Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein
Tetrathiomolybdate (TM) and Cu-ATPases, e.g. Wilson (WLN) protein, affect the efficacy of common anticancer drug cisplatin. Here, the authors show that TM generates a protein dimer with a WLN domain by expelling copper and provide insight into the synergy of TM and cisplatin in cancer chemotherapy.
Bibliographic Details
| Main Authors: |
Tiantian Fang,
Wanbiao Chen,
Yaping Sheng,
Siming Yuan,
Qiaowei Tang,
Gongyu Li,
Guangming Huang,
Jihu Su,
Xuan Zhang,
Jianye Zang,
Yangzhong Liu |
|---|
| Format: | Article
|
|---|
| Language: | English |
|---|
| Published: |
Nature Publishing Group
2019-01-01
|
|---|
| Series: | Nature Communications
|
|---|
| Online Access: | https://doi.org/10.1038/s41467-018-08102-z
|
|---|
