Publications

Found 129 results
Filters: First Letter Of Last Name is H  [Clear All Filters]
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
Hymel, D., Tsuji, K., Grant, R. A., Chingle, R. M., Kunciw, D. L., Yaffe, M. B., and Burke, T. R. (2021) Design and synthesis of a new orthogonally protected glutamic acid analog and its use in the preparation of high affinity polo-like kinase 1 polo-box domain - binding peptide macrocycles. Org Biomol Chem. 19, 7843-7854
Hwang, T., Parker, S. S., Hill, S. M., Grant, R. A., Ilunga, M. W., Sivaraman, V., Mouneimne, G., and Keating, A. E. (2022) Native proline-rich motifs exploit sequence context to target actin-remodeling Ena/VASP protein ENAH. Elife. 10.7554/eLife.70680
Hwang, T., Parker, S. S., Hill, S. M., Ilunga, M. W., Grant, R. A., Mouneimne, G., and Keating, A. E. (2021) A distributed residue network permits conformational binding specificity in a conserved family of actin remodelers. Elife. 10.7554/eLife.70601
Huo, Y., Nam, K. Hyun, Ding, F., Lee, H., Wu, L., Xiao, Y., M Farchione, D., Zhou, S., Rajashankar, K., Kurinov, I., Zhang, R., and Ke, A. (2014) Structures of CRISPR Cas3 offer mechanistic insights into Cascade-activated DNA unwinding and degradation. Nat Struct Mol Biol. 21, 771-7
Hung, K. - W., Chang, Y. - W., Eng, E. T., Chen, J. - H., Chen, Y. - C., Sun, Y. - J., Hsiao, C. - D., Dong, G., Spasov, K. A., Unger, V. M., and Huang, T. - H. (2010) Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB. J Struct Biol. 170, 501-12
Huguenin-Dezot, N., Alonzo, D. A., Heberlig, G. W., Mahesh, M., Nguyen, D. P., Dornan, M. H., Boddy, C. N., T Schmeing, M., and Chin, J. W. (2019) Trapping biosynthetic acyl-enzyme intermediates with encoded 2,3-diaminopropionic acid. Nature. 565, 112-117
Hughes, M. P., Sawaya, M. R., Boyer, D. R., Goldschmidt, L., Rodriguez, J. A., Cascio, D., Chong, L., Gonen, T., and Eisenberg, D. S. (2018) Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks.. Science. 359, 698-701
Huff, S. (2016) Structure-guided Synthesis and Evaluation of Non-nucleoside Reversible, Competitive Inhibitors of Human Ribonucleotide Reductase as Anti-proliferative Agents. Ph.D. thesis, Case Western Reserve University, OhioLINK Electronic Theses and Dissertations Center
Hudson, J. D., Tamilselvan, E., Sotomayor, M., and Cooper, S. R. (2021) A complete Protocadherin-19 ectodomain model for evaluating epilepsy-causing mutations and potential protein interaction sites. Structure. 29, 1128-1143.e4
Hubin, E. A. (2016) Structural and functional studies of mycobacterial general transcription factors RbpA and CarD. Ph.D. thesis, The Rockefeller University, New York City, New York
Hubin, E. A., Lilic, M., Darst, S. A., and Campbell, E. A. (2017) Structural insights into the mycobacteria transcription initiation complex from analysis of X-ray crystal structures. Nat Commun. 8, 16072
Hubin, E. A., Fay, A., Xu, C., Bean, J. M., Saecker, R. M., Glickman, M. S., Darst, S. A., and Campbell, E. A. (2017) Structure and function of the mycobacterial transcription initiation complex with the essential regulator RbpA. Elife. 10.7554/eLife.22520
Huang, H., Levin, E. J., Liu, S., Bai, Y., Lockless, S. W., and Zhou, M. (2014) Structure of a membrane-embedded prenyltransferase homologous to UBIAD1. PLoS Biol. 12, e1001911
Huang, H., Ceccarelli, D. F., Orlicky, S., St-Cyr, D. J., Ziemba, A., Garg, P., Plamondon, S., Auer, M., Sidhu, S., Marinier, A., Kleiger, G., Tyers, M., and Sicheri, F. (2014) E2 enzyme inhibition by stabilization of a low-affinity interface with ubiquitin. Nat Chem Biol. 10, 156-163
Huang, J., Chen, S., J Zhang, J., and Huang, X. - Y. (2013) Crystal structure of oligomeric β1-adrenergic G protein-coupled receptors in ligand-free basal state.. Nat Struct Mol Biol. 20, 419-25
Huang, H., Deng, Z., Vladimirova, O., Wiedmer, A., Lu, F., Lieberman, P. M., and Patel, D. J. (2016) Structural basis underlying viral hijacking of a histone chaperone complex. Nat Commun. 7, 12707
Huang, J., Makabe, K., Biancalana, M., Koide, A., and Koide, S. (2009) Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution. J Mol Biol. 392, 1221-31
Huang, H., Strømme, C. B., Saredi, G., Hödl, M., Strandsby, A., González-Aguilera, C., Chen, S., Groth, A., and Patel, D. J. (2015) A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nat Struct Mol Biol. 22, 618-26
Huang, F., Lu, X., Yu, C., Sliz, P., Wang, L., and Zhu, B. (2021) Molecular Dissection of the Primase and Polymerase Activities of Deep-Sea Phage NrS-1 Primase-Polymerase. Front Microbiol. 12, 766612
Huang, L., Ishibe-Murakami, S., Patel, D. J., and Serganov, A. (2011) Long-range pseudoknot interactions dictate the regulatory response in the tetrahydrofolate riboswitch. Proc Natl Acad Sci U S A. 108, 14801-6
Huang, D. T., Ayrault, O., Hunt, H. W., Taherbhoy, A. M., Duda, D. M., Scott, D. C., Borg, L. A., Neale, G., Murray, P. J., Roussel, M. F., and Schulman, B. A. (2009) E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Mol Cell. 33, 483-95
Huang, P. - T., Summers, B. James, Xu, C., Perilla, J. R., Malikov, V., Naghavi, M. H., and Xiong, Y. (2019) FEZ1 Is Recruited to a Conserved Cofactor Site on Capsid to Promote HIV-1 Trafficking. Cell Rep. 28, 2373-2385.e7
Huang, H., Zeqiraj, E., Dong, B., Jha, B. Kant, Duffy, N. M., Orlicky, S., Thevakumaran, N., Talukdar, M., Pillon, M. C., Ceccarelli, D. F., Wan, L. C. K., Juang, Y. - C., Mao, D. Y. L., Gaughan, C., Brinton, M. A., Perelygin, A. A., Kourinov, I., Guarné, A., Silverman, R. H., and Sicheri, F. (2014) Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity. Mol Cell. 53, 221-34
Huang, H. - T., Seo, H. - S., Zhang, T., Wang, Y., Jiang, B., Li, Q., Buckley, D. L., Nabet, B., Roberts, J. M., Paulk, J., Dastjerdi, S., Winter, G. E., McLauchlan, H., Moran, J., Bradner, J. E., Eck, M. J., Dhe-Paganon, S., Zhao, J. J., and Gray, N. S. (2017) MELK is not necessary for the proliferation of basal-like breast cancer cells. Elife. 10.7554/eLife.26693
Huang, W. Mun, DaGloria, J., Fox, H., Ruan, Q., Tillou, J., Shi, K., Aihara, H., Aron, J., and Casjens, S. (2012) Linear chromosome-generating system of Agrobacterium tumefaciens C58: protelomerase generates and protects hairpin ends. J Biol Chem. 287, 25551-63

Pages