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Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Becker, A., Kannan, T. R., Taylor, A. B., Pakhomova, O. N., Zhang, Y., Somarajan, S. R., Galaleldeen, A., Holloway, S. P., Baseman, J. B., and P Hart, J. (2015) Structure of CARDS toxin, a unique ADP-ribosylating and vacuolating cytotoxin from Mycoplasma pneumoniae. Proc Natl Acad Sci U S A. 112, 5165-70
Benavides, B. S., Valandro, S., Cioloboc, D., Taylor, A. B., Schanze, K. S., and Kurtz, D. M. (2020) Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction. Biochemistry. 59, 1618-1629
Benjamin, B., Goldgur, Y., Jork, N., Jessen, H. J., Schwer, B., and Shuman, S. (2022) Structures of Fission Yeast Inositol Pyrophosphate Kinase Asp1 in Ligand-Free, Substrate-Bound, and Product-Bound States. mBio. 10.1128/mbio.03087-22
Berman, A. J., Kamtekar, S., Goodman, J. L., Lázaro, J. M., de Vega, M., Blanco, L., Salas, M., and Steitz, T. A. (2007) Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases. EMBO J. 26, 3494-505
Bertoletti, N., Chan, A. H., Schinazi, R. F., Y Yin, W., and Anderson, K. S. (2019) Structural insights into the recognition of nucleoside reverse transcriptase inhibitors by HIV-1 reverse transcriptase: First crystal structures with reverse transcriptase and the active triphosphate forms of lamivudine and emtricitabine. Protein Sci. 28, 1664-1675
Beyett, T. S., Rana, J. K., Schaeffner, I. K., Heppner, D. E., and Eck, M. J. (2024) Structural Analysis of the Macrocyclic Inhibitor BI-4020 Binding to EGFR Kinase. ChemMedChem. 19, e202300343
Bhattacharya, S., Lou, X., Hwang, P., Rajashankar, K. R., Wang, X., Gustafsson, J. - Å., Fletterick, R. J., Jacobson, R. H., and Webb, P. (2014) Structural and functional insight into TAF1-TAF7, a subcomplex of transcription factor II D. Proc Natl Acad Sci U S A. 111, 9103-8
Bhattacharya, A., Alam, S. L., Fricke, T., Zadrozny, K., Sedzicki, J., Taylor, A. B., Demeler, B., Pornillos, O., Ganser-Pornillos, B. K., Diaz-Griffero, F., Ivanov, D. N., and Yeager, M. (2014) Structural basis of HIV-1 capsid recognition by PF74 and CPSF6. Proc Natl Acad Sci U S A. 111, 18625-30
Bhuket, P. Ratnatilak, Eastwood, J. R. B., Qin, Z., Kessler, J. L., Li, Y., Katz, D., Whitby, F. G., Hill, C. P., Kirshenbaum, K., and S Yu, M. (2026) Structural and Positional Effects of Peptoid Residues on Triple Helix Stability. Biomacromolecules. 10.1021/acs.biomac.5c02232
Bigalke, J. M., and Heldwein, E. E. (2015) Structural basis of membrane budding by the nuclear egress complex of herpesviruses. EMBO J. 34, 2921-36
Bilokapic, S., and Schwartz, T. U. (2013) Structural and functional studies of the 252 kDa nucleoporin ELYS reveal distinct roles for its three tethered domains. Structure. 21, 572-80
Bitto, E., Bingman, C. A., Wesenberg, G. E., McCoy, J. G., and Phillips, G. N. (2006) Structure of pyrimidine 5'-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning. J Biol Chem. 281, 20521-9
Blair, J. A., Rauh, D., Kung, C., Yun, C. -hong, Fan, Q. - W., Rode, H., Zhang, C., Eck, M. J., Weiss, W. A., and Shokat, K. M. (2007) Structure-guided development of affinity probes for tyrosine kinases using chemical genetics. Nat Chem Biol. 3, 229-38
Blank, P. N., Barrow, G. H., Chou, W. K. W., Duan, L., Cane, D. E., and Christianson, D. W. (2017) Substitution of Aromatic Residues with Polar Residues in the Active Site Pocket of epi-Isozizaene Synthase Leads to the Generation of New Cyclic Sesquiterpenes. Biochemistry. 10.1021/acs.biochem.7b00895
Blank, P. N., Shinsky, S. A., and Christianson, D. W. (2019) Structure of Sesquisabinene Synthase 1, a Terpenoid Cyclase That Generates a Strained [3.1.0] Bridged-Bicyclic Product. ACS Chem Biol. 10.1021/acschembio.9b00218
Blus, B. J., Hashimoto, H., Seo, H. - S., Krolak, A., and Debler, E. W. (2019) Substrate Affinity and Specificity of the ScSth1p Bromodomain Are Fine-Tuned for Versatile Histone Recognition. Structure. 27, 1460-1468.e3
Bobik, T. A., Morales, E. J., Shin, A., Cascio, D., Sawaya, M. R., Arbing, M., Yeates, T. O., and Rasche, M. E. (2014) Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii. Acta Crystallogr F Struct Biol Commun. 70, 1472-9
Bodnar, N. O., Kim, K. H., Ji, Z., Wales, T. E., Svetlov, V., Nudler, E., Engen, J. R., Walz, T., and Rapoport, T. A. (2018) Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4. Nat Struct Mol Biol. 25, 616-622
Boehmer, T., Jeudy, S., Berke, I. C., and Schwartz, T. U. (2008) Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex. Mol Cell. 30, 721-31
Bogner, A. N., Ji, J., and Tanner, J. J. (2022) Structure-based engineering of minimal Proline dehydrogenase domains for inhibitor discovery. Protein Eng Des Sel. 10.1093/protein/gzac016
Bogner, A. N., Stiers, K. M., McKay, C. M., Becker, D. F., and Tanner, J. J. (2021) Structural Basis for the Stereospecific Inhibition of the Dual Proline/Hydroxyproline Catabolic Enzyme ALDH4A1 by Trans-4-Hydroxy-L-Proline. Protein Sci. 10.1002/pro.4131
Bogner, A. N., and Tanner, J. J. (2022) Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase. Org Biomol Chem. 10.1039/d1ob02328d
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503
Bolla, J. Reddy, Do, S. V., Long, F., Dai, L., Su, C. - C., Lei, H. - T., Chen, X., Gerkey, J. E., Murphy, D. C., Rajashankar, K. R., Zhang, Q., and Yu, E. W. (2012) Structural and functional analysis of the transcriptional regulator Rv3066 of Mycobacterium tuberculosis. Nucleic Acids Res. 40, 9340-55

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