Hydrogen peroxide dependent interaction of peroxiredoxin 2 with ERp46

2012 ◽  
Vol 53 ◽  
pp. S210
Author(s):  
P.E. Pace⁎ ◽  
A.V. Peskin ◽  
M.B. Hampton ◽  
C.C. Winterbourn
2021 ◽  
pp. 100494
Author(s):  
Alexander V. Peskin ◽  
Flavia C. Meotti ◽  
Kelsey M. Kean ◽  
Christoph Göbl ◽  
Albert Souza Peixoto ◽  
...  

Redox Biology ◽  
2021 ◽  
Vol 43 ◽  
pp. 101980
Author(s):  
Andree G. Pearson ◽  
Juliet M. Pullar ◽  
John Cook ◽  
Emma S. Spencer ◽  
Margreet CM. Vissers ◽  
...  

2014 ◽  
Vol 93 (5) ◽  
pp. 992-1009 ◽  
Author(s):  
Suyeon Kim ◽  
Ye-Ji Bang ◽  
Dukyun Kim ◽  
Jong Gyu Lim ◽  
Man Hwan Oh ◽  
...  

2013 ◽  
Vol 47 (3) ◽  
pp. 164-171 ◽  
Author(s):  
E. Nagababu ◽  
J. G. Mohanty ◽  
J. S. Friedman ◽  
J. M. Rifkind

Talanta ◽  
2013 ◽  
Vol 107 ◽  
pp. 146-153 ◽  
Author(s):  
Guang-Li Wang ◽  
Xiao-Ying Zhu ◽  
Yu-Ming Dong ◽  
Huan-Jun Jiao ◽  
Xiu-Ming Wu ◽  
...  

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Deepti Talwar ◽  
Joris Messens ◽  
Tobias P. Dick

Abstract Hydrogen peroxide (H2O2) is recognized to act as a signaling molecule. Peroxiredoxins (Prxs) have the ability to transfer H2O2-derived oxidizing equivalents to redox-regulated target proteins, thus facilitating the transmission of H2O2 signals. It has remained unclear how Prxs and their target proteins are brought together to allow for target-specific protein thiol oxidation. Addressing the specific case of Prx2-dependent STAT3 oxidation, we here show that the association of the two proteins occurs prior to Prx oxidation and depends on a scaffolding protein, the membrane chaperone annexin A2. Deletion or depletion of annexin A2 interrupts the transfer of oxidizing equivalents from Prx2 to STAT3, which is observed to take place on membranes. These findings support the notion that the Prx2-STAT3 redox relay is part of a highly organized membrane signaling domain.


2009 ◽  
Vol 43 (1) ◽  
pp. 68-73 ◽  
Author(s):  
Susana Rocha ◽  
Elísio Costa ◽  
Susana Coimbra ◽  
Henrique Nascimento ◽  
Cristina Catarino ◽  
...  

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