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Thomsen1988_AdenylateCyclase_Inhibition


ABSTRACT: This model was created according to the paper Inhibition of Adenylate Cyclase Is Mediated by the High Affinity Conformation of the alpha2-Adrenergic Receptor published in 1988. The figure4 (steady state curve) in the paper has been simulated having the same plot with Copasi 4.0.19 (development) and roadRunner(online).Because the initial concentration of R and D were not given in the paper ,so we gave it 1e-9 Mol/L and 1e-8 Mol/L respectively. Pay attention that the simulations of steady state concentration of species in arbitrary units are shown for figure4 and figure6 in the paper.

SUBMITTER: Enuo He  

PROVIDER: BIOMD0000000082 | BioModels | 2006-09-26

REPOSITORIES: BioModels

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Inhibition of adenylate cyclase is mediated by the high affinity conformation of the alpha 2-adrenergic receptor.

Thomsen W J WJ   Jacquez J A JA   Neubig R R RR  

Molecular pharmacology 19881201 6


The functional significance of high affinity agonist binding to receptors that interact with guanine nucleotide regulatory proteins has remained controversial. Preincubation of human platelet membranes with the full alpha 2-agonist UK 14,304 in the absence of GTP increases the potency of the agonist to inhibit adenylate cyclase in a pre-steady state (15-sec) assay. The EC50 after preincubation (6 +/- 1 nM) is within a factor of 2 of the high affinity Kd for [3H]UK 14,304 binding determined under  ...[more]

Publication: 1/3

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