The Nonactive Site Cysteine Residues of Yeast Protein Disulfide Isomerase Are Not Required for Cell Viability

1998 ◽  
Vol 248 (3) ◽  
pp. 621-627 ◽  
Author(s):  
José M. Luz ◽  
William J. Lennarz
2020 ◽  
Vol 21 (24) ◽  
pp. 9351
Author(s):  
Shingo Kanemura ◽  
Motonori Matsusaki ◽  
Kenji Inaba ◽  
Masaki Okumura

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.


2004 ◽  
Vol 320 (2) ◽  
pp. 359-365 ◽  
Author(s):  
Taiji Kimura ◽  
Yasuhiro Hosoda ◽  
Yukiko Kitamura ◽  
Hideshi Nakamura ◽  
Tomohisa Horibe ◽  
...  

2009 ◽  
Vol 3 (1) ◽  
pp. 27-32
Author(s):  
PURKAN PURKAN ◽  
LALU RUDYAT TELLY SAVALAS ◽  
MULIAWATI SINDUMARTA ◽  
DESSY NATALIA

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