Evidence map›Paper›PMID 31092913›Full record

ArticleNature protocols2019

Mass spectrometry-based identification of MHC-bound peptides for immunopeptidomics.

Anthony W Purcell, Sri H Ramarathinam, Nicola Ternette

Open access · greenAbstract read
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In one paragraph

Article in Nature protocols, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 224 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
224citing papers in PubMed, 1 pooled it
13.8field-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

224 citing papers in PubMed, 1 synthesis or guideline pooled it, 364 citations in OpenAlex.

  1. Pooled it
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  19. Molecular origin, discovery, validation and application of neoantigens.Asian journal of pharmaceutical sciences · 2026
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164 more citing papers are in PubMed but not listed here.

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 at 3 institutions in 3 countries.

Anthony W PurcellDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia. anthony.purcell@monash.edu.ORCID http://orcid.org/0000-0003-0532-8331
Sri H RamarathinamDepartment of Biochemistry and Molecular Biology, Infection and Immunity Program, Biomedicine Discovery Institute, Monash University, Clayton, VIC, Australia.ORCID http://orcid.org/0000-0002-2787-1282
Nicola TernetteThe Jenner Institute, Mass Spectrometry Laboratory, Target Discovery Institute, University of Oxford, Oxford, UK. nicola.ternette@ndm.ox.ac.uk.
Australian Regenerative Medicine Institute · AUDiscovery Institute · USUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide antigens bound to molecules encoded by the major histocompatibility complex (MHC) and presented on the cell surface form the targets of T lymphocytes. This critical arm of the adaptive immune system facilitates the eradication of pathogen-infected and cancerous cells, as well as the production of antibodies. Methods to identify these peptide antigens are critical to the development of new vaccines, for which the goal is the generation of effective adaptive immune responses and long-lasting immune memory. Here, we describe a robust protocol for the identification of MHC-bound peptides from cell lines and tissues, using nano-ultra-performance liquid chromatography coupled to high-resolution mass spectrometry (nUPLC-MS/MS) and recent improvements in methods for isolation and characterization of these peptides. The protocol starts with the immunoaffinity capture of naturally processed MHC-peptide complexes. The peptides dissociate from the class I human leukocyte antigens (HLAs) upon acid denaturation. This peptide cargo is then extracted and separated into fractions by HPLC, and the peptides in these fractions are identified using nUPLC-MS/MS. With this protocol, several thousand peptides can be identified from a wide variety of cell types, including cancerous and infected cells and those from tissues, with a turnaround time of 2-3 d.

Indexed as

Amino Acid SequenceAnimalsCell LineCells, CulturedChemical PrecipitationChromatography, AffinityChromatography, High Pressure LiquidHistocompatibility AntigensHistocompatibility Antigens Class IHumansMajor Histocompatibility ComplexMicePeptidesTandem Mass SpectrometryHistocompatibility AntigensHistocompatibility Antigens Class IPeptides

Identifiers

PMID31092913
OpenAlexW2945679805

What OpenQuestion 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 OpenQuestion graph.