Publications

Found 1711 results
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2016
Harrison, O. J., Brasch, J., Lasso, G., Katsamba, P. S., Ahlsen, G., Honig, B., and Shapiro, L. (2016) Structural basis of adhesive binding by desmocollins and desmogleins. Proc Natl Acad Sci U S A. 113, 7160-5
Stein, B. J., Grant, R. A., Sauer, R. T., and Baker, T. A. (2016) Structural Basis of an N-Degron Adaptor with More Stringent Specificity. Structure. 24, 232-42
Goodman, K. Marie, Rubinstein, R., Thu, C. Aye, Bahna, F., Mannepalli, S., Ahlsen, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins.. Neuron. 90, 709-23
Dharmaiah, S., Bindu, L., Tran, T. H., Gillette, W. K., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2016) Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.. Proc Natl Acad Sci U S A. 113, E6766-E6775
Dhindwal, S., Gomez-Gil, L., Neau, D. B., Pham, T. Thanh My, Sylvestre, M., Eltis, L. D., Bolin, J. T., and Kumar, P. (2016) Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase. J Bacteriol. 198, 1499-512
Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54
Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54
Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54
Bradley, T., Fera, D., Bhiman, J., Eslamizar, L., Lu, X., Anasti, K., Zhang, R., Sutherland, L. L., Scearce, R. M., Bowman, C. M., Stolarchuk, C., Lloyd, K. E., Parks, R., Eaton, A., Foulger, A., Nie, X., Karim, S. S. Abdool, Barnett, S., Kelsoe, G., Kepler, T. B., S Alam, M., Montefiori, D. C., M Moody, A., Liao, H. - X., Morris, L., Santra, S., Harrison, S. C., and Haynes, B. F. (2016) Structural Constraints of Vaccine-Induced Tier-2 Autologous HIV Neutralizing Antibodies Targeting the Receptor-Binding Site. Cell Rep. 14, 43-54
Hofmann, L., Tsybovsky, Y., Alexander, N. S., Babino, D., Leung, N. Y., Montell, C., Banerjee, S., von Lintig, J., and Palczewski, K. (2016) Structural Insights into the Drosophila melanogaster Retinol Dehydrogenase, a Member of the Short-Chain Dehydrogenase/Reductase Family. Biochemistry. 55, 6545-6557
Hofmann, L., Tsybovsky, Y., Alexander, N. S., Babino, D., Leung, N. Y., Montell, C., Banerjee, S., von Lintig, J., and Palczewski, K. (2016) Structural Insights into the Drosophila melanogaster Retinol Dehydrogenase, a Member of the Short-Chain Dehydrogenase/Reductase Family. Biochemistry. 55, 6545-6557
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
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
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
Doamekpor, S. K., Lee, J. - W., Hepowit, N. L., Wu, C., Charenton, C., Leonard, M., Bengtson, M. H., Rajashankar, K. R., Sachs, M. S., Lima, C. D., and Joazeiro, C. A. P. (2016) Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits. Proc Natl Acad Sci U S A. 113, E4151-60
Li, H., Hwang, Y., Perry, K., Bushman, F., and Van Duyne, G. D. (2016) Structure and Metal Binding Properties of a Poxvirus Resolvase. J Biol Chem. 291, 11094-104
Li, X., Wang, J., Coutavas, E., Shi, H., Hao, Q., and Blobel, G. (2016) Structure of human Niemann-Pick C1 protein. Proc Natl Acad Sci U S A. 113, 8212-7
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Petrou, V. I., Herrera, C. M., Schultz, K. M., Clarke, O. B., Vendome, J., Tomasek, D., Banerjee, S., Rajashankar, K. R., Dufrisne, M. Belcher, Kloss, B., Kloppmann, E., Rost, B., Klug, C. S., M Trent, S., Shapiro, L., and Mancia, F. (2016) Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science. 351, 608-12
Matthews, M. M., Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., and Beal, P. A. (2016) Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. Nat Struct Mol Biol. 23, 426-33
Zhang, W., Wu, K. - P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., Mukherjee, M., Li, N., Doye, A., Walker, J. R., Sheng, Y., Hao, Z., Li, Y., Brown, K. R., Lemichez, E., Chen, J., Tong, Y., J Harper, W., Moffat, J., Rotin, D., Schulman, B. A., and Sidhu, S. S. (2016) System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes. Mol Cell. 62, 121-36

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