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Nature|August 15, 1985
Ethylation interference and X-ray crystallography identify similar interactions between 434 repressor and operatorF D Bushman, J E Anderson, S C Harrison, et al.Nature|April 6, 1987
Structure of the repressor-operator complex of bacteriophage 434J E Anderson, M Ptashne, S C HarrisonNature|August 15, 1985
A phage repressor-operator complex at 7 A resolutionJ E Anderson, M Ptashne, S C HarrisonProceedings of the National Academy of Sciences of the United States of America|December 1, 1986
Activation of transcription by the bacteriophage 434 repressorF D Bushman, M PtashneCell|September 22, 1989
A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressorF D Bushman, C Shang, M PtashneProceedings of the National Academy of Sciences of the United States of America|March 1, 1984
Cocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operatorJ Anderson, M Ptashne, S C HarrisonNature|April 6, 1987
Effect of non-contacted bases on the affinity of 434 operator for 434 repressor and CroG B Koudelka, S C Harrison, M PtashneNature|April 2, 1992
DNA recognition by GAL4: structure of a protein-DNA complexR Marmorstein, M Carey, M Ptashne, et al.Biophysical Chemistry|February 1, 1988
Recognition of DNA sequences by the repressor of bacteriophage 434S C Harrison, J E Anderson, G B Koudelka, et al.Pageof 58