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cAMP receptor protein.
NtcA, a conserved cAMP receptor protein-type transcription factor among cyanobacteria, regulates gene expression in response to nitrogen status.
Here, we aimed to improve the organic solvent tolerance of Escherichia coli by engineering its global transcription factor cAMP receptor protein (CRP).
Here, we tried to improve strain acidic tolerance from its transcription level, i.e. we adopted error-prone PCR method to engineer global regulator cAMP receptor protein (CRP) of Escherichia coli to improve its performance at low pH.
In this study, engineering of the cAMP receptor protein (CRP) was explored with the aim of subtly balancing entire pathway networks and potentially improving lycopene production without significant genetic intervention in other pathways.
The cAMP receptor protein (CRP) is a conserved regulator in bacteria and involved in regulation of energy metabolism, such as glucose, galactose, and citrate (Green et al., 2014 [1]).
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Moreover, A-kinase-anchoring proteins (AKAPs) and newly discovered cAMP receptors, Epac (exchange protein directly activated by cAMP), may give us a further chance to enter into new dimensions of cAMP signal transmissions that potentially may bring us closer to AHR physiology.
G protein-coupled receptors (GPCRs) have been grouped into five somewhat distinct families: one resembling rhodopsin, another identified with the secretin receptor, a class related to the metabotropic glutamate receptor, another to the fungal pheromone receptor, and a class of CAMP receptors.
cAMP receptors, such as Car1 that mediate the response to extracellular cAMP during aggregation belong to this family of proteins.
This membrane permeable cAMP analogue does not activate the extracellular cAMP receptors but enters the cells and directly activates cAMP-dependent protein kinase [22].
The cGMP-binding site of PKG and CNG channels has a threonine residue distinct from the cAMP receptors, and previous models based on the known structures of PKA and HCN channels have predicted that the hydroxyl group of these threonine residues interacts with the guanine 2-NH2 grofp of syn-cGMP through hydrogen bonds.
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