Evidence map›Paper›PMID 31606074›Full record

ArticleMethods in enzymology2019

Isolation and characterization of glycosylated neuropeptides.

Yang Liu, Qinjingwen Cao, Lingjun Li

Abstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Proteomics techniques in protein biomarker discovery.Quantitative biology (Beijing, China) · 2024
    Review
  3. Review
  4. Article
  5. Mass Spectrometric Profiling of Neuropeptides inACS chemical neuroscience · 2020
    Article
  6. 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

3 authors.

Yang LiuDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI, United States.
Qinjingwen CaoDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI, United States.
Lingjun LiDepartment of Chemistry, University of Wisconsin-Madison, Madison, WI, United States; School of Pharmacy, University of Wisconsin-Madison, Madison, WI, United States. Electronic address: lingjun.li@wisc.edu.

Funding

Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
Di-Leu-enabled multiplexed quantitation for biomarker discovery and validation in Alzheimer's diseaseRF1AG052324 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2018 to 2018
$2.4M
MULTIPLEX CHEMICAL TAGS FOR HIGH-THROUGHPUT GLYCAN AND GLYCOPEPTIDE QUANTITATION AND CHARACTERIZATIONU01CA231081 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI LI, LINGJUN · 2018 to 2020
$1.3M
NCI NIH HHS U01 CA231081NIA NIH HHS RF1 AG052324NIDDK NIH HHS R01 DK071801
6 · The paper itself

Abstract

Glycosylation is one of the most ubiquitous and complex post-translational modifications (PTMs). It plays pivotal roles in various biological processes. Studies at the glycopeptide level are typically considered as a downstream work resulting from enzymatic digested glycoproteins. Less attention has been focused on glycosylated endogenous signaling peptides due to their low abundance, structural heterogeneity and the lack of enabling analytical tools. Here, protocols are presented to isolate and characterize glycosylated neuropeptides utilizing nanoflow liquid chromatography coupled with mass spectrometry (LC-MS). We first demonstrate how to extract neuropeptides from raw tissues and perform further separation/cleanup before MS analysis. Then we describe hybrid MS methods for glycosylated neuropeptide profiling and site-specific analysis. We also include recommendations for data analysis to identify glycosylated neuropeptides in crustaceans where a complete neuropeptide database is still lacking. Other strategies and future directions are discussed to provide readers with alternative approaches and further unravel biological complexity rendered by glycosylation.

Indexed as

AnimalsChromatography, LiquidGlycopeptidesGlycosylationHumansIsomerismMass SpectrometryModels, MolecularNeuropeptidesPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryGlycopeptidesNeuropeptidesPolysaccharidesCharacterizationDerivatizationEnrichmentESIEThcDGlycopeptideGlycosylationLC-MS/MSMALDISeparation

Identifiers

PMID31606074
PMCPMC7170398

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.