Evidence map›Paper›PMID 39346323›Full record

ReviewJournal of pharmacy & bioallied sciences2024

E3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers: Narrative Review.

Azfar Jamal

Abstract readReview
In one paragraph

Review in Journal of pharmacy & bioallied sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
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

1 author.

Azfar JamalDepartment of Biology, College of Science, Al-Zulfi-, Majmaah University, Majmaah, Riyadh, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

E3 ubiquitin ligases are a class of enzymes, essential for maintaining the equilibrium of cells by binding ubiquitin molecules to substrates to mark them for destruction. Since many cancer-related proteins, including both oncogenic and tumor-suppressive ones, are controlled by the ubiquitin-proteasome system, E3 ligases have drawn a great deal of interest as potential targets for the creation of anti-cancer drugs. This is because E3 ligases function as modules that select the substrates that are intended for degradation, giving them the ability to particularly affect proteins that are connected to cancer. Their molecular properties and the ways in which they work serve as the basis for these distinctions. Investment in the creation of bioactive substances that can target E3 ligases is essential given the crucial roles they play in cancer. These substances have the potential to be powerful cancer-fighting tools. In this review, we explore the crucial roles that E3 ligases play in the biology of cancer. We also examine the current bioactive substances that have been created to target different E3 ligases, emphasizing their potential as candidates for treating the cancers.

Indexed as

E3 ligaseMDM2NEDD4RING (really interesting new genes)ubiquitin

Identifiers

PMID39346323
PMCPMC11426868

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.