Publications

Found 1110 results
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Brown, J. A., Bulkley, D., Wang, J., Valenstein, M. L., Yario, T. A., Steitz, T. A., and Steitz, J. A. (2014) Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nat Struct Mol Biol. 21, 633-40
Geng, Y., Mosyak, L., Kurinov, I., Zuo, H., Sturchler, E., Cheng, T. Cheung, Subramanyam, P., Brown, A. P., Brennan, S. C., Mun, H. - C., Bush, M., Chen, Y., Nguyen, T. X., Cao, B., Chang, D. D., Quick, M., Conigrave, A. D., Colecraft, H. M., McDonald, P., and Fan, Q. R. (2016) Structural mechanism of ligand activation in human calcium-sensing receptor. Elife. 10.7554/eLife.13662
Geng, Y., Mosyak, L., Kurinov, I., Zuo, H., Sturchler, E., Cheng, T. Cheung, Subramanyam, P., Brown, A. P., Brennan, S. C., Mun, H. - C., Bush, M., Chen, Y., Nguyen, T. X., Cao, B., Chang, D. D., Quick, M., Conigrave, A. D., Colecraft, H. M., McDonald, P., and Fan, Q. R. (2016) Structural mechanism of ligand activation in human calcium-sensing receptor. Elife. 10.7554/eLife.13662
Geng, Y., Mosyak, L., Kurinov, I., Zuo, H., Sturchler, E., Cheng, T. Cheung, Subramanyam, P., Brown, A. P., Brennan, S. C., Mun, H. - C., Bush, M., Chen, Y., Nguyen, T. X., Cao, B., Chang, D. D., Quick, M., Conigrave, A. D., Colecraft, H. M., McDonald, P., and Fan, Q. R. (2016) Structural mechanism of ligand activation in human calcium-sensing receptor. Elife. 10.7554/eLife.13662
Geng, Y., Bush, M., Mosyak, L., Wang, F., and Fan, Q. R. (2013) Structural mechanism of ligand activation in human GABA(B) receptor. Nature. 504, 254-9
Kirouac, K. N., Basu, A. K., and Ling, H. (2013) Structural mechanism of replication stalling on a bulky amino-polycyclic aromatic hydrocarbon DNA adduct by a y family DNA polymerase. J Mol Biol. 425, 4167-76
Braffman, N. R., Piscotta, F. J., Hauver, J., Campbell, E. A., A Link, J., and Darst, S. A. (2019) Structural mechanism of transcription inhibition by lasso peptides microcin J25 and capistruin. Proc Natl Acad Sci U S A. 116, 1273-1278
Baconguis, I., and Gouaux, E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature. 489, 400-5
Soriano, E. V., Rajashankar, K. R., Hanes, J. W., Bale, S., Begley, T. P., and Ealick, S. E. (2008) Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor. Biochemistry. 47, 1346-57
Soriano, E. V., Rajashankar, K. R., Hanes, J. W., Bale, S., Begley, T. P., and Ealick, S. E. (2008) Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor. Biochemistry. 47, 1346-57
Fisher, O. S., Zhang, R., Li, X., Murphy, J. W., Demeler, B., and Boggon, T. J. (2013) Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. FEBS Lett. 587, 272-7
Jones, J. Christophe, Banerjee, R., Shi, K., Aihara, H., and Lipscomb, J. D. (2020) Structural Studies of OB3b Soluble Methane Monooxygenase Hydroxylase and Regulatory Component Complex Reveal a Transient Substrate Tunnel. Biochemistry. 10.1021/acs.biochem.0c00459
McCulloch, K. M., Kinsland, C., Begley, T. P., and Ealick, S. E. (2008) Structural studies of thiamin monophosphate kinase in complex with substrates and products. Biochemistry. 47, 3810-21
Pemberton, T. A., Srivastava, D., Sanyal, N., Henzl, M. T., Becker, D. F., and Tanner, J. J. (2014) Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state.. Biochemistry. 53, 1350-9
Zhang, Y., Colabroy, K. L., Begley, T. P., and Ealick, S. E. (2005) Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry. 44, 7632-43
Dhakshnamoorthy, B., Ziervogel, B. K., Blachowicz, L., and Roux, B. (2013) A structural study of ion permeation in OmpF porin from anomalous X-ray diffraction and molecular dynamics simulations. J Am Chem Soc. 135, 16561-8
Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Barton, W. A., Liu, B. P., Tzvetkova, D., Jeffrey, P. D., Fournier, A. E., Sah, D., Cate, R., Strittmatter, S. M., and Nikolov, D. B. (2003) Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins. EMBO J. 22, 3291-302
Montemayor, E. J., Didychuk, A. L., Liao, H., Hu, P., Brow, D. A., and Butcher, S. E. (2017) Structure and conformational plasticity of the U6 small nuclear ribonucleoprotein core. Acta Crystallogr D Struct Biol. 73, 1-8
Montemayor, E. J., Didychuk, A. L., Liao, H., Hu, P., Brow, D. A., and Butcher, S. E. (2017) Structure and conformational plasticity of the U6 small nuclear ribonucleoprotein core. Acta Crystallogr D Struct Biol. 73, 1-8
Pascolutti, R., Sun, X., Kao, J., Maute, R. L., Ring, A. M., Bowman, G. R., and Kruse, A. C. (2016) Structure and Dynamics of PD-L1 and an Ultra-High-Affinity PD-1 Receptor Mutant. Structure. 24, 1719-1728
Kono, A., Chou, T. - H., Radhakrishnan, A., Bolla, J. Reddy, Sankar, K., Shome, S., Su, C. - C., Jernigan, R. L., Robinson, C. V., Yu, E. W., and Spalding, M. H. (2020) Structure and Function of LCI1: A plasma membrane CO channel in the Chlamydomonas CO concentrating mechanism. Plant J. 10.1111/tpj.14745
Su, C. - C., Bolla, J. Reddy, Kumar, N., Radhakrishnan, A., Long, F., Delmar, J. A., Chou, T. - H., Rajashankar, K. R., Shafer, W. M., and Yu, E. W. (2015) Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps. Cell Rep. 11, 61-70
Zheng, J., Sagar, V., Smolinsky, A., Bourke, C., LaRonde-LeBlanc, N., and T Cropp, A. (2009) Structure and function of the macrolide biosensor protein, MphR(A), with and without erythromycin. J Mol Biol. 387, 1250-60

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