Structural Analysis of the Glucocorticoid Receptor Ligand-Binding Domain in Complex with Triamcinolone Acetonide and a Fragment of the Atypical Coregulator, Small Heterodimer Partner.

about

Nucleotide Binding to ARL2 in the TBCD∙ARL2∙β-Tubulin Complex Drives Conformational Changes in β-Tubulin.Preclinical pharmacology of AZD9977: A novel mineralocorticoid receptor modulator separating organ protection from effects on electrolyte excretion.

P2860

Q47712841-3716BF86-469F-49B2-81DF-A1DD74883D3D Q52688314-0E7B5CD2-A8B2-4CB3-AD90-5337797B9A58

P2860

Structural Analysis of the Glucocorticoid Receptor Ligand-Binding Domain in Complex with Triamcinolone Acetonide and a Fragment of the Atypical Coregulator, Small Heterodimer Partner.

Item

http://www.wikidata.org/entity/Q38843487

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

Structural Analysis of the Glu ...... or, Small Heterodimer Partner.

@en

type

Item

label

Structural Analysis of the Glu ...... or, Small Heterodimer Partner.

@en

prefLabel

Structural Analysis of the Glu ...... or, Small Heterodimer Partner.

@en

P1476

Structural Analysis of the Glu ...... or, Small Heterodimer Partner.

@en

P2093

C Denise Okafor

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

Emily R Weikum

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

Emma H D'Agostino

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

Jennifer K Colucci

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

P2860

A transcriptional inhibitor targeted by the atypical orphan nuclear receptor SHP

Modulation of human nuclear receptor LRH-1 activity by phospholipids and SHP

The orphan nuclear receptor SHP utilizes conserved LXXLL-related motifs for interactions with ligand-activated estrogen receptors

The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Crystal structure of an ancient protein: evolution by conformational epistasis

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Processing of X-ray diffraction data collected in oscillation mode

Glucocorticoid receptor signaling in health and disease

Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

P304

12-21

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

P31

scholarly article

P356

10.1124/MOL.117.108506

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

P433

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

P478

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

P50

Eric A. Ortlund

P577

2017-04-10T00:00:00Z

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

P698

28396564

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

P921

ligand binding

P932

5452056

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

Structural Analysis of the Glucocorticoid Receptor Ligand-Binding Domain in Complex with Triamcinolone Acetonide and a Fragment of the Atypical Coregulator, Small Heterodimer Partner.

about

P2860

P2860

Structural Analysis of the Glucocorticoid Receptor Ligand-Binding Domain in Complex with Triamcinolone Acetonide and a Fragment of the Atypical Coregulator, Small Heterodimer Partner.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932