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Inhibition of Proteasomal Deubiquitinase by Silver Complex Induces Apoptosis in Non-Small Cell Lung Cancer Cells
Author(s) -
Xin Chen,
Qianqian Yang,
Jinghong Chen,
Peiquan Zhang,
Qingtian Huang,
Xiaolan Zhang,
Yang Li,
Dacai Xu,
Chong Zhao,
Xuejun Wang,
Jinbao Liu
Publication year - 2018
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000493041
Subject(s) - deubiquitinating enzyme , proteasome , viability assay , ubiquitin , apoptosis , chemistry , flow cytometry , microbiology and biotechnology , intracellular , cancer cell , cancer research , cell growth , biology , biochemistry , cancer , genetics , gene
The ubiquitin proteasome system (UPS) is responsible for the degradation of most intracellular proteins, and proteasomal deubiquitinases (DUBs) have recently been highlighted as novel anticancer targets. It is well documented that copper complexes can inhibit UPS function through targeting both 20S proteasome and proteasomal DUBs. The antineoplastic activities of silver complexes have received much attention, but the exact mechanisms are not fully elucidated. In this study, we aim to investigate the effects of a novel silver complex [Ag(S2CN(C2H5)2)]6 (AgDT) on UPS function and its anticancer potential in non-small cell lung cancer (NSCLC).

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