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Hao, B., Zheng, N., Schulman, B. A., Wu, G., Miller, J. J., Pagano, M., and Pavletich, N. P. (2005) Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol Cell. 20, 9-19
Hari, S. B., Grant, R. A., and Sauer, R. T. (2018) Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase.. Structure. 10.1016/j.str.2018.06.008
Harris, G. G., Lombardi, P. M., Pemberton, T. A., Matsui, T., Weiss, T. M., Cole, K. E., Köksal, M., Murphy, F. V., L Vedula, S., Chou, W. K. W., Cane, D. E., and Christianson, D. W. (2015) Structural Studies of Geosmin Synthase, a Bifunctional Sesquiterpene Synthase with αα Domain Architecture That Catalyzes a Unique Cyclization-Fragmentation Reaction Sequence.. Biochemistry. 54, 7142-55
Harrison, O. J., Brasch, J., Lasso, G., Katsamba, P. S., Ahlsen, G., Honig, B., and Shapiro, L. (2016) Structural basis of adhesive binding by desmocollins and desmogleins. Proc Natl Acad Sci U S A. 113, 7160-5
Harvey, C. M., O'Toole, K. H., Liu, C., Mariano, P., Dunaway-Mariano, D., and Allen, K. N. (2020) Structural Analysis of Binding Determinants of Trehalose-6-phosphate Phosphatase Using Ground-State Complexes. Biochemistry. 59, 3247-3257
Hashimoto, H., Kafková, L., Raczkowski, A., Jordan, K. D., Read, L. K., and Debler, E. W. (2019) Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme). J Mol Biol. 10.1016/j.jmb.2019.11.002
Hausmann, J., Kamtekar, S., Christodoulou, E., Day, J. E., Wu, T., Fulkerson, Z., Albers, H. M. H. G., van Meeteren, L. A., Houben, A. J. S., van Zeijl, L., Jansen, S., Andries, M., Hall, ii, T., Pegg, L. E., Benson, T. E., Kasiem, M., Harlos, K., Kooi, C. W. Vander, Smyth, S. S., Ovaa, H., Bollen, M., Morris, A. J., Moolenaar, W. H., and Perrakis, A. (2011) Structural basis of substrate discrimination and integrin binding by autotaxin. Nat Struct Mol Biol. 18, 198-204
Hayes, R. P., Xiao, Y., Ding, F., van Erp, P. B. G., Rajashankar, K., Bailey, S., Wiedenheft, B., and Ke, A. (2016) Structural basis for promiscuous PAM recognition in type I-E Cascade from E. coli. Nature. 530, 499-503
He, F., DuPrez, K., Hilario, E., Chen, Z., and Fan, L. (2020) Structural basis of the XPB helicase-Bax1 nuclease complex interacting with the repair bubble DNA. Nucleic Acids Res. 48, 11695-11705
Heppner, D. E., Günther, M., Wittlinger, F., Laufer, S. A., and Eck, M. J. (2020) Structural Basis for EGFR Mutant Inhibition by Trisubstituted Imidazole Inhibitors. J Med Chem. 10.1021/acs.jmedchem.0c00200
Heppner, D. E., Wittlinger, F., Beyett, T. S., Shaurova, T., Urul, D. A., Buckley, B., Pham, C. D., Schaeffner, I. K., Yang, B., Ogboo, B. C., May, E. W., Schaefer, E. M., Eck, M. J., Laufer, S. A., and Hershberger, P. A. (2022) Structural Basis for Inhibition of Mutant EGFR with Lazertinib (YH25448). ACS Med Chem Lett. 13, 1856-1863
Herbst-Gervasoni, C. J., Steimbach, R. R., Morgen, M., Miller, A. K., and Christianson, D. W. (2020) Structural Basis for the Selective Inhibition of HDAC10, the Cytosolic Polyamine Deacetylase. ACS Chem Biol. 10.1021/acschembio.0c00362
Hicks, K. A., Yuen, M. E., Zhen, W. Feng, Gerwig, T. J., Story, R. W., Kopp, M. C., and Snider, M. J. (2016) Structural and Biochemical Characterization of 6-Hydroxynicotinic Acid 3-Monooxygenase, A Novel Decarboxylative Hydroxylase Involved in Aerobic Nicotinate Degradation. Biochemistry. 55, 3432-46
Hicks, K. A., O'Leary, S. E., Begley, T. P., and Ealick, S. E. (2013) Structural and mechanistic studies of HpxO, a novel flavin adenine dinucleotide-dependent urate oxidase from Klebsiella pneumoniae. Biochemistry. 52, 477-87
Higgins, L. J., Yan, F., Liu, P., Liu, H. -wen, and Drennan, C. L. (2005) Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature. 437, 838-44
Hinshaw, S. M., Makrantoni, V., Kerr, A., Marston, A. L., and Harrison, S. C. (2015) Structural evidence for Scc4-dependent localization of cohesin loading. Elife. 4, e06057
Hirano, Y., Gao, Y. - G., Stephenson, D. J., Vu, N. T., Malinina, L., Simanshu, D. K., Chalfant, C. E., Patel, D. J., and Brown, R. E. (2019) Structural basis of phosphatidylcholine recognition by the C2-domain of cytosolic phospholipase Aα.. Elife. 10.7554/eLife.44760
Hirschi, M. Marianne (2017) Structural and Functional Studies of Nucleoside Transporters. Ph.D. thesis, Duke University, Durham, North Carolina
Hlinkova, V., Xing, G., Bauer, J., Shin, Y. Jung, Dionne, I., Rajashankar, K. R., Bell, S. D., and Ling, H. (2008) Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening. Acta Crystallogr D Biol Crystallogr. 64, 941-9
Ho, M. - C., Cassera, M. B., Madrid, D. C., Ting, L. - M., Tyler, P. C., Kim, K., Almo, S. C., and Schramm, V. L. (2009) Structural and metabolic specificity of methylthiocoformycin for malarial adenosine deaminases. Biochemistry. 48, 9618-26
Hochberg, G. K. A., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M. R., Collier, M. P., Stroud, J., Carver, J. A., Baldwin, A. J., Robinson, C. V., Eisenberg, D. S., Benesch, J. L. P., and Laganowsky, A. (2014) The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity.. Proc Natl Acad Sci U S A. 111, E1562-70
Hoelper, D., Huang, H., Jain, A. Y., Patel, D. J., and Lewis, P. W. (2017) Structural and mechanistic insights into ATRX-dependent and -independent functions of the histone chaperone DAXX. Nat Commun. 8, 1193
Hoffer, E. D., Miles, S. J., and Dunham, C. M. (2017) The structure and function of Mycobacterium tuberculosis MazF-mt6 toxin provide insights into conserved features of MazF endonucleases. J Biol Chem. 292, 7718-7726
Hoffer, E., Hong, S., Sunita, S., Maehigashi, T., Gonzalez, R. L., Whitford, P., and Dunham, C. M. (2020) Structural insights into mRNA reading frame regulation by tRNA modification and slippery codon-anticodon pairing. Elife. 10.7554/eLife.51898
Hofmann, L., Tsybovsky, Y., Alexander, N. S., Babino, D., Leung, N. Y., Montell, C., Banerjee, S., von Lintig, J., and Palczewski, K. (2016) Structural Insights into the Drosophila melanogaster Retinol Dehydrogenase, a Member of the Short-Chain Dehydrogenase/Reductase Family. Biochemistry. 55, 6545-6557

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