scholarly journals Role of Glutathione S‐Transferase Activity in Endoplasmic Reticulum Chaperone DsbA‐L in the Assembly of Adipocyte Homrone Adiponectin

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Laurel B. Kartchner ◽  
Pamela Malinowski ◽  
Tsu‐Shuen Tsao
2009 ◽  
Vol 18 (2) ◽  
pp. 433-443 ◽  
Author(s):  
Oxana Doroshyenko ◽  
Uwe Fuhr ◽  
Daria Kunz ◽  
Dorothee Frank ◽  
Martina Kinzig ◽  
...  

1995 ◽  
Vol 77 (5) ◽  
pp. 316-319 ◽  
Author(s):  
Juan A. Monti ◽  
Cristina E. Carnovale ◽  
Celina Scapini ◽  
Cristián Favre ◽  
María C. Carrillo

2014 ◽  
Vol 457 (3) ◽  
pp. 485-496 ◽  
Author(s):  
Monika Słomińska-Wojewódzka ◽  
Anna Pawlik ◽  
Iwona Sokołowska ◽  
Jakub Antoniewicz ◽  
Grzegorz Węgrzyn ◽  
...  

In this study we have investigated the role of the endoplasmic reticulum chaperone protein EDEM2 in ricin cytotoxicity and its retrotranslocation from the endoplasmic reticulum to the cytosol.


2015 ◽  
Vol 28 (1) ◽  
pp. 129-133 ◽  
Author(s):  
M Tesauro ◽  
S Nisticò ◽  
A Noce ◽  
A Tarantino ◽  
G Marrone ◽  
...  

Blood ◽  
1982 ◽  
Vol 60 (5) ◽  
pp. 1227-1230 ◽  
Author(s):  
JW Harvey ◽  
E Beutler

Human erythrocyte glutathione S-transferase activity is inhibited, probably competitively, by hemin with a Ki of 10(-7) M. It is postulated that glutathione S-transferase functions physiologically as a hemin-binding and/or transport protein in developing erythroid cells.


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