Publications

Found 1108 results
Filters: First Letter Of Last Name is L  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
C
Everett, B. A., Litzau, L. A., Tompkins, K., Shi, K., Nelson, A., Aihara, H., Iii, R. L. Evans, and Gordon, W. R. (2019) Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 75, 744-749
Lomakin, I. B., Xiong, Y., and Steitz, T. A. (2007) The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell. 129, 319-32
Luo, M., Arentson, B. W., Srivastava, D., Becker, D. F., and Tanner, J. J. (2012) Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry. 51, 10099-108
Lin, D. Yin-wei, Huang, S., and Chen, J. (2015) Crystal structures of a polypeptide processing and secretion transporter. Nature. 523, 425-30
Zhang, Z., Liu, Q., and Hendrickson, W. A. (2014) Crystal structures of apparent saccharide sensors from histidine kinase receptors prevalent in a human gut symbiont. FEBS J. 281, 4263-79
Lei, H. - T., Shen, Z., Surana, P., Routh, M. D., Su, C. - C., Zhang, Q., and Yu, E. W. (2011) Crystal structures of CmeR-bile acid complexes from Campylobacter jejuni. Protein Sci. 20, 712-23
Lei, H. - T., Bolla, J. Reddy, Bishop, N. R., Su, C. - C., and Yu, E. W. (2014) Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation. J Mol Biol. 426, 403-11
Maurici, N., Savidge, N., Lee, B. Uk, Brewer, S. H., and Phillips-Piro, C. M. (2018) Crystal structures of green fluorescent protein with the unnatural amino acid 4-nitro-L-phenylalanine. Acta Crystallogr F Struct Biol Commun. 74, 650-655
Shi, K., Cho, S., Aukema, K. G., Lee, T., Bera, A. K., Seffernick, J. L., Wackett, L. P., and Aihara, H. (2019) Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis. PLoS One. 14, e0216979
Arbing, M. A., Handelman, S. K., Kuzin, A. P., Verdon, G., Wang, C., Su, M., Rothenbacher, F. P., Abashidze, M., Liu, M., Hurley, J. M., Xiao, R., Acton, T., Inouye, M., Montelione, G. T., Woychik, N. A., and Hunt, J. F. (2010) Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure. 18, 996-1010
Long, F., Su, C. - C., Zimmermann, M. T., Boyken, S. E., Rajashankar, K. R., Jernigan, R. L., and Yu, E. W. (2010) Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature. 467, 484-8
Lu, C., Smith, A. M., Fuchs, R. T., Ding, F., Rajashankar, K., Henkin, T. M., and Ke, A. (2008) Crystal structures of the SAM-III/S(MK) riboswitch reveal the SAM-dependent translation inhibition mechanism. Nat Struct Mol Biol. 15, 1076-83
Laganowsky, A., Benesch, J. L. P., Landau, M., Ding, L., Sawaya, M. R., Cascio, D., Huang, Q., Robinson, C. V., Horwitz, J., and Eisenberg, D. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci. 19, 1031-43
Laganowsky, A., Benesch, J. L. P., Landau, M., Ding, L., Sawaya, M. R., Cascio, D., Huang, Q., Robinson, C. V., Horwitz, J., and Eisenberg, D. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci. 19, 1031-43
Huai, Q., Zhou, A., Lin, L., Mazar, A. P., Parry, G. C., Callahan, J., Shaw, D. E., Furie, B., Furie, B. C., and Huang, M. (2008) Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes. Nat Struct Mol Biol. 15, 422-3
Suzuki, T., Miller, C., Guo, L. - T., Ho, J. M. L., Bryson, D. I., Wang, Y. - S., Liu, D. R., and Söll, D. (2017) Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase. Nat Chem Biol. 10.1038/nchembio.2497
Su, C. - C., Long, F., McDermott, G., Shafer, W. M., and Yu, E. W. (2008) Crystallization and preliminary X-ray diffraction analysis of the multidrug efflux transporter NorM from Neisseria gonorrhoeae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 64, 289-92
McLaughlin, M. I., Lanz, N. D., Goldman, P. J., Lee, K. - H., Booker, S. J., and Drennan, C. L. (2016) Crystallographic snapshots of sulfur insertion by lipoyl synthase. Proc Natl Acad Sci U S A. 113, 9446-50
McLaughlin, M. I., Lanz, N. D., Goldman, P. J., Lee, K. - H., Booker, S. J., and Drennan, C. L. (2016) Crystallographic snapshots of sulfur insertion by lipoyl synthase. Proc Natl Acad Sci U S A. 113, 9446-50
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
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
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
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
D
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

Pages