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Melillo, B., Liang, S., Park, J., Schön, A., Courter, J. R., Lalonde, J. M., Wendler, D. J., Princiotto, A. M., Seaman, M. S., Freire, E., Sodroski, J., Madani, N., Hendrickson, W. A., and Smith, A. B. (2016) Small-Molecule CD4-Mimics: Structure-Based Optimization of HIV-1 Entry Inhibition. ACS Med Chem Lett. 7, 330-4
Minuesa, G., Albanese, S. K., Xie, W., Kazansky, Y., Worroll, D., Chow, A., Schurer, A., Park, S. - M., Rotsides, C. Z., Taggart, J., Rizzi, A., Naden, L. N., Chou, T., Gourkanti, S., Cappel, D., Passarelli, M. C., Fairchild, L., Adura, C., J Glickman, F., Schulman, J., Famulare, C., Patel, M., Eibl, J. K., Ross, G. M., Bhattacharya, S., Tan, D. S., Leslie, C. S., Beuming, T., Patel, D. J., Goldgur, Y., Chodera, J. D., and Kharas, M. G. (2019) Small-molecule targeting of MUSASHI RNA-binding activity in acute myeloid leukemia. Nat Commun. 10, 2691
Oh, Y. - S., Gao, P., Lee, K. - W., Ceglia, I., Seo, J. - S., Zhang, X., Ahn, J. - H., Chait, B. T., Patel, D. J., Kim, Y., and Greengard, P. (2013) SMARCA3, a chromatin-remodeling factor, is required for p11-dependent antidepressant action. Cell. 152, 831-43
Jones, J. C., Banerjee, R., Shi, K., Semonis, M. M., Aihara, H., Pomerantz, W. C. K., and Lipscomb, J. D. (2021) Soluble Methane Monooxygenase Component Interactions Monitored by F NMR. Biochemistry. 60, 1995-2010
Wittenborn, E. C., Guendon, C., Merrouch, M., Benvenuti, M., Fourmond, V., Léger, C., Drennan, C. L., and Dementin, S. (2020) The Solvent-Exposed Fe-S D-Cluster Contributes to Oxygen-Resistance in Ni-Fe Carbon Monoxide Dehydrogenase. ACS Catal. 10, 7328-7335
Vance, T. D. R., Yip, P., Jiménez, E., Li, S., Gawol, D., Byrnes, J., Usón, I., Ziyyat, A., and Lee, J. E. (2022) SPACA6 ectodomain structure reveals a conserved superfamily of gamete fusion-associated proteins. Commun Biol. 5, 984
Vance, T. D. R., Yip, P., Jiménez, E., Li, S., Gawol, D., Byrnes, J., Usón, I., Ziyyat, A., and Lee, J. E. (2022) SPACA6 ectodomain structure reveals a conserved superfamily of gamete fusion-associated proteins. Commun Biol. 5, 984
Di Paolo, J. A., Huang, T., Balazs, M., Barbosa, J., Barck, K. H., Bravo, B. J., Carano, R. A. D., Darrow, J., Davies, D. R., DeForge, L. E., Diehl, L., Ferrando, R., Gallion, S. L., Giannetti, A. M., Gribling, P., Hurez, V., Hymowitz, S. G., Jones, R., Kropf, J. E., Lee, W. P., Maciejewski, P. M., Mitchell, S. A., Rong, H., Staker, B. L., J Whitney, A., Yeh, S., Young, W. B., Yu, C., Zhang, J., Reif, K., and Currie, K. S. (2011) Specific Btk inhibition suppresses B cell- and myeloid cell-mediated arthritis. Nat Chem Biol. 7, 41-50
Shao, Y., Huang, H., Qin, D., Li, N. - S., Koide, A., Staley, J. P., Koide, S., Kossiakoff, A. A., and Piccirilli, J. A. (2016) Specific Recognition of a Single-Stranded RNA Sequence by a Synthetic Antibody Fragment. J Mol Biol. 428, 4100-4114
Liu, H., Wang, C., Lee, S., Ning, F., Wang, Y., Zhang, Q., Chen, Z., Zang, J., Nix, J., Dai, S., Marrack, P., Hagman, J., Kappler, J., and Zhang, G. (2018) Specific Recognition of Arginine Methylated Histone Tails by JMJD5 and JMJD7. Sci Rep. 8, 3275
Liu, H., Wang, C., Lee, S., Ning, F., Wang, Y., Zhang, Q., Chen, Z., Zang, J., Nix, J., Dai, S., Marrack, P., Hagman, J., Kappler, J., and Zhang, G. (2018) Specific Recognition of Arginine Methylated Histone Tails by JMJD5 and JMJD7. Sci Rep. 8, 3275
A Saraswati, P., Relitti, N., Brindisi, M., Osko, J. D., Chemi, G., Federico, S., Grillo, A., Brogi, S., McCabe, N. H., Turkington, R. C., Ibrahim, O., O'Sullivan, J., Lamponi, S., Ghanim, M., Kelly, V. P., Zisterer, D., Amet, R., Barroeta, P. Hannon, Vanni, F., Ulivieri, C., Herp, D., Sarno, F., Di Costanzo, A., Saccoccia, F., Ruberti, G., Jung, M., Altucci, L., Gemma, S., Butini, S., Christianson, D. W., and Campiani, G. (2020) Spiroindoline-Capped Selective HDAC6 Inhibitors: Design, Synthesis, Structural Analysis, and Biological Evaluation. ACS Med Chem Lett. 11, 2268-2276
