Evidence map›Paper›PMID 22822185›Full record

ArticleMolecular & cellular proteomics : MCP2012

Driving forces of proteasome-catalyzed peptide splicing in yeast and humans.

Michele Mishto, Andrean Goede, Kathrin Textoris Taube, Christin Keller, Katharina Janek, Petra Henklein, Agathe Niewienda, Alexander Kloss, Sabrina Gohlke, Burkhardt Dahlmann and 2 more

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Neo-Splicetopes in Tumor Therapy: A Lost Case?Frontiers in immunology · 2022
    Review
  10. Review
  11. Article
  12. Spliced HLA-bound peptides: a Black Swan event in immunology.Clinical and experimental immunology · 2021
    Review
  13. Article
  14. Archaeal Connectase is a specific and efficient protein ligase related to proteasome β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Response: Commentary: AnFrontiers in immunology · 2021
    Article
  16. Review
  17. Article
  18. Proteasome-GeneratedFrontiers in immunology · 2021
    Article
  19. Article
  20. Are There Indeed Spliced Peptides in the Immunopeptidome?Molecular & cellular proteomics : MCP · 2021
    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

12 authors.

Michele MishtoInstitut für Biochemie, Charité - Universitätsmedizin Berlin, Oudenarder Straβe 16, 13347 Berlin, Germany. michele.mishto@charite.de
Andrean Goede
Kathrin Textoris Taube
Christin Keller
Katharina Janek
Petra Henklein
Agathe Niewienda
Alexander Kloss
Sabrina Gohlke
Burkhardt Dahlmann
Cordula Enenkel
Peter Michael Kloetzel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteasome-catalyzed peptide splicing (PCPS) represents an additional activity of mammalian 20S proteasomes recently identified in connection with antigen presentation. We show here that PCPS is not restricted to mammalians but that it is also a feature of yeast 20S proteasomes catalyzed by all three active site β subunits. No major differences in splicing efficiency exist between human 20S standard- and immuno-proteasome or yeast 20S proteasome. Using H(2)(18)O to monitor the splicing reaction we also demonstrate that PCPS occurs via direct transpeptidation that slightly favors the generation of peptides spliced in cis over peptides spliced in trans. Splicing efficiency itself is shown to be controlled by proteasomal cleavage site preference as well as by the sequence characteristics of the spliced peptides. By use of kinetic data and quantitative analyses of PCPS obtained by mass spectrometry we developed a structural model with two PCPS binding sites in the neighborhood of the active Thr1.

Indexed as

Protein SplicingAmino Acid SequenceBiocatalysisB-LymphocytesCell Line, TransformedChromatography, LiquidHumansMolecular Sequence DataPeptidesProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationPeptidesProteasome Endopeptidase Complex

Identifiers

PMID22822185
PMCPMC3494140

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.