Publications

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Cook, J. D., Sultana, A., and Lee, J. E. (2017) Structure of the infectious salmon anemia virus receptor complex illustrates a unique binding strategy for attachment. Proc Natl Acad Sci U S A. 114, E2929-E2936
Chen, B., Liu, Z., Perry, K., and Jin, R. (2022) Structure of the glucosyltransferase domain of TcdA in complex with RhoA provides insights into substrate recognition. Sci Rep. 12, 9028
Cheung, J., Mahmood, A., Kalathur, R., Liu, L., and Carlier, P. R. (2018) Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance. Structure. 26, 130-136.e2
Cheung, J., Mahmood, A., Kalathur, R., Liu, L., and Carlier, P. R. (2018) Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance. Structure. 26, 130-136.e2
Chen, P., Lam, K. - H., Liu, Z., Mindlin, F. A., Chen, B., Gutierrez, C. B., Huang, L., Zhang, Y., Hamza, T., Feng, H., Matsui, T., Bowen, M. E., Perry, K., and Jin, R. (2019) Structure of the full-length Clostridium difficile toxin B. Nat Struct Mol Biol. 10.1038/s41594-019-0268-0
Chen, P., Lam, K. - H., Liu, Z., Mindlin, F. A., Chen, B., Gutierrez, C. B., Huang, L., Zhang, Y., Hamza, T., Feng, H., Matsui, T., Bowen, M. E., Perry, K., and Jin, R. (2019) Structure of the full-length Clostridium difficile toxin B. Nat Struct Mol Biol. 10.1038/s41594-019-0268-0
Papadopoulos, E., Jenni, S., Kabha, E., Takrouri, K. J., Yi, T., Salvi, N., Luna, R. E., Gavathiotis, E., Mahalingam, P., Arthanari, H., Rodriguez-Mias, R., Yefidoff-Freedman, R., Aktas, B. H., Chorev, M., Halperin, J. A., and Wagner, G. (2014) Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G. Proc Natl Acad Sci U S A. 111, E3187-95
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nat Microbiol. 1, 16154
Cho, J., Lee, C. - J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis. Nature Microbiology. 10.1038/nmicrobiol.2016.154
Chitrakar, I., Ahmed, S. Fardin, Torelli, A. T., and French, J. B. (2021) Structure of the E. coli agmatinase, SPEB. PLoS One. 16, e0248991
Senturia, R., Faller, M., Yin, S., Loo, J. A., Cascio, D., Sawaya, M. R., Hwang, D., Clubb, R. T., and Guo, F. (2010) Structure of the dimerization domain of DiGeorge critical region 8. Protein Sci. 19, 1354-65
Senturia, R., Faller, M., Yin, S., Loo, J. A., Cascio, D., Sawaya, M. R., Hwang, D., Clubb, R. T., and Guo, F. (2010) Structure of the dimerization domain of DiGeorge critical region 8. Protein Sci. 19, 1354-65
Economou, N. J., Zentner, I. J., Lazo, E., Jakoncic, J., Stojanoff, V., Weeks, S. D., Grasty, K. C., Cocklin, S., and Loll, P. J. (2013) Structure of the complex between teicoplanin and a bacterial cell-wall peptide: use of a carrier-protein approach. Acta Crystallogr D Biol Crystallogr. 69, 520-33
Mahoney, B. J., Takayesu, A., Zhou, A., Cascio, D., and Clubb, R. T. (2022) The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing. Proteins. 10.1002/prot.26326
Mahoney, B. J., Takayesu, A., Zhou, A., Cascio, D., and Clubb, R. T. (2022) The structure of the Clostridium thermocellum RsgI9 ectodomain provides insight into the mechanism of biomass sensing. Proteins. 10.1002/prot.26326
Galaleldeen, A., Taylor, A. B., Chen, D., Schuermann, J. P., Holloway, S. P., Hou, S., Gong, S., Zhong, G., and P Hart, J. (2013) Structure of the Chlamydia trachomatis immunodominant antigen Pgp3. J Biol Chem. 288, 22068-79
Corbett, K. D., and Berger, J. M. (2010) Structure of the ATP-binding domain of Plasmodium falciparum Hsp90. Proteins. 78, 2738-44
Reha-Krantz, L. J., Hariharan, C., Subuddhi, U., Xia, S., Zhao, C., Beckman, J., Christian, T., and Konigsberg, W. (2011) Structure of the 2-aminopurine-cytosine base pair formed in the polymerase active site of the RB69 Y567A-DNA polymerase. Biochemistry. 50, 10136-49
Jiang, J., Chan, H., Cash, D. D., Miracco, E. J., Loo, R. R. Ogorzale, Upton, H. E., Cascio, D., Johnson, R. O. 'Brien, Collins, K., Loo, J. A., Z Zhou, H., and Feigon, J. (2015) Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions. Science. 350, aab4070
Jiang, J., Chan, H., Cash, D. D., Miracco, E. J., Loo, R. R. Ogorzale, Upton, H. E., Cascio, D., Johnson, R. O. 'Brien, Collins, K., Loo, J. A., Z Zhou, H., and Feigon, J. (2015) Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions. Science. 350, aab4070
Jiang, J., Chan, H., Cash, D. D., Miracco, E. J., Loo, R. R. Ogorzale, Upton, H. E., Cascio, D., Johnson, R. O. 'Brien, Collins, K., Loo, J. A., Z Zhou, H., and Feigon, J. (2015) Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions. Science. 350, aab4070
Jiang, J., Chan, H., Cash, D. D., Miracco, E. J., Loo, R. R. Ogorzale, Upton, H. E., Cascio, D., Johnson, R. O. 'Brien, Collins, K., Loo, J. A., Z Zhou, H., and Feigon, J. (2015) Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions. Science. 350, aab4070
Basu, R., Eichhorn, C. D., Cheng, R., Peterson, R. D., and Feigon, J. (2020) Structure of telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins. RNA Biol. 10.1080/15476286.2020.1836891
Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9
Blank, P. N., Shinsky, S. A., and Christianson, D. W. (2019) Structure of Sesquisabinene Synthase 1, a Terpenoid Cyclase That Generates a Strained [3.1.0] Bridged-Bicyclic Product. ACS Chem Biol. 10.1021/acschembio.9b00218

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