Publications

Found 2720 results
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2018
Lee, S., Choi, J., Mohanty, J., Sousa, L. P., Tome, F., Pardon, E., Steyaert, J., Lemmon, M. A., Lax, I., and Schlessinger, J. (2018) Structures of β-klotho reveal a 'zip code'-like mechanism for endocrine FGF signalling.. Nature. 10.1038/nature25010
Gallagher-Jones, M., Glynn, C., Boyer, D. R., Martynowycz, M. W., Hernandez, E., Miao, J., Zee, C. - T., Novikova, I. V., Goldschmidt, L., McFarlane, H. T., Helguera, G. F., Evans, J. E., Sawaya, M. R., Cascio, D., Eisenberg, D. S., Gonen, T., and Rodriguez, J. A. (2018) Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.. Nat Struct Mol Biol. 10.1038/s41594-017-0018-0
Schaefer, K., Owens, T. W., Kahne, D., and Walker, S. (2018) Substrate Preferences Establish the Order of Cell Wall Assembly in Staphylococcus aureus. J Am Chem Soc. 140, 2442-2445
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Shi, K., Bohl, T. E., Park, J., Zasada, A., Malik, S., Banerjee, S., Tran, V., Li, N., Yin, Z., Kurniawan, F., Orellana, K., and Aihara, H. (2018) T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction. Nucleic Acids Res. 10.1093/nar/gky776
Gulati, S., Jin, H., Masuho, I., Orban, T., Cai, Y., Pardon, E., Martemyanov, K. A., Kiser, P. D., Stewart, P. L., Ford, C. P., Steyaert, J., and Palczewski, K. (2018) Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor. Nat Commun. 9, 1996
Gulati, S., Jin, H., Masuho, I., Orban, T., Cai, Y., Pardon, E., Martemyanov, K. A., Kiser, P. D., Stewart, P. L., Ford, C. P., Steyaert, J., and Palczewski, K. (2018) Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor. Nat Commun. 9, 1996
Mondal, S., Jacoby, G., Sawaya, M. R., Arnon, Z. A., Adler-Abramovich, L., Rehak, P., Vuković, L., Shimon, L. J. W., Král, P., Beck, R., and Gazit, E. (2018) Transition of metastable cross-α crystals into cross-β fibrils by β-turn flipping.. J Am Chem Soc. 10.1021/jacs.8b10289
Mondal, S., Jacoby, G., Sawaya, M. R., Arnon, Z. A., Adler-Abramovich, L., Rehak, P., Vuković, L., Shimon, L. J. W., Král, P., Beck, R., and Gazit, E. (2018) Transition of metastable cross-α crystals into cross-β fibrils by β-turn flipping.. J Am Chem Soc. 10.1021/jacs.8b10289
Narui, Y., and Sotomayor, M. (2018) Tuning Inner-Ear Tip-Link Affinity Through Alternatively Spliced Variants of Protocadherin-15. Biochemistry. 10.1021/acs.biochem.7b01075
Hanczyc, P., Mikhailovsky, A., Boyer, D. R., Sawaya, M. R., Heeger, A., and Eisenberg, D. (2018) Ultrafast Time-Resolved Studies on Fluorescein for Recognition Strands Architecture in Amyloid Fibrils. J Phys Chem B. 122, 8-18
Chen, Y., Bensing, B. A., Seepersaud, R., Mi, W., Liao, M., Jeffrey, P. D., Shajahan, A., Sonon, R. N., Azadi, P., Sullam, P. M., and Rapoport, T. A. (2018) Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from. J Biol Chem. 10.1074/jbc.RA117.000963
Chen, Y., Bensing, B. A., Seepersaud, R., Mi, W., Liao, M., Jeffrey, P. D., Shajahan, A., Sonon, R. N., Azadi, P., Sullam, P. M., and Rapoport, T. A. (2018) Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from. J Biol Chem. 10.1074/jbc.RA117.000963
