Publications

Found 1344 results
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2016
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
Dowling, D. P., Kung, Y., Croft, A. K., Taghizadeh, K., Kelly, W. L., Walsh, C. T., and Drennan, C. L. (2016) Structural elements of an NRPS cyclization domain and its intermodule docking domain. Proc Natl Acad Sci U S A. 113, 12432-12437
Dowling, D. P., Kung, Y., Croft, A. K., Taghizadeh, K., Kelly, W. L., Walsh, C. T., and Drennan, C. L. (2016) Structural elements of an NRPS cyclization domain and its intermodule docking domain. Proc Natl Acad Sci U S A. 113, 12432-12437
Chung, B. C., Mashalidis, E. H., Tanino, T., Kim, M., Matsuda, A., Hong, J., Ichikawa, S., and Lee, S. - Y. (2016) Structural insights into inhibition of lipid I production in bacterial cell wall synthesis. Nature. 533, 557-560
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
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
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
AhYoung, A. P., Koehl, A., Vizcarra, C. L., Cascio, D., and Egea, P. F. (2016) Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen Plasmodium falciparum. Protein Sci. 25, 689-701
Dimitrova, Y. N., Jenni, S., Valverde, R., Khin, Y., and Harrison, S. C. (2016) Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly. Cell. 167, 1014-1027.e12
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
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
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
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Taabazuing, C. Y., Fermann, J., Garman, S., and Knapp, M. J. (2016) Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.. Biochemistry. 55, 277-86
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
Golani, L. K., Wallace-Povirk, A., Deis, S. M., Wong, J., Ke, J., Gu, X., Raghavan, S., Wilson, M. R., Li, X., Polin, L., de Waal, P. W., White, K., Kushner, J., O'Connor, C., Hou, Z., H Xu, E., Melcher, K., Dann, C. E., Matherly, L. H., and Gangjee, A. (2016) Tumor Targeting with Novel 6-Substituted Pyrrolo [2,3-d] Pyrimidine Antifolates with Heteroatom Bridge Substitutions via Cellular Uptake by Folate Receptor α and the Proton-Coupled Folate Transporter and Inhibition of de Novo Purine Nucleotide Biosynthes. J Med Chem. 59, 7856-76
Golani, L. K., Wallace-Povirk, A., Deis, S. M., Wong, J., Ke, J., Gu, X., Raghavan, S., Wilson, M. R., Li, X., Polin, L., de Waal, P. W., White, K., Kushner, J., O'Connor, C., Hou, Z., H Xu, E., Melcher, K., Dann, C. E., Matherly, L. H., and Gangjee, A. (2016) Tumor Targeting with Novel 6-Substituted Pyrrolo [2,3-d] Pyrimidine Antifolates with Heteroatom Bridge Substitutions via Cellular Uptake by Folate Receptor α and the Proton-Coupled Folate Transporter and Inhibition of de Novo Purine Nucleotide Biosynthes. J Med Chem. 59, 7856-76
Pierson, W. E., Hoffer, E. D., Keedy, H. E., Simms, C. L., Dunham, C. M., and Zaher, H. S. (2016) Uniformity of Peptide Release Is Maintained by Methylation of Release Factors. Cell Rep. 17, 11-8

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