Evidence map›Paper›PMID 23142973›Full record

ArticleJournal of inorganic biochemistry2013

Cellular and computational studies of proteasome inhibition and apoptosis induction in human cancer cells by amino acid Schiff base-copper complexes.

Jian Zuo, Caifeng Bi, Yuhua Fan, Daniela Buac, Chiara Nardon, Kenyon G Daniel, Q Ping Dou

Abstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 107 citations in OpenAlex.

  1. Copper Complexes: Main Mechanisms as Anticancer Agents.Molecules (Basel, Switzerland) · 2026
    Review
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  9. Role of Copper on Mitochondrial Function and Metabolism.Frontiers in molecular biosciences · 2021
    Review
  10. Review
  11. Article
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  13. Review
  14. Article
  15. Article
  16. Review
  17. L-Ornithine Schiff base-copper and -cadmium complexes as new proteasome inhibitors and apoptosis inducers in human cancer cells.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
  18. Article
  19. Article
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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

7 authors at 5 institutions in 3 countries.

Jian ZuoCollege of Chemistry and Chemical Engineering, Ocean University of China, Qingdao, Shandong 266100, People's Republic of China.
Caifeng Bi
Yuhua Fan
Daniela Buac
Chiara Nardon
Kenyon G Daniel
Q Ping Dou
Ocean University of China · CNThe Barbara Ann Karmanos Cancer Institute · USUniversity of Padua · ITUniversity of South Florida · USWayne State University · US

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI PAUL M STEMMER · 1985 to 2026
$68.4M
Roles of polymorphic COMT, tea polyphenols and proteasome in cancer preventionR01CA120009 · NCI · WAYNE STATE UNIVERSITY · PI DOU, QING PING · 2006 to 2010
$1.5M
The BCA2 Ubiquitin E3 Ligase as a Target in Breast CancerR01CA127258 · NCI · WAYNE STATE UNIVERSITY · PI DOU, QING PING · 2007 to 2011
$1.2M
NCI NIH HHS 1R01CA120009NCI NIH HHS 3R01CA120009-04S1NCI NIH HHS 5R01CA127258NCI NIH HHS P30 CA022453NCI NIH HHS R01 CA120009NCI NIH HHS R01 CA127258
6 · The paper itself

Abstract

Proliferation and apoptosis pathways are tightly regulated in a cell by the ubiquitin-proteasome system (UPS) and alterations in the UPS may result in cellular transformation or other pathological conditions. Indeed, the proteasome is often found to be overactive in cancer cells. It has also been found that cancer cells are more sensitive to proteasome inhibition than normal cells, and therefore proteasome inhibitors are pursued as antitumor drugs. The use of the proteasome inhibitor Bortezomib for treatment of multiple myeloma and mantle cell lymphoma has proved this principle. Recent studies have suggested that copper complexes can inhibit proteasome activity and induce apoptosis in some human cancer cells. However, the involved molecular mechanism is unknown. In this study, we investigated the biological activities of four amino acid Schiff base-copper(II) complexes by using human breast (MDA-MB-231 and MCF-7) and prostate (PC-3) cancer cells. The complexes C1 and C3, but not their counterparts C2 and C4, inhibit the chymotrypsin-like activity of purified 20S proteasome and human cancer cellular 26S proteasome, cause accumulation of proteasome target proteins Bax and IκB-α, and induce growth inhibition and apoptosis in concentration- and time-dependent manners. Docking analysis shows that C1, but not C2 has hydrophobic, pi-pi, pi-cation and hydrogen bond interactions with the proteasomal chymotrypsin-like pocket and could stably fit into the S3 region, leading to specific inhibition. Our study has identified the mechanism of action of these copper complexes on inhibiting tumor cell proteasome and suggested their great potential as novel anticancer agents.

Indexed as

Amino AcidsAntineoplastic AgentsApoptosisCatalytic DomainCell Line, TumorCell ProliferationCell SurvivalCoordination ComplexesCrystallography, X-RayHumansMolecular ConformationMolecular Docking SimulationProteasome Endopeptidase ComplexProteasome InhibitorsProtein BindingSchiff BasesAmino AcidsAntineoplastic AgentsCoordination ComplexesProteasome Endopeptidase ComplexProteasome InhibitorsSchiff Bases

Identifiers

PMID23142973
PMCPMC3676669
OpenAlexW1991078204

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.