@article{7fe07874785643b895eca13fb8783e0b,
title = "Pdi family members as guides for client folding and assembly",
abstract = "Complicated and sophisticated protein homeostasis (proteostasis) networks in the endoplasmic reticulum (ER), comprising disulfide catalysts, molecular chaperones, and their regulators, help to maintain cell viability. Newly synthesized proteins inserted into the ER need to fold and assemble into unique native structures to fulfill their physiological functions, and this is assisted by protein disulfide isomerase (PDI) family. Herein, we focus on recent advances in understanding the detailed mechanisms of PDI family members as guides for client folding and assembly to ensure the efficient production of secretory proteins.",
keywords = "Assembly, Disassembly, Disulfide, Endoplasmic reticulum (ER), Protein disulfide isomerase (PDI) family, Protein folding, Redox",
author = "Shingo Kanemura and Motonori Matsusaki and Kenji Inaba and Masaki Okumura",
note = "Funding Information: This research was funded by JSPS KAKENHI Grant Number JP17H06521 (to S.K.), JP19K16092 (to S.K.), JP19J00893 (to M.M.), and JP20K15969 (to M.M.). We acknowledge, with thanks, funding from a Grant-in-Aid for Scientific Research on Innovative Areas from MEXT (19H04799 and 20H04688 to M.O.), the Takeda Science Foundation (to K.I. and M.O.), the Mochida Memorial Foundation for Medical and Pharmaceutical Research (to M.O.), the Japan Foundation of Applied Enzymology (to M.O.), the Building of Consortia for the Development of Human Resources in Science and Technology (to M.O.), the Naito foundation (to S.K.), a Grant-in-Aid for Scientific Research (C) to M.O (19K06520) and Scientific Research (A) to KI (18H03978), and the Promotion of Joint International Research (Fostering Joint International Research (B)) (20345793) (to M.O. and S.K.). Publisher Copyright: {\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland.",
year = "2020",
month = dec,
day = "2",
doi = "10.3390/ijms21249351",
language = "English",
volume = "21",
pages = "1--20",
journal = "International Journal of Molecular Sciences",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "24",
}