Evidence map›Paper›PMID 39716010›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Mass Spectrometry-Based Glycomics and Proteomics Profiling of On-Slide Digested Tissue from Complex Biological Samples.

Sayantani Chatterjee, Joseph Zaia, Manveen K Sethi

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Sayantani ChatterjeeDepartment of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA.
Joseph ZaiaDepartment of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA.
Manveen K SethiDepartment of Biochemistry, Center for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA. msethi@bu.edu.

Funding

Project-005UL1TR001430 · NCATS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BAIR-MERRITT, MEGAN H, CENTER, DAVID M. · 2015 to 2024
$52.3M
Selecting HA glycosylation for improved vaccine responsesR01AI155975 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI WAN, XIUFENG HENRY, WOODS, ROBERT J · 2021 to 2025
$4.0M
Cerebrovascular Remodeling and Neurodegenerative Changes in Alzheimer's DiseaseR01AG075876 · NIA · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI Thor Stein, JOSEPH ZAIA · 2022 to 2026
$3.9M
Methods for measuring matrisome molecule similarity during disease processesR35GM144090 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI JOSEPH ZAIA · 2022 to 2026
$2.1M
NCATS NIH HHS UL1 TR001430NIAID NIH HHS R01 AI155975NIA NIH HHS R01 AG075876NIGMS NIH HHS R35 GM144090
6 · The paper itself

Abstract

Mass spectrometry-based investigation of the heterogeneous glycoproteome from complex biological specimens is a robust approach to mapping the structure, function, and dynamics of the glycome and proteome. Sampling whole wet tissues often provides a large amount of starting material; however, there is a reasonable variability in tissue handling prior to downstream processing steps, and it is difficult to capture all the different biomolecules from a specific region. The on-slide tissue digestion approach, outlined in this protocol chapter, is a simple and cost-effective method that allows comprehensive mapping of the glycoproteome from a single spot of tissue of 1 mm or greater diameter. It provides a selection of target areas on tissue slides appropriate for tissue volumes of 10 nL or greater, corresponding to a 1 μL droplet of enzyme solution applied to a 1-mm diameter target on a 10-μm-thick tissue slice. Sequential enzymatic digestions and desalting of the biomolecules without any prior derivatization from the surface of fresh frozen or formalin-fixed paraffin-embedded tissue slides enable the simultaneous identification of glycosaminoglycan disaccharides such as hyaluronan, chondroitin sulfate and heparan sulfate, asparagine or N-linked glycans, and intact (glyco)peptides using liquid chromatography-tandem mass spectrometry. The in-depth information obtained from this method including the disaccharide compositions, glycan structures, peptide abundances, and site-specific glycan occupancies provides a detailed profiling of a single spot of tissue which has the potential to be disseminated to biomedical laboratories.

Indexed as

GlycomicsProteomicsAnimalsChromatography, LiquidGlycoproteinsGlycosaminoglycansHumansMass SpectrometryPolysaccharidesProteomeTandem Mass SpectrometryGlycoproteinsGlycosaminoglycansPolysaccharidesProteomeFormalin-fixed paraffin-embedded tissueFresh frozen tissueGlycomicsGlycoproteomicsLiquid chromatographyMass spectrometryOn-slide tissue digestionProteomics

Identifiers

PMID39716010
PMCPMC12671056

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.