Evidence map›Paper›PMID 23027972›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Using intein catalysis to probe the origin of major histocompatibility complex class I-presented peptides.

Diego J Farfán-Arribas, Lawrence J Stern, Kenneth L Rock

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Role for ribosome-associated quality control in sampling proteins for MHC class I-mediated antigen presentation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  3. Article
  4. Review
  5. Evaluating the Role of HLA-DM in MHC Class II-Peptide Association Reactions.Journal of immunology (Baltimore, Md. : 1950) · 2015
    Article
  6. Article
  7. Article
  8. The nature and extent of contributions by defective ribosome products to the HLA peptidome.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Diego J Farfán-ArribasDepartment of Pathology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Lawrence J Stern
Kenneth L Rock
University of Massachusetts Chan Medical School · US

Funding

PILOT AND FEASIBILITY PROGRAMP30DK032520 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI CZECH, MICHAEL P · 1986 to 2010
$14.6M
T cell and transgenic core U19AI109858 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SELIN, LIISA KAARINA · 2014 to 2018
$11.9M
IMMUNOLOGY OF MHC RESTRICTION OF T CELLSR01AI020248 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ROCK, KENNETH L · 1985 to 2013
$2.0M
NIAID NIH HHS R01 AI020248NIAID NIH HHS U19 AI109858NIDDK NIH HHS DK32520NIDDK NIH HHS P30 DK032520
6 · The paper itself

Abstract

All vertebrate nucleated cells generate peptides from their expressed gene products and then display them at the cell surface bound to MHC class I molecules. This allows CD8(+) T cells to detect and eliminate abnormal cells that are synthesizing foreign proteins, e.g., from viruses or mutations. To permit the immune system to more uniformly monitor a cell's proteins, regardless of their half-life or location, it has been thought that the products of rapid degradation of the mistakes of protein synthesis (defective ribosomal products, DRiPs) preferentially contribute to the class I-presented peptides. However, using intein catalysis to generate peptide sequences exclusively by posttranslational splicing of mature proteins, we show here that presented peptides can be generated from fully folded and functional proteins. Remarkably, the presentation of peptides from two model mature proteins is just as efficient as from newly synthesized proteins subject to errors in translation or folding. These results indicate that for the constructs we have analyzed, DRiPs are not a more efficient source of class I peptides for antigen presentation than the turnover of mature functional proteins. Accordingly, our data suggest that one of the major ways the immune system evaluates the health of cells is by monitoring the breakdown products of the proteome.

Indexed as

Peptide BiosynthesisAnimalsAntigen PresentationCatalysisCell LineCloning, MolecularFluorescent Antibody TechniqueGenes, MHC Class IImmunologic SurveillanceInteinsMiceMice, TransgenicPeptidesProtein Processing, Post-TranslationalProteomePeptidesProteome

Identifiers

PMID23027972
PMCPMC3479494
OpenAlexW2129387423

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.