Evidence map›Paper›PMID 30066579›Full record

ReviewFuture medicinal chemistry2018

Discovering proteasomal deubiquitinating enzyme inhibitors for cancer therapy: lessons from rational design, nature and old drug reposition.

Kush Patel, Zainab So Ahmed, Xuemei Huang, Qianqian Yang, Elmira Ekinci, Christine M Neslund-Dudas, Bharati Mitra, Fawzy Aem Elnady, Young-Hoon Ahn, Huanjie Yang and 2 more

Abstract readReview
In one paragraph

Review in Future medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Degradation of CaMKII is stimulated by its active conformation.The Journal of biological chemistry · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Deubiquitinases: Modulators of Different Types of Regulated Cell Death.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Small molecules that target the ubiquitin system.Biochemical Society transactions · 2020
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. A patent review of the ubiquitin ligase system: 2015-2018.Expert opinion on therapeutic patents · 2018
    Review
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

12 authors at 6 institutions in 3 countries.

Kush PatelDepartments of Oncology, Pharmacology & Pathology, School of Medicine, Barbara Ann Karmanos Cancer Institute, Wayne State University, Detroit, MI 48201, USA.
Zainab So AhmedDepartments of Oncology, Pharmacology & Pathology, School of Medicine, Barbara Ann Karmanos Cancer Institute, Wayne State University, Detroit, MI 48201, USA.
Xuemei HuangDepartments of Oncology, Pharmacology & Pathology, School of Medicine, Barbara Ann Karmanos Cancer Institute, Wayne State University, Detroit, MI 48201, USA.
Qianqian YangProtein Modification & Degradation Lab, School of Basic Medical Sciences, Affiliated Tumor Hospital of Guangzhou Medical University, Guangzhou 510000, PR China.
Elmira EkinciDepartments of Oncology, Pharmacology & Pathology, School of Medicine, Barbara Ann Karmanos Cancer Institute, Wayne State University, Detroit, MI 48201, USA.
Christine M Neslund-DudasDepartment of Public Health Sciences & Henry Ford Cancer Institute, Henry Ford Health System, One Ford Place, Suite 5C, Detroit, MI 48202, USA.
Bharati MitraDepartment of Biochemistry, Microbiology & Immunology, Wayne State University School of Medicine, 540 E. Canfield Avenue, Detroit, MI 48201, USA.
Fawzy Aem ElnadyDepartment of Anatomy & Embryology, Faculty of Veterinary Medicine, Cairo University, Giza, Giza 12613, Egypt.
Young-Hoon AhnDepartment of Chemistry, Wayne State University, Detroit, MI 48202, USA.
Huanjie YangSchool of Life Science & Technology, Harbin Institute of Technology, Harbin 150001, PR China.
Jinbao LiuProtein Modification & Degradation Lab, School of Basic Medical Sciences, Affiliated Tumor Hospital of Guangzhou Medical University, Guangzhou 510000, PR China.
Qing Ping DouDepartments of Oncology, Pharmacology & Pathology, School of Medicine, Barbara Ann Karmanos Cancer Institute, Wayne State University, Detroit, MI 48201, USA.
Guangzhou Medical University · CNThe Barbara Ann Karmanos Cancer Institute · USWayne State University · USCairo University · EGHarbin Institute of Technology · CNHenry Ford Health System · US

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI PAUL M STEMMER · 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

The ubiquitin proteasome system has been validated as a target of cancer therapies evident by the US FDA approval of anticancer 20S proteasome inhibitors. Deubiquitinating enzymes (DUBs), an essential component of the ubiquitin proteasome system, regulate cellular processes through the removal of ubiquitin from ubiquitinated-tagged proteins. The deubiquitination process has been linked with cancer and other pathologies. As such, the study of proteasomal DUBs and their inhibitors has garnered interest as a novel strategy to improve current cancer therapies, especially for cancers resistant to 20S proteasome inhibitors. This article reviews proteasomal DUB inhibitors in the context of: discovery through rational design approach, discovery from searching natural products and discovery from repurposing old drugs, and offers a future perspective.

Indexed as

Drug DesignAnimalsAntineoplastic AgentsDeubiquitinating EnzymesDrug DiscoveryDrug RepositioningHumansNeoplasmsProteasome Endopeptidase ComplexProteasome InhibitorsUbiquitinUbiquitinationAntineoplastic AgentsDeubiquitinating EnzymesProteasome Endopeptidase ComplexProteasome InhibitorsUbiquitin19S26Scancerdeubiquitinating enzymesdrug repositionDUB inhibitorsmolecular targetingrational designubiquitin proteasome system

Identifiers

PMID30066579
PMCPMC6123888
OpenAlexW2887490389

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.