Evidence map›Paper›PMID 20109157›Full record

ReviewCellular microbiology2010

Pupylation versus ubiquitylation: tagging for proteasome-dependent degradation.

Kristin E Burns, K Heran Darwin

Abstract readReview
In one paragraph

Review in Cellular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Selective Phenylimidazole-Based Inhibitors of theJournal of medicinal chemistry · 2019
    Article
  6. Article
  7. Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Article
  9. Article
  10. Prokaryotic ubiquitin-like protein modification.Annual review of microbiology · 2014
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Context-dependent resistance to proteolysis of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2011
    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

2 authors.

Kristin E BurnsDepartment of Microbiology, New York University School of Medicine, New York, NY 10016, USA. kristin.burns@nyumc.org
K Heran Darwin

Funding

Virulence Regulation by the Mycobacterium Tuberculosis ProteasomeR01HL092774 · NHLBI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DARWIN, KATERINA HERAN · 2007 to 2017
$4.0M
NHLBI NIH HHS HL092774NHLBI NIH HHS R01 HL092774Wellcome Trust
6 · The paper itself

Abstract

Prokaryotic ubiquitin-like protein (Pup) is the first identified prokaryotic protein that is functionally analogous to ubiquitin. Despite using the proteasome as the end-point for proteolysis, Pup differs from ubiquitin both biochemically and structurally. We will discuss these differences that have been highlighted by several recent studies. Finally, we will speculate on the possible interactions between the two analogous pathways in pathogen and host.

Indexed as

Bacterial ProteinsMetabolic Networks and PathwaysModels, BiologicalProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalUbiquitinationBacterial ProteinsProteasome Endopeptidase Complex

Identifiers

PMID20109157
PMCPMC3647454

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.