Evidence map›Paper›PMID 28007963›Full record

ArticleThe Journal of biological chemistry2017

Interaction of p190A RhoGAP with eIF3A and Other Translation Preinitiation Factors Suggests a Role in Protein Biosynthesis.

Prasanna Parasuraman, Peter Mulligan, James A Walker, Bihua Li, Myriam Boukhali, Wilhelm Haas, Andre Bernards

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. 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
0.7field-weighted citation impact, top 25% 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, 22 citations in OpenAlex.

  1. Remodelled ribosomal populations synthesize a specific proteome in proliferating plant tissue during cold.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  2. Article
  3. Article
  4. Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022
    Review
  5. Article
  6. Article
  7. p190RhoGAPs, theCells · 2019
    Review
  8. 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 1 institution in 1 country.

Prasanna ParasuramanFrom the Massachusetts General Hospital Center for Cancer Research and Harvard Medical School, Charlestown, Massachusetts 02129.
Peter MulliganFrom the Massachusetts General Hospital Center for Cancer Research and Harvard Medical School, Charlestown, Massachusetts 02129.
James A WalkerFrom the Massachusetts General Hospital Center for Cancer Research and Harvard Medical School, Charlestown, Massachusetts 02129.
Bihua LiFrom the Massachusetts General Hospital Center for Cancer Research and Harvard Medical School, Charlestown, Massachusetts 02129.
Myriam BoukhaliFrom the Massachusetts General Hospital Center for Cancer Research and Harvard Medical School, Charlestown, Massachusetts 02129.
Wilhelm HaasFrom the Massachusetts General Hospital Center for Cancer Research and Harvard Medical School, Charlestown, Massachusetts 02129.
Andre BernardsFrom the Massachusetts General Hospital Center for Cancer Research and Harvard Medical School, Charlestown, Massachusetts 02129 abernards@partners.org.ORCID 0000-0001-6590-2337
Harvard University · US

Funding

Signal integration via phospho-regulation of RhoGAPsR01GM087386 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI BERNARDS, ANDRE · 2010 to 2013
$1.4M
NIGMS NIH HHS R01 GM087386
6 · The paper itself

Abstract

The negative regulator of Rho family GTPases, p190A RhoGAP, is one of six mammalian proteins harboring so-called FF motifs. To explore the function of these and other p190A segments, we identified interacting proteins by tandem mass spectrometry. Here we report that endogenous human p190A, but not its 50% identical p190B paralog, associates with all 13 eIF3 subunits and several other translational preinitiation factors. The interaction involves the first FF motif of p190A and the winged helix/PCI domain of eIF3A, is enhanced by serum stimulation and reduced by phosphatase treatment. The p190A/eIF3A interaction is unaffected by mutating phosphorylated p190A-Tyr

Indexed as

Protein BiosynthesisAnimalsChromatography, AffinityEukaryotic Initiation Factor-3Gene Knockdown TechniquesGuanine Nucleotide Exchange FactorsHeLa CellsHumansMiceMutation, MissenseNIH 3T3 CellsProtein BindingRepressor ProteinsSubcellular FractionsARHGAP35 protein, humanEIF3A protein, humanEukaryotic Initiation Factor-3Guanine Nucleotide Exchange FactorsRepressor Proteinscell biologyGTPase activating protein (GAP)mass spectrometry (MS)protein biosynthesisprotein complexesprotein domainsRho (Rho GTPase)translational initiationtranslation initranslation initiation factor

Identifiers

PMID28007963
PMCPMC5314166
OpenAlexW2567043124

What OpenQuestion holds

Textmetadata
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.