G. Roberts
Molecular Biology · with Youn · 2006–2008
A researcher in the Science corpus: 3 papers; trusts 1 researcher and is trusted by 2 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 10 citations into it; #13,502 of 17,773 by trust here, #13,009 by citations
Whom G. Roberts trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts G. Roberts overall
Papers from G. Roberts's perspective
Ordered by how strongly the researchers G. Roberts trusts endorse each paper. Same corpus, a different order for every researcher.
- Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA
- The role of dynamics in allosteric regulation. (Current Opinion in Structural Biology)
- Allosteric Mechanisms of Signal Transduction (Science)
- Transcriptional regulation by cAMP and its receptor protein.
- Study of Highly Constitutively Active Mutants Suggests How cAMP Activates cAMP Receptor Protein*
- Allosteric regulation of the cAMP receptor protein.
- Proposed structural mechanism of Escherichia coli cAMP receptor protein cAMP-dependent proteolytic cleavage protection and selective and nonselective DNA binding.
- Dynamically driven protein allostery
- A C-helix Residue, Arg-123, Has Important Roles in Both the Active and Inactive Forms of the cAMP Receptor Protein*
- Analogs of cyclic AMP that elicit the biochemically defined conformational change in catabolite gene activator protein (CAP) but do not stimulate binding to DNA.
Their papers
- Study of Highly Constitutively Active Mutants Suggests How cAMP Activates cAMP Receptor Protein* (2006) — 50 citations
- 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) — 24 citations
- A C-helix Residue, Arg-123, Has Important Roles in Both the Active and Inactive Forms of the cAMP Receptor Protein* (2006) — 14 citations