Evidence map›Paper›PMID 25435400›Full record

ArticleTrends in biochemical sciences2015

Nuclear receptor full-length architectures: confronting myth and illusion with high resolution.

Fraydoon Rastinejad, Vincent Ollendorff, Igor Polikarpov

Abstract read
In one paragraph

Article in Trends in biochemical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed.

  1. Article
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  19. Farnesoid X receptor (FXR): Structures and ligands.Computational and structural biotechnology journal · 2021
    Review
  20. The PPARPPAR research · 2020
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Fraydoon RastinejadSanford-Burnham Medical Research Institute, Metabolic Disease Program, 6400 Sanger Road, Lake Nona, FL 32827, USA. Electronic address: frastinejad@sanfordburnham.org.
Vincent OllendorffINRA, UMR866 Dynamique Musculaire et Métabolisme, F-34060 Montpellier Université Montpellier 1, F-34000 Montpellier - Université Montpellier 2, F-34000 Montpellier, France.
Igor PolikarpovInstituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador São-Carlense, 400, São Carlos, SP, 13560-970, Brazil.

Funding

Identification of Allsoteric Ligands for Hepatic Nuclear Factor 4-alphaR01DK097475 · NIDDK · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RASTINEJAD, FRAYDOON · 2013 to 2015
$1.8M
Identification of Rev-Erb alpha/beta nuclear receptor modulatorsR01DK101520 · NIDDK · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RASTINEJAD, FRAYDOON · 2014 to 2016
$1.7M
Structural Characterization of Metabolic Gene RegulatorsR01DK094147 · NIDDK · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RASTINEJAD, FRAYDOON · 2011 to 2014
$1.7M
NIDDK NIH HHS R01 DK094147NIDDK NIH HHS R01 DK097475NIDDK NIH HHS R01 DK101520
6 · The paper itself

Abstract

The crystal structures of three nuclear receptor (NR) complexes have emerged to reveal their multidomain architectures on DNA. These pictures provide unprecedented views of interfacial couplings between the DNA-binding domains (DBDs) and ligand-binding domains (LBDs). The detailed pictures contrast with previous interpretations of low-resolution electron microscopy (EM) and small angle X-ray scattering (SAXS) data, which had suggested a common architecture with noninteracting DBDs and LBDs. Revisiting both historical and recent interpretations of NR architecture, we invoke new principles underlying higher-order quaternary organization and the allosteric transmission of signals between domains. We also discuss how NR architectures are being probed in living cells to understand dimerization and DNA-binding events in real time.

Indexed as

Protein ConformationProtein Structure, TertiaryBinding SitesCrystallography, X-RayDNADNA-Binding ProteinsLigandsMicroscopy, ElectronReceptors, Cytoplasmic and NuclearScattering, Small AngleStructure-Activity RelationshipDNADNA-Binding ProteinsLigandsReceptors, Cytoplasmic and NuclearallosteryBRETelectron microscopynuclear receptorSAXStranscription factorX-ray crystallography

Identifiers

PMID25435400
PMCPMC4274238

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.