Publications

Found 1123 results
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2015
Košutić, M., Neuner, S., Ren, A., Flür, S., Wunderlich, C., Mairhofer, E., Vušurović, N., Seikowski, J., Breuker, K., Höbartner, C., Patel, D. J., Kreutz, C., and Micura, R. (2015) A Mini-Twister Variant and Impact of Residues/Cations on the Phosphodiester Cleavage of this Ribozyme Class. Angew Chem Int Ed Engl. 54, 15128-15133
Price, I. R., Gaballa, A., Ding, F., Helmann, J. D., and Ke, A. (2015) Mn(2+)-sensing mechanisms of yybP-ykoY orphan riboswitches. Mol Cell. 57, 1110-1123
Sekiyama, N., Arthanari, H., Papadopoulos, E., Rodriguez-Mias, R. A., Wagner, G., and Léger-Abraham, M. (2015) Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1. Proc Natl Acad Sci U S A. 112, E4036-45
Calmettes, C., Ing, C., Buckwalter, C. M., Bakkouri, M. El, Lai, C. Chieh- Lin, Pogoutse, A., Gray-Owen, S. D., Pomès, R., and Moraes, T. F. (2015) The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. Nat Commun. 6, 7996
Calmettes, C., Ing, C., Buckwalter, C. M., Bakkouri, M. El, Lai, C. Chieh- Lin, Pogoutse, A., Gray-Owen, S. D., Pomès, R., and Moraes, T. F. (2015) The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. Nat Commun. 6, 7996
Zhang, J., Kiser, P. D., Badiee, M., Palczewska, G., Dong, Z., Golczak, M., Tochtrop, G. P., and Palczewski, K. (2015) Molecular pharmacodynamics of emixustat in protection against retinal degeneration. J Clin Invest. 125, 2781-94
Zhang, J., Kiser, P. D., Badiee, M., Palczewska, G., Dong, Z., Golczak, M., Tochtrop, G. P., and Palczewski, K. (2015) Molecular pharmacodynamics of emixustat in protection against retinal degeneration. J Clin Invest. 125, 2781-94
Qian, W. - J., Park, J. - E., Grant, R., Lai, C. C., Kelley, J. A., Yaffe, M. B., Lee, K. S., and Burke, T. R. (2015) Neighbor-directed histidine N (τ)-alkylation: A route to imidazolium-containing phosphopeptide macrocycles.. Biopolymers. 104, 663-73
Wang, K. H., Penmatsa, A., and Gouaux, E. (2015) Neurotransmitter and psychostimulant recognition by the dopamine transporter. Nature. 521, 322-7
Noey, E. L., Tibrewal, N., Jiménez-Osés, G., Osuna, S., Park, J., Bond, C. M., Cascio, D., Liang, J., Zhang, X., Huisman, G. W., Tang, Y., and Houk, K. N. (2015) Origins of stereoselectivity in evolved ketoreductases. Proc Natl Acad Sci U S A. 112, E7065-72
Saoji, M., Zhang, D., and Paukstelis, P. J. (2015) Probing the role of sequence in the assembly of three-dimensional DNA crystals. Biopolymers. 103, 618-26
Mateja, A., Paduch, M., Chang, H. - Y., Szydlowska, A., Kossiakoff, A. A., Hegde, R. S., and Keenan, R. J. (2015) Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo. Science. 347, 1152-5
Chen, S., Yang, Z., Wilkinson, A. W., Deshpande, A. J., Sidoli, S., Krajewski, K., Strahl, B. D., Garcia, B. A., Armstrong, S. A., Patel, D. J., and Gozani, O. (2015) The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79. Mol Cell. 60, 319-27
Brown, N. G., VanderLinden, R., Watson, E. R., Qiao, R., Grace, C. R. R., Yamaguchi, M., Weissmann, F., Frye, J. J., Dube, P., Cho, S. Ei, Actis, M. L., Rodrigues, P., Fujii, N., Peters, J. - M., Stark, H., and Schulman, B. A. (2015) RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex. Proc Natl Acad Sci U S A. 112, 5272-9
Chowdhury, C., Chun, S., Pang, A., Sawaya, M. R., Sinha, S., Yeates, T. O., and Bobik, T. A. (2015) Selective molecular transport through the protein shell of a bacterial microcompartment organelle. Proc Natl Acad Sci U S A. 112, 2990-5
Saoji, M., and Paukstelis, P. J. (2015) Sequence-dependent structural changes in a self-assembling DNA oligonucleotide. Acta Crystallogr D Biol Crystallogr. 71, 2471-8
Broussard, T. C., Pakhomova, S., Neau, D. B., Bonnot, R., and Waldrop, G. L. (2015) Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase. Biochemistry. 54, 3860-70
Ren, A., Xue, Y., Peselis, A., Serganov, A., Al-Hashimi, H. M., and Patel, D. J. (2015) Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch. Cell Rep. 13, 1800-13
Ren, A., Xue, Y., Peselis, A., Serganov, A., Al-Hashimi, H. M., and Patel, D. J. (2015) Structural and Dynamic Basis for Low-Affinity, High-Selectivity Binding of L-Glutamine by the Glutamine Riboswitch. Cell Rep. 13, 1800-13
Fan, H., Hahm, J., Diggs, S., J Perry, J. P., and Blaha, G. (2015) Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli. J Biol Chem. 290, 20856-64
Taylor, A. B., Pica-Mattoccia, L., Polcaro, C. M., Donati, E., Cao, X., Basso, A., Guidi, A., Rugel, A. R., Holloway, S. P., Anderson, T. J. C., P Hart, J., Cioli, D., and LoVerde, P. T. (2015) Structural and Functional Characterization of the Enantiomers of the Antischistosomal Drug Oxamniquine. PLoS Negl Trop Dis. 9, e0004132
Taylor, A. B., Pica-Mattoccia, L., Polcaro, C. M., Donati, E., Cao, X., Basso, A., Guidi, A., Rugel, A. R., Holloway, S. P., Anderson, T. J. C., P Hart, J., Cioli, D., and LoVerde, P. T. (2015) Structural and Functional Characterization of the Enantiomers of the Antischistosomal Drug Oxamniquine. PLoS Negl Trop Dis. 9, e0004132
Cappadocia, L., Pichler, A., and Lima, C. D. (2015) Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase. Nat Struct Mol Biol. 22, 968-75
Patra, A., Banerjee, S., Salyard, T. L. Johnson, Malik, C. K., Christov, P. P., Rizzo, C. J., Stone, M. P., and Egli, M. (2015) Structural Basis for Error-Free Bypass of the 5-N-Methylformamidopyrimidine-dG Lesion by Human DNA Polymerase η and Sulfolobus solfataricus P2 Polymerase IV.. J Am Chem Soc. 137, 7011-4
Jost, M., Fernández-Zapata, J., Polanco, M. Carmen, Ortiz-Guerrero, J. Manuel, Chen, P. Yang- Ting, Kang, G., Padmanabhan, S., Elías-Arnanz, M., and Drennan, C. L. (2015) Structural basis for gene regulation by a B12-dependent photoreceptor. Nature. 526, 536-41

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