Evidence map›Paper›PMID 25475908›Full record

ArticleImmunogenetics2015

Role of peptide processing predictions in T cell epitope identification: contribution of different prediction programs.

Jorg J A Calis, Peter Reinink, Christin Keller, Peter M Kloetzel, Can Keşmir

Open access · hybridAbstract read
In one paragraph

Article in Immunogenetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. In Silico Tools for Predicting Novel Epitopes.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Therapeutic cancer vaccines: advancements, challenges, and prospects.Signal transduction and targeted therapy · 2023
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Neoantigens in Hematologic Malignancies.Frontiers in immunology · 2020
    Review
  18. Review
  19. Review
  20. Review
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

5 authors at 3 institutions in 2 countries.

Jorg J A CalisTheoretical Biology & Bioinformatics, Biology Department, Utrecht University, Padualaan 8, 3584, CH Utrecht, The Netherlands.
Peter Reinink
Christin Keller
Peter M Kloetzel
Can Keşmir
Utrecht University · NLCharité - Universitätsmedizin Berlin · DEHumboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteolysis is the general term to describe the process of protein degradation into peptides. Proteasomes are the main actors in cellular proteolysis, and their activity can be measured in in vitro digestion experiments. However, in vivo proteolysis can be different than what is measured in these experiments if other proteases participate or if proteasomal activity is different in vivo. The in vivo proteolysis can be measured only indirectly, by the analysis of peptides presented on MHC-I molecules. MHC-I presented peptides are protected from further degradation, thus enabling an indirect view on the underlying in vivo proteolysis. The ligands presented on different MHC-I molecules enable different views on this process; in combination, they might give a complete picture. Based on in vitro proteasome-only digestions and MHC-I ligand data, different proteolysis predictors have been developed. With new in vitro digestion and MHC-I ligand data sets, we benchmarked how well these predictors capture in vitro proteasome-only activity and in vivo whole-cell proteolysis, respectively. Even though the in vitro proteasome digestion patterns were best captured by methods trained on such data (ProteaSMM and NetChop 20S), the in vivo whole-cell proteolysis was best predicted by a method trained on MHC-I ligand data (NetChop Cterm). Follow-up analysis showed that the likely source of this difference is the activity from proteases other than the proteasome, such as TPPII. This non-proteasomal in vivo activity is captured by NetChop Cterm and should be taken into account in MHC-I ligand predictions.

Indexed as

SoftwareAntigen PresentationBinding SitesDatabases, ProteinEpitopes, T-LymphocyteHistocompatibility Antigens Class IHIV-1HIV AntigensHumansLigandsPeptide FragmentsProteasome Endopeptidase ComplexProteolysisEpitopes, T-LymphocyteHistocompatibility Antigens Class IHIV AntigensLigandsPeptide FragmentsProteasome Endopeptidase Complex

Identifiers

PMID25475908
PMCPMC4297296
OpenAlexW2146832614

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.