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Found 868 results
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B
Korasick, D. A., Singh, H., Pemberton, T. A., Luo, M., Dhatwalia, R., and Tanner, J. J. (2017) Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J. 10.1111/febs.14165
van Rosenburgh, I. K. van Alde, Lu, D. M., Grant, M. J., Stayrook, S. E., Phadke, M., Walther, Z., Goldberg, S. B., Politi, K., Lemmon, M. A., Ashtekar, K. D., and Tsutsui, Y. (2022) Biochemical and structural basis for differential inhibitor sensitivity of EGFR with distinct exon 19 mutations. Nat Commun. 13, 6791
Winter, J. M., Cascio, D., Dietrich, D., Sato, M., Watanabe, K., Sawaya, M. R., Vederas, J. C., and Tang, Y. (2015) Biochemical and Structural Basis for Controlling Chemical Modularity in Fungal Polyketide Biosynthesis. J Am Chem Soc. 137, 9885-93
Gao, P., Zillinger, T., Wang, W., Ascano, M., Dai, P., Hartmann, G., Tuschl, T., Deng, L., Barchet, W., and Patel, D. J. (2014) Binding-pocket and lid-region substitutions render human STING sensitive to the species-specific drug DMXAA. Cell Rep. 8, 1668-1676
Ilies, M., Di Costanzo, L., Dowling, D. P., Thorn, K. J., and Christianson, D. W. (2011) Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.. J Med Chem. 54, 5432-43
McLaughlin, J. E., Rudolph, M. J., Dutta, A., Li, X. - P., Tsymbal, A. M., Chen, Y., Bhattacharya, S., Algava, B., Goger, M., Roberge, J. Y., and Tumer, N. E. (2025) Binding of small molecules at the P-stalk site of ricin A subunit trigger conformational changes that extend into the active site. J Biol Chem. 10.1016/j.jbc.2025.108310
McLaughlin, J. E., Rudolph, M. J., Dutta, A., Li, X. - P., Tsymbal, A. M., Chen, Y., Bhattacharya, S., Algava, B., Goger, M., Roberge, J. Y., and Tumer, N. E. (2025) Binding of small molecules at the P-stalk site of ricin A subunit trigger conformational changes that extend into the active site. J Biol Chem. 10.1016/j.jbc.2025.108310
An, L., Said, M., Tran, L., Majumder, S., Goreshnik, I., Lee, G. Rie, Juergens, D., Dauparas, J., Anishchenko, I., Coventry, B., Bera, A. K., Kang, A., Levine, P. M., Alvarez, V., Pillai, A., Norn, C., Feldman, D., Zorine, D., Hicks, D. R., Li, X., Sanchez, M. Garcia, Vafeados, D. K., Salveson, P. J., Vorobieva, A. A., and Baker, D. (2024) Binding and sensing diverse small molecules using shape-complementary pseudocycles. Science. 385, 276-282
Seckute, J., McCloskey, D. E., H Thomas, J., Secrist, J. A., Pegg, A. E., and Ealick, S. E. (2011) Binding and inhibition of human spermidine synthase by decarboxylated S-adenosylhomocysteine. Protein Sci. 20, 1836-44
Chen, C. - W., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., Osterman, I. A., Sumbatyan, N. V., and Polikanov, Y. S. (2021) Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome. Antibiotics (Basel). 10.3390/antibiotics10040390
Chen, C. - W., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., Osterman, I. A., Sumbatyan, N. V., and Polikanov, Y. S. (2021) Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome. Antibiotics (Basel). 10.3390/antibiotics10040390
Tereshchenkov, A. G., Dobosz-Bartoszek, M., Osterman, I. A., Marks, J., Sergeeva, V. A., Kasatsky, P., Komarova, E. S., Stavrianidi, A. N., Rodin, I. A., Konevega, A. L., Sergiev, P. V., Sumbatyan, N. V., Mankin, A. S., Bogdanov, A. A., and Polikanov, Y. S. (2018) Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome. J Mol Biol. 10.1016/j.jmb.2018.01.016
Batool, Z., Pavlova, J. A., Paranjpe, M. N., Tereshchenkov, A. G., Lukianov, D. A., Osterman, I. A., Bogdanov, A. A., Sumbatyan, N. V., and Polikanov, Y. S. (2024) Berberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity. Structure. 10.1016/j.str.2024.06.013
