| Literature DB >> 33302492 |
Shingo Kanemura1, Motonori Matsusaki2,3, Kenji Inaba2, Masaki Okumura3.
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.Entities:
Keywords: assembly; disassembly; disulfide; endoplasmic reticulum (ER); protein disulfide isomerase (PDI) family; protein folding; redox
Year: 2020 PMID: 33302492 PMCID: PMC7763558 DOI: 10.3390/ijms21249351
Source DB: PubMed Journal: Int J Mol Sci ISSN: 1422-0067 Impact factor: 5.923