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Ho, M. - C., Sturm, M. B., Almo, S. C., and Schramm, V. L. (2009) Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins. Proc Natl Acad Sci U S A. 106, 20276-81
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
Campbell, A. C., Stiers, K. M., Del Campo, J. S. Martin, Mehra-Chaudhary, R., Sobrado, P., and Tanner, J. J. (2020) Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics. J Biol Chem. 10.1074/jbc.RA120.014750
Bryk, R., Arango, N., Venugopal, A., J Warren, D., Park, Y. - H., Patel, M. S., Lima, C. D., and Nathan, C. (2010) Triazaspirodimethoxybenzoyls as selective inhibitors of mycobacterial lipoamide dehydrogenase . Biochemistry. 49, 1616-27
Tsai, W. - W., Wang, Z., Yiu, T. T., Akdemir, K. C., Xia, W., Winter, S., Tsai, C. - Y., Shi, X., Schwarzer, D., Plunkett, W., Aronow, B., Gozani, O., Fischle, W., Hung, M. - C., Patel, D. J., and Barton, M. Craig (2010) TRIM24 links a non-canonical histone signature to breast cancer. Nature. 468, 927-32
Lou, X., Ma, B., Zhuang, Y., Xiao, X., Minze, L. J., Xing, J., Zhang, Z., and Li, X. C. (2023) TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions. Comput Struct Biotechnol J. 21, 2801-2808
Ye, Q., Rosenberg, S. C., Moeller, A., Speir, J. A., Su, T. Y., and Corbett, K. D. (2015) TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. Elife. 10.7554/eLife.07367
Zhang, H., Pan, Y., Hu, L., M Hudson, A., Hofstetter, K. S., Xu, Z., Rong, M., Wang, Z., Prasad, B. V. Venkatar, Lockless, S. W., Chiu, W., and Zhou, M. (2020) TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential. Nat Commun. 11, 547
Grigg, J. C., Price, I. R., and Ke, A. (2022) tRNA Fusion to Streamline RNA Structure Determination: Case Studies in Probing Aminoacyl-tRNA Sensing Mechanisms by the T-Box Riboswitch. doi:10.3390/cryst12050694
Indurthi, V. S. K., Jensen, J. L., Leclerc, E., Sinha, S., Colbert, C. L., and Vetter, S. W. (2020) The Trp triad within the V-domain of the receptor for advanced glycation end products modulates folding, stability and ligand binding. Biosci Rep. 10.1042/BSR20193360
Chen, J., Zehr, E. A., Gruschus, J. M., Szyk, A., Liu, Y., Tanner, M. E., Tjandra, N., and Roll-Mecak, A. (2024) Tubulin code eraser CCP5 binds branch glutamates by substrate deformation. Nature. 631, 905-912
Golani, L. K., Wallace-Povirk, A., Deis, S. M., Wong, J., Ke, J., Gu, X., Raghavan, S., Wilson, M. R., Li, X., Polin, L., de Waal, P. W., White, K., Kushner, J., O'Connor, C., Hou, Z., H Xu, E., Melcher, K., Dann, C. E., Matherly, L. H., and Gangjee, A. (2016) Tumor Targeting with Novel 6-Substituted Pyrrolo [2,3-d] Pyrimidine Antifolates with Heteroatom Bridge Substitutions via Cellular Uptake by Folate Receptor α and the Proton-Coupled Folate Transporter and Inhibition of de Novo Purine Nucleotide Biosynthes. J Med Chem. 59, 7856-76
Chandrasekaran, S., Schneps, C. M., Dunleavy, R., Lin, C., DeOliveira, C. C., Ganguly, A., and Crane, B. R. (2021) Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome. Commun Biol. 4, 249
Narui, Y., and Sotomayor, M. (2018) Tuning Inner-Ear Tip-Link Affinity Through Alternatively Spliced Variants of Protocadherin-15. Biochemistry. 10.1021/acs.biochem.7b01075
Yee, E. F., Dzikovski, B., and Crane, B. R. (2019) Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping. J Am Chem Soc. 141, 17571-17587
Bassetto, M., Zaluski, J., Li, B., Zhang, J., Badiee, M., Kiser, P. D., and Tochtrop, G. P. (2023) Tuning the Metabolic Stability of Visual Cycle Modulators through Modification of an RPE65 Recognition Motif. J Med Chem. 66, 8140-8158
Tripathi, A., Mandon, E. C., Gilmore, R., and Rapoport, T. A. (2017) Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins. J Biol Chem. 292, 8007-8018
Mishra, A., Devarajan, B., Reardon, M. E., Dwivedi, P., Krishnan, V., Cisar, J. O., Das, A., Narayana, S. V. L., and Ton-That, H. (2011) Two autonomous structural modules in the fimbrial shaft adhesin FimA mediate Actinomyces interactions with streptococci and host cells during oral biofilm development. Mol Microbiol. 81, 1205-20
Mir, A., Chen, J., Robinson, K., Lendy, E., Goodman, J., Neau, D., and Golden, B. L. (2015) Two Divalent Metal Ions and Conformational Changes Play Roles in the Hammerhead Ribozyme Cleavage Reaction. Biochemistry. 54, 6369-81
Lam, K. - H., Perry, K., Shoemaker, C. B., and Jin, R. (2020) Two VHH Antibodies Neutralize Botulinum Neurotoxin E1 by Blocking Its Membrane Translocation in Host Cells. Toxins (Basel). 10.3390/toxins12100616
Unciuleac, M. - C., Goldgur, Y., and Shuman, S. (2017) Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NAD(+)-dependent polynucleotide ligases. Proc Natl Acad Sci U S A. 114, 2592-2597
Ha, B. Hak, Davis, M. J., Chen, C., Lou, H. Jane, Gao, J., Zhang, R., Krauthammer, M., Halaban, R., Schlessinger, J., Turk, B. E., and Boggon, T. J. (2012) Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Proc Natl Acad Sci U S A. 109, 16107-12
Gao, P., Yang, H., Rajashankar, K. R., Huang, Z., and Patel, D. J. (2016) Type V CRISPR-Cas Cpf1 endonuclease employs a unique mechanism for crRNA-mediated target DNA recognition. Cell Res. 26, 901-13
Hitosugi, T., Zhou, L., Fan, J., Elf, S., Zhang, L., Xie, J., Wang, Y., Gu, T. - L., Alečković, M., LeRoy, G., Kang, Y., Kang, H. - B., Seo, J. - H., Shan, C., Jin, P., Gong, W., Lonial, S., Arellano, M. L., Khoury, H. J., Chen, G. Z., Shin, D. M., Khuri, F. R., Boggon, T. J., Kang, S., He, C., and Chen, J. (2013) Tyr26 phosphorylation of PGAM1 provides a metabolic advantage to tumours by stabilizing the active conformation. Nat Commun. 4, 1790

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