Evidence map›Paper›PMID 30449221›Full record

ReviewExpert opinion on therapeutic patents2018

A patent review of the ubiquitin ligase system: 2015-2018.

Xin Li, Ekinci Elmira, Sagar Rohondia, Jicang Wang, Jinbao Liu, Q Ping Dou

Abstract readReview
In one paragraph

Review in Expert opinion on therapeutic patents, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
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

45 citing papers in PubMed, 72 citations in OpenAlex.

  1. Ubiquitin-conjugating Enzymes in Cancer.International journal of biological sciences · 2026
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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

6 authors at 5 institutions in 2 countries.

Xin Lia Department of Biotechnology , Guangdong Polytechnic of Science and Trade , Guangzhou , Guangdong , China.
Ekinci Elmirac Barbara Ann Karmanos Cancer Institute, and Departments of Oncology, Pharmacology and Pathology, School of Medicine , Wayne State University , Detroit , MI , USA.
Sagar Rohondiac Barbara Ann Karmanos Cancer Institute, and Departments of Oncology, Pharmacology and Pathology, School of Medicine , Wayne State University , Detroit , MI , USA.
Jicang Wangc Barbara Ann Karmanos Cancer Institute, and Departments of Oncology, Pharmacology and Pathology, School of Medicine , Wayne State University , Detroit , MI , USA.
Jinbao Liue Protein Modification and Degradation Lab, School of Basic Medical Sciences , Affiliated Tumor Hospital of Guangzhou Medical University , Guangzhou , China.
Q Ping Douc Barbara Ann Karmanos Cancer Institute, and Departments of Oncology, Pharmacology and Pathology, School of Medicine , Wayne State University , Detroit , MI , USA.
Guangzhou Medical University · CNHenan University of Science and Technology · CNSouth China University of Technology · CNThe Barbara Ann Karmanos Cancer Institute · USWayne State University · US

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI Julie Lynn Boerner · 1985 to 2026
$68.4M
(PQA1) Regulation of Metformin Response by Breast Cancer Associated Gene 2 (BCA2)R21CA184788 · NCI · WAYNE STATE UNIVERSITY · PI DOU, QING PING · 2014 to 2015
$364k
NCI NIH HHS P30 CA022453NCI NIH HHS R21 CA184788
6 · The paper itself

Abstract

introductionUbiquitin-proteasome system (UPS) has been validated as a novel anticancer drug target in the past 20 years. The UPS contains two distinct steps: ubiquitination of a substrate protein by ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin ligase (E3), and substrate degradation by the 26S proteasome complex. The E3 enzyme is the central player in the ubiquitination step and has a wide range of specific substrates in cancer cells, offering great opportunities for discovery and development of selective drugs. Areas covered: This review summarizes the recent advances in small molecule inhibitors of E1s, E2s, and E3s, with a focus on the latest patents (from 2015 to 2018) of E3 inhibitors and modulators. Expert opinion: One strategy to overcome limitations of current 20S proteasome inhibitors is to discover inhibitors of the upstream key components of the UPS, such as E3 enzymes. E3s play important roles in cancer development and determine the specificity of substrate ubiquitination, offering novel target opportunities. E3 modulators could be developed by rational design, natural compound or library screening, old drug repurposes, and application of other novel technologies. Further understanding of mechanisms of E3-substrate interaction will be essential for discovering and developing next-generation E3 inhibitors as effective anticancer drugs.

Indexed as

AnimalsAntineoplastic AgentsDrug DesignHumansNeoplasmsPatents as TopicProteasome Endopeptidase ComplexProteasome InhibitorsUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesAntineoplastic AgentsProteasome Endopeptidase ComplexProteasome InhibitorsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasescancer therapydrug discoveryE3protein ubiquitination and degradationubiquitin-proteasome system

Identifiers

PMID30449221
PMCPMC6398165
OpenAlexW2900958920

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.