Published in Nature on July 29, 1982
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Recognition sequences of repressor and polymerase in the operators of bacteriophage lambda. Cell (1975) 4.28
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Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol Cell (2000) 3.52
Bacteriophage lambda repressor and cro protein: interactions with operator DNA. Methods Enzymol (1980) 3.52
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Refined 1.8 A crystal structure of the lambda repressor-operator complex. J Mol Biol (1992) 3.09
DNA recognition by beta-sheets in the Arc repressor-operator crystal structure. Nature (1994) 3.07
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Alternative packing arrangements in the hydrophobic core of lambda repressor. Nature (1989) 2.89
The role of internal packing interactions in determining the structure and stability of a protein. J Mol Biol (1991) 2.83
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SsrA-mediated peptide tagging caused by rare codons and tRNA scarcity. EMBO J (1999) 2.76
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Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP. Genes Dev (1999) 2.73
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Metal-dependent folding of a single zinc finger from transcription factor IIIA. Proc Natl Acad Sci U S A (1987) 2.53
Getting a handhold on DNA: design of poly-zinc finger proteins with femtomolar dissociation constants. Proc Natl Acad Sci U S A (1998) 2.51
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Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry (1989) 2.27
Changing the DNA-binding specificity of a repressor. Cell (1983) 2.24
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Lambda repressor mutations that increase the affinity and specificity of operator binding. Cell (1985) 2.12
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Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature (1990) 1.70
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