Pub. Date : 2015 Nov 27
PMID : 26370085
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Mechanism of cAMP Partial Agonism in Protein Kinase G (PKG). | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 2 | Mechanism of cAMP Partial Agonism in Protein Kinase G (PKG). | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 3 | Hence, the selective activation of PKG by cGMP versus cAMP is critical. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 4 | Although the C-terminal cyclic nucleotide-binding domain B of PKG binds cGMP with higher affinity than cAMP, the intracellular concentrations of cAMP are typically higher than those of cGMP, suggesting that the cGMP-versus-cAMP selectivity of PKG is not controlled uniquely through affinities. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 5 | Although the C-terminal cyclic nucleotide-binding domain B of PKG binds cGMP with higher affinity than cAMP, the intracellular concentrations of cAMP are typically higher than those of cGMP, suggesting that the cGMP-versus-cAMP selectivity of PKG is not controlled uniquely through affinities. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 6 | Although the C-terminal cyclic nucleotide-binding domain B of PKG binds cGMP with higher affinity than cAMP, the intracellular concentrations of cAMP are typically higher than those of cGMP, suggesting that the cGMP-versus-cAMP selectivity of PKG is not controlled uniquely through affinities. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 7 | Here, we show that cAMP is a partial agonist for PKG, and we elucidate the mechanism for cAMP partial agonism through the comparative NMR analysis of the apo, cGMP-, and cAMP-bound forms of the PKG cyclic nucleotide-binding domain B. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 8 | Here, we show that cAMP is a partial agonist for PKG, and we elucidate the mechanism for cAMP partial agonism through the comparative NMR analysis of the apo, cGMP-, and cAMP-bound forms of the PKG cyclic nucleotide-binding domain B. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 9 | Here, we show that cAMP is a partial agonist for PKG, and we elucidate the mechanism for cAMP partial agonism through the comparative NMR analysis of the apo, cGMP-, and cAMP-bound forms of the PKG cyclic nucleotide-binding domain B. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |
| 10 | Here, we show that cAMP is a partial agonist for PKG, and we elucidate the mechanism for cAMP partial agonism through the comparative NMR analysis of the apo, cGMP-, and cAMP-bound forms of the PKG cyclic nucleotide-binding domain B. | Cyclic AMP | protein kinase cGMP-dependent 1 | Homo sapiens |