Publications

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Journal Article
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
Wan, L. C. K., Mao, D. Y. L., Neculai, D., Strecker, J., Chiovitti, D., Kurinov, I., Poda, G., Thevakumaran, N., Yuan, F., Szilard, R. K., Lissina, E., Nislow, C., Caudy, A. A., Durocher, D., and Sicheri, F. (2013) Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Res. 41, 6332-46
Chatterjee, A., Li, Y., Zhang, Y., Grove, T. L., Lee, M., Krebs, C., Booker, S. J., Begley, T. P., and Ealick, S. E. (2008) Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily. Nat Chem Biol. 4, 758-65
Liang, J., Singh, N., Carlson, C. R., Albuquerque, C. P., Corbett, K. D., and Zhou, H. (2017) Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity. Genes Dev. 31, 802-815
Lim, D. C., Joukov, V., T Rettenmaier, J., Kumagai, A., Dunphy, W. G., Wells, J. A., and Yaffe, M. B. (2020) Redox priming promotes Aurora A activation during mitosis. Sci Signal. 10.1126/scisignal.abb6707
Wittenborn, E. C., Merrouch, M., Ueda, C., Fradale, L., Léger, C., Fourmond, V., Pandelia, M. - E., Dementin, S., and Drennan, C. L. (2018) Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Elife. 10.7554/eLife.39451
Chao, F. - A., Chan, A. H., Dharmaiah, S., Schwieters, C. D., Tran, T. H., Taylor, T., Ramakrishnan, N., Esposito, D., Nissley, D. V., McCormick, F., Simanshu, D. K., and Cornilescu, G. (2023) Reduced dynamic complexity allows structure elucidation of an excited state of KRAS. Commun Biol. 6, 594
LaRonde-LeBlanc, N., Resto, M., and Gerratana, B. (2009) Regulation of active site coupling in glutamine-dependent NAD(+) synthetase. Nat Struct Mol Biol. 16, 421-9
Johnson, C. W., Seo, H. - S., Terrell, E. M., Yang, M. - H., KleinJan, F., Gebregiworgis, T., Gasmi-Seabrook, G. M. C., Geffken, E. A., Lakhani, J., Song, K., Bashyal, P., Popow, O., Paulo, J. A., Liu, A., Mattos, C., Marshall, C. B., Ikura, M., Morrison, D. K., Dhe-Paganon, S., and Haigis, K. M. (2022) Regulation of GTPase function by autophosphorylation. Mol Cell. 82, 950-968.e14
Xiong, S., Couzens, A. L., Kean, M. J., Mao, D. Y., Guettler, S., Kurinov, I., Gingras, A. - C., and Sicheri, F. (2017) Regulation of Protein Interactions by Mps One Binder (MOB1) Phosphorylation. Mol Cell Proteomics. 16, 1111-1125
Chuenchor, W., Doukov, T. I., Resto, M., Chang, A., and Gerratana, B. (2012) Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase. Biochem J. 443, 417-26
Fagan, C. E., Dunkle, J. A., Maehigashi, T., Dang, M. N., Devaraj, A., Miles, S. J., Qin, D., Fredrick, K., and Dunham, C. M. (2013) Reorganization of an intersubunit bridge induced by disparate 16S ribosomal ambiguity mutations mimics an EF-Tu-bound state. Proc Natl Acad Sci U S A. 110, 9716-21
Sukumar, N., Choi, M., and Davidson, V. L. (2011) Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. J Inorg Biochem. 105, 1638-44
Orlova, N., Gerding, M., Ivashkiv, O., Olinares, P. Dominic B., Chait, B. T., Waldor, M. K., and Jeruzalmi, D. (2017) The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators. Nucleic Acids Res. 45, 3724-3737
Kirouac, K. N., Basu, A. K., and Ling, H. (2013) Replication of a carcinogenic nitropyrene DNA lesion by human Y-family DNA polymerase. Nucleic Acids Res. 41, 2060-71
Liebschner, D., Dauter, M., Brzuszkiewicz, A., and Dauter, Z. (2013) On the reproducibility of protein crystal structures: five atomic resolution structures of trypsin. Acta Crystallogr D Biol Crystallogr. 69, 1447-62
Hill, M. E., MacPherson, D. J., Wu, P., Julien, O., Wells, J. A., and Hardy, J. A. (2016) Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition. ACS Chem Biol. 11, 1603-12
Li, R., Chou, W. K. W., Himmelberger, J. A., Litwin, K. M., Harris, G. G., Cane, D. E., and Christianson, D. W. (2014) Reprogramming the chemodiversity of terpenoid cyclization by remolding the active site contour of epi-isozizaene synthase. Biochemistry. 53, 1155-68
Eaton, S. A., and Christianson, D. W. (2023) Reprogramming the Cyclization Cascade of -Isozizaene Synthase to Generate Alternative Terpene Products. Biochemistry. 62, 2301-2313
Uervirojnangkoorn, M., Lyubimov, A. Y., Zhou, Q., Weis, W. I., and Brunger, A. T. (2019) Resolving indexing ambiguities in X-ray free-electron laser diffraction patterns. Acta Crystallogr D Struct Biol. 75, 234-241

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