Evidence map›Paper›PMID 25605945›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

The first step of peptide selection in antigen presentation by MHC class I molecules.

Malgorzata A Garstka, Alexander Fish, Patrick H N Celie, Robbie P Joosten, George M C Janssen, Ilana Berlin, Rieuwert Hoppes, Magda Stadnik, Lennert Janssen, Huib Ovaa and 3 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing 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

58 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Halogen bonds between ligands and proteins: Can we use them in validation?Protein science : a publication of the Protein Society · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Id-neoantigen vaccine induces therapeutic CD8Journal for immunotherapy of cancer · 2023
    Article
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

13 authors.

Malgorzata A GarstkaDepartments of Cell Biology and.
Alexander FishBiochemistry, Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and.
Patrick H N CelieBiochemistry, Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and.
Robbie P JoostenBiochemistry, Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and.
George M C JanssenDepartment of Immunohematology and Blood Transfusion, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands.
Ilana BerlinDepartments of Cell Biology and.
Rieuwert HoppesDepartments of Cell Biology and.
Magda StadnikBiochemistry, Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and.
Lennert JanssenDepartments of Cell Biology and.
Huib OvaaDepartments of Cell Biology and.
Peter A van VeelenDepartment of Immunohematology and Blood Transfusion, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands.
Anastassis PerrakisBiochemistry, Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands; and.
Jacques NeefjesDepartments of Cell Biology and j.neefjes@nki.nl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MHC class I molecules present a variable but limited repertoire of antigenic peptides for T-cell recognition. Understanding how peptide selection is achieved requires mechanistic insights into the interactions between the MHC I and candidate peptides. We find that, at first encounter, MHC I H-2K(b) considers a wide range of peptides, including those with expanded N termini and unfitting anchor residues. Discrimination occurs in the second step, when noncanonical peptides dissociate with faster exchange rates. This second step exhibits remarkable temperature sensitivity, as illustrated by numerous noncanonical peptides presented by H-2K(b) in cells cultured at 26 °C relative to 37 °C. Crystallographic analyses of H-2K(b)-peptide complexes suggest that a conformational adaptation of H-2K(b) drives the decisive step in peptide selection. We propose that MHC class I molecules consider initially a large peptide pool, subsequently refined by a temperature-sensitive induced-fit mechanism to retain the canonical peptide repertoire.

Indexed as

Amino Acid SequenceCrystallography, X-RayEntropyHistocompatibility Antigens Class IKineticsPeptidesHistocompatibility Antigens Class IPeptidesanchor residuesantigen presentationdynamicsentropypeptide binding

Identifiers

PMID25605945
PMCPMC4321303

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.