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  1. 1.   Elements in the ? Immunity Region Regulate Phage Development: Beyond the "Genetic Switch"
  2. Thomason,Lynn; Morrill, Kathleen; Murray, Gillian; Court,Carolyn; Shafer, Brenda; Schneider,Tom; Court,Don
  3. Molecular microbiology. 2019, DEC; 112(6): 1798-1813.
  1. 2.   Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination
  2. Stagno, J. R.; Altieri, A. S.; Bubunenko, M.; Tarasov, S. G.; Li, J.; Court, D. L.; Byrd, R. A.; Ji, X. H.
  3. Nucleic Acids Research. 2011, Sep; 39(17): 7803-7815.
  1. 3.   NusA Interaction with the alpha Subunit of E-coil RNA Polymerase Is via the UP Element Site and Releases Autoinhibition
  2. Schweimer, K.; Prasch, S.; Sujatha, P. S.; Bubunenko, M.; Gottesman, M. E.; Rosch, P.
  3. Structure. 2011, Jul; 19(7): 945-954.
  1. 4.   Probing Cellular Processes with Oligo-Mediated Recombination and Using the Knowledge Gained to Optimize Recombineering
  2. Sawitzke, J. A.; Costantino, N.; Li, X. T.; Thomason, L. C.; Bubunenko, M.; Court, C.; Court, D. L.
  3. Journal of Molecular Biology. 2011, Mar; 407(1): 45-59.
  1. 5.   Sequences required for transcription termination at the intrinsic lambda tI terminator
  2. Martinez-Trujillo, M.; Sanchez-Trujillo, A.; Ceja, V.; Avila-Moreno, F.; Bermudez-Cruz, R. M.; Court, D.; Montanez, C.
  3. Canadian Journal of Microbiology. 2010, Feb; 56(2): 168-177.
  1. 6.   Recombineering: a homologous recombination-based method of genetic engineering
  2. Sharan, S. K.; Thomason, L. C.; Kuznetsov, S. G.; Court, D. L.
  3. Nature Protocols. 2009 4(2): 206-223.
  1. 7.   A stepwise model for double-stranded RNA processing by ribonuclease III
  2. Gan, J.; Shaw, G.; Tropea, J. E.; Waugh, D. S.; Court, D. L.; Ji, X.
  3. Molecular Microbiology. 2008 67(1): 143-154.
  1. 8.   Structural and Functional Analysis of the E. coli NusB-S10 Transcription Antitermination Complex
  2. Luo, X.; Hsiao, H. H.; Bubunenko, M.; Weber, G.; Court, D. L.; Gottesman, M. E.; Urlaub, H.; Wahl, M. C.
  3. Molecular Cell. 2008 32(6): 791-802.
  1. 9.   Host responses influence on the induction of lambda prophage
  2. Rokney, A.; Kobiler, O.; Amir, A.; Court, D. L.; Stavans, J.; Adhya, S.; Oppenheim, A. B.
  3. Molecular Microbiology. 2008 68(1): 29-36.
  1. 10.   Multicopy plasmid modification with phage lambda red recombineering
  2. Thomason, L. C.; Costantino, N.; Shaw, D. V.; Court, D. L.
  3. Plasmid. 2007, Sep; 58(2): 148-158.
  1. 11.   A recombineering based approach for high-throughput conditional knockout targeting vector construction
  2. Chan, W.; Costantino, N.; Li, R. X.; Lee, S. C.; Su, Q.; Melvin, D.; Court, D. L.; Liu, P. T.
  3. Nucleic Acids Research. 2007, Apr; 35(8):
  1. 12.   Recombineering: In vivo genetic engineering in E-coli, S-enterica, and beyond
  2. Sawitzke, J. A.; Thomason, L. C.; Costantino, N.; Bubunenko, M.; Datta, S.; Court, D. L.
  3. Advanced Bacterial Genetics: Use of Transposons and Phage for Genomic Engieering. 2007; 421 : 171-199.
  1. 13.   A new look at bacteriophage lambda genetic networks
  2. Court, D. L.; Oppertheim, A. B.; Adhya, S. L.
  3. Journal of Bacteriology. 2007, Jan; 189(2): 298-304.
  1. 14.   Role of an RNase III binding site in transcription termination at lambda nutL by HK022 Nun protein
  2. Washburn, R. S.; Court, D. L.; Gottesman, M. E.
  3. Journal of Bacteriology. 2006, Oct; 188(19): 6824-6831.
  1. 15.   A set of recombineering plasmids for gram-negative bacteria
  2. Datta, S.; Costantino, N.; Court, D. L.
  3. Gene. 2006, Sep; 379: 109-115.
  1. 16.   Structural basis for non-catalytic and catalytic activities of ribonuclease III
  2. Ji, X. H.
  3. Acta Crystallographica Section D-Biological Crystallography. 2006, Aug; 62: 933-940.
  1. 17.   Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III
  2. Gan, J. H.; Tropea, J. E.; Austin, B. P.; Court, D. L.; Waugh, D. S.; Ji, X. H.
  3. Cell. 2006, JAN 27; 124(2): 355-366.
  1. 18.   Quantitative kinetic analysis of the bacteriophage lambda genetic network
  2. Kobiler, O.; Rokney, A.; Friedman, N.; Court, D. L.; Stavans, J.; Oppenheim, A. B.
  3. Proceedings of the National Academy of Sciences of the United States of America. 2005 102(12): 4470-4475.
  1. 19.   On the role of Cro in lambda prophage induction
  2. Svenningsen, S. L.; Costantino, N.; Court, D. L.; Adhya, S.
  3. Proceedings of the National Academy of Sciences of the United States of America. 2005 102(12): 4465-4469.
  1. 20.   Switches in bacteriophage lambda development
  2. Oppenheim, A. B.; Kobiler, O.; Stavans, J.; Court, D. L.; Adhya, S.
  3. Annual Review of Genetics. 2005 39: 409-429.
  1. 21.   Crystal structure of a truncated version of the phage lambda protein gpD
  2. Chang, C. S.; Pluckthun, A.; Wlodawer, A.
  3. Proteins-Structure Function and Bioinformatics. 2004, DEC 1; 57(4): 866-868.
  1. 22.   Kinetic stability and crystal structure of the viral capsid protein SHP
  2. Forrer, P.; Chang, C. S.; Ott, D.; Wlodawer, A.; Pluckthun, A.
  3. Journal of Molecular Biology. 2004, NOV 12; 344(1): 179-193.
  1. 23.   In vivo recombineering of bacteriophage lambda by PCR fragments and single-strand oligonucleotides
  2. Oppenheim, A. B.; Rattray, A. J.; Bubunenko, M.; Thomason, L. C.; Court, D. L.
  3. Virology. 2004 319(2): 185-189.
  1. 24.   A novel cell-free protein synthesis system
  2. Sitaraman, K.; Esposito, D.; Klarmann, G.; Le Grice, S. F.; Hartley, J. L.; Chatterjee, D. K.
  3. Journal of Biotechnology. 2004 110(3): 257-263.
  1. 25.   A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site- directed mutants
  2. Knowlton, J. R.; Bubunenko, M.; Andrykovitch, M.; Guo, W.; Routzahn, K. M.; Waugh, D. S.; Court, D. L.; Ji, X. H.
  3. Biochemistry. 2003 42(8): 2275-2281.
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