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Doamekpor, S. K., Gozdek, A., Kwasnik, A., Kufel, J., and Tong, L. (2020) A novel 5'-hydroxyl dinucleotide hydrolase activity for the DXO/Rai1 family of enzymes. Nucleic Acids Res. 48, 349-358
Doamekpor, S. K., Sanchez, A. M., Schwer, B., Shuman, S., and Lima, C. D. (2014) How an mRNA capping enzyme reads distinct RNA polymerase II and Spt5 CTD phosphorylation codes. Genes Dev. 28, 1323-36
Doamekpor, S. K., Grudzien-Nogalska, E., Mlynarska-Cieslak, A., Kowalska, J., Kiledjian, M., and Tong, L. (2020) DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs. Nucleic Acids Res. 48, 6136-6148
Doamekpor, S. K., Lee, J. - W., Hepowit, N. L., Wu, C., Charenton, C., Leonard, M., Bengtson, M. H., Rajashankar, K. R., Sachs, M. S., Lima, C. D., and Joazeiro, C. A. P. (2016) Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits. Proc Natl Acad Sci U S A. 113, E4151-60
Do, T. D., LaPointe, N. E., Sangwan, S., Teplow, D. B., Feinstein, S. C., Sawaya, M. R., Eisenberg, D. S., and Bowers, M. T. (2014) Factors that drive peptide assembly from native to amyloid structures: experimental and theoretical analysis of [leu-5]-enkephalin mutants. J Phys Chem B. 118, 7247-56
Do, T. D., Sangwan, S., de Almeida, N. E. C., Ilitchev, A. I., Giammona, M., Sawaya, M. R., Buratto, S. K., Eisenberg, D. S., and Bowers, M. T. (2018) Distal Amyloid β-Protein Fragments Template Amyloid Assembly.. Protein Sci. 10.1002/pro.3375
Diver, M. M., Pedi, L., Koide, A., Koide, S., and Long, S. B. (2018) Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT. Nature. 10.1038/nature25439
Dippel, A. B., Olenginski, G. M., Maurici, N., Liskov, M. T., Brewer, S. H., and Phillips-Piro, C. M. (2016) Probing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study. Acta Crystallogr D Struct Biol. 72, 121-30
Dionne, G., Qiu, X., Rapp, M., Liang, X., Zhao, B., Peng, G., Katsamba, P. S., Ahlsen, G., Rubinstein, R., Potter, C. S., Carragher, B., Honig, B., Müller, U., and Shapiro, L. (2018) Mechanotransduction by PCDH15 Relies on a Novel cis-Dimeric Architecture. Neuron. 99, 480-492.e5
Ding, F., Lu, C., Zhao, W., Rajashankar, K. R., Anderson, D. L., Jardine, P. J., Grimes, S., and Ke, A. (2011) Structure and assembly of the essential RNA ring component of a viral DNA packaging motor. Proc Natl Acad Sci U S A. 108, 7357-62
Dimitrova, Y. N., Jenni, S., Valverde, R., Khin, Y., and Harrison, S. C. (2016) Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly. Cell. 167, 1014-1027.e12
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
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
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
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
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
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
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
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
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
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
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
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

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