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Ruiz, V. G., Czyzyk, D. J., Kumar, V. P., Jorgensen, W. L., and Anderson, K. S. (2020) Targeting the TS dimer interface in bifunctional Cryptosporidium hominis TS-DHFR from parasitic protozoa: Virtual screening identifies novel TS allosteric inhibitors. Bioorg Med Chem Lett. 30, 127292
Chen, M. (2016) Terpene Synthases: One Fold, Many Products. Ph.D. thesis, University of Pennsylvania, Philadelphia, Pennsylvania
Chen, M. (2016) Terpene Synthases: One Fold, Many Products. Ph.D. thesis, University of Pennsylvania, Philadelphia, Pennsylvania
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
Broussard, T. C., Kobe, M. J., Pakhomova, S., Neau, D. B., Price, A. E., Champion, T. S., and Waldrop, G. L. (2013) The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase. Structure. 21, 650-7
Koirala, S., Klein, J., Zheng, Y., Glenn, N. O., Eisemann, T., Tacer, K. Fon, Miller, D. J., Kulak, O., Lu, M., Finkelstein, D. B., Neale, G., Tillman, H., Vogel, P., Strand, D. W., Lum, L., Brautigam, C. A., Pascal, J. M., Clements, W. K., and Potts, P. Ryan (2020) Tissue-Specific Regulation of the Wnt/β-Catenin Pathway by PAGE4 Inhibition of Tankyrase.. Cell Rep. 32, 107922
Soragni, A., Yousefi, S., Stoeckle, C., Soriaga, A. B., Sawaya, M. R., Kozlowski, E., Schmid, I., Radonjic-Hoesli, S., Boutet, S., Williams, G. J., Messerschmidt, M., M Seibert, M., Cascio, D., Zatsepin, N. A., Burghammer, M., Riekel, C., Colletier, J. - P., Riek, R., Eisenberg, D. S., and Simon, H. - U. (2015) Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation. Mol Cell. 57, 1011-21
Soragni, A., Yousefi, S., Stoeckle, C., Soriaga, A. B., Sawaya, M. R., Kozlowski, E., Schmid, I., Radonjic-Hoesli, S., Boutet, S., Williams, G. J., Messerschmidt, M., M Seibert, M., Cascio, D., Zatsepin, N. A., Burghammer, M., Riekel, C., Colletier, J. - P., Riek, R., Eisenberg, D. S., and Simon, H. - U. (2015) Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation. Mol Cell. 57, 1011-21
Chatterjee, D., Sanchez, A. M., Goldgur, Y., Shuman, S., and Schwer, B. (2016) Transcription of lncRNA prt, clustered prt RNA sites for Mmi1 binding, and RNA polymerase II CTD phospho-sites govern the repression of pho1 gene expression under phosphate-replete conditions in fission yeast. RNA. 22, 1011-25
Le Thomas, A., Stuwe, E., Li, S., Du, J., Marinov, G., Rozhkov, N., Chen, Y. - C. Ariel, Luo, Y., Sachidanandam, R., Toth, K. Fejes, Patel, D., and Aravin, A. A. (2014) Transgenerationally inherited piRNAs trigger piRNA biogenesis by changing the chromatin of piRNA clusters and inducing precursor processing. Genes Dev. 28, 1667-80
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
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
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
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
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
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
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
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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