Evidence map›Paper›PMID 32913119›Full record

ArticleThe Journal of biological chemistry2020

Mode of targeting to the proteasome determines GFP fate.

Christopher Eric Bragança, Daniel Adam Kraut

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
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  6. Phase separation of polyubiquitinated proteins in UBQLN2 condensates controls substrate fate.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  7. Article
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  9. Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Ubiquitin modulates 26Science advances · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Proteasomal conformation controls unfolding ability.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

2 authors.

Christopher Eric BragançaDepartment of Chemistry, Villanova University, Villanova, Pennsylvania, USA.
Daniel Adam KrautDepartment of Chemistry, Villanova University, Villanova, Pennsylvania, USA. Electronic address: daniel.kraut@villanova.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin-proteasome system is the canonical pathway for protein degradation in eukaryotic cells. GFP is frequently used as a reporter in proteasomal degradation assays. However, there are multiple variants of GFP in use, and these variants have different intrinsic stabilities. Further, there are multiple means by which substrates are targeted to the proteasome, and these differences could also affect the proteasome's ability to unfold and degrade substrates. Herein we investigate how the fate of GFP variants of differing intrinsic stabilities is determined by the mode of targeting to the proteasome. We compared two targeting systems: linear Ub

Indexed as

ProteolysisUbiquitinationDNA-Binding ProteinsGreen Fluorescent ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsGreen Fluorescent ProteinsProteasome Endopeptidase ComplexRAD23 protein, S cerevisiaeRPN13 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsATPases associated with diverse cellular activities (AAA)ATP-dependent proteaseenzyme kineticsenzyme mechanismpre–steady-state kineticsproteasomeprotein degradationprotein unfolding

Identifiers

PMID32913119
PMCPMC7681031

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.