Structural overview on the allosteric activation of cyclic AMP receptor protein.

By H. Won, Yoo-Sup Lee, Sung-Hee Lee, Bong‐Jin Lee. 2009

55 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. M. Bott
2. Yusuf Tutar
3. P. Kivistik

In Molecular Biology

1. M. Bott
2. Yusuf Tutar
3. P. Kivistik
4. Alfred Pühler

Citations in the corpus

• ColR-ColS signalling system and transposition of Tn4652 in the adaptation of Pseudomonas putida (2010, background): “Regulatory pathways can also be divided according to the magnitude of their function, some regulators affect very many cellular targets and are called global (Baker et al., 2006; Magnusson et al., 2005; Won et al., 2009), whereas the others regulate only very specific processes or genes.”
• The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors (2014, background): “Although the apo- and holo-structures of a number of members of the CRP/FNR family have been structurally characterized, our understanding of the structural and dynamics changes caused by ligand-binding is still limited [52].”
• Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein (2013, background): “The hinge region appears to play a key role by modulating the interdomain interactions and stabilizing the altered domain movements leading to the transcriptional activation [2,14,20].”
• Neglected role of cAMP receptor protein monomer (2011, background): “The N-terminal and C-terminal domains are coupled by an unstructured peptide hinge (residues 134–138) [ 3 , 4]. Changes in the CRP hinge lead to protrusion of the F-helix and CRP interacts specifically with DNA.”
• Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, background): “The atomic details of these conformational changes are described below and validate the previous identification of crucial residues for the allosteric transition (Won et al., 2009; Harman, 2001; Passner et al., 2000; Tomlinson et al., 2006).”