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Regulation of signal transduction by -adrenergic hormone receptors

Ernst Helmreich, Thomas Pfeuffer

Open publisher page 6 citations

Abstract

Research on structure and function of ~-adrenergic receptors and its interactions with guanyl nucleotide binding proteins which activate or inhibit adenylate cyclase has progressed to the molecular level. The purification of all components of the signal transfer chain from ~-receptor to adenylate cyclase now allows the interaction of pure components to be studied in 'reconstituted' lipid vesicles.

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What this paper is about

Research on structure and function of ~-adrenergic receptors and its interactions with guanyl nucleotide binding proteins which activate or inhibit adenylate cyclase has progressed to the molecular level. The purification of all components of the signal transfer chain from ~-receptor to adenylate cyclase now allows the interaction of pure components to be studied in 'reconstituted' lipid vesicles.

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OpenAlex reports 6 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

Research on structure and function of ~-adrenergic receptors and its interactions with guanyl nucleotide binding proteins which activate or inhibit adenylate cyclase has progressed to the molecular level. The purification of all components of the signal transfer chain from ~-receptor to adenylate cyclase now allows the interaction of pure components to be studied in 'reconstituted' lipid vesicles.

Key concepts: Adenylate kinase, Cyclase, Receptor, Growth-hormone-releasing hormone receptor, Signal transduction, G protein-coupled receptor, Cell biology, Chemistry

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