Light‐controlled Tyrosine Nitration of Proteins

Author(s):  
Tengfang Long ◽  
Lei Liu ◽  
Youqi Tao ◽  
Wanli Zhang ◽  
Jiale Quan ◽  
...  
Keyword(s):  
2003 ◽  
Vol 8 (4) ◽  
pp. 407-412 ◽  
Author(s):  
M H Tran ◽  
K Yamada ◽  
A Nakajima ◽  
M Mizuno ◽  
J He ◽  
...  

2008 ◽  
Vol 7 (6) ◽  
pp. 1188-1189
Author(s):  
Xianquan Zhan ◽  
Yunpeng Du ◽  
John S. Crabb ◽  
Xiaorong Gu ◽  
Timothy S. Kern ◽  
...  

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Benedikt Frieg ◽  
Boris Görg ◽  
Holger Gohlke ◽  
Dieter Häussinger

Abstract Glutamine synthetase (GS) in the liver is expressed in a small perivenous, highly specialized hepatocyte population and is essential for the maintenance of low, non-toxic ammonia levels in the organism. However, GS activity can be impaired by tyrosine nitration of the enzyme in response to oxidative/nitrosative stress in a pH-sensitive way. The underlying molecular mechanism as investigated by combined molecular simulations and in vitro experiments indicates that tyrosine nitration can lead to a fully reversible and pH-sensitive regulation of protein function. This approach was also used to understand the functional consequences of several recently described point mutations of human GS with clinical relevance and to suggest an approach to restore impaired GS activity.


2011 ◽  
Vol 32 (13) ◽  
pp. 1692-1705 ◽  
Author(s):  
Joy D. Guingab-Cagmat ◽  
Stanley M. Stevens ◽  
Mary V. Ratliff ◽  
Zhiqun Zhang ◽  
Mark S. Gold ◽  
...  
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2009 ◽  
Vol 60 (15) ◽  
pp. 4221-4234 ◽  
Author(s):  
Mounira Chaki ◽  
Raquel Valderrama ◽  
Ana M. Fernández-Ocaña ◽  
Alfonso Carreras ◽  
Javier López-Jaramillo ◽  
...  

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