Evidence map›Paper›PMID 36168305›Full record

ArticleAging cell2022

Reprograming of proteasomal degradation by branched chain amino acid metabolism.

Sonia Ravanelli, Qiaochu Li, Andrea Annibal, Aleksandra Trifunovic, Adam Antebi, Thorsten Hoppe

Open access · goldAbstract read
In one paragraph

Article in Aging cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

9 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Role of amino acid metabolism in mitochondrial homeostasis.Frontiers in cell and developmental biology · 2023
    Review
  8. Article
  9. 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

6 authors at 2 institutions in 1 country.

Sonia RavanelliInstitute for Genetics, University of Cologne, Cologne, Germany.ORCID https://orcid.org/0000-0002-8511-9339
Qiaochu LiInstitute for Genetics, University of Cologne, Cologne, Germany.ORCID https://orcid.org/0000-0001-8032-9110
Andrea AnnibalMax Planck Institute for Biology of Ageing, Cologne, Germany.ORCID https://orcid.org/0000-0003-4311-5417
Aleksandra TrifunovicCologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.ORCID https://orcid.org/0000-0002-5472-3517
Adam AntebiCologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne, Germany.ORCID https://orcid.org/0000-0002-7241-3029
Thorsten HoppeInstitute for Genetics, University of Cologne, Cologne, Germany.ORCID https://orcid.org/0000-0002-4734-9352
University of Cologne · DEMax Planck Institute for Biology of Ageing · DE

Funding

Alexander von Humboldt FoundationDeutsche Forschungsgemeinschaft EXC 2030 - 390661388Deutsche Forschungsgemeinschaft FKZ: ZUK81/1Deutsche Forschungsgemeinschaft SFB 1218
6 · The paper itself

Abstract

Branched-chain amino acid (BCAA) metabolism is a central hub for energy production and regulation of numerous physiological processes. Controversially, both increased and decreased levels of BCAAs are associated with longevity. Using genetics and multi-omics analyses in Caenorhabditis elegans, we identified adaptive regulation of the ubiquitin-proteasome system (UPS) in response to defective BCAA catabolic reactions after the initial transamination step. Worms with impaired BCAA metabolism show a slower turnover of a GFP-based proteasome substrate, which is suppressed by loss-of-function of the first BCAA catabolic enzyme, the branched-chain aminotransferase BCAT-1. The exogenous supply of BCAA-derived carboxylic acids, which are known to accumulate in the body fluid of patients with BCAA metabolic disorders, is sufficient to regulate the UPS. The link between BCAA intermediates and UPS function presented here sheds light on the unexplained role of BCAAs in the aging process and opens future possibilities for therapeutic interventions.

Indexed as

Amino Acids, Branched-ChainProteasome Endopeptidase ComplexAnimalsCaenorhabditis elegansAmino Acids, Branched-ChainProteasome Endopeptidase Complexagingbranched-chain amino acidbranched-chain aminotransferaseCaenorhabditis elegansmetabolismproteasomeproteostasisubiquitin

Identifiers

PMID36168305
PMCPMC9741504
OpenAlexW4297329385

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.