Publications

Found 16 results
Filters: Author is Rapoport, Tom A  [Clear All Filters]
Journal Article
Chen, Y., Bauer, B. W., Rapoport, T. A., and Gumbart, J. C. (2015) Conformational Changes of the Clamp of the Protein Translocation ATPase SecA. J Mol Biol. 427, 2348-59
Wu, X., and Rapoport, T. A. (2021) Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies). Proc Natl Acad Sci U S A. 10.1073/pnas.2115001118
Li, L., Park, E., Ling, J. J., Ingram, J., Ploegh, H., and Rapoport, T. A. (2016) Crystal structure of a substrate-engaged SecY protein-translocation channel. Nature. 531, 395-399
Van den Berg, B., Black, P. N., Clemons, W. M., and Rapoport, T. A. (2004) Crystal structure of the long-chain fatty acid transporter FadL. Science. 304, 1506-9
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Chen, Y., Seepersaud, R., Bensing, B. A., Sullam, P. M., and Rapoport, T. A. (2016) Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein. Proc Natl Acad Sci U S A. 113, E1190-9
Sever, N., Miličić, G., Bodnar, N. O., Wu, X., and Rapoport, T. A. (2020) Mechanism of Lamellar Body Formation by Lung Surfactant Protein B. Mol Cell. 10.1016/j.molcel.2020.10.042
Zimmer, J., Li, W., and Rapoport, T. A. (2006) A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA. J Mol Biol. 364, 259-65
Feng, P., Wu, X., Erramilli, S. K., Paulo, J. A., Knejski, P., Gygi, S. P., Kossiakoff, A. A., and Rapoport, T. A. (2022) A peroxisomal ubiquitin ligase complex forms a retrotranslocation channel. Nature. 607, 374-380
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
Li, W., Schulman, S., Dutton, R. J., Boyd, D., Beckwith, J., and Rapoport, T. A. (2010) Structure of a bacterial homologue of vitamin K epoxide reductase. Nature. 463, 507-12
Zimmer, J., Nam, Y., and Rapoport, T. A. (2008) Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature. 455, 936-43
Bodnar, N. O., Kim, K. H., Ji, Z., Wales, T. E., Svetlov, V., Nudler, E., Engen, J. R., Walz, T., and Rapoport, T. A. (2018) Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat Struct Mol Biol. 25, 616-622
Tripathi, A., Mandon, E. C., Gilmore, R., and Rapoport, T. A. (2017) Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins. J Biol Chem. 292, 8007-8018
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
Van den Berg, B., Clemons, W. M., Collinson, I., Modis, Y., Hartmann, E., Harrison, S. C., and Rapoport, T. A. (2004) X-ray structure of a protein-conducting channel. Nature. 427, 36-44