Evidence map›Paper›PMID 30583962›Full record

ReviewTrends in biochemical sciences2019

Uncovering the Structural Basis of a New Twist in Protein Ubiquitination.

Kedar Puvar, Zhao-Qing Luo, Chittaranjan Das

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2019. 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
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Emerging Role of Ubiquitination in the Regulation of PD-1/PD-L1 in Cancer Immunotherapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2021
    Review
  12. Article
  13. ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. 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.

Kedar PuvarDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47906, USA.
Zhao-Qing LuoPurdue Institute of Immunology, Inflammation, and Infectious Diseases and the Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47906, USA. Electronic address: luoz@purdue.edu.
Chittaranjan DasDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47906, USA. Electronic address: cdas@purdue.edu.
Purdue University West Lafayette · USState Street (United States) · US

Funding

Mechanism of atypical ubiquitination and deubiquitination by bacterial effectorsR01GM126296 · NIGMS · PURDUE UNIVERSITY · PI Chittaranjan Das · 2018 to 2026
$3.6M
Effector-mediated Ubiquitin Manipulation in Legionella Pneumophila PathogenesisR01AI127465 · NIAID · PURDUE UNIVERSITY · PI Qing Deng · 2017 to 2026
$3.4M
NIAID NIH HHS R01 AI127465NIGMS NIH HHS R01 GM126296
6 · The paper itself

Abstract

Members of the SidE effector family from Legionella pneumophila represent a new paradigm in the ubiquitin world. These enzymes catalyze ubiquitination of target proteins via a mechanism different from that of conventional E1-E2-E3 biochemistry and play important roles in L. pneumophila virulence. They combine mono-ADP-ribosylation and phosphodiesterase activities to attach ubiquitin onto substrates, in great contrast to the orthodox pathway. A series of recent structural and mechanistic studies have clarified the action of these enzymes. Herein, we summarize the key insights into the structure and function of these proteins, emphasizing their modular nature, and discuss the biochemical implications of these proteins as well as areas of further exploration.

Indexed as

Bacterial ProteinsLegionella pneumophilaMembrane ProteinsProtein ConformationUbiquitinUbiquitinationBacterial ProteinsMembrane ProteinsUbiquitinADP-ribosylationbacteriaeffectorsLegionellasignalingubiquitination

Identifiers

PMID30583962
PMCPMC6465118
OpenAlexW2906453347

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.