Evidence map›Paper›PMID 26690337›Full record

ReviewDrug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy2015

Dysregulation of ubiquitin ligases in cancer.

Jianfei Qi, Ze'ev A Ronai

Open access · greenAbstract readReview
In one paragraph

Review in Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

41 citing papers in PubMed, 70 citations in OpenAlex.

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  8. Exploring the molecular mechanism of Xiao Ji (Asian biomedicine : research, reviews and news · 2025
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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 2 institutions in 1 country.

Jianfei QiUniversity of Maryland School of Medicine, Baltimore, 21201, USA. Electronic address: jqi@som.umaryland.edu.
Ze'ev A RonaiSanford Burnham Prebys Medical Discovery Institute, La Jolla, 92037, USA. Electronic address: zeev@ronailab.net.
Discovery Institute · USUniversity of Maryland, Baltimore · US

Funding

Tumor Assessment CoreP01CA128814 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI SMITH, JEFFREY W · 2009 to 2020
$19.1M
Novel Insights in the regulation of HIF1alpha StabilityR01CA111515 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RONAI, ZEEV A. · 2004 to 2014
$3.8M
Role of JMJD1A in hypoxia-induced EMT and prostate cancer stem cellsR00CA154888 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI QI, JIANFEI · 2013 to 2015
$685k
Role of Jmjd1a in hypoxia-induced EMT and prostate cancer stem cellsK99CA154888 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI QI, JIANFEI · 2011 to 2012
$215k
NCI NIH HHS CA111515NCI NIH HHS CA128814NCI NIH HHS CA154888NCI NIH HHS K99 CA154888NCI NIH HHS P01 CA128814NCI NIH HHS R00 CA154888NCI NIH HHS R01 CA111515
6 · The paper itself

Abstract

Ubiquitin ligases (UBLs) are critical components of the ubiquitin proteasome system (UPS), which governs fundamental processes regulating normal cellular homeostasis, metabolism, and cell cycle in response to external stress signals and DNA damage. Among multiple steps of the UPS system required to regulate protein ubiquitination and stability, UBLs define specificity, as they recognize and interact with substrates in a temporally- and spatially-regulated manner. Such interactions are required for substrate modification by ubiquitin chains, which marks proteins for recognition and degradation by the proteasome or alters their subcellular localization or assembly into functional complexes. UBLs are often deregulated in cancer, altering substrate availability or activity in a manner that can promote cellular transformation. Such deregulation can occur at the epigenetic, genomic, or post-translational levels. Alterations in UBL can be used to predict their contributions, affecting tumor suppressors or oncogenes in select tumors. Better understanding of mechanisms underlying UBL expression and activities is expected to drive the development of next generation modulators that can serve as novel therapeutic modalities. This review summarizes our current understanding of UBL deregulation in cancer and highlights novel opportunities for therapeutic interventions.

Indexed as

Gene Expression Regulation, NeoplasticProtein Processing, Post-TranslationalAntineoplastic AgentsCell CycleCell Transformation, NeoplasticEpigenesis, GeneticHumansNeoplasmsOncogene ProteinsProteasome Endopeptidase ComplexProteolysisSignal TransductionTumor Suppressor ProteinsUbiquitinUbiquitinationUbiquitin-Protein LigasesAntineoplastic AgentsOncogene ProteinsProteasome Endopeptidase ComplexTumor Suppressor ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID26690337
PMCPMC4688568
OpenAlexW2210282509

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.