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Shen, G., Cui, W., Zhang, H., Zhou, F., Huang, W., Liu, Q., Yang, Y., Li, S., Bowman, G. R., J Sadler, E., Gross, M. L., and Li, W. (2017) Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer. Nat Struct Mol Biol. 24, 69-76
Li, K., Yatsunyk, L., and Neidle, S. (2021) Water spines and networks in G-quadruplex structures. Nucleic Acids Res. 49, 519-528
Schirle, N. T., Sheu-Gruttadauria, J., Chandradoss, S. D., Joo, C., and MacRae, I. J. (2015) Water-mediated recognition of t1-adenosine anchors Argonaute2 to microRNA targets. Elife. 10.7554/eLife.07646
Smiley, A. T., Tompkins, K. J., Pawlak, M. R., Krueger, A. J., Evans, R. L., Shi, K., Aihara, H., and Gordon, W. R. (2022) Watson-Crick Base-Pairing Requirements for ssDNA Recognition and Processing in Replication-Initiating HUH Endonucleases. mBio. 10.1128/mbio.02587-22
Luo, Z., Rajashankar, K., and Dauter, Z. (2014) Weak data do not make a free lunch, only a cheap meal. Acta Crystallogr D Biol Crystallogr. 70, 253-60
Ginn, J., Jiang, X., Sun, S., Michino, M., Huggins, D. J., Mbambo, Z., Jansen, R., Rhee, K. Y., Arango, N., Lima, C. D., Liverton, N., Imaeda, T., Okamoto, R., Kuroita, T., Aso, K., Stamford, A., Foley, M., Meinke, P. T., Nathan, C., and Bryk, R. (2021) Whole Cell Active Inhibitors of Mycobacterial Lipoamide Dehydrogenase Afford Selectivity over the Human Enzyme through Tight Binding Interactions. ACS Infect Dis. 7, 435-444
Rugel, A. R., Guzman, M. A., Taylor, A. B., Chevalier, F. D., Tarpley, R. S., McHardy, S. F., Cao, X., Holloway, S. P., Anderson, T. J. C., P Hart, J., and LoVerde, P. T. (2020) Why does oxamniquine kill Schistosoma mansoni and not S. haematobium and S. japonicum?. Int J Parasitol Drugs Drug Resist. 13, 8-15
Rizzolo, K., Cohen, S. E., Weitz, A. C., Muñoz, M. M. López, Hendrich, M. P., Drennan, C. L., and Elliott, S. J. (2019) A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state. Nat Commun. 10, 1101
Bradshaw, N., Levdikov, V. M., Zimanyi, C. M., Gaudet, R., Wilkinson, A. J., and Losick, R. (2017) A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases. Elife. 10.7554/eLife.26111
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Goldman, P. J., Grove, T. L., Booker, S. J., and Drennan, C. L. (2013) X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry. Proc Natl Acad Sci U S A. 110, 15949-54
Fan, C., Fan, M., Orlando, B. J., Fastman, N. M., Zhang, J., Xu, Y., Chambers, M. G., Xu, X., Perry, K., Liao, M., and Feng, L. (2018) X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature. 559, 575-579
Agdanowski, M. P., Castells-Graells, R., Sawaya, M. R., Cascio, D., Yeates, T. O., and Arbing, M. A. (2024) X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation. Acta Crystallogr F Struct Biol Commun. 80, 107-115
Han, S., Le, B. V., Hajare, H. S., Baxter, R. H. G., and Miller, S. J. (2014) X-ray crystal structure of teicoplanin A₂-2 bound to a catalytic peptide sequence via the carrier protein strategy.. J Org Chem. 79, 8550-6
Jones, J. C., Banerjee, R., Semonis, M. M., Shi, K., Aihara, H., and Lipscomb, J. D. (2022) X-ray Crystal Structures of Methane Monooxygenase Hydroxylase Complexes with Variants of Its Regulatory Component: Correlations with Altered Reaction Cycle Dynamics. Biochemistry. 61, 21-33
Caldwell, J. T., Mermelstein, D. J., Walker, R. C., Bernstein, S. I., and Huxford, T. (2019) X-ray crystallographic and molecular dynamic analyses of Drosophila melanogaster embryonic muscle myosin define domains responsible for isoform-specific properties. J Mol Biol. 10.1016/j.jmb.2019.11.013
Wada, M., Heux, L., Nishiyama, Y., and Langan, P. (2009) X-ray crystallographic, scanning microprobe X-ray diffraction, and cross-polarized/magic angle spinning 13C NMR studies of the structure of cellulose III(II). Biomacromolecules. 10, 302-9
Herbst-Gervasoni, C. J., and Christianson, D. W. (2021) X-ray Crystallographic Snapshots of Substrate Binding in the Active Site of Histone Deacetylase 10. Biochemistry. 10.1021/acs.biochem.0c00936
Zhu, N., Mealka, M., Mitchel, S., Milani, C., Acuña, L. M., Rogers, E., Lahana, A. N., and Huxford, T. (2023) X-ray Crystallographic Study of Preferred Spacing by the NF-κB p50 Homodimer on κB DNA.. Biomolecules. 10.3390/biom13091310
Banerjee, S. (2020) X-ray Crystallography - An Interdisciplinary Science. Nurture Program for JBNSTS Junior Scholar of Batch 2018 & 2019
Wan, Q., Ahmad, M. Faiz, Fairman, J., Gorzelle, B., de la Fuente, M., Dealwis, C., and Maguire, M. E. (2011) X-ray crystallography and isothermal titration calorimetry studies of the Salmonella zinc transporter ZntB. Structure. 19, 700-10
Chen, P. Yang- Ting, DeColli, A. A., Meyers, C. L. Freel, and Drennan, C. L. (2019) X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. J Biol Chem. 294, 12405-12414
Sazinsky, M. H., Dunten, P. W., McCormick, M. S., DiDonato, A., and Lippard, S. J. (2006) X-ray structure of a hydroxylase-regulatory protein complex from a hydrocarbon-oxidizing multicomponent monooxygenase, Pseudomonas sp. OX1 phenol hydroxylase. Biochemistry. 45, 15392-404
Bai, Y., McCoy, J. G., Levin, E. J., Sobrado, P., Rajashankar, K. R., Fox, B. G., and Zhou, M. (2015) X-ray structure of a mammalian stearoyl-CoA desaturase. Nature. 524, 252-6
Van den Berg, B., Clemons, W. M., Collinson, I., Modis, Y., Hartmann, E., Harrison, S. C., and Rapoport, T. A. (2004) X-ray structure of a protein-conducting channel. Nature. 427, 36-44

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