Evidence map›Paper›PMID 30174148›Full record

ArticleStructure (London, England : 1993)2018

The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase.

Amy L Stiegler, Titus J Boggon

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    Review
  2. Review
  3. Article
  4. Review
  5. p190RhoGAPs, theCells · 2019
    Review
  6. Article
  7. PseudoGTPase domains in p190RhoGAP proteins: a mini-review.Biochemical Society transactions · 2018
    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

2 authors at 2 institutions in 1 country.

Amy L StieglerDepartment of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
Titus J BoggonDepartment of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA; Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA; Yale Cancer Center, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA. Electronic address: titus.boggon@yale.edu.
Yale Cancer Center · USYale University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structure-directed investigations into the regulation of Ste20 kinasesR01GM102262 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2012 to 2025
$4.2M
Molecular assembly and regulation of the cerebral cavernous malformation complexR01NS085078 · NINDS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, CALDERWOOD, DAVID A · 2013 to 2017
$1.8M
Upgrade of a home source macromolecular X-ray diffraction system.S10OD018007 · OD · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON · 2014 to 2014
$460k
NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM102262NIH HHS S10 OD018007NINDS NIH HHS R01 NS085078
6 · The paper itself

Abstract

The pseudoGTPases are a rapidly growing and important group of pseudoenzymes. p190RhoGAP proteins are critical regulators of Rho signaling and contain two previously identified pseudoGTPase domains. Here we report that p190RhoGAP proteins contain a third pseudoGTPase domain, termed N-GTPase. We find that GTP constitutively purifies with the N-GTPase domain, and a 2.8-Å crystal structure of p190RhoGAP-A co-purified with GTP reveals an unusual GTP-Mg

Indexed as

AnimalsBinding SitesCrystallography, X-RayDNA Mutational AnalysisGuanosine TriphosphateHumansMagnesiumModels, MolecularProtein DomainsProtein Structure, SecondaryPseudogenesRatsRepressor ProteinsArhgap35 protein, ratGuanosine TriphosphateMagnesiumRepressor ProteinsARHGAP35ARHGAP5crystal structurepseudoenzymePseudoGTPaseRho signaling

Identifiers

PMID30174148
PMCPMC6249675
OpenAlexW2889409114

What OpenQuestion holds

Textmetadata
LicenceTDM
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.