diosgenin-glucoside and eglumetad

diosgenin-glucoside has been researched along with eglumetad* in 1 studies

*eglumetad: LY-354740 is the active isomer, LY-366563 is the inactive isomer, and LY 314582 is the racemate; structure given in first source [MeSH]

Other Studies

1 other study(ies) available for diosgenin-glucoside and eglumetad

Article	Year
Allosteric modulators enhance agonist efficacy by increasing the residence time of a GPCR in the active state. Nature communications, 2021, 09-14, Volume: 12, Issue:1 Much hope in drug development comes from the discovery of positive allosteric modulators (PAM) that display target subtype selectivity and act by increasing agonist potency and efficacy. How such compounds can allosterically influence agonist action remains unclear. Metabotropic glutamate receptors (mGlu) are G protein-coupled receptors that represent promising targets for brain diseases, and for which PAMs acting in the transmembrane domain have been developed. Here, we explore the effect of a PAM on the structural dynamics of mGlu2 in optimized detergent micelles using single molecule FRET at submillisecond timescales. We show that glutamate only partially stabilizes the extracellular domains in the active state. Full activation is only observed in the presence of a PAM or the G Topics: Allosteric Regulation; Allosteric Site; Amino Acids; Biphenyl Compounds; Bridged Bicyclo Compounds; Bridged Bicyclo Compounds, Heterocyclic; Catalytic Domain; Cell Membrane; Cholesterol Esters; Diosgenin; Disaccharides; Fluorescence Resonance Energy Transfer; Gene Expression; Glucosides; Glutamic Acid; Glycolipids; HEK293 Cells; Humans; Indans; Micelles; Octoxynol; Protein Binding; Protein Conformation; Protein Multimerization; Receptors, Metabotropic Glutamate; Recombinant Proteins; Single Molecule Imaging; Xanthenes	2021

Article

Year

Allosteric modulators enhance agonist efficacy by increasing the residence time of a GPCR in the active state.

Nature communications, 2021, 09-14, Volume: 12, Issue:1

Much hope in drug development comes from the discovery of positive allosteric modulators (PAM) that display target subtype selectivity and act by increasing agonist potency and efficacy. How such compounds can allosterically influence agonist action remains unclear. Metabotropic glutamate receptors (mGlu) are G protein-coupled receptors that represent promising targets for brain diseases, and for which PAMs acting in the transmembrane domain have been developed. Here, we explore the effect of a PAM on the structural dynamics of mGlu2 in optimized detergent micelles using single molecule FRET at submillisecond timescales. We show that glutamate only partially stabilizes the extracellular domains in the active state. Full activation is only observed in the presence of a PAM or the G

Topics: Allosteric Regulation; Allosteric Site; Amino Acids; Biphenyl Compounds; Bridged Bicyclo Compounds; Bridged Bicyclo Compounds, Heterocyclic; Catalytic Domain; Cell Membrane; Cholesterol Esters; Diosgenin; Disaccharides; Fluorescence Resonance Energy Transfer; Gene Expression; Glucosides; Glutamic Acid; Glycolipids; HEK293 Cells; Humans; Indans; Micelles; Octoxynol; Protein Binding; Protein Conformation; Protein Multimerization; Receptors, Metabotropic Glutamate; Recombinant Proteins; Single Molecule Imaging; Xanthenes

2021