Sequence-specific interaction of the Salmonella Hin recombinase in both major and minor grooves of DNA.

References

Page 1

	Year	Citations
ACETYLORNITHINASE OF ESCHERICHIA COLI: PARTIAL PURIFICATION AND SOME PROPERTIES Henry J. Vogel, David M. Bonner Journal of Biological Chemistry BiosynthesisEngineeringBiotransformationBiochemistryBacteriology	1956	4K
Sequence-specific recognition of double helical nucleic acids by proteins. Nadrian C. Seeman, John M. Rosenberg, Alexander Rich Proceedings of the National Academy of Sciences Base PairNucleic Acid ChemistryBiochemistryProtein AssemblyProtein Folding	1976	1.1K
Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: A framework for understanding homeodomain-DNA interactions Charles R. Kissinger, Beishan Liu, Enrique Martı́n-Blanco, Cell	1990	997
Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA David McKay, Thomas A. Steitz Nature BiochemistryLeft-handed B-dnaNatural SciencesStructural BioinformaticsDna Replication	1981	652
Structure of the cro repressor from bacteriophage λ and its interaction with DNA W.F. Anderson, D.H. Ohlendorf, Yoshinori Takeda, Nature Natural SciencesPhage BiologyBacteriologyBacteriophageMolecular Biology	1981	547
The operator-binding domain of λ repressor: structure and DNA recognition Carl O. Pabo, Mitchell Lewis Nature Structural BioinformaticsNatural SciencesTranscription RegulationGene StructureDna Replication	1982	527
Structure of the DNA-Eco RI Endonuclease Recognition Complex at 3 Å Resolution Judith A. McClarin, Christin Frederick, Bi‐Cheng Wang, Science Eco Ri EndonucleaseCrystal StructureNucleic Acid ChemistryBiochemistryProtein Assembly	1986	491
Protein-DNA contacts in the structure of a homeodomain-DNA complex determined by nuclear magnetic resonance spectroscopy in solution. Gottfried Otting, Y. Q. Qian, Martin Billeter, The EMBO Journal BiochemistryNatural SciencesHomeodomain-dna ComplexBiomolecular AnalysisProtein X-ray Crystallography	1990	458
Homology among DNA-binding proteins suggests use of a conserved super-secondary structure Robert T. Sauer, R. Rogers Yocum, Russell F. Doolittle, Nature ChromatinProtein AssemblyStructural BioinformaticsProtein FoldingGenetics	1982	429
The three-dimensional structure of trp repressor Richard W. Schevitz, A. Joachimiak, Catherine L. Lawson, Nature Trp RepressorPhysicsTwistor Theory	1985	343

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