Publications

Found 1682 results
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2014
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
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
Feld, G. K., El-Etr, S., Corzett, M. H., Hunter, M. S., Belhocine, K., Monack, D. M., Frank, M., Segelke, B. W., and Rasley, A. (2014) Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host cell invasion. J Biol Chem. 289, 30668-30679
Yang, T., Liu, Q., Kloss, B., Bruni, R., Kalathur, R. C., Guo, Y., Kloppmann, E., Rost, B., Colecraft, H. M., and Hendrickson, W. A. (2014) Structure and selectivity in bestrophin ion channels. Science. 346, 355-9
Strunk, R. J., Piemonte, K. M., Petersen, N. M., Koutsioulis, D., Bouriotis, V., Perry, K., and Cole, K. E. (2014) Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis. Acta Crystallogr F Struct Biol Commun. 70, 156-9
Thompson, M. C., Crowley, C. S., Kopstein, J., Bobik, T. A., and Yeates, T. O. (2014) Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor. Acta Crystallogr F Struct Biol Commun. 70, 1584-90
Huang, H., Levin, E. J., Liu, S., Bai, Y., Lockless, S. W., and Zhou, M. (2014) Structure of a membrane-embedded prenyltransferase homologous to UBIAD1. PLoS Biol. 12, e1001911
McNamara, D. E., Cascio, D., Jorda, J., Bustos, C., Wang, T. - C., Rasche, M. E., Yeates, T. O., and Bobik, T. A. (2014) Structure of dihydromethanopterin reductase, a cubic protein cage for redox transfer. J Biol Chem. 289, 8852-64
McNamara, D. E., Cascio, D., Jorda, J., Bustos, C., Wang, T. - C., Rasche, M. E., Yeates, T. O., and Bobik, T. A. (2014) Structure of dihydromethanopterin reductase, a cubic protein cage for redox transfer. J Biol Chem. 289, 8852-64
Kobe, M. J., Neau, D. B., Mitchell, C. E., Bartlett, S. G., and Newcomer, M. E. (2014) The structure of human 15-lipoxygenase-2 with a substrate mimic. J Biol Chem. 289, 8562-9
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
Liu, Z., Frutos, S., Bick, M. J., Vila-Perelló, M., Debelouchina, G. T., Darst, S. A., and Muir, T. W. (2014) Structure of the branched intermediate in protein splicing. Proc Natl Acad Sci U S A. 111, 8422-7
Bobik, T. A., Morales, E. J., Shin, A., Cascio, D., Sawaya, M. R., Arbing, M., Yeates, T. O., and Rasche, M. E. (2014) Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii. Acta Crystallogr F Struct Biol Commun. 70, 1472-9
Lou, X., Toresson, G., Benod, C., Suh, J. Ho, Philips, K. J., Webb, P., and Gustafsson, J. - Å. (2014) Structure of the retinoid X receptor α-liver X receptor β (RXRα-LXRβ) heterodimer on DNA.. Nat Struct Mol Biol. 21, 277-81
Hochberg, G. K. A., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M. R., Collier, M. P., Stroud, J., Carver, J. A., Baldwin, A. J., Robinson, C. V., Eisenberg, D. S., Benesch, J. L. P., and Laganowsky, A. (2014) The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity.. Proc Natl Acad Sci U S A. 111, E1562-70
Hochberg, G. K. A., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M. R., Collier, M. P., Stroud, J., Carver, J. A., Baldwin, A. J., Robinson, C. V., Eisenberg, D. S., Benesch, J. L. P., and Laganowsky, A. (2014) The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity.. Proc Natl Acad Sci U S A. 111, E1562-70
Singh, H., Arentson, B. W., Becker, D. F., and Tanner, J. J. (2014) Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci U S A. 111, 3389-94
Quan, B., Seo, H. - S., Blobel, G., and Ren, Y. (2014) Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1 • Nup98).. Proc Natl Acad Sci U S A. 111, 9127-32
Han, S., Le, B. V., Hajare, H. S., Baxter, R. H. G., and Miller, S. J. (2014) X-ray crystal structure of teicoplanin A₂-2 bound to a catalytic peptide sequence via the carrier protein strategy.. J Org Chem. 79, 8550-6
Althoff, T., Hibbs, R. E., Banerjee, S., and Gouaux, E. (2014) X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature. 512, 333-7
2013
Soriano, E. V., Zhang, Y., Colabroy, K. L., Sanders, J. M., Settembre, E. C., Dorrestein, P. C., Begley, T. P., and Ealick, S. E. (2013) Active-site models for complexes of quinolinate synthase with substrates and intermediates. Acta Crystallogr D Biol Crystallogr. 69, 1685-96
Yildiz, M., Ghosh, S., Bell, J. A., Sherman, W., and Hardy, J. A. (2013) Allosteric inhibition of the NS2B-NS3 protease from dengue virus. ACS Chem Biol. 8, 2744-52
Xia, S., Wood, M., Bradley, M. J., De La Cruz, E. M., and Konigsberg, W. H. (2013) Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Res. 41, 9077-89
Demirci, H., Wang, L., Murphy, F. V., Murphy, E. L., Carr, J. F., Blanchard, S. C., Jogl, G., Dahlberg, A. E., and Gregory, S. T. (2013) The central role of protein S12 in organizing the structure of the decoding site of the ribosome. RNA. 19, 1791-801
Xu, K., Rockx, B., Xie, Y., DeBuysscher, B. L., Fusco, D. L., Zhu, Z., Chan, Y. - P., Xu, Y., Luu, T., Cer, R. Z., Feldmann, H., Mokashi, V., Dimitrov, D. S., Bishop-Lilly, K. A., Broder, C. C., and Nikolov, D. B. (2013) Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody. PLoS Pathog. 9, e1003684

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