Publications

Found 116 results
Filters: First Letter Of Last Name is P  [Clear All Filters]
A B C D E F G H I J K L M N O P Q R S T U V W X Y Z 
P
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Papp-Wallace, K. M., Nguyen, N. Q., Jacobs, M. R., Bethel, C. R., Barnes, M. D., Kumar, V., Bajaksouzian, S., Rudin, S. D., Rather, P. N., Bhavsar, S., Ravikumar, T., Deshpande, P. K., Patil, V., Yeole, R., Bhagwat, S. S., Patel, M. V., van den Akker, F., and Bonomo, R. A. (2018) Strategic Approaches to Overcome Resistance against Gram-Negative Pathogens Using β-Lactamase Inhibitors and β-Lactam Enhancers: Activity of Three Novel Diazabicyclooctanes WCK 5153, Zidebactam (WCK 5107), and WCK 4234.. J Med Chem. 61, 4067-4086
Paranjpe, M. N., Marina, V. I., Grachev, A. A., Maviza, T. P., Tolicheva, O. A., Paleskava, A., Osterman, I. A., Sergiev, P. V., Konevega, A. L., Polikanov, Y. S., and Gagnon, M. G. (2023) Insights into the molecular mechanism of translation inhibition by the ribosome-targeting antibiotic thermorubin.. Nucleic Acids Res. 51, 449-462
Park, E., Kim, N., Ficarro, S. B., Zhang, Y., Lee, B. Il, Cho, A., Kim, K., Park, A. K. J., Park, W. - Y., Murray, B., Meyerson, M., Beroukhim, R., Marto, J. A., Cho, J., and Eck, M. J. (2015) Structure and mechanism of activity-based inhibition of the EGF receptor by Mig6. Nat Struct Mol Biol. 22, 703-711
Park, E., Rawson, S., Li, K., Kim, B. - W., Ficarro, S. B., Del Pino, G. Gonzalez-, Sharif, H., Marto, J. A., Jeon, H., and Eck, M. J. (2019) Architecture of autoinhibited and active BRAF-MEK1-14-3-3 complexes. Nature. 575, 545-550
Park, K. - S., Xiong, Y., Yim, H., Velez, J., Babault, N., Kumar, P., Liu, J., and Jin, J. (2022) Discovery of the First-in-Class G9a/GLP Covalent Inhibitors. J Med Chem. 10.1021/acs.jmedchem.2c00652
Park, M. Seul, Phan, H. - D., Busch, F., Hinckley, S. H., Brackbill, J. A., Wysocki, V. H., and Nakanishi, K. (2017) Human Argonaute3 has slicer activity. Nucleic Acids Res. 10.1093/nar/gkx916
Park, H. Ho, and Wu, H. (2007) Crystallization and preliminary X-ray crystallographic studies of the oligomeric death-domain complex between PIDD and RAIDD. Acta Crystallogr Sect F Struct Biol Cryst Commun. 63, 229-32
Park, E., Graziano, B. R., Zheng, W., Garabedian, M., Goode, B. L., and Eck, M. J. (2015) Structure of a Bud6/Actin Complex Reveals a Novel WH2-like Actin Monomer Recruitment Motif. Structure. 23, 1492-1499
Park, J. Sung, Choi, J., Cao, L., Mohanty, J., Suzuki, Y., Park, A., Baker, D., Schlessinger, J., and Lee, S. (2022) Isoform-specific inhibition of FGFR signaling achieved by a de-novo-designed mini-protein. Cell Rep. 41, 111545

Pages