Evidence map›Paper›PMID 31333493›Full record

ReviewFrontiers in physiology2019

Enzymatic Logic of Ubiquitin Chain Assembly.

Kirandeep K Deol, Sonja Lorenz, Eric R Strieter

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Selective Lysine Ubiquitination Using Activated Phenol Esters.Chembiochem : a European journal of chemical biology · 2025
    Article
  6. Article
  7. Review
  8. Review
  9. Covalent inhibition ofiScience · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Bacterial mimicry of eukaryotic HECT ubiquitin ligation.bioRxiv : the preprint server for biology · 2023
    Article

7 more citing papers are in PubMed but not listed here.

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 2 countries.

Kirandeep K DeolDepartment of Chemistry, University of Massachusetts, Amherst, MA, United States.
Sonja LorenzRudolf Virchow Center for Experimental Biomedicine, University of Würzburg, Würzburg, Germany.
Eric R StrieterDepartment of Chemistry, University of Massachusetts, Amherst, MA, United States.
University of Massachusetts Amherst · USUniversity of Würzburg · DE

Funding

Understanding the Function of Deubiquitinases Using Chemical Tools: Administrative SupplementR01GM110543 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI STRIETER, ERIC ROBERT · 2014 to 2022
$2.9M
NIGMS NIH HHS R01 GM110543
6 · The paper itself

Abstract

Protein ubiquitination impacts virtually every biochemical pathway in eukaryotic cells. The fate of a ubiquitinated protein is largely dictated by the type of ubiquitin modification with which it is decorated, including a large variety of polymeric chains. As a result, there have been intense efforts over the last two decades to dissect the molecular details underlying the synthesis of ubiquitin chains by ubiquitin-conjugating (E2) enzymes and ubiquitin ligases (E3s). In this review, we highlight these advances. We discuss the evidence in support of the alternative models of transferring one ubiquitin at a time to a growing substrate-linked chain (sequential addition model) versus transferring a pre-assembled ubiquitin chain (en bloc model) to a substrate. Against this backdrop, we outline emerging principles of chain assembly: multisite interactions, distinct mechanisms of chain initiation and elongation, optimal positioning of ubiquitin molecules that are ultimately conjugated to each other, and substrate-assisted catalysis. Understanding the enzymatic logic of ubiquitin chain assembly has important biomedical implications, as the misregulation of many E2s and E3s and associated perturbations in ubiquitin chain formation contribute to human disease. The resurgent interest in bifunctional small molecules targeting pathogenic proteins to specific E3s for polyubiquitination and subsequent degradation provides an additional incentive to define the mechanisms responsible for efficient and specific chain synthesis and harness them for therapeutic benefit.

Indexed as

E2 conjugating enzymeE3 ligating enzymeen bloc transfersequential additionubiquitin

Identifiers

PMID31333493
PMCPMC6624479
OpenAlexW2954426419

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.