, E. C., Halaban, R., Schlessinger, J., and Boggon, T. J. (2013) RAC1P29S is a spontaneously activating cancer-associated GTPase. Proc Natl Acad Sci U S A. 110, 912-7
Brzezinski, K., Dauter, Z., Baj, A., Wałejko, P., and Witkowski, S. (2011) rac-6-Hy-droxy-2,5,7,8-tetra-methyl-chroman-2-carboxamide from synchrotron data. Acta Crystallogr Sect E Struct Rep Online. 67, o503-4
Dowling, D. P., Bruender, N. A., Young, A. P., McCarty, R. M., Bandarian, V., and Drennan, C. L. (2014) Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism. Nat Chem Biol. 10, 106-12
Castel, P., Dharmaiah, S., Sale, M. J., Messing, S., Rizzuto, G., Cuevas-Navarro, A., Cheng, A., Trnka, M. J., Urisman, A., Esposito, D., Simanshu, D. K., and McCormick, F. (2021) RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity. Proc Natl Acad Sci U S A. 10.1073/pnas.2103261118
Blum, E., Zhang, J., Zaluski, J., Einstein, D. E., Korshin, E. E., Kubas, A., Gruzman, A., Tochtrop, G. P., Kiser, P. D., and Palczewski, K. (2021) Rational Alteration of Pharmacokinetics of Chiral Fluorinated and Deuterated Derivatives of Emixustat for Retinal Therapy. J Med Chem. 10.1021/acs.jmedchem.1c00279
LoVerde, P. T., Alwan, S. N., Taylor, A. B., Rhodes, J., Chevalier, F. D., Anderson, T. Jc, and McHardy, S. F. (2021) Rational approach to drug discovery for human schistosomiasis. Int J Parasitol Drugs Drug Resist. 16, 140-147
Doherty, E. E., Wilcox, X. E., Fiet, Lvan Sint, Kemmel, C., Turunen, J. J., Klein, B., Tantillo, D. J., Fisher, A. J., and Beal, P. A. (2021) Rational Design of RNA Editing Guide Strands: Cytidine Analogs at the Orphan Position. J Am Chem Soc. 143, 6865-6876
Joshi, S., Chen, L., Winter, M. B., Lin, Y. - L., Yang, Y., Shapovalova, M., Smith, P. M., Liu, C., Li, F., and LeBeau, A. M. (2017) The Rational Design of Therapeutic Peptides for Aminopeptidase N using a Substrate-Based Approach. Sci Rep. 7, 1424
Kiser, P. D., Zhang, J., Badiee, M., Kinoshita, J., Peachey, N. S., Tochtrop, G. P., and Palczewski, K. (2017) Rational Tuning of Visual Cycle Modulator Pharmacodynamics. J Pharmacol Exp Ther. 362, 131-145
Boekhout, M., Karasu, M. E., Wang, J., Acquaviva, L., Pratto, F., Brick, K., Eng, D. Y., Xu, J., R Camerini-Otero, D., Patel, D. J., and Keeney, S. (2019) REC114 Partner ANKRD31 Controls Number, Timing, and Location of Meiotic DNA Breaks. Mol Cell. 10.1016/j.molcel.2019.03.023
Roark, R. S., Li, H., Williams, W. B., Chug, H., Mason, R. D., Gorman, J., Wang, S., Lee, F. - H., Rando, J., Bonsignori, M., Hwang, K. - K., Saunders, K. O., Wiehe, K., M Moody, A., Hraber, P. T., Wagh, K., Giorgi, E. E., Russell, R. M., Bibollet-Ruche, F., Liu, W., Connell, J., Smith, A. G., DeVoto, J., Murphy, A. I., Smith, J., Ding, W., Zhao, C., Chohan, N., Okumura, M., Rosario, C., Ding, Y., Lindemuth, E., Bauer, A. M., Bar, K. J., Ambrozak, D., Chao, C. W., Chuang, G. - Y., Geng, H., Lin, B. C., Louder, M. K., Nguyen, R., Zhang, B., Lewis, M. G., Raymond, D., Doria-Rose, N. A., Schramm, C. A., Douek, D. C., Roederer, M., Kepler, T. B., Kelsoe, G., Mascola, J. R., Kwong, P. D., Korber, B. T., Harrison, S. C., Haynes, B. F., Hahn, B. H., and Shaw, G. M. (2020) Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth. Science. 10.1126/science.abd2638
Ruthenburg, A. J., Li, H., Milne, T. A., Dewell, S., McGinty, R. K., Yuen, M., Ueberheide, B., Dou, Y., Muir, T. W., Patel, D. J., and C Allis, D. (2011) Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions. Cell. 145, 692-706
Shen, A., Higgins, D. E., and Panne, D. (2009) Recognition of AT-rich DNA binding sites by the MogR repressor. Structure. 17, 769-77
Murn, J., Teplova, M., Zarnack, K., Shi, Y., and Patel, D. J. (2016) Recognition of distinct RNA motifs by the clustered CCCH zinc fingers of neuronal protein Unkempt. Nat Struct Mol Biol. 23, 16-23
MacDonald, E. A., Frey, G., Namchuk, M. N., Harrison, S. C., Hinshaw, S. M., and Windsor, I. W. (2021) Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease. ACS Infect Dis. 10.1021/acsinfecdis.1c00237
Min, J. - H., and Pavletich, N. P. (2007) Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature. 449, 570-5
Békés, M., van Noort, G. J. van der, Ekkebus, R., Ovaa, H., Huang, T. T., and Lima, C. D. (2016) Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease. Mol Cell. 62, 572-85
Dong, C., Chen, S. - J., Melnykov, A., Weirich, S., Sun, K., Jeltsch, A., Varshavsky, A., and Min, J. (2020) Recognition of nonproline N-terminal residues by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 117, 14158-14167
Singh, H., Schuermann, J. P., Reilly, T. J., Calcutt, M. J., and Tanner, J. J. (2010) Recognition of nucleoside monophosphate substrates by Haemophilus influenzae class C acid phosphatase. J Mol Biol. 404, 639-49
Chetty, A. K., Sexton, J. A., Ha, B. Hak, Turk, B. E., and Boggon, T. J. (2020) Recognition of physiological phosphorylation sites by p21-activated kinase 4. J Struct Biol. 211, 107553
Armstrong, A. A., Mohideen, F., and Lima, C. D. (2012) Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2. Nature. 483, 59-63
Cho, U. - S., and Harrison, S. C. (2011) Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. Proc Natl Acad Sci U S A. 108, 9367-71
Kuznedelov, K., Lamour, V., Patikoglou, G., Chlenov, M., Darst, S. A., and Severinov, K. (2006) Recombinant Thermus aquaticus RNA polymerase for structural studies. J Mol Biol. 359, 110-21