DNA binding of cAMP receptor protein and its N‐terminal core stabilizes the double helix and is modulated by the allosteric effector cAMP
- 8 March 1982
- journal article
- Published by Wiley in FEBS Letters
- Vol. 139 (1) , 37-40
- https://doi.org/10.1016/0014-5793(82)80481-x
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Electron microscope observation of a fibre structure formed by non-specific binding of cAMP receptor protein to DNAJournal of Molecular Biology, 1981
- Mechanism for transcriptional action of cyclic AMP in Escherichia coli: entry into DNA to disrupt DNA secondary structure.Proceedings of the National Academy of Sciences, 1981
- Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNANature, 1981
- Interaction of catabolite activator protein of Escherichia coli with single-stranded deoxyribonucleic acidBiochemistry, 1981
- An equilibrium study of the cooperative binding of adenosine cyclic 3',5'-monophosphate and guanosine cyclic 3',5'-monophosphate to the adenosine cyclic 3',5'-monophosphate receptor protein from Escherichia coliBiochemistry, 1980
- The Escherichia coli L-arabinose operon: binding sites of the regulatory proteins and a mechanism of positive and negative regulation.Proceedings of the National Academy of Sciences, 1980
- Interaction site of Escherichia coli cyclic AMP receptor protein on DNA of galactose operon promoters.Proceedings of the National Academy of Sciences, 1979
- Theoretical calculations of the helix–coil transition of DNA in the presence of large, cooperatively binding ligandsBiopolymers, 1976
- Specific binding of CAP factor to lac promoter DNANature, 1975
- Mechanism of Activation of Catabolite-Sensitive Genes: A Positive Control SystemProceedings of the National Academy of Sciences, 1970