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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. 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
Padayatti, P., Palczewska, G., Sun, W., Palczewski, K., and Salom, D. (2012) Imaging of protein crystals with two-photon microscopy. Biochemistry. 51, 1625-37

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