Evidence map›Paper›PMID 24909783›Full record

ArticleStructure (London, England : 1993)2014

Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry.

Devrishi Goswami, Celetta Callaway, Bruce D Pascal, Raj Kumar, Dean P Edwards, Patrick R Griffin

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Devrishi GoswamiDepartment of Molecular Therapeutics, The Scripps Research Institute, Jupiter, FL 33458, USA.
Celetta CallawayDepartments of Molecular and Cellular Biology and Pathology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Bruce D PascalDepartment of Molecular Therapeutics, The Scripps Research Institute, Jupiter, FL 33458, USA.
Raj KumarDepartment of Basic Sciences, The Commonwealth Medical College, Scranton, PA 18510, USA.
Dean P EdwardsDepartments of Molecular and Cellular Biology and Pathology and Immunology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Patrick R GriffinDepartment of Molecular Therapeutics, The Scripps Research Institute, Jupiter, FL 33458, USA. Electronic address: pgriffin@scripps.edu.
Scripps Research Institute · USBaylor College of Medicine · USCommonwealth Medical College · US

Funding

PROGESTERONE RECEPTOR INTERACTIONR01CA046938 · NCI · UNIVERSITY OF COLORADO DENVER · PI EDWARDS, DEAN P · 1988 to 2013
$3.3M
Development of H/D exchange technology for the study of large protein complexesR01GM084041 · NIGMS · SCRIPPS FLORIDA · PI GRIFFIN, PATRICK ROBERT · 2009 to 2012
$1.6M
Acquisition of a LTQ/Orbitrap MS to advance the study of protein dynamicsS10RR027270 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI GRIFFIN, PATRICK ROBERT · 2010 to 2010
$500k
NCI NIH HHS CA046938NCI NIH HHS P30CA123125NCI NIH HHS R01 CA046938NCRR NIH HHS S10 RR027270NIGMS NIH HHS GM84041NIGMS NIH HHS R01 GM084041
6 · The paper itself

Abstract

Structural and functional details of the N-terminal activation function 1 (AF1) of most nuclear receptors are poorly understood due to the highly dynamic intrinsically disordered nature of this domain. A hydrogen/deuterium exchange (HDX) mass-spectrometry-based investigation of TATA box-binding protein (TBP) interaction with various domains of progesterone receptor (PR) demonstrate that agonist-bound PR interaction with TBP via AF1 impacts the mobility of the C-terminal AF2. Results from HDX and other biophysical studies involving agonist- and antagonist-bound full-length PR and isolated PR domains reveal the molecular mechanism underlying synergistic transcriptional activation mediated by AF1 and AF2, dominance of PR-B isoform over PR-A, and the necessity of AF2 for full AF1-mediated transcriptional activity. These results provide a comprehensive picture elaborating the underlying mechanism of PR-TBP interactions as a model for studying nuclear receptor (NR)-transcription factor functional interactions.

Indexed as

Protein ConformationProtein Structure, TertiaryAmino Acid SequenceAnimalsDeuterium Exchange MeasurementHumansLigandsMass SpectrometryMifepristoneModels, MolecularMolecular Sequence DataPromegestoneProtein BindingReceptors, Cytoplasmic and NuclearReceptors, ProgesteroneSf9 CellsLigandsMifepristonePromegestoneReceptors, Cytoplasmic and NuclearReceptors, ProgesteroneTATA-Box Binding ProteinTBP protein, human

Identifiers

PMID24909783
PMCPMC4393884
OpenAlexW2043496549

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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.