Evidence map›Paper›PMID 31877746›Full record

ArticleCells2019

Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology.

Mark Andrew White, Tamara Tsalkova, Fang C Mei, Xiaodong Cheng

Open access · goldAbstract read
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Protein SUMOylation promotes cAMP-independent EPAC1 activation.Cellular and molecular life sciences : CMLS · 2024
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
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

4 authors at 2 institutions in 1 country.

Mark Andrew WhiteSealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX 77555, USA.ORCID 0000-0003-1057-4203
Tamara TsalkovaDepartment of Pharmacology and Toxicology, The University of Texas Medical Branch, Galveston, TX 77555, USA.
Fang C MeiDepartment of Integrative Biology & Pharmacology, University of Texas Health Science Center at Houston, Houston, TX 77030, USA.
Xiaodong ChengDepartment of Integrative Biology & Pharmacology, University of Texas Health Science Center at Houston, Houston, TX 77030, USA.ORCID 0000-0002-3479-1694
The University of Texas Health Science Center at Houston · USThe University of Texas Medical Branch at Galveston · US

Funding

Preclinical Development of Novel Rickettsiosis Therapeutics Targeting EPAC1R01AI111464 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI CHENG, XIAODONG, WALKER, DAVID H · 2014 to 2018
$6.5M
Epac/cAMP-GEF, A Novel Intracellular cAMP ReceptorR01GM066170 · NIGMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI CHENG, XIAODONG · 2003 to 2017
$4.6M
Exchange Protein directly Activated by cAMP (EPAC): Structure, Function and TherapeuticsR35GM122536 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI CHENG, XIAODONG · 2017 to 2021
$1.9M
NIAID NIH HHS R01 AI111464NIGMS NIH HHS R01GM066170NIGMS NIH HHS R35 GM122536NIGMS NIH HHS R35GM122536
6 · The paper itself

Abstract

Exchange proteins directly activated by cAMP (EPAC1 and EPAC2) are important allosteric regulators of cAMP-mediated signal transduction pathways. To understand the molecular mechanism of EPAC activation, we performed detailed Small-Angle X-ray Scattering (SAXS) analysis of EPAC1 in its apo (inactive), cAMP-bound, and effector (Rap1b)-bound states. Our study demonstrates that we can model the solution structures of EPAC1 in each state using ensemble analysis and homology models derived from the crystal structures of EPAC2. The

Indexed as

Cyclic AMPCyclic AMP-Dependent Protein KinasesGuanine Nucleotide Exchange FactorsHumansProtein Bindingrap GTP-Binding ProteinsScattering, Small AngleSignal TransductionStructure-Activity RelationshipX-Ray DiffractionCyclic AMPCyclic AMP-Dependent Protein KinasesGuanine Nucleotide Exchange FactorsRAP1B protein, humanRAPGEF3 protein, humanrap GTP-Binding ProteinsEPAC1EPAC2guanine nucleotide exchange factorSmall-Angle X-ray Scattering (SAXS)

Identifiers

PMID31877746
PMCPMC7016869
OpenAlexW2995252055

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.