Evidence map›Paper›PMID 42401773›Full record

ReviewAdvances in experimental medicine and biology2026

Advanced (Nano)material-Based Enrichment Strategies for Quantitative Phosphoproteomics Analysis by Mass Spectrometry.

Inmaculada Ortiz-Gómez, Francisco Calderón Celis

Abstract readReview
PubMed Publisher
In one paragraph

Review in Advances in experimental medicine and biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Inmaculada Ortiz-GómezCentro Tecnológico de Componentes-CTC, Scientific and Technological Park of Cantabria (PCTCAN), Santander, Spain.
Francisco Calderón CelisInstitute of Biomedicine and Biotechnology of Cantabria (IBBTEC), University of Cantabria-Spanish National Research Council (CSIC), Santander, Spain. calderonf@unican.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation is one of the most prevalent and dynamic post-translational modifications. It regulates aspects of cellular signaling, metabolism, and disease progression. Comprehensive characterization of phosphoproteins and their phosphorylation remain analytically challenging due to their low abundance, the dynamic nature of the phosphorylation, substoichiometric modification levels, and the complexity of biological matrices. However, recent advancements in enrichment strategies have substantially increased the depth and precision of phosphoproteomics analyses using mass spectrometry. Strategies such as immobilized metal ion affinity chromatography and metal oxide affinity chromatography refine the selective isolation of phosphorylated peptides from complex mixtures. Emerging materials, such as advanced metal nanoparticles, MXenes, and carbon-based nanostructures, are increasingly being used in phosphoproteomics enrichment due to their inherent features such as high surface areas, easily tunable surface chemistry, and strong structural stability, which provide enhanced enrichment efficiency and selectivity. Here, we outline strategies and innovations in phosphoprotein enrichment materials in quantitative proteomics MS platforms.

Indexed as

Mass SpectrometryNanostructuresPhosphoproteinsProteomicsAnimalsChromatography, AffinityHumansPhosphorylationProtein Processing, Post-TranslationalPhosphoproteinsChromatographyEnrichment strategiesMass spectrometryNanomaterialsPhosphoproteomicsPhosphorylation

Identifiers

What Socratic 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 Socratic graph.