ArticleACS chemical biology2016
SR2067 Reveals a Unique Kinetic and Structural Signature for PPARγ Partial Agonism.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 35 citations in OpenAlex.
- Network Pharmacology and Molecular Docking Approach to Identify and Investigate the Mechanisms of Active Components of Areca Catechu in Relation to Gut Disorders.Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH · 2025Article
- HIt Discovery using docking ENriched by GEnerative Modeling (HIDDEN GEM): A novel computational workflow for accelerated virtual screening of ultra-large chemical libraries.Molecular informatics · 2024Article
- Discovery by Virtual Screening of an Inhibitor of CDK5-Mediated PPARγ Phosphorylation.ACS medicinal chemistry letters · 2022Article
- Structural mechanism underlying ligand binding and activation of PPARγ.Structure (London, England : 1993) · 2021Article
- A Novel N-Substituted Valine Derivative with Unique Peroxisome Proliferator-Activated Receptor γ Binding Properties and Biological Activities.Journal of medicinal chemistry · 2020Article
- Deep Docking: A Deep Learning Platform for Augmentation of Structure Based Drug Discovery.ACS central science · 2020Article
- Type II diabetes mellitus and obesity: Common links, existing therapeutics and future developments.Journal of biosciences · 2019Article
- PPARγ in Complex with an Antagonist and Inverse Agonist: a Tumble and Trap Mechanism of the Activation Helix.iScience · 2018Article
- Structural and Dynamic Elucidation of a Non-acid PPARNuclear receptor research · 2018Article
- Article
- Structure-Activity Relationship of 2,4-Dichloro-N-(3,5-dichloro-4-(quinolin-3-yloxy)phenyl)benzenesulfonamide (INT131) Analogs for PPARγ-Targeted Antidiabetics.Journal of medicinal chemistry · 2017Article
- Sanggenol F exerts anti-diabetic effects via promoting adipocyte differentiation and modifying adipokines expression.Endocrine · 2017Article
- Investigations on Binding Pattern of Kinase Inhibitors with PPARPPAR research · 2017Article
- Structural basis for PPAR partial or full activation revealed by a novel ligand binding mode.Scientific reports · 2016Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Synthetic full agonists of PPARγ have been prescribed for the treatment of diabetes due to their ability to regulate glucose homeostasis and insulin sensitization. While the use of full agonists of PPARγ has been hampered due to severe side effects, partial agonists have shown promise due to their decreased incidence of such side effects in preclinical models. No kinetic information has been forthcoming in regard to the mechanism of full versus partial agonism of PPARγ to date. Here, we describe the discovery of a partial agonist, SR2067. A co-crystal structure obtained at 2.2 Å resolution demonstrates that interactions with the β-sheet are driven exclusively via hydrophobic interactions mediated through a naphthalene group, an observation that is unique from other partial agonists. Surface plasmon resonance revealed that SR2067 binds to the receptor with higher affinity (KD = 513 nM) as compared to that of full agonist rosiglitazone, yet it has a much slower off rate compared to that of rosiglitazone.
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