Evidence map›Paper›PMID 31838952›Full record

ArticleJournal of biomolecular structure & dynamics2020

An atypical heterotrimeric Gα protein has substantially reduced nucleotide binding but retains nucleotide-independent interactions with its cognate RGS protein and Gβγ dimer.

Fei Lou, Tigran M Abramyan, Haiyan Jia, Alexander Tropsha, Alan M Jones

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular structure & dynamics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
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  5. Review
  6. An atypical heterotrimeric Gα and its interactome suggest an extra-large role in overcoming abiotic and biotic stress.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. 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

5 authors at 1 institution in 1 country.

Fei LouDepartments of Pharmacology, University of North Carolina at Chapel Hill, NC, USA.
Tigran M AbramyanDivision of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, NC, USA.
Haiyan JiaDepartments of Pharmacology, University of North Carolina at Chapel Hill, NC, USA.
Alexander TropshaDivision of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, NC, USA.
Alan M JonesDepartments of Pharmacology, University of North Carolina at Chapel Hill, NC, USA.ORCID http://orcid.org/0000-0002-2365-6462
University of North Carolina at Chapel Hill · US

Funding

Novel Mechanisms Regulating the Heterotrimeric G Protein ComplexR01GM065989 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JONES, ALAN M. · 2002 to 2023
$5.5M
NIGMS NIH HHS R01 GM065989
6 · The paper itself

Abstract

Plants uniquely have a family of proteins called extra-large G proteins (XLG) that share homology in their C-terminal half with the canonical Gα subunits; we carefully detail here that Arabidopsis XLG2 lacks critical residues requisite for nucleotide binding and hydrolysis which is consistent with our quantitative analyses. Based on microscale thermophoresis, Arabidopsis XLG2 binds GTPγS with an affinity 100 times lower than that to canonical Gα subunits. This means that given the concentration range of guanine nucleotide in plant cells, XLG2 is not likely bound by GTP

Indexed as

ArabidopsisArabidopsis ProteinsRGS ProteinsNucleotidesProtein BindingSignal TransductionArabidopsis ProteinsNucleotidesRGS ProteinsAGB1ArabidopsisAtGPA1AtRGS1dominant negative G alphaextra-large G proteinGβγXLG2

Identifiers

PMID31838952
PMCPMC7308192
OpenAlexW2996672878

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.