Evidence map›Paper›PMID 16768454›Full record

ArticleBiochemistry2006

NMR analysis of Caenorhabditis elegans FLP-18 neuropeptides: implications for NPR-1 activation.

Aaron T Dossey, Vincenzina Reale, Heather Chatwin, Cherian Zachariah, Mario deBono, Peter D Evans, Arthur S Edison

Open access · greenAbstract readComparative Study
In one paragraph

Article in Biochemistry, 2006. 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
0.2field-weighted citation impact, top 56% 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. Nitric oxide suppresses cilia activity in ctenophores.bioRxiv : the preprint server for biology · 2023
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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

7 authors at 3 institutions in 2 countries.

Aaron T DosseyMcKnight Brain Institute, University of Florida, 100 South Newell Drive, Building 59, Room LG-150, Gainesville, Florida 32611, USA.
Vincenzina Reale
Heather Chatwin
Cherian Zachariah
Mario deBono
Peter D Evans
Arthur S Edison
MRC Laboratory of Molecular Biology · GBBabraham Institute · GBUniversity of Florida · US

Funding

SUSCEPTIBILITY CORRECTION INVESTIGATIONS AT HIGH FIELDP41RR016105 · NCRR · UNIVERSITY OF FLORIDA · PI SMITH, MIKE U. · 2001 to 2006
$5.7M
Medical Research Council MC_U105178786NCRR NIH HHS 5P41RR016105NCRR NIH HHS P41 RR016105
6 · The paper itself

Abstract

Phe-Met-Arg-Phe-NH2 (FMRFamide)-like peptides (FLPs) are the largest neuropeptide family in animals, particularly invertebrates. FLPs are characterized by a C-N-terminal gradient of decreasing amino acid conservation. Neuropeptide receptor 1 (NPR-1) is a G-protein coupled receptor (GPCR), which has been shown to be a strong regulator of foraging behavior and aggregation responses in Caenorhabditis elegans. Recently, ligands for NPR-1 were identified as neuropeptides coded by the precursor genes flp-18 and flp-21 in C. elegans. The flp-18 gene encodes eight FLPs including DFDGAMPGVLRF-NH2 and EMPGVLRF-NH2. These peptides exhibit considerably different activities on NPR-1, with the longer one showing a lower potency. We have used nuclear magnetic resonance and biological activity to investigate structural features that may explain these activity differences. Our data demonstrate that long-range electrostatic interactions exist between N-terminal aspartates and the C-terminal penultimate arginine as well as N-terminal hydrogen-bonding interactions that form transient loops within DFDGAMPGVLRF-NH2. We hypothesize that these loops, along with peptide charge, diminish the activity of this peptide on NPR-1 relative to that of EMPGVLRF-NH2. These results provide some insight into the large amino acid diversity in FLPs.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmino Acid SequenceAnimalsArginineAspartic AcidCaenorhabditis elegansCaenorhabditis elegans ProteinsConserved SequenceDose-Response Relationship, DrugFemaleGenes, HelminthHelminth ProteinsHydrogen BondingHydrogen-Ion ConcentrationMolecular Sequence DataNeuropeptidesArginineAspartic AcidCaenorhabditis elegans ProteinsHelminth ProteinsNeuropeptidesNPR-1 protein, C elegansReceptors, Neuropeptide Y

Identifiers

PMID16768454
PMCPMC2517133
OpenAlexW178021340

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.