Phosphoinositides in Subcellular Targeting and Enzyme Activation

2004 ◽  
2018 ◽  
Author(s):  
Fei He ◽  
Li Mi ◽  
Yanfei Shen ◽  
Toshiyuki Mori ◽  
Songqin Liu ◽  
...  

Developing highly efficient artificial enzymes that directly employ O<sub>2</sub> as terminal oxidant has long been pursued but has rarely achieved yet. We report Fe-N-C has unusual enzyme-like activity in both dehydrogenation and monoxygenation of organic substrates with ~100% selectivity by direct using O<sub>2</sub>.


Author(s):  
Vimala Bondada ◽  
Jozsef Gal ◽  
Charles Mashburn ◽  
David W. Rodgers ◽  
Katherine E. Larochelle ◽  
...  

2011 ◽  
Vol 1 (1) ◽  
Author(s):  
Gabriel Ortega ◽  
Ana Laín ◽  
Xavier Tadeo ◽  
Blanca López-Méndez ◽  
David Castaño ◽  
...  

2014 ◽  
Vol 23 (24) ◽  
pp. 3049-3064 ◽  
Author(s):  
Jill A. Slater ◽  
Sichang Zhou ◽  
Elizabeth Ella Puscheck ◽  
Daniel A. Rappolee

2005 ◽  
Vol 187 (3) ◽  
pp. 1192-1195 ◽  
Author(s):  
Hiromi Sato ◽  
Jimmy B. Feix ◽  
Cecilia J. Hillard ◽  
Dara W. Frank

ABSTRACT Recombinant ExoU (rExoU) and yeast extract were used to optimize an in vitro phospholipase assay as a basis for identifying the mechanism for enzyme activation and substrate specificity. Our results support a model in which a eukaryotic protein cofactor or complex facilitates the interaction of rExoU with phospholipid substrates.


2011 ◽  
Vol 13 (6) ◽  
pp. 2307-2313 ◽  
Author(s):  
Olga A. Sytina ◽  
Maxime T. Alexandre ◽  
Derren J. Heyes ◽  
C. Neil Hunter ◽  
Bruno Robert ◽  
...  

2011 ◽  
Vol 6 (7) ◽  
pp. 1026-1029 ◽  
Author(s):  
Nadav Sorek ◽  
Yoav Henis ◽  
Shaul Yalovsky

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