Evidence map›Paper›PMID 30581045›Full record

ArticleStructure (London, England : 1993)2019

A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain.

Yi Peng, Shufen Cao, Janna Kiselar, Xiangzhu Xiao, Zhanwen Du, An Hsieh, Soobin Ko, Yinghua Chen, Prashansa Agrawal, Wenwei Zheng and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
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

31 citing papers in PubMed, 48 citations in OpenAlex.

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  15. Incorporation of DThe journal of physical chemistry. B · 2022
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  19. Small, but powerful and attractive:Structure (London, England : 1993) · 2022
    Review
  20. Mechanism of RNA recognition by a Musashi RNA-binding protein.Current research in structural biology · 2022
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors at 4 institutions in 1 country.

Yi PengCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Shufen CaoDepartment of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Janna KiselarCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Xiangzhu XiaoDepartment of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Zhanwen DuCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
An HsiehCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Soobin KoCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Yinghua ChenDepartment of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Prashansa AgrawalChemistry-NMR Facility, Case Western Reserve University, Cleveland, OH 44106, USA.
Wenwei ZhengCollege of Integrative Sciences and Arts, Arizona State University, Mesa, AZ 85212, USA.
Wuxian ShiCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Wei JiangArgonne Leadership Computing Facility, Argonne National Laboratory, Lemont, IL 60439, USA.
Lin YangPhoton Sciences Directorate, Brookhaven National Laboratory, Upton, NY 11973, USA.
Mark R ChanceCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA; Case Comprehensive Cancer Center, Case Western Reserve University, Cleveland, OH 44106, USA.
Witold K SurewiczDepartment of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
Matthias BuckDepartment of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA; Case Comprehensive Cancer Center, Case Western Reserve University, Cleveland, OH 44106, USA.
Sichun YangCenter for Proteomics and Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA; Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA; Case Comprehensive Cancer Center, Case Western Reserve University, Cleveland, OH 44106, USA. Electronic address: sichun.yang@case.edu.
Case Western Reserve University · USArgonne National Laboratory · USArizona State University · USBrookhaven National Laboratory · US

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Development of high-dose time-resolved x-ray footprinting technologies to enable the next level of structural analysis for challenging biological problemsR01GM126218 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI RALSTON, CORIE Y · 2018 to 2025
$3.4M
Multifaceted Modeling of Estrogen ReceptorR01GM114056 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI YANG, SICHUN · 2015 to 2024
$3.3M
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS P30 GM133893NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM114056NIGMS NIH HHS R01 GM126218
6 · The paper itself

Abstract

The N-terminal transactivation domain (NTD) of estrogen receptor alpha, a well-known member of the family of intrinsically disordered proteins, mediates the receptor's transactivation function. However, an accurate molecular dissection of NTD's structure-function relationships remains elusive. Here, we show that the NTD adopts a mostly disordered, unexpectedly compact conformation that undergoes structural expansion on chemical denaturation. By combining small-angle X-ray scattering, hydroxyl radical protein footprinting, and computational modeling, we derive the ensemble-structures of the NTD and determine its ensemble-contact map revealing metastable long-range contacts, e.g., between residues I33 and S118. We show that mutation at S118, a known phosphorylation site, promotes conformational changes and increases coactivator binding. We further demonstrate via fluorine-19 (

Indexed as

MutationEstrogen Receptor alphaFluorine-19 Magnetic Resonance ImagingHumansIsoleucineModels, MolecularProtein BindingProtein ConformationProtein DomainsScattering, Small AngleSerineTranscriptional ActivationX-Ray DiffractionESR1 protein, humanEstrogen Receptor alphaIsoleucineSerinecontact metastabilityintrinsically disordered proteinmulti-technique data integrationprotein footprintingSAXSstructural disorder

Identifiers

PMID30581045
PMCPMC6365180
OpenAlexW2950763631

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.