Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10591602 | Bioorganic & Medicinal Chemistry Letters | 2014 | 4 Pages |
Abstract
The highly constitutively active G protein-coupled receptor US28 of human cytomegalovirus (HCMV) is thought to camouflage agonism by mediating constitutive endocytosis. With the use of the US28Î300 mutant, which is largely devoid of constitutive internalization, I have demonstrated that the coupling of the receptor to its downstream signaling partners is responsible for the inverse agonism to agonism efficacy switch in some small-weight ligands of US28.
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Authors
Nuska Tschammer,