PPARγ helix 12 exhibits an antagonist conformation.

about

PPARγ non-covalent antagonists exhibit mutable binding modes with a similar free energy of binding: a case study.A structural mechanism for directing corepressor-selective inverse agonism of PPARγ

P2860

Q51526335-085C2F61-D76F-41DC-A255-5908B00D2170 Q58586525-6F7ECEB6-9694-4E0F-9662-C340E61D0DE6

P2860

PPARγ helix 12 exhibits an antagonist conformation.

Item

http://www.wikidata.org/entity/Q51445412

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

PPARγ helix 12 exhibits an antagonist conformation.

@en

PPARγ helix 12 exhibits an antagonist conformation.

@nl

type

Item

label

PPARγ helix 12 exhibits an antagonist conformation.

@en

PPARγ helix 12 exhibits an antagonist conformation.

@nl

prefLabel

PPARγ helix 12 exhibits an antagonist conformation.

@en

PPARγ helix 12 exhibits an antagonist conformation.

@nl

P1476

PPARγ helix 12 exhibits an antagonist conformation.

@en

P2860

Convergence and reproducibility in molecular dynamics simulations of the DNA duplex d(GCACGAACGAACGAACGC)

Well-Tempered Metadynamics: A Smoothly Converging and Tunable Free-Energy Method

Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha

Partial agonists activate PPARgamma using a helix 12 independent mechanism

Prediction of the tissue-specificity of selective estrogen receptor modulators by using a single biochemical method

Structural basis for the activation of PPARgamma by oxidized fatty acids

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 conformations

Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes

Improved Reweighting of Accelerated Molecular Dynamics Simulations for Free Energy Calculation.

Escaping free-energy minima.

P304

9272-9280

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1039/C5CP06729D

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Filip Fratev

P577

2016-03-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

26975214

http://www.w3.org/2001/XMLSchema#string

PPARγ helix 12 exhibits an antagonist conformation.

about

P2860

P2860

PPARγ helix 12 exhibits an antagonist conformation.

description

name

type

label

prefLabel

P1433

P1476

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698