Shen, G., Li, S., Cui, W., Liu, S., Liu, Q., Yang, Y., Gross, M., and Li, W. (2018) Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. J Thromb Haemost. 16, 1164-1175
Shen, G., Li, S., Cui, W., Liu, S., Liu, Q., Yang, Y., Gross, M., and Li, W. (2018) Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. J Thromb Haemost. 16, 1164-1175
Shen, G., Li, S., Cui, W., Liu, S., Liu, Q., Yang, Y., Gross, M., and Li, W. (2018) Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. J Thromb Haemost. 16, 1164-1175
Shen, G., Li, S., Cui, W., Liu, S., Liu, Q., Yang, Y., Gross, M., and Li, W. (2018) Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. J Thromb Haemost. 16, 1164-1175
Bonsignori, M., Kreider, E. F., Fera, D., R Meyerhoff, R., Bradley, T., Wiehe, K., S Alam, M., Aussedat, B., Walkowicz, W. E., Hwang, K. - K., Saunders, K. O., Zhang, R., Gladden, M. A., Monroe, A., Kumar, A., Xia, S. - M., Cooper, M., Louder, M. K., McKee, K., Bailer, R. T., Pier, B. W., Jette, C. A., Kelsoe, G., Williams, W. B., Morris, L., Kappes, J., Wagh, K., Kamanga, G., Cohen, M. S., Hraber, P. T., Montefiori, D. C., Trama, A., Liao, H. - X., Kepler, T. B., M Moody, A., Gao, F., Danishefsky, S. J., Mascola, J. R., Shaw, G. M., Hahn, B. H., Harrison, S. C., Korber, B. T., and Haynes, B. F. (2017) Staged induction of HIV-1 glycan-dependent broadly neutralizing antibodies. Sci Transl Med. 10.1126/scitranslmed.aai7514
Bonsignori, M., Kreider, E. F., Fera, D., R Meyerhoff, R., Bradley, T., Wiehe, K., S Alam, M., Aussedat, B., Walkowicz, W. E., Hwang, K. - K., Saunders, K. O., Zhang, R., Gladden, M. A., Monroe, A., Kumar, A., Xia, S. - M., Cooper, M., Louder, M. K., McKee, K., Bailer, R. T., Pier, B. W., Jette, C. A., Kelsoe, G., Williams, W. B., Morris, L., Kappes, J., Wagh, K., Kamanga, G., Cohen, M. S., Hraber, P. T., Montefiori, D. C., Trama, A., Liao, H. - X., Kepler, T. B., M Moody, A., Gao, F., Danishefsky, S. J., Mascola, J. R., Shaw, G. M., Hahn, B. H., Harrison, S. C., Korber, B. T., and Haynes, B. F. (2017) Staged induction of HIV-1 glycan-dependent broadly neutralizing antibodies. Sci Transl Med. 10.1126/scitranslmed.aai7514
Morehouse, B. R., Govande, A. A., Millman, A., Keszei, A. F. A., Lowey, B., Ofir, G., Shao, S., Sorek, R., and Kranzusch, P. J. (2020) STING cyclic dinucleotide sensing originated in bacteria. Nature. 10.1038/s41586-020-2719-5
Ernst, A., Avvakumov, G., Tong, J., Fan, Y., Zhao, Y., Alberts, P., Persaud, A., Walker, J. R., Neculai, A. - M., Neculai, D., Vorobyov, A., Garg, P., Beatty, L., Chan, P. - K., Juang, Y. - C., Landry, M. - C., Yeh, C., Zeqiraj, E., Karamboulas, K., Allali-Hassani, A., Vedadi, M., Tyers, M., Moffat, J., Sicheri, F., Pelletier, L., Durocher, D., Raught, B., Rotin, D., Yang, J., Moran, M. F., Dhe-Paganon, S., and Sidhu, S. S. (2013) A strategy for modulation of enzymes in the ubiquitin system. Science. 339, 590-5
Wang, C., Chung, B. C., Yan, H., Wang, H. - G., Lee, S. - Y., and Pitt, G. S. (2014) Structural analyses of Ca²⁺/CaM interaction with NaV channel C-termini reveal mechanisms of calcium-dependent regulation.. Nat Commun. 5, 4896
Phelps, C. B., Huang, R. J., Lishko, P. V., Wang, R. R., and Gaudet, R. (2008) Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels. Biochemistry. 47, 2476-84
Li, L., Fierer, J. O., Rapoport, T. A., and Howarth, M. (2014) Structural analysis and optimization of the covalent association between SpyCatcher and a peptide Tag. J Mol Biol. 426, 309-17
Harvey, C. M., O'Toole, K. H., Liu, C., Mariano, P., Dunaway-Mariano, D., and Allen, K. N. (2020) Structural Analysis of Binding Determinants of Trehalose-6-phosphate Phosphatase Using Ground-State Complexes. Biochemistry. 59, 3247-3257
Aranda, R., Cai, H., Worley, C. E., Levin, E. J., Li, R., Olson, J. S., Phillips, G. N., and Richards, M. P. (2009) Structural analysis of fish versus mammalian hemoglobins: effect of the heme pocket environment on autooxidation and hemin loss. Proteins. 75, 217-30

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