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Susan M. Fisher

Researcher at Bristol-Myers Squibb

Publications -  11
Citations -  735

Susan M. Fisher is an academic researcher from Bristol-Myers Squibb. The author has contributed to research in topics: Receptor & Binding site. The author has an hindex of 11, co-authored 11 publications receiving 702 citations.

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Cloning and functional expression of a cDNA encoding a human type 2 neuropeptide Y receptor.

TL;DR: NPY induced calcium mobilization and inhibited forskolin-stimulated cAMP accumulation in Chinese hamster ovary cells that stably express the Y2 receptors cDNA, indicating that the recombinant Y2 receptor is functionally coupled to second messenger systems.
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Bacillaene, a novel inhibitor of procaryotic protein synthesis produced by Bacillus subtilis: production, taxonomy, isolation, physico-chemical characterization and biological activity.

TL;DR: Bacillaene, a novel polyene antibiotic, was discovered and isolated from fermentation broths of a strain of Bacillus subtilis and indicates that the antibiotic is a bacteriostatic agent.
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Mutation of peptide binding site in transmembrane region of a G protein-coupled receptor accounts for endothelin receptor subtype selectivity.

TL;DR: Estimation of the wild-type and mutant ETA receptors in COS-7 cells revealed that the binding profile of one of the ETA mutants, Tyr129-->Ala, was characteristic of the ETB receptor, and these data represent the first example of peptide interactions with a transmembrane region of a G protein-coupled receptor and indicate that Tyr129 is a critical component for determination of endothelin receptor subtype-selective ligand binding.
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Molecular Genetic Analysis of a Human Neuropeptide Y Receptor THE HUMAN HOMOLOG OF THE MURINE “Y5” RECEPTOR MAY BE A PSEUDOGENE

TL;DR: The isolation, by low stringency homology cloning from a hypothalamic library, of a cDNA encoding the human homolog of the murine neuropeptide Y receptor is reported, indicating that this receptor subtype may be a transcribed pseudogene in humans.
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Aspartate mutation distinguishes ETA but not ETB receptor subtype-selective ligand binding while abolishing phospholipase C activation in both receptors.

TL;DR: Data support the hypothesis that Asp126 and Asp133 flanking Tyr129 in TM2 of the ETA receptor play a role in defining ETA subtype‐selective ligand binding but Asp147 and AsP154 that flank the His150 in TM 2 of the ETB receptor do not.