Evidence map›Paper›PMID 41479003›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Method for Measuring the Kinetic Stability of Peptides Bound onto MHC Class I Using MALDI-TOF Mass Spectrometry.

George Mavridis, Manousos Makridakis, Jerome Zoidakis, Efstratios Stratikos

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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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

4 authors.

George MavridisDepartment of Chemistry, National and Kapodistrian University of Athens, Athens, Greece.
Manousos MakridakisCenter of Systems Biology, Biomedical Research Foundation of the Academy of Athens, Athens, Greece.
Jerome ZoidakisDepartment of Biology, National and Kapodistrian University of Athens, Athens, Greece.
Efstratios StratikosDepartment of Chemistry, National and Kapodistrian University of Athens, Athens, Greece.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The kinetic stability of peptides bound onto MHC class I molecules is a critical parameter that helps shape their interaction with immune receptors and consequently their antigenic potential. We present here a method for measuring the kinetic stability and sensitivity to proteolytic degradation of peptides bound onto MHC class I molecules after in vitro refolding, by analyzing the time-resolved MALDI-TOF Mass Spec signal from the peptide, using the whole MHC-I/peptide complex in situ. This approach can provide important information on the dynamic nature of the MHC-peptide interaction, the kinetic half-life of binding and the sensitivity of the peptide to external proteolytic digestion or other modifications.

Indexed as

Histocompatibility Antigens Class IPeptidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationHumansKineticsProtein BindingProtein StabilityProteolysisHistocompatibility Antigens Class IPeptidesEnzymeERAP1KineticsMALDI-TOFMass spectrometryMHCPeptide

Identifiers

PMID41479003

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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.