Evidence map›Paper›PMID 35159190›Full record

ReviewCells2022

From

Valérie C Cabana, Marc P Lussier

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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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 at 1 institution in 1 country.

Valérie C CabanaDépartement de Chimie, Université du Québec à Montréal, Montréal, QC H2X 2J6, Canada.
Marc P LussierDépartement de Chimie, Université du Québec à Montréal, Montréal, QC H2X 2J6, Canada.ORCID 0000-0001-5568-0072
Université du Québec à Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin-proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes. Ubiquitination, a type of protein post-translational modification, involves complex enzymatic machinery, such as E3 ubiquitin ligases. The E3 ligases regulate the covalent attachment of ubiquitin to a target protein and are involved in various cellular mechanisms, including the cell cycle, cell division, endoplasmic reticulum stress, and neurotransmission. Because the E3 ligases regulate so many physiological events, they are also associated with pathologic conditions, such as cancer, neurological disorders, and immune-related diseases. This review focuses specifically on the protease-associated transmembrane-containing the Really Interesting New Gene (RING) subset of E3 ligases. We describe the structure, partners, and physiological functions of the

Indexed as

DrosophilaUbiquitin-Protein LigasesAnimalsDNA-Binding ProteinsDrosophila ProteinsHumansProtein Processing, Post-TranslationalProteinsUbiquitinUbiquitinationDNA-Binding ProteinsDrosophila Proteinsgzl protein, DrosophilaProteinsRNF13 protein, humanTTC3 protein, humanUbiquitinUbiquitin-Protein LigasesZNRF4 protein, humanE3 ligaseGodzillapathological dysfunctionPA-TM-RING familyRNF13RNF167ubiquitinZNRF4

Identifiers

PMID35159190
PMCPMC8834447
OpenAlexW4206994211

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.