scholarly journals Multiple protein disulfide isomerases support thrombosis

2018 ◽  
Vol 25 (5) ◽  
pp. 395-402 ◽  
Author(s):  
David W. Essex ◽  
Yi Wu
Keyword(s):  
Protein Disulfide Isomerases ◽  
Multiple Protein ◽  
Disulfide Isomerases ◽  
Protein Disulfide

scholarly journals Characterization of Two Protein Disulfide Isomerases from the Endocytic Pathway of Bloodstream Forms of Trypanosoma brucei

2005 ◽  
Vol 280 (11) ◽  
pp. 10410-10418 ◽  
Author(s):  
Joyce Rubotham ◽  
Katherine Woods ◽  
Jose A. Garcia-Salcedo ◽  
Etienne Pays ◽  
Derek P. Nolan
Keyword(s):  
Trypanosoma Brucei ◽  
Endocytic Pathway ◽  
Protein Disulfide Isomerases ◽  
Disulfide Isomerases ◽  
Protein Disulfide

scholarly journals Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A

PLoS ONE ◽  
2017 ◽  
Vol 12 (3) ◽  
pp. e0174753 ◽  
Author(s):  
Benjamin Selles ◽  
Flavien Zannini ◽  
Jérémy Couturier ◽  
Jean-Pierre Jacquot ◽  
Nicolas Rouhier
Keyword(s):  
Catalytic Properties ◽  
Protein Disulfide Isomerases ◽  
Disulfide Isomerases ◽  
Protein Disulfide

Molecular Evolution of the Domain Structures of Protein Disulfide Isomerases

1998 ◽  
Vol 47 (2) ◽  
pp. 200-210 ◽  
Author(s):  
Satoru Kanai ◽  
Hiroyuki Toh ◽  
Toshiya Hayano ◽  
Masakazu Kikuchi
Keyword(s):  
Molecular Evolution ◽  
Domain Structures ◽  
Protein Disulfide Isomerases ◽  
Disulfide Isomerases ◽  
Protein Disulfide

scholarly journals Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases

2014 ◽  
Vol 461 (1) ◽  
pp. 107-113 ◽  
Author(s):  
Colin Shepherd ◽  
Ojore B. V. Oka ◽  
Neil J. Bulleid
Keyword(s):  
Endoplasmic Reticulum ◽  
Catalytic Activity ◽  
Specific Protein ◽  
Disulfide Formation ◽  
Protein Disulfide Isomerases ◽  
Disulfide Isomerases ◽  
Protein Disulfide

The formation of disulfides in proteins that enter the endoplasmic reticulum is essential for their folding. We show in the present study that a key component of the machinery for disulfide formation is negatively regulated by the product of its catalytic activity.

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