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Michael J. Garabedian

Researcher at University of California, San Francisco

Publications -  5
Citations -  853

Michael J. Garabedian is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Receptor & Glucocorticoid receptor. The author has an hindex of 5, co-authored 5 publications receiving 829 citations.

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Reduced levels of hsp90 compromise steroid receptor action in vivo

TL;DR: This work has taken advantage of the capacity of mammalian steroid receptors to function in yeast and constructed a strain of Saccharomyces cerevisiae in which hsp90 expression was regulatable and could be reduced more than 20-fold relative to wild type, providing the first biological evidence that hSp90 acts in the signal transduction pathway for steroid receptors.
Journal ArticleDOI

Modular Structure of Glucocorticoid Receptor Domains Is Not Equivalent to Functional Independence STABILITY AND ACTIVITY OF THE STEROID BINDING DOMAIN ARE CONTROLLED BY SEQUENCES IN SEPARATE DOMAINS

TL;DR: In this article, the exact boundaries of the steroid binding domain of glucocorticoid receptors have been examined with a variety of receptor deletion constructs, and it was shown that three independent regions appear to be required for the generation of the steroids binding form of receptors.
Journal ArticleDOI

Genetic Approaches to Mammalian Nuclear Receptor Function in Yeast

TL;DR: V vectors for the expression of mammalian receptors in yeast, reporter genes, yeast host strains, and simple assays that monitor receptor transcriptional activity are described.
Journal ArticleDOI

Glucocorticoid receptor phosphorylation in v-mos-transformed cells

TL;DR: It is shown here that GRs from v-mos-transformed cells are hyperphosphorylated on a specific peptide and maintain hormone-induced phosphorylations upon a prolonged hormone treatment that is associated with disruptions in its nucleocytoplasmic shuttling.
Patent

Super glucocorticoid receptors: receptors with increased affinity and specificity for glucocorticoid steriods

TL;DR: In this paper, the equivalent of the cysteine-656 of the rat glucocorticoid receptor was altered to either serine or glycine for the production of super-glucocyte receptors which retain full biological activity in intact cells and have higher affinity and specificity for glucoc corticoid steroid binding than the original receptor.