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Insights into the PPARR Phosphorylation and Its Inhibition Through Direct and Allosteric Mechanisms

https://doi.org/10.2139/ssrn.3205415

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Crystal Structure of the Peroxisome Proliferator-Activated Receptor γ (PPARγ) Ligand Binding Domain Complexed with a Novel Partial Agonist: A New Region of the Hydrophobic Pocket Could Be Exploited for Drug Design

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Structural Insight into Peroxisome Proliferator-Activated Receptor γ Binding of Two Ureidofibrate-Like Enantiomers by Molecular Dynamics, Cofactor Interaction Analysis, and Site-Directed Mutagenesis

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The PPARs: From Orphan Receptors to Drug Discovery

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Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators

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Anti-diabetic drugs inhibit obesity-linked phosphorylation of PPARγ by Cdk5

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Antidiabetic actions of a non-agonist PPARγ ligand blocking Cdk5-mediated phosphorylation

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An alternate binding site for PPARγ ligands

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PPARs and the complex journey to obesity

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A suite of oligomeric GFP variants

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Small-molecule ligand docking into comparative models with Rosetta

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Mechanistic elucidation guided by covalent inhibitors for the development of anti-diabetic PPARγ ligands

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Canonical sampling through velocity rescaling

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Tectonic controls on the long-term carbon isotope mass balance

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Fatty acids and eicosanoids regulate gene expression through direct interactions with peroxisome proliferator-activated receptors α and γ

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Insights into the Mechanism of Partial Agonism

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Giovanni Piemontese

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Hydrogen/deuterium‐exchange (H/D‐Ex) of PPARγ LBD in the presence of various modulators

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The Peroxisome Proliferator‐activated Receptors: Ligands and Activatorsa

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The Mechanisms of Action of PPARs

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Thiazolidinedione Use, Fluid Retention, and Congestive Heart Failure

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Risk of Fractures with Glitazones

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Reviewers

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The American Diabetes Association, the American Cancer Society, and the American Heart Association

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Structure and regulation of the CDK5-p25(nck5a) complex

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