PPARγ helix 12 exhibits an antagonist conformation

scientific article published on 15 March 2016

PPARγ helix 12 exhibits an antagonist conformation is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1039/C5CP06729D
P698PubMed publication ID26975214

P50authorFilip FratevQ44609835
P2860cites workConvergence and reproducibility in molecular dynamics simulations of the DNA duplex d(GCACGAACGAACGAACGC)Q27332083
Well-Tempered Metadynamics: A Smoothly Converging and Tunable Free-Energy MethodQ27336076
Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalphaQ27637763
Partial agonists activate PPARgamma using a helix 12 independent mechanismQ27648786
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Peroxisome proliferator-activated receptor gamma (PPARγ) has multiple binding points that accommodate ligands in various conformations: Structurally similar PPARγ partial agonists bind to PPARγ LBD in different conformationsQ27700925
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Force-Field Induced Bias in the Structure of Aβ21-30: A Comparison of OPLS, AMBER, CHARMM, and GROMOS Force FieldsQ40249851
Structural and Dynamical Insight into PPARγ Antagonism: In Silico Study of the Ligand-Receptor Interactions of Non-Covalent AntagonistsQ40726727
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Dynamics of nuclear receptor Helix-12 switch of transcription activation by modeling time-resolved fluorescence anisotropy decaysQ42031668
Hydrogen/deuterium-exchange (H/D-Ex) of PPARgamma LBD in the presence of various modulatorsQ42237982
Structural design and synthesis of arylalkynyl amide-type peroxisome proliferator-activated receptor γ (PPARγ)-selective antagonists based on the helix12-folding inhibition hypothesisQ42469523
The phosphorylation specificity of B-RAF WT, B-RAF D594V, B-RAF V600E and B-RAF K601E kinases: an in silico study.Q43186762
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PPARγ non-covalent antagonists exhibit mutable binding modes with a similar free energy of binding: a case studyQ51526335
P433issue13
P407language of work or nameEnglishQ1860
P304page(s)9272-9280
P577publication date2016-03-15
P1433published inPhysical Chemistry Chemical PhysicsQ3018671
P1476titlePPARγ helix 12 exhibits an antagonist conformation
P478volume18

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cites work (P2860)
Q58586525A structural mechanism for directing corepressor-selective inverse agonism of PPARγ
Q51526335PPARγ non-covalent antagonists exhibit mutable binding modes with a similar free energy of binding: a case study
Q92935598Prediction of Accurate Binding Modes Using Combination of Classical and Accelerated Molecular Dynamics and Free-Energy Perturbation Calculations: An Application to Toxicity Studies

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