@inbook{5145caaef0394b358344a26aaa030f9c,
title = "Protein disulfide isomerase family mediated redox regulation in cancer",
abstract = "Protein disulfide isomerase (PDI) and its superfamilies are mainly endoplasmic reticulum (ER) resident proteins with essential roles in maintaining cellular homeostasis, via thiol oxidation/reduction cycles, chaperoning, and isomerization of client proteins. Since PDIs play an important role in ER homeostasis, their upregulation supports cell survival and they are found in a variety of cancer types. Despite the fact that the importance of PDI to tumorigenesis remains to be understood, it is emerging as a new therapeutic target in cancer. During the past decade, several PDI inhibitors has been developed and commercialized, but none has been approved for clinical use. In this review, we discuss the properties and redox regulation of PDIs within the ER and provide an overview of the last 5 years of advances regarding PDI inhibitors.",
keywords = "Cancer, ER stress, Inhibitors, Protein disulfide isomerase, Redox regualtion",
author = "Ye, \{Zhi wei\} and Jie Zhang and Muhammad Aslam and Anna Blumental-Perry and Tew, \{Kenneth D.\} and Townsend, \{Danyelle M.\}",
note = "Publisher Copyright: {\textcopyright} 2023",
year = "2023",
month = jan,
doi = "10.1016/bs.acr.2023.06.001",
language = "English",
isbn = "9780443192807",
series = "Advances in Cancer Research",
publisher = "Academic Press Inc.",
pages = "83--106",
editor = "Tew, \{Kenneth D.\} and Fisher, \{Paul B.\}",
booktitle = "Advances in Cancer Research",
address = "United States",
}