Publications

Found 61 results
Filters: Author is Steitz, Thomas A  [Clear All Filters]
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Kavran, J. M., and Steitz, T. A. (2007) Structure of the base of the L7/L12 stalk of the Haloarcula marismortui large ribosomal subunit: analysis of L11 movements. J Mol Biol. 371, 1047-59
Yin, F. Fang, Bailey, S., C Innis, A., Ciubotaru, M., Kamtekar, S., Steitz, T. A., and Schatz, D. G. (2009) Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nat Struct Mol Biol. 16, 499-508
Zuo, Y., and Steitz, T. A. (2017) A structure-based kinetic model of transcription. Transcription. 8, 1-8
T Schmeing, M., Moore, P. B., and Steitz, T. A. (2003) Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA. 9, 1345-52
Liu, B., Zuo, Y., and Steitz, T. A. (2016) Structures of E. coli σS-transcription initiation complexes provide new insights into polymerase mechanism.. Proc Natl Acad Sci U S A. 113, 4051-6
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
Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., and Steitz, T. A. (2016) Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Res. 44, 2439-50
Stanley, R. E., Blaha, G., Grodzicki, R. L., Strickler, M. D., and Steitz, T. A. (2010) The structures of the anti-tuberculosis antibiotics viomycin and capreomycin bound to the 70S ribosome. Nat Struct Mol Biol. 17, 289-93
Gürel, G., Blaha, G., Steitz, T. A., and Moore, P. B. (2009) Structures of triacetyloleandomycin and mycalamide A bind to the large ribosomal subunit of Haloarcula marismortui. Antimicrob Agents Chemother. 53, 5010-4
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Kamtekar, S., Hohn, M. J., Park, H. - S., Schnitzbauer, M., Sauerwald, A., Söll, D., and Steitz, T. A. (2007) Toward understanding phosphoseryl-tRNACys formation: the crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase. Proc Natl Acad Sci U S A. 104, 2620-5
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Gürel, G., Blaha, G., Moore, P. B., and Steitz, T. A. (2009) U2504 determines the species specificity of the A-site cleft antibiotics: the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome. J Mol Biol. 389, 146-56

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