Publications

Found 1344 results
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2017
Koenigsberg, A. L., and Heldwein, E. E. (2017) Crystal structure of the N-terminal half of the traffic controller UL37 from Herpes Simplex virus Type 1. J Virol. 10.1128/JVI.01244-17
Kumar, N., Su, C. - C., Chou, T. - H., Radhakrishnan, A., Delmar, J. A., Rajashankar, K. R., and Yu, E. W. (2017) Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN. Proc Natl Acad Sci U S A. 114, 6557-6562
Kim, S. Kyung, Barron, L., Hinck, C. S., Petrunak, E. M., Cano, K. E., Thangirala, A., Iskra, B., Brothers, M., Vonberg, M., Leal, B., Richter, B., Kodali, R., Taylor, A. B., Du, S., Barnes, C. O., Sulea, T., Calero, G., P Hart, J., Hart, M. J., Demeler, B., and Hinck, A. P. (2017) An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.. J Biol Chem. 292, 7173-7188
Kim, S. Kyung, Barron, L., Hinck, C. S., Petrunak, E. M., Cano, K. E., Thangirala, A., Iskra, B., Brothers, M., Vonberg, M., Leal, B., Richter, B., Kodali, R., Taylor, A. B., Du, S., Barnes, C. O., Sulea, T., Calero, G., P Hart, J., Hart, M. J., Demeler, B., and Hinck, A. P. (2017) An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.. J Biol Chem. 292, 7173-7188
Silvaroli, J. A., Pleshinger, M. J., Banerjee, S., Kiser, P. D., and Golczak, M. (2017) Enzyme That Makes You Cry-Crystal Structure of Lachrymatory Factor Synthase from Allium cepa. ACS Chem Biol. 10.1021/acschembio.7b00336
Jenson, J. M., Ryan, J. A., Grant, R. A., Letai, A., and Keating, A. E. (2017) Epistatic mutations in PUMA BH3 drive an alternate binding mode to potently and selectively inhibit anti-apoptotic Bfl-1. Elife. 10.7554/eLife.25541
Hangasky, J. A., Taabazuing, C. Y., Martin, C. B., Eron, S. J., and Knapp, M. J. (2017) The facial triad in the α-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to O activation.. J Inorg Biochem. 166, 26-33
Moody, J. D., Levy, S., Mathieu, J., Xing, Y., Kim, W., Dong, C., Tempel, W., Robitaille, A. M., Dang, L. T., Ferreccio, A., Detraux, D., Sidhu, S., Zhu, L., Carter, L., Xu, C., Valensisi, C., Wang, Y., R Hawkins, D., Min, J., Moon, R. T., Orkin, S. H., Baker, D., and Ruohola-Baker, H. (2017) First critical repressive H3K27me3 marks in embryonic stem cells identified using designed protein inhibitor. Proc Natl Acad Sci U S A. 10.1073/pnas.1706907114
Hameed, U., Price, I., Ke, A., Wilson, D. B., and Mirza, O. (2017) Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization. Biochim Biophys Acta. 1865, 1237-1245
Xiao, Y., Ng, S., Nam, K. Hyun, and Ke, A. (2017) How type II CRISPR-Cas establish immunity through Cas1-Cas2-mediated spacer integration. Nature. 550, 137-141
Lam, K. - H., Qi, R., Liu, S., Kroh, A., Yao, G., Perry, K., Rummel, A., and Jin, R. (2017) The hypothetical protein P47 of Clostridium botulinum E1 strain Beluga has a structural topology similar to bactericidal/permeability-increasing protein. Toxicon. 10.1016/j.toxicon.2017.10.012
Puleo, D. E., Kucera, K., Hammarén, H. M., Ungureanu, D., Newton, A. S., Silvennoinen, O., Jorgensen, W. L., and Schlessinger, J. (2017) Identification and Characterization of JAK2 Pseudokinase Domain Small Molecule Binders. ACS Med Chem Lett. 8, 618-621
Dang, B., Shen, R., Kubota, T., Mandal, K., Bezanilla, F., Roux, B., and Kent, S. B. H. (2017) Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin. Angew Chem Int Ed Engl. 56, 3324-3328
Dang, B., Shen, R., Kubota, T., Mandal, K., Bezanilla, F., Roux, B., and Kent, S. B. H. (2017) Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin. Angew Chem Int Ed Engl. 56, 3324-3328
