Evidence map›Paper›PMID 22304392›Full record

ArticleJournal of proteome research2012

Peptidomic analysis of HEK293T cells: effect of the proteasome inhibitor epoxomicin on intracellular peptides.

Lloyd D Fricker, Julia S Gelman, Leandro M Castro, Fabio C Gozzo, Emer S Ferro

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

  1. Limitations of Mass Spectrometry-Based Peptidomic Approaches.Journal of the American Society for Mass Spectrometry · 2015
    Pooled it
  2. Neuropeptidomics of Genetically Defined Cell Types in Mouse Brain.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  3. Quantitative Peptidomics: General Considerations.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Peptidome: Chaos or Inevitability.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Review
  9. Review
  10. Discovery of Missing Methylation Sites on Endogenous Peptides of Human Cell Lines.Journal of the American Society for Mass Spectrometry · 2019
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Quantitative Peptidomics with Five-plex Reductive Methylation labels.Journal of the American Society for Mass Spectrometry · 2018
    Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 3 institutions in 2 countries.

Lloyd D FrickerDepartment of Molecular Pharmacology, Albert Einstein College of Medicine , Bronx, New York 10461, United States.
Julia S Gelman
Leandro M Castro
Fabio C Gozzo
Emer S Ferro
Albert Einstein College of Medicine · USUniversidade de São Paulo · BRUniversidade Estadual de Campinas (UNICAMP) · BR

Funding

REGULATION OF ENKEPHALIN CONVERTASE--CARBOXYPEPTIDASE ER01DA004494 · NIDA · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1987 to 2015
$5.9M
NIDA NIH HHS DA-004494NIDA NIH HHS R01 DA004494
6 · The paper itself

Abstract

Peptides derived from cytosolic, mitochondrial, and nuclear proteins have been detected in extracts of animal tissues and cell lines. To test whether the proteasome is involved in their formation, HEK293T cells were treated with epoxomicin (0.2 or 2 μM) for 1 h and quantitative peptidomics analysis was performed. Altogether, 147 unique peptides were identified by mass spectrometry sequence analysis. Epoxomicin treatment decreased the levels of the majority of intracellular peptides, consistent with inhibition of the proteasome beta-2 and beta-5 subunits. Treatment with the higher concentration of epoxomicin elevated the levels of some peptides. Most of the elevated peptides resulted from cleavages at acidic residues, suggesting that epoxomicin increased the processing of proteins through the beta-1 subunit. Interestingly, some of the peptides that were elevated by the epoxomicin treatment had hydrophobic residues in P1 cleavage sites. Taken together, these findings suggest that, while the proteasome is the major source of intracellular peptides, other peptide-generating mechanisms exist. Because intracellular peptides are likely to perform intracellular functions, studies using proteasome inhibitors need to be interpreted with caution, as it is possible that the effects of these inhibitors are due to a change in the peptide levels rather than inhibition of protein degradation.

Indexed as

Proteasome InhibitorsAmino Acid SequenceCytosolHEK293 CellsHumansMolecular Sequence DataOligopeptidesPeptide FragmentsPeptide MappingProteasome Endopeptidase ComplexProteomeSequence Analysis, ProteinTandem Mass SpectrometryepoxomicinOligopeptidesPeptide FragmentsProteasome Endopeptidase ComplexProteasome InhibitorsProteome

Identifiers

PMID22304392
PMCPMC3315381
OpenAlexW2089129607

What OpenQuestion holds

Textmetadata
LicenceTDM
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.