Simanshu, D. K., Xu, R., Stice, J. P., Czyzyk, D. J., Feng, S., Denson, J. - P., Riegler, E., Yang, Y., Zhang, C., Donovan, S., Smith, B. P., Abreu-Blanco, M., Chen, M., Feng, C., Fu, L., Rabara, D., Young, L. C., Dyba, M., Yan, W., Lin, K., Ghorbanpoorvalukolaie, S., Larsen, E. K., Malik, W., Champagne, A., Parker, K., Ju, J. Hyun, Jeknic, S., Esposito, D., Turner, D. M., Lightstone, F. C., Wang, B., Wehn, P. M., Wang, K., Stephen, A. G., Maciag, A. E., Hata, A. N., Sinkevicius, K. W., Nissley, D. V., Wallace, E. M., McCormick, F., and Beltran, P. J. (2025) BBO-10203 inhibits tumor growth without inducing hyperglycemia by blocking RAS-PI3Kα interaction.. Science. 10.1126/science.adq2004
Zwe, Y. Htut, Yadav, M., Ten, M. Mei Zhen, Srinivasan, M., Jobichen, C., Sivaraman, J., and Li, D. (2021) Bacterial Antagonism of Chromobacterium haemolyticum and Characterization of its Putative Type VI Secretion System. Res Microbiol. 10.1016/j.resmic.2021.103918
A
Tookmanian, E. M., Phillips-Piro, C. M., Fenlon, E. E., and Brewer, S. H. (2015) Azidoethoxyphenylalanine as a Vibrational Reporter and Click Chemistry Partner in Proteins. Chemistry. 21, 19096-103
Steimbach, R. R., Herbst-Gervasoni, C. J., Lechner, S., Stewart, T. Murray, Klinke, G., Ridinger, J., Géraldy, M. N. E., Tihanyi, G., Foley, J. R., Uhrig, U., Kuster, B., Poschet, G., Casero, R. A., Médard, G., Oehme, I., Christianson, D. W., Gunkel, N., and Miller, A. K. (2022) Aza-SAHA Derivatives Are Selective Histone Deacetylase 10 Chemical Probes That Inhibit Polyamine Deacetylation and Phenocopy HDAC10 Knockout. J Am Chem Soc. 144, 18861-18875
Casanova-Sepúlveda, G., Sexton, J. A., Turk, B. E., and Boggon, T. J. (2023) Autoregulation of the LIM kinases by their PDZ domain. Nat Commun. 14, 8441
G Hobbs, A., Baker, N. M., Miermont, A. M., Thurman, R. D., Pierobon, M., Tran, T. H., Anderson, A. O., Waters, A. M., J Diehl, N., Papke, B., Hodge, R. G., Klomp, J. E., Goodwin, C. M., DeLiberty, J. M., Wang, J., Ng, R. W. S., Gautam, P., Bryant, K. L., Esposito, D., Campbell, S. L., Petricoin, E. F., Simanshu, D. K., Aguirre, A. J., Wolpin, B. M., Wennerberg, K., Rudloff, U., Cox, A. D., and Der, C. J. (2019) Atypical KRASG12R Mutant Is Impaired in PI3K Signaling and Macropinocytosis in Pancreatic Cancer. Cancer Discov. 10.1158/2159-8290.CD-19-1006
G Hobbs, A., Baker, N. M., Miermont, A. M., Thurman, R. D., Pierobon, M., Tran, T. H., Anderson, A. O., Waters, A. M., J Diehl, N., Papke, B., Hodge, R. G., Klomp, J. E., Goodwin, C. M., DeLiberty, J. M., Wang, J., Ng, R. W. S., Gautam, P., Bryant, K. L., Esposito, D., Campbell, S. L., Petricoin, E. F., Simanshu, D. K., Aguirre, A. J., Wolpin, B. M., Wennerberg, K., Rudloff, U., Cox, A. D., and Der, C. J. (2019) Atypical KRASG12R Mutant Is Impaired in PI3K Signaling and Macropinocytosis in Pancreatic Cancer. Cancer Discov. 10.1158/2159-8290.CD-19-1006
Tanaka, S., Kerfeld, C. A., Sawaya, M. R., Cai, F., Heinhorst, S., Cannon, G. C., and Yeates, T. O. (2008) Atomic-level models of the bacterial carboxysome shell. Science. 319, 1083-6
Guenther, E. L., Ge, P., Trinh, H., Sawaya, M. R., Cascio, D., Boyer, D. R., Gonen, T., Z Zhou, H., and Eisenberg, D. S. (2018) Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2. Nat Struct Mol Biol. 10.1038/s41594-018-0045-5
Laganowsky, A., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., Cascio, D., Glabe, C., and Eisenberg, D. (2012) Atomic view of a toxic amyloid small oligomer. Science. 335, 1228-31
Guenther, E. L., Cao, Q., Trinh, H., Lu, J., Sawaya, M. R., Cascio, D., Boyer, D. R., Rodriguez, J. A., Hughes, M. P., and Eisenberg, D. S. (2018) Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. Nat Struct Mol Biol. 10.1038/s41594-018-0064-2
Taherbhoy, A. M., Tait, S. W., Kaiser, S. E., Williams, A. H., Deng, A., Nourse, A., Hammel, M., Kurinov, I., Rock, C. O., Green, D. R., and Schulman, B. A. (2011) Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway. Mol Cell. 44, 451-61

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