scholarly journals Protein disulfide isomerases are promising targets for predicting the survival and tumor progression in glioma patients

Aging ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 2347-2372 ◽  
Author(s):  
Zhigang Peng ◽  
Yu Chen ◽  
Hui Cao ◽  
Hecun Zou ◽  
Xin Wan ◽  
...  
Keyword(s):  
Tumor Progression ◽  
Protein Disulfide Isomerases ◽  
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.

scholarly journals Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

EMBO Reports ◽  
2002 ◽  
Vol 3 (2) ◽  
pp. 136-140 ◽  
Author(s):  
Robert B. Freedman ◽  
Peter Klappa ◽  
Lloyd W. Ruddock
Keyword(s):  
Specific Binding ◽  
Binding Domains ◽  
Protein Disulfide Isomerases ◽  
Disulfide Isomerases ◽  
Protein Disulfide
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