Evidence map›Paper›PMID 26630263›Full record

ReviewFuture medicinal chemistry2015

Targeting ubiquitination for cancer therapies.

John Kenneth Morrow, Hui-Kuan Lin, Shao-Cong Sun, Shuxing Zhang

Open access · greenAbstract readReview
In one paragraph

Review in Future medicinal chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 9% 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

66 citing papers in PubMed, 1 synthesis or guideline pooled it, 108 citations in OpenAlex.

  1. Pooled it
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  10. Frontiers in cell and developmental biology · 2024
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6 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

4 authors at 1 institution in 1 country.

John Kenneth MorrowIntegrated Molecular Discovery Laboratory, Department of Experimental Therapeutics, MD Anderson Cancer Center, Houston, TX 77030, USA.
Hui-Kuan LinDepartment of Molecular & Cellular Oncology, MD Anderson Cancer Center, Houston, TX 77030, USA.
Shao-Cong SunDepartment of Immunology, MD Anderson Cancer Center, Houston, TX 77030, USA.
Shuxing ZhangIntegrated Molecular Discovery Laboratory, Department of Experimental Therapeutics, MD Anderson Cancer Center, Houston, TX 77030, USA.
The University of Texas MD Anderson Cancer Center · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
Disposition of Flavonoids via Metabolic InterplayR01GM070737 · NIGMS · UNIVERSITY OF HOUSTON · PI HU, MING · 2006 to 2017
$3.7M
Regulation of T-cell function and autoimmune inflammation by deubiquitinases.R37AI064639 · NIAID · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI SUN, SHAO-CONG · 2015 to 2021
$2.8M
NCI NIH HHS NIH/NCI P30CA016672NCI NIH HHS P30 CA016672NIAID NIH HHS R37 AI064639NIGMS NIH HHS R01 GM070737PHS HHS NIH/NIGMSGM070737
6 · The paper itself

Abstract

Ubiquitination, the structured degradation and turnover of cellular proteins, is regulated by the ubiquitin-proteasome system (UPS). Most proteins that are critical for cellular regulations and functions are targets of the process. Ubiquitination is comprised of a sequence of three enzymatic steps, and aberrations in the pathway can lead to tumor development and progression as observed in many cancer types. Recent evidence indicates that targeting the UPS is effective for certain cancer treatment, but many more potential targets might have been previously overlooked. In this review, we will discuss the current state of small molecules that target various elements of ubiquitination. Special attention will be given to novel inhibitors of E3 ubiquitin ligases, especially those in the SCF family.

Indexed as

Carrier ProteinsHumansImmunosuppressive AgentsNeoplasmsProteasome InhibitorsProtein Interaction Domains and MotifsUbiquitinationUbiquitin-Protein LigasesUbiquitinsCarrier ProteinsImmunosuppressive AgentsProteasome InhibitorsUbiquitin-Protein LigasesUbiquitinscancer therapeuticsdeubiquitinaseE3 ligase inhibitionhigh-throughput virtual screeninghot spotsin silico modelingSCF complexSkp2 inhibitorssmall molecule inhibitorsubiquitination

Identifiers

PMID26630263
PMCPMC4976843
OpenAlexW2183803121

What OpenQuestion holds

Textmetadata
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.