Unknown

Dataset Information

0

The role of ubiquitin-specific peptidases in cancer progression.


ABSTRACT: Protein ubiquitination is an important mechanism for regulating the activity and levels of proteins under physiological conditions. Loss of regulation by protein ubiquitination leads to various diseases, such as cancer. Two types of enzymes, namely, E1/E2/E3 ligases and deubiquitinases, are responsible for controlling protein ubiquitination. The ubiquitin-specific peptidases (USPs) are the main members of the deubiquitinase family. Many studies have addressed the roles of USPs in various diseases. An increasing number of studies have indicated that USPs are critical for cancer progression, and some USPs have been used as targets to develop inhibitors for cancer prevention. Herein we collect and organize most of the recent studies on the roles of USPs in cancer progression and discuss the development of USP inhibitors for cancer therapy in the future.

SUBMITTER: Young MJ 

PROVIDER: S-EPMC6537419 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

The role of ubiquitin-specific peptidases in cancer progression.

Young Ming-Jer MJ   Hsu Kai-Cheng KC   Lin Tony Eight TE   Chang Wen-Chang WC   Hung Jan-Jong JJ  

Journal of biomedical science 20190527 1


Protein ubiquitination is an important mechanism for regulating the activity and levels of proteins under physiological conditions. Loss of regulation by protein ubiquitination leads to various diseases, such as cancer. Two types of enzymes, namely, E1/E2/E3 ligases and deubiquitinases, are responsible for controlling protein ubiquitination. The ubiquitin-specific peptidases (USPs) are the main members of the deubiquitinase family. Many studies have addressed the roles of USPs in various disease  ...[more]

Similar Datasets

| S-EPMC8304380 | biostudies-literature
| S-EPMC7377023 | biostudies-literature
| S-EPMC4362669 | biostudies-literature
| S-EPMC6693180 | biostudies-literature
2014-06-01 | E-GEOD-57139 | biostudies-arrayexpress
| S-EPMC5850909 | biostudies-other
| S-EPMC5481909 | biostudies-literature
| S-EPMC8469789 | biostudies-literature
| S-EPMC7862665 | biostudies-literature
| S-EPMC8484750 | biostudies-literature