Publications

Found 2725 results
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
H
Hirschi, M., Johnson, Z. Lee, and Lee, S. - Y. (2017) Visualizing multistep elevator-like transitions of a nucleoside transporter. Nature. 545, 66-70
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
Hinshaw, S. M., Makrantoni, V., Harrison, S. C., and Marston, A. L. (2017) The Kinetochore Receptor for the Cohesin Loading Complex. Cell. 171, 72-84.e13
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
Hinshaw, S. M., and Harrison, S. C. (2013) An Iml3-Chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation. Cell Rep. 5, 29-36
Himanen, J. - P., Saha, N., and Nikolov, D. B. (2007) Cell-cell signaling via Eph receptors and ephrins. Curr Opin Cell Biol. 19, 534-42
Himanen, J. P., Goldgur, Y., Miao, H., Myshkin, E., Guo, H., Buck, M., Nguyen, M., Rajashankar, K. R., Wang, B., and Nikolov, D. B. (2009) Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex. EMBO Rep. 10, 722-8
Himanen, J. P., Yermekbayeva, L., Janes, P. W., Walker, J. R., Xu, K., Atapattu, L., Rajashankar, K. R., Mensinga, A., Lackmann, M., Nikolov, D. B., and Dhe-Paganon, S. (2010) Architecture of Eph receptor clusters. Proc Natl Acad Sci U S A. 107, 10860-5
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
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
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
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., and Ealick, S. E. (2016) Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol. 72, 808-16
Hickerson, B. T., Daniels-Wells, T. R., Payes, C., Clark, L. E., Candelaria, P. V., Bailey, K. W., Sefing, E. J., Zink, S., Ziegenbein, J., Abraham, J., Helguera, G., Penichet, M. L., and Gowen, B. B. (2022) Host receptor-targeted therapeutic approach to counter pathogenic New World mammarenavirus infections. Nat Commun. 13, 558
Hibbs, R. E., and Gouaux, E. (2011) Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature. 474, 54-60
Herp, D., Ridinger, J., Robaa, D., Shinsky, S. A., Schmidtkunz, K., Yesiloglu, T. Z., Bayer, T., Steimbach, R. R., Herbst-Gervasoni, C. J., Merz, A., Romier, C., Sehr, P., Gunkel, N., Miller, A. K., Christianson, D. W., Oehme, I., Sippl, W., and Jung, M. (2022) First Fluorescent Acetylspermidine Deacetylation Assay for HDAC10 Identifies Selective Inhibitors with Cellular Target Engagement. Chembiochem. 10.1002/cbic.202200180
Hernandez, A. R., Shao, Y., Hoshika, S., Yang, Z., Shelke, S. A., Herrou, J., Kim, H. - J., Kim, M. - J., Piccirilli, J. A., and Benner, S. A. (2015) A Crystal Structure of a Functional RNA Molecule Containing an Artificial Nucleobase Pair. Angew Chem Int Ed Engl. 54, 9853-6
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
Herbst-Gervasoni, C. J., and Christianson, D. W. (2019) Binding of -Acetylspermidine Analogues to Histone Deacetylase 10 Reveals Molecular Strategies for Blocking Polyamine Deacetylation. Biochemistry. 10.1021/acs.biochem.9b00906
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
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
Henneberg, L. T., Singh, J., Duda, D. M., Baek, K., Yanishevski, D., Murray, P. J., Mann, M., Sidhu, S. S., and Schulman, B. A. (2023) Activity-based profiling of cullin-RING E3 networks by conformation-specific probes. Nat Chem Biol. 19, 1513-1523
Hellman, L. M., Foley, K. C., Singh, N. K., Alonso, J. A., Riley, T. P., Devlin, J. R., Ayres, C. M., Keller, G. L. J., Zhang, Y., Kooi, C. W. Vander, Nishimura, M. I., and Baker, B. M. (2018) Improving T Cell Receptor On-Target Specificity via Structure-Guided Design. Mol Ther. 10.1016/j.ymthe.2018.12.010
Heldwein, E. E., Lou, H., Bender, F. C., Cohen, G. H., Eisenberg, R. J., and Harrison, S. C. (2006) Crystal structure of glycoprotein B from herpes simplex virus 1. Science. 313, 217-20

Pages