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Papini, C., Ullah, I., Ranjan, A. P., Zhang, S., Wu, Q., Spasov, K. A., Zhang, C., Mothes, W., Crawford, J. M., Lindenbach, B. D., Uchil, P. D., Kumar, P., Jorgensen, W. L., and Anderson, K. S. (2024) Proof-of-concept studies with a computationally designed M inhibitor as a synergistic combination regimen alternative to Paxlovid. Proc Natl Acad Sci U S A. 121, e2320713121
Papadopoulos, E., Jenni, S., Kabha, E., Takrouri, K. J., Yi, T., Salvi, N., Luna, R. E., Gavathiotis, E., Mahalingam, P., Arthanari, H., Rodriguez-Mias, R., Yefidoff-Freedman, R., Aktas, B. H., Chorev, M., Halperin, J. A., and Wagner, G. (2014) Structure of the eukaryotic translation initiation factor eIF4E in complex with 4EGI-1 reveals an allosteric mechanism for dissociating eIF4G. Proc Natl Acad Sci U S A. 111, E3187-95
Papadaki, G. F., Ani, O., Florio, T. J., Young, M. C., Danon, J. N., Sun, Y., Dersh, D., and Sgourakis, N. G. (2023) Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules. Front Immunol. 14, 1116906
Pantel, L., Florin, T., Dobosz-Bartoszek, M., Racine, E., Sarciaux, M., Serri, M., Houard, J., Campagne, J. - M., de Figueiredo, R. Marcia, Midrier, C., Gaudriault, S., Givaudan, A., Lanois, A., Forst, S., Aumelas, A., Cotteaux-Lautard, C., Bolla, J. - M., Lundberg, C. Vingsbo, Huseby, D. L., Hughes, D., Villain-Guillot, P., Mankin, A. S., Polikanov, Y. S., and Gualtieri, M. (2018) Odilorhabdins, Antibacterial Agents that Cause Miscoding by Binding at a New Ribosomal Site. Mol Cell. 70, 83-94.e7
Pandya, R. K., Partridge, J. R., Love, K. Routenberg, Schwartz, T. U., and Ploegh, H. L. (2010) A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities. J Biol Chem. 285, 5664-73
Pan, C., Zimmer, A., Shah, M., Huynh, M. Sang, Lai, C. Chieh- Lin, Sit, B., Hooda, Y., Curran, D. M., and Moraes, T. F. (2021) Actinobacillus utilizes a binding-protein dependent ABC transporter to acquire the active form of Vitamin B. J Biol Chem. 10.1016/j.jbc.2021.101046
Pallapati, A. R., Korkmaz, F., Rojekar, S., Sims, S., Misra, A., Gimenez-Roig, J., Gangadhar, A., Laurencin, V., Gumerova, A., Cheliadinova, U., Sultana, F., Vasilyeva, D., Cullen, L., Schuermann, J., Munitz, J., Kannangara, H., Parte, S., Pevnev, G., Burganova, G., Tumoglu, Z., Witztum, R., Wizman, S., Kramskiy, N., Igel, L., Sen, F., Ranzenigo, A., Macdonald, A., Hutchison, S., Teunissen, A. Jp, Burkart, H., Saxena, M., Ginzburg, Y., Goosens, K., Zhou, W., Ryu, V., Moldavski, O., Barak, O., Pazianas, M., Caminis, J., Bhasin, S., Fitzgerald, R., Kim, S. - M., Quinn, M., Haider, S., Appt, S., Frolinger, T., Rosen, C. J., Lizneva, D., Gupta, Y. K., Yuen, T., and Zaidi, M. (2025) Efficacy and safety of a therapeutic humanized FSH-blocking antibody in obesity and Alzheimer's disease models. J Clin Invest. 10.1172/JCI182702
Palioura, S., R Sherrer, L., Steitz, T. A., Söll, D., and Simonovic, M. (2009) The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science. 325, 321-5
Palani, S., Machida, Y., Alvey, J. R., Mishra, V., Welter, A. L., Cui, G., Bragantini, B., Botuyan, M. Victoria, Cong, A. T. Q., Mer, G., Schellenberg, M. J., and Machida, Y. J. (2024) Dimerization-dependent serine protease activity of FAM111A prevents replication fork stalling at topoisomerase 1 cleavage complexes. Nat Commun. 15, 2064
Pakotiprapha, D., Liu, Y., Verdine, G. L., and Jeruzalmi, D. (2009) A structural model for the damage-sensing complex in bacterial nucleotide excision repair. J Biol Chem. 284, 12837-44
Pakotiprapha, D., Inuzuka, Y., Bowman, B. R., Moolenaar, G. F., Goosen, N., Jeruzalmi, D., and Verdine, G. L. (2008) Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Mol Cell. 29, 122-33
Pakotiprapha, D., Samuels, M., Shen, K., Hu, J. H., and Jeruzalmi, D. (2012) Structure and mechanism of the UvrA-UvrB DNA damage sensor. Nat Struct Mol Biol. 19, 291-8
Pakhomova, S., Boeglin, W. E., Neau, D. B., Bartlett, S. G., Brash, A. R., and Newcomer, M. E. (2019) An ensemble of lipoxygenase structures reveals novel conformations of the Fe coordination sphere. Protein Sci. 10.1002/pro.3602
Pak, J. S., DeLoughery, Z. J., Wang, J., Acharya, N., Park, Y., Jaworski, A., and zkan, E. Ö. (2020) NELL2-Robo3 complex structure reveals mechanisms of receptor activation for axon guidance. Nat Commun. 11, 1489
Padayatti, P., Palczewska, G., Sun, W., Palczewski, K., and Salom, D. (2012) Imaging of protein crystals with two-photon microscopy. Biochemistry. 51, 1625-37
Padayatti, P. S., Leung, J. H., Mahinthichaichan, P., Tajkhorshid, E., Ishchenko, A., Cherezov, V., S Soltis, M., J Jackson, B., C Stout, D., Gennis, R. B., and Zhang, Q. (2017) Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure. 25, 1111-1119.e3

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