Evidence map›Paper›PMID 31285264›Full record

ArticleThe Journal of biological chemistry2019

Inhibiting ubiquitination causes an accumulation of SUMOylated newly synthesized nuclear proteins at PML bodies.

Zhe Sha, Tamara Blyszcz, Román González-Prieto, Alfred C O Vertegaal, Alfred L Goldberg

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. Spirocyclic β-lactone secondary metabolites modulate spliceosome function.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
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  11. Article
  12. PML Body Biogenesis: A Delicate Balance of Interactions.International journal of molecular sciences · 2023
    Review
  13. Article
  14. Review
  15. Article
  16. SUMO enhances unfolding of SUMO-polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
  19. Insights in Post-Translational Modifications: Ubiquitin and SUMO.International journal of molecular sciences · 2022
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Zhe ShaDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.
Tamara BlyszczDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden 2333 ZA, The Netherlands.
Román González-PrietoDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden 2333 ZA, The Netherlands.ORCID 0000-0001-8997-2321
Alfred C O VertegaalDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden 2333 ZA, The Netherlands vertegaal@lumc.nl.
Alfred L GoldbergDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115 alfred_goldberg@hms.harvard.edu.
Leiden University Medical Center · NLHarvard University · US

Funding

MOLECULAR CHAPERONES AND PROTEIN DEGRADATIONR01GM051923 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLDBERG, ALFRED L · 1995 to 2020
$10.1M
European Research CouncilNIGMS NIH HHS R01 GM051923
6 · The paper itself

Abstract

Protein ubiquitination and SUMOylation are required for the maintenance of cellular protein homeostasis, and both increase in proteotoxic conditions (

Indexed as

Cell LineHumansIntranuclear Inclusion BodiesNuclear ProteinsPromyelocytic Leukemia ProteinSmall Ubiquitin-Related Modifier ProteinsSumoylationUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9UbiquitinsNuclear ProteinsPromyelocytic Leukemia ProteinSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitinsnuclear bodypromyelocytic leukemia (PML)proteasomesmall ubiquitin-like modifier (SUMO)SUMO-conjugating enzyme UBC9sumoylationTAK243ubiquitinubiquitin-activating enzyme (UAE/E1))ubiquitylation (ubiquitination)

Identifiers

PMID31285264
PMCPMC6802522
OpenAlexW2956906556

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.