Metelev, M., Osterman, I. A., Ghilarov, D., Khabibullina, N. F., Yakimov, A., Shabalin, K., Utkina, I., Travin, D. Y., Komarova, E. S., Serebryakova, M., Artamonova, T., Khodorkovskii, M., Konevega, A. L., Sergiev, P. V., Severinov, K., and Polikanov, Y. S. (2017) Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel. Nat Chem Biol. 10.1038/nchembio.2462
Metelev, M., Osterman, I. A., Ghilarov, D., Khabibullina, N. F., Yakimov, A., Shabalin, K., Utkina, I., Travin, D. Y., Komarova, E. S., Serebryakova, M., Artamonova, T., Khodorkovskii, M., Konevega, A. L., Sergiev, P. V., Severinov, K., and Polikanov, Y. S. (2017) Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel. Nat Chem Biol. 10.1038/nchembio.2462
Metelev, M., Osterman, I. A., Ghilarov, D., Khabibullina, N. F., Yakimov, A., Shabalin, K., Utkina, I., Travin, D. Y., Komarova, E. S., Serebryakova, M., Artamonova, T., Khodorkovskii, M., Konevega, A. L., Sergiev, P. V., Severinov, K., and Polikanov, Y. S. (2017) Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel. Nat Chem Biol. 10.1038/nchembio.2462
Metelev, M., Osterman, I. A., Ghilarov, D., Khabibullina, N. F., Yakimov, A., Shabalin, K., Utkina, I., Travin, D. Y., Komarova, E. S., Serebryakova, M., Artamonova, T., Khodorkovskii, M., Konevega, A. L., Sergiev, P. V., Severinov, K., and Polikanov, Y. S. (2017) Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel. Nat Chem Biol. 10.1038/nchembio.2462
Osterman, I. A., Khabibullina, N. F., Komarova, E. S., Kasatsky, P., Kartsev, V. G., Bogdanov, A. A., Dontsova, O. A., Konevega, A. L., Sergiev, P. V., and Polikanov, Y. S. (2017) Madumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. Nucleic Acids Res. 10.1093/nar/gkx413
Osterman, I. A., Khabibullina, N. F., Komarova, E. S., Kasatsky, P., Kartsev, V. G., Bogdanov, A. A., Dontsova, O. A., Konevega, A. L., Sergiev, P. V., and Polikanov, Y. S. (2017) Madumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. Nucleic Acids Res. 10.1093/nar/gkx413
Osterman, I. A., Khabibullina, N. F., Komarova, E. S., Kasatsky, P., Kartsev, V. G., Bogdanov, A. A., Dontsova, O. A., Konevega, A. L., Sergiev, P. V., and Polikanov, Y. S. (2017) Madumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. Nucleic Acids Res. 10.1093/nar/gkx413
Osterman, I. A., Khabibullina, N. F., Komarova, E. S., Kasatsky, P., Kartsev, V. G., Bogdanov, A. A., Dontsova, O. A., Konevega, A. L., Sergiev, P. V., and Polikanov, Y. S. (2017) Madumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. Nucleic Acids Res. 10.1093/nar/gkx413
Osterman, I. A., Khabibullina, N. F., Komarova, E. S., Kasatsky, P., Kartsev, V. G., Bogdanov, A. A., Dontsova, O. A., Konevega, A. L., Sergiev, P. V., and Polikanov, Y. S. (2017) Madumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state. Nucleic Acids Res. 10.1093/nar/gkx413
Chevalier, A., Silva, D. - A., Rocklin, G. J., Hicks, D. R., Vergara, R., Murapa, P., Bernard, S. M., Zhang, L., Lam, K. - H., Yao, G., Bahl, C. D., Miyashita, S. - I., Goreshnik, I., Fuller, J. T., Koday, M. T., Jenkins, C. M., Colvin, T., Carter, L., Bohn, A., Bryan, C. M., D Fernández-Velasco, A., Stewart, L., Dong, M., Huang, X., Jin, R., Wilson, I. A., Fuller, D. H., and Baker, D. (2017) Massively parallel de novo protein design for targeted therapeutics. Nature. 550, 74-79
Yang, Y., Ke, N., Liu, S., and Li, W. (2017) Methods for Structural and Functional Analyses of Intramembrane Prenyltransferases in the UbiA Superfamily. Methods Enzymol. 584, 309-347

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