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Found 137 results
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Deo, C., Abdelfattah, A. S., Bhargava, H. K., Berro, A. J., Falco, N., Farrants, H., Moeyaert, B., Chupanova, M., Lavis, L. D., and Schreiter, E. R. (2021) The HaloTag as a general scaffold for far-red tunable chemigenetic indicators. Nat Chem Biol. 17, 718-723
Deochand, D. K., Perera, I. C., Crochet, R. B., Gilbert, N. C., Newcomer, M. E., and Grove, A. (2016) Histidine switch controlling pH-dependent protein folding and DNA binding in a transcription factor at the core of synthetic network devices. Mol Biosyst. 12, 2417-26
Deshmukh, M. G., Ippolito, J. A., Zhang, C. - H., Stone, E. A., Reilly, R. A., Miller, S. J., Jorgensen, W. L., and Anderson, K. S. (2021) Structure-guided design of a perampanel-derived pharmacophore targeting the SARS-CoV-2 main protease. Structure. 10.1016/j.str.2021.06.002
Dessanti, P., Zhang, Y., Allegrini, S., Tozzi, M. Grazia, Sgarrella, F., and Ealick, S. E. (2012) Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase. Acta Crystallogr D Biol Crystallogr. 68, 239-48
Dessau, M., and Modis, Y. (2013) Crystal structure of glycoprotein C from Rift Valley fever virus. Proc Natl Acad Sci U S A. 110, 1696-701
Devlin, J. R., Alonso, J. A., Ayres, C. M., Keller, G. L. J., Bobisse, S., Kooi, C. W. Vander, Coukos, G., Gfeller, D., Harari, A., and Baker, B. M. (2020) Structural dissimilarity from self drives neoepitope escape from immune tolerance. Nat Chem Biol. 10.1038/s41589-020-0610-1
Dhakshnamoorthy, B., Rohaim, A., Rui, H., Blachowicz, L., and Roux, B. (2016) Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola. Nat Commun. 7, 12753
Dhakshnamoorthy, B., Ziervogel, B. K., Blachowicz, L., and Roux, B. (2013) A structural study of ion permeation in OmpF porin from anomalous X-ray diffraction and molecular dynamics simulations. J Am Chem Soc. 135, 16561-8
Dharmaiah, S., Tran, T. H., Messing, S., Agamasu, C., Gillette, W. K., Yan, W., Waybright, T., Alexander, P., Esposito, D., Nissley, D. V., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2019) Structures of N-terminally processed KRAS provide insight into the role of N-acetylation. Sci Rep. 9, 10512
Dharmaiah, S., Bindu, L., Tran, T. H., Gillette, W. K., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2016) Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.. Proc Natl Acad Sci U S A. 113, E6766-E6775
Dhatwalia, R., Singh, H., Oppenheimer, M., Karr, D. B., Nix, J. C., Sobrado, P., and Tanner, J. J. (2012) Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. J Biol Chem. 287, 9041-51
Dhatwalia, R., Singh, H., Reilly, T. J., and Tanner, J. J. (2015) Crystal structure and tartrate inhibition of Legionella pneumophila histidine acid phosphatase. Arch Biochem Biophys. 585, 32-38
Dhatwalia, R., Singh, H., Solano, L. M., Oppenheimer, M., Robinson, R. M., Ellerbrock, J. F., Sobrado, P., and Tanner, J. J. (2012) Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase. J Am Chem Soc. 134, 18132-8
Dhatwalia, R., Singh, H., Oppenheimer, M., Sobrado, P., and Tanner, J. J. (2012) Crystal structures of Trypanosoma cruzi UDP-galactopyranose mutase implicate flexibility of the histidine loop in enzyme activation. Biochemistry. 51, 4968-79
Dhayalan, B., Fitzpatrick, A., Mandal, K., Whittaker, J., Weiss, M. A., Tokmakoff, A., and Kent, S. B. H. (2016) Efficient Total Chemical Synthesis of (13) C=(18) O Isotopomers of Human Insulin for Isotope-Edited FTIR. Chembiochem. 17, 415-20
Dhayalan, B., Mandal, K., Rege, N., Weiss, M. A., Eitel, S. H., Meier, T., Schoenleber, R. O., and Kent, S. B. H. (2017) Scope and Limitations of Fmoc Chemistry SPPS-Based Approaches to the Total Synthesis of Insulin Lispro via Ester Insulin. Chemistry. 23, 1709-1716
Dhindwal, S., Gomez-Gil, L., Neau, D. B., Pham, T. Thanh My, Sylvestre, M., Eltis, L. D., Bolin, J. T., and Kumar, P. (2016) Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase. J Bacteriol. 198, 1499-512
Di Costanzo, L., Ilies, M., Thorn, K. J., and Christianson, D. W. (2010) Inhibition of human arginase I by substrate and product analogues. Arch Biochem Biophys. 496, 101-8
Di Paolo, J. A., Huang, T., Balazs, M., Barbosa, J., Barck, K. H., Bravo, B. J., Carano, R. A. D., Darrow, J., Davies, D. R., DeForge, L. E., Diehl, L., Ferrando, R., Gallion, S. L., Giannetti, A. M., Gribling, P., Hurez, V., Hymowitz, S. G., Jones, R., Kropf, J. E., Lee, W. P., Maciejewski, P. M., Mitchell, S. A., Rong, H., Staker, B. L., J Whitney, A., Yeh, S., Young, W. B., Yu, C., Zhang, J., Reif, K., and Currie, K. S. (2011) Specific Btk inhibition suppresses B cell- and myeloid cell-mediated arthritis. Nat Chem Biol. 7, 41-50
Diao, J., Liu, R., Rong, Y., Zhao, M., Zhang, J., Lai, Y., Zhou, Q., Wilz, L. M., Li, J., Vivona, S., Pfuetzner, R. A., Brunger, A. T., and Zhong, Q. (2015) ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes. Nature. 520, 563-6
Dias, S. M. G., Wilson, K. F., Rojas, K. S., Ambrosio, A. L. B., and Cerione, R. A. (2009) The molecular basis for the regulation of the cap-binding complex by the importins. Nat Struct Mol Biol. 16, 930-7
Dickson, V. Kane, Pedi, L., and Long, S. B. (2014) Structure and insights into the function of a Ca(2+)-activated Cl(-) channel. Nature. 516, 213-8
Dickson, V. Kane (2016) Phasing and structure of bestrophin-1: a case study in the use of heavy-atom cluster compounds with multi-subunit transmembrane proteins. Acta Crystallogr D Struct Biol. 72, 319-25
Didovyk, A., and Verdine, G. L. (2012) Structural origins of DNA target selection and nucleobase extrusion by a DNA cytosine methyltransferase. J Biol Chem. 287, 40099-105
Didychuk, A. L., Montemayor, E. J., Carrocci, T. J., DeLaitsch, A. T., Lucarelli, S. E., Westler, W. M., Brow, D. A., Hoskins, A. A., and Butcher, S. E. (2017) Usb1 controls U6 snRNP assembly through evolutionarily divergent cyclic phosphodiesterase activities. Nat Commun. 8, 497

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