Evidence map›Paper›PMID 33288721›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

DIA-based systems biology approach unveils E3 ubiquitin ligase-dependent responses to a metabolic shift.

Ozge Karayel, André C Michaelis, Matthias Mann, Brenda A Schulman, Christine R Langlois

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  4. Review
  5. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Review
  15. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. 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 1 institution in 1 country.

Ozge KarayelDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.ORCID 0000-0003-2541-1159
André C MichaelisDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.ORCID 0000-0002-7519-3295
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; mmann@biochem.mpg.de Schulman@biochem.mpg.de langlois@biochem.mpg.de.ORCID 0000-0003-1292-4799
Brenda A SchulmanDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany mmann@biochem.mpg.de Schulman@biochem.mpg.de langlois@biochem.mpg.de.ORCID 0000-0002-3083-1126
Christine R LangloisDepartment of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany mmann@biochem.mpg.de Schulman@biochem.mpg.de langlois@biochem.mpg.de.ORCID 0000-0003-1567-3577
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast

Indexed as

CarbonCulture MediaFructose-BisphosphataseGlucoseMalate DehydrogenaseMass SpectrometryPoint MutationPyruvate DecarboxylaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSodium-Potassium-Exchanging ATPaseStress, PhysiologicalSystems BiologyUbiquitin-Protein LigasesWorkflowARO10 protein, S cerevisiaeCarbonCulture MediaENA1 protein, S cerevisiaeFBP1 protein, S cerevisiaeFructose-BisphosphataseGlucoseMalate DehydrogenaseMDH2 protein, S cerevisiaePyruvate DecarboxylaseSaccharomyces cerevisiae ProteinsSodium-Potassium-Exchanging ATPaseUbiquitin-Protein LigasesGID E3 ligasemass spectrometryproteomicsstressyeast systems biology

Identifiers

PMID33288721
PMCPMC7768684
OpenAlexW3112041806

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.