Interplay between site-specific mutations and cyclic nucleotides in modulating DNA recognition by Escherichia coli cyclic AMP receptor protein.
By Jia‐Chun Dai, Shwu-Hwa Lin, Carly M. Kemmis, A. J. Chin, J. Lee. 2004
30 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Genetics
- Lars-Oliver Essen
- E. Krol
- Anke Becker
- H. Youn
- Charalampos G. Kalodimos
- Junseock Koh
- G. Roberts
- R. Ebright
In Molecular Biology
- Junseock Koh
- H. Youn
- G. Roberts
- Charalampos G. Kalodimos
- Marco Tonelli
- E. Krol
- R. Ebright
- Anke Becker
Citations in the corpus
- Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, background): “As a result, the flexibility of the flanking regions of the recognition sequence might be distinguished by Clr, adding another layer of specificity (56, 57).”
- cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review (2008, background): “Moreover, CRP binding to the specific DNA sequences depends not only on the presence of the consensus sequence but also on the presence of proper flanking sequences of DNA [Dai et al., 2004].”
- Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli (2008, background): “T127L/S128I CRP (7, 39), should be treated differently.”
- Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, result): “5B), in agreement with biochemical data (19, 20).”