Evidence map›Paper›PMID 33805528›Full record

ReviewInternational journal of molecular sciences2021

Cellular Control of Protein Turnover via the Modification of the Amino Terminus.

Nikola Winter, Maria Novatchkova, Andreas Bachmair

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 12 citations in OpenAlex.

  1. A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Review
  5. N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Review
  6. Review
  7. 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
  8. Review
  9. Article
  10. Article
  11. 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
  12. Post-translational Modifications of the Protein Termini.Frontiers in cell and developmental biology · 2021
    Review
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 2 institutions in 1 country.

Nikola WinterMax Perutz Labs, Department of Biochemistry and Cell Biology, University of Vienna, A-1030 Vienna, Austria.ORCID 0000-0003-0107-1989
Maria NovatchkovaVienna BioCenter, Research Institute of Molecular Pathology, A-1030 Vienna, Austria.
Andreas BachmairMax Perutz Labs, Department of Biochemistry and Cell Biology, University of Vienna, A-1030 Vienna, Austria.
University of Vienna · ATInstitute of Molecular Biotechnology · AT

Funding

Austrian Science Fund F7904-BAustrian Science Fund P31114Austrian Science Fund FWF P 31114
6 · The paper itself

Abstract

The first amino acid of a protein has an important influence on its metabolic stability. A number of ubiquitin ligases contain binding domains for different amino-terminal residues of their substrates, also known as N-degrons, thereby mediating turnover. This review summarizes, in an exemplary way, both older and more recent findings that unveil how destabilizing amino termini are generated. In most cases, a step of proteolytic cleavage is involved. Among the over 500 proteases encoded in the genome of higher eukaryotes, only a few are known to contribute to the generation of N-degrons. It can, therefore, be expected that many processing paths remain to be discovered.

Indexed as

Bacterial ProteinsCaspasesEndopeptidasesEndoplasmic ReticulumHumansMethionyl AminopeptidasesProteinsProtein Sorting SignalsProteolysisRibosomesUbiquitin-Protein LigasesBacterial ProteinsCaspasesEndopeptidasesMethionyl AminopeptidasesProteinsProtein Sorting SignalsUbiquitin-Protein LigasesautophagyendoproteaseN-degronprotein turnoverproteolytic processingubiquitin proteasome pathway

Identifiers

PMID33805528
PMCPMC8037982
OpenAlexW3146871486

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.