Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli

By H. Youn, Junseock Koh, G. Roberts. 2008

24 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

1. H. Youn
2. Charalampos G. Kalodimos
3. R. Ebright
4. Nataliya Popovych

In Molecular Biology

1. H. Youn
2. Charalampos G. Kalodimos
3. Marco Tonelli
4. R. Ebright
5. Nataliya Popovych

Citations in the corpus

• Directed Evolution of the Escherichia coli cAMP Receptor Protein at the cAMP Pocket* (2015, methodology): “Separately, we have shown that the presence of constitutive activity leads to increased cAMP affinity in CRP through the equilibrium-shift mechanism, independent of hydrogen bonding (10).”
• Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, result): “5B), in agreement with biochemical data (19, 20).”