Evidence map›Paper›PMID 25701549›Full record

ReviewBiochimie2015

Ubiquitination of newly synthesized proteins at the ribosome.

Feng Wang, Larissa A Canadeo, Jon M Huibregtse

Abstract readReview
In one paragraph

Review in Biochimie, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. A second chance for protein targeting/folding: Ubiquitination and deubiquitination of nascent proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Review
  6. PARK2 regulates eIF4B-driven lymphomagenesis.Molecular cancer research : MCR · 2022
    Article
  7. Article
  8. Article
  9. Chronic social stress alters protein metabolism in juvenile rainbow trout, Oncorhynchus mykiss.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2021
    Article
  10. Review
  11. Recognition of nonproline N-terminal residues by the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Gid10 as an alternative N-recognin of the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Proteomic response ofFood science and biotechnology · 2019
    Article
  15. Article
  16. Review
  17. Differentially expressed proteins identified by TMT proteomics analysis in bone marrow microenvironment of osteoporotic patients.Osteoporosis international : a journal established as result of cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA · 2019
    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

3 authors at 1 institution in 1 country.

Feng WangDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
Larissa A CanadeoDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
Jon M HuibregtseDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: huibregtse@austin.utexas.edu.
The University of Texas at Austin · US

Funding

Mechanism and Function of ISG15 ConjugationR01AI096090 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI HUIBREGTSE, JON · 2011 to 2025
$5.9M
Mechanism and Function of Protein UbiquitinationR01GM103619 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI HUIBREGTSE, JON · 2012 to 2020
$2.5M
NIAID NIH HHS AI096090NIAID NIH HHS R01 AI096090NIGMS NIH HHS GM103619NIGMS NIH HHS R01 GM103619
6 · The paper itself

Abstract

Newly synthesized proteins can be misfolded or damaged because of errors during synthesis or environmental insults (e.g., heat shock), placing a significant burden on protein quality control systems. In addition, numerous human diseases are associated with a deficiency in eliminating aberrant proteins or accumulation of aggregated proteins. Understanding the mechanisms of protein quality control and disposal pathways for misfolded proteins is therefore crucial for therapeutic intervention in these diseases. Quality control processes function at many points in the life cycle of proteins, and a subset act at the actual site of protein synthesis, the ribosome. Here we summarize recent advances in the role of the ubiquitin proteasome system in protein quality control during the process of translation.

Indexed as

Protein BiosynthesisUbiquitinationAnimalsHumansProtein FoldingRibosomesUbiquitin-Protein LigasesUbiquitin-Protein LigasesCo-translational ubiquitinationLtn1Protein quality controlRibosomeUbiquitin

Identifiers

PMID25701549
PMCPMC4458410
OpenAlexW2003693048

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.