Evidence map›Paper›PMID 35723467›Full record

ArticleJournal of visualized experiments : JoVE2022

Multi-Faceted Mass Spectrometric Investigation of Neuropeptides in Callinectes sapidus.

Ashley Phetsanthad, Nhu Q Vu, Lingjun Li

Open access · greenAbstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 57% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

3 authors at 1 institution in 1 country.

Ashley Phetsanthad *Department of Chemistry, University of Wisconsin-Madison.
Nhu Q Vu *Department of Chemistry, University of Wisconsin-Madison.
Lingjun LiDepartment of Chemistry, University of Wisconsin-Madison; School of Pharmacy, University of Wisconsin-Madison; lingjun.li@wisc.edu.
University of Wisconsin–Madison · US

Funding

Training Program in Translational Cardiovascular Science (TPTCS)T32HL007936 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Lee Lochbaum Eckhardt, Gail A Robertson · 2001 to 2026
$11.6M
Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Biotechnology Training ProgramT32GM135066 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI SCOTT M. COYLE, BRIAN G FOX · 2020 to 2026
$7.0M
Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
Acquisition of a High-Field Dual Source FTICR-MS for Pharmaceutical ResearchS10RR029531 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2011 to 2011
$2.1M
In Situ Protein Characterization and Visualization in the Brains of Mouse Models for AutismR56MH110215 · NIMH · UNIVERSITY OF WISCONSIN-MADISON · PI IKONOMIDOU, HRISSANTHI, LI, LINGJUN · 2017 to 2018
$752k
Acquisition of a High Resolution High Speed MALDI Mass Spectrometer for Biomedical Research at UW-MadisonS10OD025084 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2018 to 2018
$598k
NCRR NIH HHS S10 RR029531NHLBI NIH HHS T32 HL007936NIDDK NIH HHS R01 DK071801NIGMS NIH HHS T32 GM008505NIGMS NIH HHS T32 GM135066NIH HHS S10 OD025084NIMH NIH HHS R56 MH110215
6 · The paper itself

Abstract

Neuropeptides are signaling molecules that regulate almost all physiological and behavioral processes, such as development, reproduction, food intake, and response to external stressors. Yet, the biochemical mechanisms and full complement of neuropeptides and their functional roles remain poorly understood. Characterization of these endogenous peptides is hindered by the immense diversity within this class of signaling molecules. Additionally, neuropeptides are bioactive at concentrations 100x - 1000x lower than that of neurotransmitters and are prone to enzymatic degradation after synaptic release. Mass spectrometry (MS) is a highly sensitive analytical tool that can identify, quantify, and localize analytes without comprehensive a priori knowledge. It is well-suited for globally profiling neuropeptides and aiding in the discovery of novel peptides. Due to the low abundance and high chemical diversity of this class of peptides, several sample preparation methods, MS acquisition parameters, and data analysis strategies have been adapted from proteomics techniques to allow optimal neuropeptide characterization. Here, methods are described for isolating neuropeptides from complex biological tissues for sequence characterization, quantitation, and localization using liquid chromatography (LC)-MS and matrix-assisted laser desorption/ionization (MALDI)-MS. A protocol for preparing a neuropeptide database from the blue crab, Callinectes sapidus, an organism without comprehensive genomic information, is included. These workflows can be adapted to study other classes of endogenous peptides in different species using a variety of instruments.

Indexed as

BrachyuraNeuropeptidesAnimalsChromatography, LiquidPeptidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationNeuropeptidesPeptides

Identifiers

PMID35723467
PMCPMC9306302
OpenAlexW4283221437

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.