Evidence map›Paper›PMID 23189173›Full record

ArticlePloS one2012

Structural analyses of a constitutively active mutant of exchange protein directly activated by cAMP.

Mark A White, Sheng Li, Tamara Tsalkova, Fang C Mei, Tong Liu, Virgil L Woods, Xiaodong Cheng

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Cyclic AMP sensor EPAC proteins and energy homeostasis.Trends in endocrinology and metabolism: TEM · 2014
    Review
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

7 authors at 2 institutions in 1 country.

Mark A WhiteSealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, Texas, United States of America.
Sheng Li
Tamara Tsalkova
Fang C Mei
Tong Liu
Virgil L Woods
Xiaodong Cheng
The University of Texas Medical Branch at Galveston · USUniversity of California, San Diego · US

Funding

Synthetic Organic Chemistry CoreP30ES006676 · NIEHS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI ELFERINK, CORNELIS JOHAN · 1995 to 2017
$21.7M
ACTION OF LIPOLYTIC ENZYMESR01GM020501 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 1985 to 2020
$7.3M
Epac/cAMP-GEF, A Novel Intracellular cAMP ReceptorR01GM066170 · NIGMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI CHENG, XIAODONG · 2003 to 2017
$4.6M
Regulation, Signaling, and Dynamics of Glucan PhosphatasesR01NS070899 · NINDS · UNIVERSITY OF KENTUCKY · PI GENTRY, MATTHEW S. · 2010 to 2019
$3.6M
STRUCTURE DRIVEN ANALYSIS OF EBOLA VIRUS RECEPTOR BINDING SITER01AI081982 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI SAPHIRE, ERICA OLLMANN · 2010 to 2014
$2.8M
Current Generation Integrated Instrumentation for H-D Exchange LC-MSS10RR029388 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WOODS, VIRGIL L · 2010 to 2010
$1.0M
Sensitive Deuterium Exchange MS for Membrane ProteinsR01GM093325 · NIGMS · BECKMAN RESEARCH INSTITUTE/CITY OF HOPE · PI HANDEL, TRACY M, LEE, TERRY D. · 2010 to 2012
$965k
DESIGN OF AMPHIPHILIC PEPTOID ASSEMBLIESF32GM020501 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BURKOTH, TIMOTHY S · 2000 to 2002
$75k
NCRR NIH HHS RR029388NCRR NIH HHS S10 RR029388NIAID NIH HHS AI081982NIAID NIH HHS AI2008031NIAID NIH HHS R01 AI081982NIEHS NIH HHS ES06676NIEHS NIH HHS P30 ES006676NIGMS NIH HHS F32 GM020501NIGMS NIH HHS GM020501NIGMS NIH HHS GM066170NIGMS NIH HHS GM093325NIGMS NIH HHS R01 GM020501NIGMS NIH HHS R01 GM066170NIGMS NIH HHS R01 GM093325NINDS NIH HHS NS070899NINDS NIH HHS R01 NS070899
6 · The paper itself

Abstract

Exchange proteins directly activated by cAMP (EPACs) are important allosteric regulators of cAMP-mediated signal transduction pathways. To understand the molecular mechanism of EPAC activation, we have combined site-directed mutagenesis, X-ray crystallography, and peptide amide hydrogen/deuterium exchange mass spectrometry (DXMS) to probe the structural and conformational dynamics of EPAC2-F435G, a constitutively active EPAC2 mutant. Our study demonstrates that conformational dynamics plays a critical role in cAMP-induced EPAC activation. A glycine mutation at 435 position shifts the equilibrium of conformational dynamics towards the extended active conformation.

Indexed as

Catalytic DomainCrystallography, X-RayCyclic AMPDeuteriumGuanine Nucleotide Exchange FactorsHumansHydrogenModels, MolecularMutationProtein BindingProtein ConformationProtein Interaction Domains and MotifsCyclic AMPDeuteriumGuanine Nucleotide Exchange FactorsHydrogenRAPGEF3 protein, human

Identifiers

PMID23189173
PMCPMC3506601
OpenAlexW1979957714

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.