Publications

Found 1099 results
Filters: First Letter Of Last Name is B  [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 
T
Lai, R. - Y., Huang, S., Fenwick, M. K., Hazra, A., Zhang, Y., Rajashankar, K., Philmus, B., Kinsland, C., Sanders, J. Mansell, Ealick, S. E., and Begley, T. P. (2012) Thiamin pyrimidine biosynthesis in Candida albicans : a remarkable reaction between histidine and pyridoxal phosphate. J Am Chem Soc. 134, 9157-9
Settembre, E. C., Dorrestein, P. C., Zhai, H., Chatterjee, A., McLafferty, F. W., Begley, T. P., and Ealick, S. E. (2004) Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex. Biochemistry. 43, 11647-57
Greenberg, Z. J., Monlish, D. A., Bartnett, R. L., Yang, Y., Shen, G., Li, W., Bednarski, J. J., and Schuettpelz, L. G. (2020) The Tetraspanin CD53 Regulates Early B Cell Development by Promoting IL-7R Signaling. J Immunol. 204, 58-67
Greenberg, Z. J., Monlish, D. A., Bartnett, R. L., Yang, Y., Shen, G., Li, W., Bednarski, J. J., and Schuettpelz, L. G. (2020) The Tetraspanin CD53 Regulates Early B Cell Development by Promoting IL-7R Signaling. J Immunol. 204, 58-67
Grebien, F., Hantschel, O., Wojcik, J., Kaupe, I., Kovacic, B., Wyrzucki, A. M., Gish, G. D., Cerny-Reiterer, S., Koide, A., Beug, H., Pawson, T., Valent, P., Koide, S., and Superti-Furga, G. (2011) Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis. Cell. 147, 306-19
Sivakumaren, S. Carmen, Shim, H., Zhang, T., Ferguson, F. M., Lundquist, M. R., Browne, C. M., Seo, H. - S., Paddock, M. N., Manz, T. D., Jiang, B., Hao, M. - F., Krishnan, P., Wang, D. G., T Yang, J., Kwiatkowski, N. P., Ficarro, S. B., Cunningham, J. M., Marto, J. A., Dhe-Paganon, S., Cantley, L. C., and Gray, N. S. (2020) Targeting the PI5P4K Lipid Kinase Family in Cancer Using Covalent Inhibitors. Cell Chem Biol. 10.1016/j.chembiol.2020.02.003
Zimanyi, C. M., Ando, N., Brignole, E. J., Asturias, F. J., Stubbe, J. A., and Drennan, C. L. (2012) Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase. Structure. 20, 1374-83
Stafford, R. L., Hinde, E., Knight, M. Jane, Pennella, M. A., Ear, J., Digman, M. A., Gratton, E., and Bowie, J. U. (2011) Tandem SAM domain structure of human Caskin1: a presynaptic, self-assembling scaffold for CASK. Structure. 19, 1826-36
McMillan, B. J., Schnute, B., Ohlenhard, N., Zimmerman, B., Miles, L., Beglova, N., Klein, T., and Blacklow, S. C. (2015) A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. Mol Cell. 57, 912-924
McMillan, B. J., Schnute, B., Ohlenhard, N., Zimmerman, B., Miles, L., Beglova, N., Klein, T., and Blacklow, S. C. (2015) A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. Mol Cell. 57, 912-924
Shi, K., Bohl, T. E., Park, J., Zasada, A., Malik, S., Banerjee, S., Tran, V., Li, N., Yin, Z., Kurniawan, F., Orellana, K., and Aihara, H. (2018) T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction. Nucleic Acids Res. 10.1093/nar/gky776
Shi, K., Bohl, T. E., Park, J., Zasada, A., Malik, S., Banerjee, S., Tran, V., Li, N., Yin, Z., Kurniawan, F., Orellana, K., and Aihara, H. (2018) T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction. Nucleic Acids Res. 10.1093/nar/gky776
S
Zhang, W., Wu, K. - P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., Mukherjee, M., Li, N., Doye, A., Walker, J. R., Sheng, Y., Hao, Z., Li, Y., Brown, K. R., Lemichez, E., Chen, J., Tong, Y., J Harper, W., Moffat, J., Rotin, D., Schulman, B. A., and Sidhu, S. S. (2016) System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes. Mol Cell. 62, 121-36
G Forse, J., Ram, N., D Banatao, R., Cascio, D., Sawaya, M. R., Klock, H. E., Lesley, S. A., and Yeates, T. O. (2011) Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima. Protein Sci. 20, 168-78
Lee, S., Bowman, B. R., Ueno, Y., Wang, S., and Verdine, G. L. (2008) Synthesis and structure of duplex DNA containing the genotoxic nucleobase lesion N7-methylguanine. J Am Chem Soc. 130, 11570-1
Ochoa, J. M., Nguyen, V. N., Nie, M., Sawaya, M. R., Bobik, T. A., and Yeates, T. O. (2020) Symmetry Breaking and Structural Polymorphism in a Bacterial Microcompartment Shell Protein for Choline Utilization. Protein Sci. 10.1002/pro.3941
Windsor, M. A., Hermanson, D. J., Kingsley, P. J., Xu, S., Crews, B. C., Ho, W., Keenan, C. M., Banerjee, S., Sharkey, K. A., and Marnett, L. J. (2012) Substrate-Selective Inhibition of Cyclooxygenase-2: Development and Evaluation of Achiral Profen Probes. ACS Med Chem Lett. 3, 759-763
Rosenberg, O. S., Dovala, D., Li, X., Connolly, L., Bendebury, A., Finer-Moore, J., Holton, J., Cheng, Y., Stroud, R. M., and Cox, J. S. (2015) Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. Cell. 161, 501-512
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Gao, J., Ha, B. Hak, Lou, H. Jane, Morse, E. M., Zhang, R., Calderwood, D. A., Turk, B. E., and Boggon, T. J. (2013) Substrate and inhibitor specificity of the type II p21-activated kinase, PAK6. PLoS One. 8, e77818
Blus, B. J., Hashimoto, H., Seo, H. - S., Krolak, A., and Debler, E. W. (2019) Substrate Affinity and Specificity of the ScSth1p Bromodomain Are Fine-Tuned for Versatile Histone Recognition. Structure. 27, 1460-1468.e3
Shnitsar, V., Li, J., Li, X., Calmettes, C., Basu, A., Casey, J. R., Moraes, T. F., and Reithmeier, R. A. F. (2013) A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters. J Biol Chem. 288, 33848-60
Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., and Christianson, D. W. (2017) Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry. 10.1021/acs.biochem.7b00895
Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., and Christianson, D. W. (2017) Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry. 10.1021/acs.biochem.7b00895
Gallagher-Jones, M., Glynn, C., Boyer, D. R., Martynowycz, M. W., Hernandez, E., Miao, J., Zee, C. - T., Novikova, I. V., Goldschmidt, L., McFarlane, H. T., Helguera, G. F., Evans, J. E., Sawaya, M. R., Cascio, D., Eisenberg, D. S., Gonen, T., and Rodriguez, J. A. (2018) Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.. Nat Struct Mol Biol. 10.1038/s41594-017-0018-0

Pages