Evidence map›Paper›PMID 24997265›Full record

ArticleNeuroscience2014

Functional characterization of G-protein-coupled receptors: a bioinformatics approach.

L Tovo-Rodrigues, A Roux, M H Hutz, L A Rohde, A S Woods

Abstract read
In one paragraph

Article in Neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

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  9. Functions of intrinsic disorder in transmembrane proteins.Cellular and molecular life sciences : CMLS · 2017
    Review
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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.

L Tovo-RodriguesDepartment of Genetics, Federal University of Rio Grande do Sul, Porto Alegre, RS, Brazil; Structural Biology Unit, Integrative Neuroscience Branch, NIDA IRP, NIH, MD, United States.
A RouxStructural Biology Unit, Integrative Neuroscience Branch, NIDA IRP, NIH, MD, United States.
M H HutzDepartment of Genetics, Federal University of Rio Grande do Sul, Porto Alegre, RS, Brazil.
L A RohdeChild and Adolescent Psychiatric Division, Department of Psychiatry, Federal University of Rio Grande do Sul, Porto Alegre, RS, Brazil.
A S WoodsStructural Biology Unit, Integrative Neuroscience Branch, NIDA IRP, NIH, MD, United States. Electronic address: awoods@mail.nih.gov.
Universidade Federal do Rio Grande do Sul · BR

Funding

Methodology development to map and quantify imaged molecules in brain tissueZIADA000593 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI WOODS, AMINA · 2013 to 2019
$3.5M
Demonstration of the specificity of receptor receptor interactionZIADA000594 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI WOODS, AMINA · 2015 to 2020
$1.8M
Brain lipids changes in controlled Cortical impactZIADA000589 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI WOODS, AMINA · 2013 to 2017
$1.2M
Intramural NIH HHS ZIA DA000589
6 · The paper itself

Abstract

Complex molecular and cellular mechanisms regulate G protein-coupled receptors (GPCRs). It is suggested that proteins intrinsically disordered regions (IDRs) are to play a role in GPCR's intra and extracellular regions plasticity, due to their potential for post-translational modification and interaction with other proteins. These regions are defined as lacking a stable three-dimensional (3D) structure. They are rich in hydrophilic and charged, amino acids and are capable to assume different conformations which allow them to interact with multiple partners. In this study we analyzed 75 GPCR involved in synaptic transmission using computational tools for sequence-based prediction of IDRs within a protein. We also evaluated putative ligand-binding motifs using receptor sequences. The disorder analysis indicated that neurotransmitter GPCRs have a significant amount of disorder in their N-terminus, third intracellular loop (3IL) and C-terminus. About 31%, 39% and 53% of human GPCR involved in synaptic transmission are disordered in these regions. Thirty-three percent of receptors show at least one predicted PEST motif, this being statistically greater than the estimate for the rest of human GPCRs. About 90% of the receptors had at least one putative site for dimerization in their 3IL or C-terminus. ELM instances sampled in these domains were 14-3-3, SH3, SH2 and PDZ motifs. In conclusion, the increased flexibility observed in GPCRs, added to the enrichment of linear motifs, PEST and heteromerization sites, may be critical for the nervous system's functional plasticity.

Indexed as

Binding SitesComputational BiologyDimerizationHumansProtein ConformationReceptors, G-Protein-CoupledSynaptic TransmissionReceptors, G-Protein-Coupleddisordered proteinsGPCRlinear motifsnoncovalent interactionspest motifs

Identifiers

PMID24997265
PMCPMC4164567
OpenAlexW2054480635

What Socratic 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 Socratic graph.