Evidence map›Paper›PMID 37325469›Full record

ReviewFrontiers in molecular biosciences2023

Assembly and disassembly of branched ubiquitin chains.

Justin B Gregor, Dantong Xu, Michael E French

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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 3 institutions in 1 country.

Justin B GregorDepartment of Biochemistry, Purdue University, West Lafayette, IN, United States.
Dantong XuDepartment of Chemistry and Biochemistry, Middlebury College, Middlebury, VT, United States.
Michael E FrenchDepartment of Chemistry and Biochemistry, Middlebury College, Middlebury, VT, United States.
Middlebury College · USPurdue University West Lafayette · USUniversity of Tampa · US

Funding

Drug Discovery in Infectious Disease TrainingT32AI148103 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL, YEO, YOON · 2020 to 2024
$949k
NIAID NIH HHS T32 AI148103
6 · The paper itself

Abstract

Protein ubiquitylation is an essential post-translational modification that regulates nearly all aspects of eukaryotic cell biology. A diverse collection of ubiquitylation signals, including an extensive repertoire of polymeric ubiquitin chains, leads to a range of different functional outcomes for the target protein. Recent studies have shown that ubiquitin chains can be branched and that branched chains have a direct impact on the stability or the activity of the target proteins they are attached to. In this mini review, we discuss the mechanisms that control the assembly and disassembly of branched chains by the enzymes of the ubiquitylation and deubiquitylation machinery. Existing knowledge regarding the activities of chain branching ubiquitin ligases and the deubiquitylases responsible for cleaving branched chains is summarized. We also highlight new findings concerning the formation of branched chains in response to small molecules that induce the degradation of otherwise stable proteins and examine the selective debranching of heterotypic chains by the proteasome-bound deubiquitylase UCH37.

Indexed as

branched ubiquitin chainproteasomeprotein degradationubiquitinubiquitylation (ubiquitination)

Identifiers

PMID37325469
PMCPMC10267395
OpenAlexW4379056337

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.