Evidence map›Paper›PMID 36234736›Full record

ReviewMolecules (Basel, Switzerland)2022

Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research.

Laura Darie-Ion, Danielle Whitham, Madhuri Jayathirtha, Yashveen Rai, Anca-Narcisa Neagu, Costel C Darie, Brînduşa Alina Petre

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
8.3field-weighted citation impact, top 1% 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

31 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  3. Review
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  6. A novel high-entropy TiVCrMoCJournal of pharmaceutical analysis · 2026
    Article
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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 2 institutions in 2 countries.

Laura Darie-IonLaboratory of Biochemistry, Department of Chemistry, "Alexandru Ioan Cuza" University of Iasi, Carol I bvd, No. 11, 700506 Iasi, Romania.
Danielle WhithamBiochemistry & Proteomics Laboratories, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY 13699, USA.
Madhuri JayathirthaBiochemistry & Proteomics Laboratories, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY 13699, USA.
Yashveen RaiBiochemistry & Proteomics Laboratories, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY 13699, USA.
Anca-Narcisa NeaguLaboratory of Animal Histology, Faculty of Biology, "Alexandru Ioan Cuza" University of Iasi, Carol I bvd, No. 22, 700505 Iasi, Romania.
Costel C DarieBiochemistry & Proteomics Laboratories, Department of Chemistry and Biomolecular Science, Clarkson University, 8 Clarkson Avenue, Potsdam, NY 13699, USA.ORCID 0000-0001-6402-2311
Brînduşa Alina PetreLaboratory of Biochemistry, Department of Chemistry, "Alexandru Ioan Cuza" University of Iasi, Carol I bvd, No. 11, 700506 Iasi, Romania.ORCID 0000-0002-0208-6560
Clarkson University · USAlexandru Ioan Cuza University · RO

Funding

PA-23-189 for Kaya Johnson to CA260126-01: Identifying a proteomic signature for breast cancer detection in breast milk and serumR15CA260126 · NCI · CLARKSON UNIVERSITY · PI DARIE, COSTEL C. · 2022 to 2024
$628k
NCI NIH HHS R15 CA260126NIH HHS R15CA260126
6 · The paper itself

Abstract

Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the most widely used techniques in proteomics to achieve structural identification and characterization of proteins and peptides, including their variety of proteoforms due to post-translational modifications (PTMs) or protein-protein interactions (PPIs). MALDI-MS and MALDI tandem mass spectrometry (MS/MS) have been developed as analytical techniques to study small and large molecules, offering picomole to femtomole sensitivity and enabling the direct analysis of biological samples, such as biofluids, solid tissues, tissue/cell homogenates, and cell culture lysates, with a minimized procedure of sample preparation. In the last decades, structural identification of peptides and proteins achieved by MALDI-MS/MS helped researchers and clinicians to decipher molecular function, biological process, cellular component, and related pathways of the gene products as well as their involvement in pathogenesis of diseases. In this review, we highlight the applications of MALDI ionization source and tandem approaches for MS for analyzing biomedical relevant peptides and proteins. Furthermore, one of the most relevant applications of MALDI-MS/MS is to provide "molecular pictures", which offer in situ information about molecular weight proteins without labeling of potential targets. Histology-directed MALDI-mass spectrometry imaging (MSI) uses MALDI-ToF/ToF or other MALDI tandem mass spectrometers for accurate sequence analysis of peptide biomarkers and biological active compounds directly in tissues, to assure complementary and essential spatial data compared with those obtained by LC-ESI-MS/MS technique.

Indexed as

Biomedical ResearchProteomicsPeptidesProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryPeptidesProteinsbiomarkersbiomedical researchMALDIproteomicstandem mass spectrometry (MS/MS)

Identifiers

PMID36234736
PMCPMC9570737
OpenAlexW4296614831

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.