Publications

Found 2855 results
Journal Article
Sukumar, N. (2013) Crystallographic studies on B12 binding proteins in eukaryotes and prokaryotes. Biochimie. 95, 976-88
Ryan, K. S., Howard-Jones, A. R., Hamill, M. J., Elliott, S. J., Walsh, C. T., and Drennan, C. L. (2007) Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC. Proc Natl Acad Sci U S A. 104, 15311-6
Jurgenson, C. T., and Pollard, T. D. (2015) Crystals of the Arp2/3 complex in two new space groups with structural information about actin-related protein 2 and potential WASP binding sites. Acta Crystallogr F Struct Biol Commun. 71, 1161-8
Brown, S., Gauvin, C. C., Charbonneau, A. A., Burman, N., and C Lawrence, M. (2020) Csx3 is a cyclic oligonucleotide phosphodiesterase associated with type III CRISPR-Cas that degrades the second messenger cA. J Biol Chem. 295, 14963-14972
Righetto, G. Lima, Sriranganadane, D., Halabelian, L., Chiodi, C. G., Elkins, J. M., Massirer, K. B., Gileadi, O., Menossi, M., and Couñago, R. M. (2019) The C-Terminal Domains SnRK2 Box and ABA Box Have a Role in Sugarcane SnRK2s Auto-Activation and Activity. Front Plant Sci. 10, 1105
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
Guagnini, F., Antonik, P. M., Rennie, M. L., O'Byrne, P., Khan, A. R., Pinalli, R., Dalcanale, E., and Crowley, P. B. (2018) Cucurbit[7]uril-Dimethyllysine Recognition in a Model Protein. Angew Chem Int Ed Engl. 10.1002/anie.201803232
Su, C. - C., Long, F., and Yu, E. W. (2011) The Cus efflux system removes toxic ions via a methionine shuttle. Protein Sci. 20, 6-18
Tal, N., Morehouse, B. R., Millman, A., Stokar-Avihail, A., Avraham, C., Fedorenko, T., Yirmiya, E., Herbst, E., Brandis, A., Mehlman, T., Oppenheimer-Shaanan, Y., Keszei, A. F. A., Shao, S., Amitai, G., Kranzusch, P. J., and Sorek, R. (2021) Cyclic CMP and cyclic UMP mediate bacterial immunity against phages. Cell. 184, 5728-5739.e16
Gao, P., Ascano, M., Wu, Y., Barchet, W., Gaffney, B. L., Zillinger, T., Serganov, A. A., Liu, Y., Jones, R. A., Hartmann, G., Tuschl, T., and Patel, D. J. (2013) Cyclic [G(2',5')pA(3',5')p] is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase. Cell. 153, 1094-107
Rettie, S. A., Campbell, K. V., Bera, A. K., Kang, A., Kozlov, S., De La Cruz, J., Adebomi, V., Zhou, G., DiMaio, F., Ovchinnikov, S., and Bhardwaj, G. (2023) Cyclic peptide structure prediction and design using AlphaFold. bioRxiv. 10.1101/2023.02.25.529956
Li, Y., Wei, Y., Ultsch, M., Li, W., Tang, W., Tombling, B., Gao, X., Dimitrova, Y., Gampe, C., Fuhrmann, J., Zhang, Y., Hannoush, R. N., and Kirchhofer, D. (2024) Cystine-knot peptide inhibitors of HTRA1 bind to a cryptic pocket within the active site region. Nat Commun. 15, 4359
Randau, L., Stanley, B. J., Kohlway, A., Mechta, S., Xiong, Y., and Söll, D. (2009) A cytidine deaminase edits C to U in transfer RNAs in Archaea. Science. 324, 657-9
Bollmeyer, M. M., Coleman, R. E., Majer, S. H., Ferrao, S. D., and Lancaster, K. M. (2023) Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification. J Am Chem Soc. 145, 14404-14416
