Evidence map›Paper›PMID 28880079›Full record

ArticleBiochemistry2017

Quantitative Multiple-Reaction Monitoring Proteomic Analysis of Gβ and Gγ Subunits in C57Bl6/J Brain Synaptosomes.

Yun Young Yim, W Hayes McDonald, Karren Hyde, Osvaldo Cruz-Rodríguez, John J G Tesmer, Heidi E Hamm

Abstract read
In one paragraph

Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Statins Perturb GMolecular pharmacology · 2019
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. GPCR regulation of secretion.Pharmacology & therapeutics · 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

6 authors.

Yun Young YimDepartment of Pharmacology, Vanderbilt University , Nashville, Tennessee 37232-6600, United States.ORCID 0000-0002-0061-6820
W Hayes McDonaldDepartment of Biochemistry, Vanderbilt University , Nashville, Tennessee 37232-6600, United States.
Karren HydeDepartment of Pharmacology, Vanderbilt University , Nashville, Tennessee 37232-6600, United States.
Osvaldo Cruz-Rodríguez
John J G Tesmer
Heidi E HammDepartment of Pharmacology, Vanderbilt University , Nashville, Tennessee 37232-6600, United States.

Funding

TRAINING IN PHARMACOLOGICAL SCIENCEST32GM007628 · NIGMS · VANDERBILT UNIVERSITY · PI BARNETT, JOEY VICTOR, KAVALALI, EGE T · 1985 to 2022
$11.2M
Structure, function, and inhibition of G protein-coupled receptor kinasesR01HL071818 · NHLBI · UNIVERSITY OF TEXAS AUSTIN · PI TESMER, JOHN · 2004 to 2023
$7.1M
MICHIGAN CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008597 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MONTGOMERY, JOHN · 1996 to 2018
$5.0M
G PROTEIN STRUCTURE/FUNCTIONR01EY010291 · NEI · VANDERBILT UNIVERSITY · PI HAMM, HEIDI E · 1994 to 2010
$3.9M
Structure and Function of the LPLA2/LCAT Acyltransferase FamilyR01HL122416 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESMER, JOHN · 2015 to 2018
$1.9M
GPCR Regulation of insulin secretion by modulation of the release machineryR01DK109204 · NIDDK · VANDERBILT UNIVERSITY · PI HAMM, HEIDI E · 2016 to 2019
$1.4M
Optimization of modulators of Gbg-SNARE interactionR01MH101679 · NIMH · VANDERBILT UNIVERSITY · PI HAMM, HEIDI E, STAUFFER, SHAUN R · 2014 to 2016
$1.2M
NEI NIH HHS R01 EY010291NHLBI NIH HHS R01 HL071818NHLBI NIH HHS R01 HL122416NIDDK NIH HHS R01 DK109204NIGMS NIH HHS T32 GM007628NIGMS NIH HHS T32 GM008597NIMH NIH HHS R01 MH101679
6 · The paper itself

Abstract

Gβγ dimers are one of the essential signaling units of activated G protein-coupled receptors (GPCRs). There are five Gβ and 12 Gγ subunits in humans; numerous studies have demonstrated that different Gβ and Gγ subunits selectively interact to form unique Gβγ dimers, which in turn may target specific receptors and effectors. Perturbation of Gβγ signaling can lead to impaired physiological responses. Moreover, previous targeted multiple-reaction monitoring (MRM) studies of Gβ and Gγ subunits have shown distinct regional and subcellular localization patterns in four brain regions. Nevertheless, no studies have quantified or compared their individual protein levels. In this study, we have developed a quantitative MRM method not only to quantify but also to compare the protein abundance of neuronal Gβ and Gγ subunits. In whole and fractionated crude synaptosomes, we were able to identify the most abundant neuronal Gβ and Gγ subunits and their subcellular localizations. For example, Gβ

Indexed as

ProteomicsAmino Acid SequenceAnimalsBrainGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsMiceMice, Inbred C57BLProtein MultimerizationProtein Structure, QuaternaryProtein TransportSynaptosomesGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma Subunits

Identifiers

PMID28880079
PMCPMC5769682

What OpenQuestion holds

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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.