Chen, Y., Bensing, B. A., Seepersaud, R., Mi, W., Liao, M., Jeffrey, P. D., Shajahan, A., Sonon, R. N., Azadi, P., Sullam, P. M., and Rapoport, T. A. (2018) Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from. J Biol Chem. 10.1074/jbc.RA117.000963
Chen, Y., Bensing, B. A., Seepersaud, R., Mi, W., Liao, M., Jeffrey, P. D., Shajahan, A., Sonon, R. N., Azadi, P., Sullam, P. M., and Rapoport, T. A. (2018) Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from. J Biol Chem. 10.1074/jbc.RA117.000963
Clark, L. E., Mahmutovic, S., Raymond, D. D., Dilanyan, T., Koma, T., Manning, J. T., Shankar, S., Levis, S. C., Briggiler, A. M., Enria, D. A., Wucherpfennig, K. W., Paessler, S., and Abraham, J. (2018) Vaccine-elicited receptor-binding site antibodies neutralize two New World hemorrhagic fever arenaviruses. Nat Commun. 9, 1884
Peselis, A., and Serganov, A. (2018) ykkC riboswitches employ an add-on helix to adjust specificity for polyanionic ligands. Nat Chem Biol. 14, 887-894
Jaiganesh, A., De-la-Torre, P., Patel, A. A., Termine, D. J., Velez-Cortes, F., Chen, C., and Sotomayor, M. (2018) Zooming in on Cadherin-23: Structural Diversity and Potential Mechanisms of Inherited Deafness. Structure. 10.1016/j.str.2018.06.003
2017
Li, X., Lu, F., Trinh, M. N., Schmiege, P., Seemann, J., Wang, J., and Blobel, G. (2017) 3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.. Proc Natl Acad Sci U S A. 114, 9116-9121
Li, X., Lu, F., Trinh, M. N., Schmiege, P., Seemann, J., Wang, J., and Blobel, G. (2017) 3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.. Proc Natl Acad Sci U S A. 114, 9116-9121
May, J. M., Owens, T. W., Mandler, M. D., Simpson, B. W., Lazarus, M. B., Sherman, D. J., Davis, R. M., Okuda, S., Massefski, W., Ruiz, N., and Kahne, D. (2017) The Antibiotic Novobiocin Binds and Activates the ATPase That Powers Lipopolysaccharide Transport. J Am Chem Soc. 139, 17221-17224
May, J. M., Owens, T. W., Mandler, M. D., Simpson, B. W., Lazarus, M. B., Sherman, D. J., Davis, R. M., Okuda, S., Massefski, W., Ruiz, N., and Kahne, D. (2017) The Antibiotic Novobiocin Binds and Activates the ATPase That Powers Lipopolysaccharide Transport. J Am Chem Soc. 139, 17221-17224
Sangwan, S., Zhao, A., Adams, K. L., Jayson, C. K., Sawaya, M. R., Guenther, E. L., Pan, A. C., Ngo, J., Moore, D. M., Soriaga, A. B., Do, T. D., Goldschmidt, L., Nelson, R., Bowers, M. T., Koehler, C. M., Shaw, D. E., Novitch, B. G., and Eisenberg, D. S. (2017) Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci U S A. 114, 8770-8775
Sangwan, S., Zhao, A., Adams, K. L., Jayson, C. K., Sawaya, M. R., Guenther, E. L., Pan, A. C., Ngo, J., Moore, D. M., Soriaga, A. B., Do, T. D., Goldschmidt, L., Nelson, R., Bowers, M. T., Koehler, C. M., Shaw, D. E., Novitch, B. G., and Eisenberg, D. S. (2017) Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci U S A. 114, 8770-8775
Sangwan, S., Zhao, A., Adams, K. L., Jayson, C. K., Sawaya, M. R., Guenther, E. L., Pan, A. C., Ngo, J., Moore, D. M., Soriaga, A. B., Do, T. D., Goldschmidt, L., Nelson, R., Bowers, M. T., Koehler, C. M., Shaw, D. E., Novitch, B. G., and Eisenberg, D. S. (2017) Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci U S A. 114, 8770-8775

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