Tayeb-Fligelman, E., Tabachnikov, O., Moshe, A., Goldshmidt-Tran, O., Sawaya, M. R., Coquelle, N., Colletier, J. - P., and Landau, M. (2017) The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-α amyloid-like fibril.. Science. 355, 831-833
Rajashankar, K., and Dauter, Z. (2014) Data collection for crystallographic structure determination. Methods Mol Biol. 1140, 211-37
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Elsässer, S. J., Huang, H., Lewis, P. W., Chin, J. W., C Allis, D., and Patel, D. J. (2012) DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. Nature. 491, 560-5
Kurz, T., Chou, Y. - C., Willems, A. R., Meyer-Schaller, N., Hecht, M. - L., Tyers, M., Peter, M., and Sicheri, F. (2008) Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation. Mol Cell. 29, 23-35
Joh, N. H., Wang, T., Bhate, M. P., Acharya, R., Wu, Y., Grabe, M., Hong, M., Grigoryan, G., and DeGrado, W. F. (2014) De novo design of a transmembrane Zn²⁺-transporting four-helix bundle.. Science. 346, 1520-4
Torres, S. Vázquez, J Y Leung, P., Venkatesh, P., Lutz, I. D., Hink, F., Huynh, H. - H., Becker, J., Yeh, A. Hsien- Wei, Juergens, D., Bennett, N. R., Hoofnagle, A. N., Huang, E., MacCoss, M. J., Expòsit, M., Lee, G. Rie, Bera, A. K., Kang, A., De La Cruz, J., Levine, P. M., Li, X., Lamb, M., Gerben, S. R., Murray, A., Heine, P., Korkmaz, E. Nihal, Nivala, J., Stewart, L., Watson, J. L., Rogers, J. M., and Baker, D. (2023) De novo design of high-affinity binders of bioactive helical peptides. Nature. 10.1038/s41586-023-06953-1
Kim, D. E., Jensen, D. R., Feldman, D., Tischer, D., Saleem, A., Chow, C. M., Li, X., Carter, L., Milles, L., Nguyen, H., Kang, A., Bera, A. K., Peterson, F. C., Volkman, B. F., Ovchinnikov, S., and Baker, D. (2023) De novo design of small beta barrel proteins. Proc Natl Acad Sci U S A. 120, e2207974120
Vorobieva, A. A., White, P., Liang, B., Horne, J. E., Bera, A. K., Chow, C. M., Gerben, S., Marx, S., Kang, A., Stiving, A. Q., Harvey, S. R., Marx, D. C., G Khan, N., Fleming, K. G., Wysocki, V. H., Brockwell, D. J., Tamm, L. K., Radford, S. E., and Baker, D. (2021) De novo design of transmembrane β barrels.. Science. 10.1126/science.abc8182
de Haas, R. J., Tas, R. P., van den Broek, D., Zheng, C., Nguyen, H., Kang, A., Bera, A. K., King, N. P., Voets, I. K., and de Vries, R. (2023) De novo designed ice-binding proteins from twist-constrained helices. Proc Natl Acad Sci U S A. 120, e2220380120
Torres, S. Vázquez, Valle, M. Benard, Mackessy, S. P., Menzies, S. K., Casewell, N. R., Ahmadi, S., Burlet, N. J., Muratspahić, E., Sappington, I., Overath, M. D., Rivera-de-Torre, E., Ledergerber, J., Laustsen, A. H., Boddum, K., Bera, A. K., Kang, A., Brackenbrough, E., Cardoso, I. A., Crittenden, E. P., Edge, R. J., Decarreau, J., Ragotte, R. J., Pillai, A. S., Abedi, M., Han, H. L., Gerben, S. R., Murray, A., Skotheim, R., Stuart, L., Stewart, L., Fryer, T. J. A., Jenkins, T. P., and Baker, D. (2025) De novo designed proteins neutralize lethal snake venom toxins. Nature. 10.1038/s41586-024-08393-x

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