proteomics tool
Recently Published Documents


TOTAL DOCUMENTS

17
(FIVE YEARS 1)

H-INDEX

9
(FIVE YEARS 1)

Author(s):  
Juan J. Calvete ◽  
José María Gutiérrez ◽  
Libia Sanz ◽  
Davinia Pla ◽  
Bruno Lomonte
Keyword(s):  

2015 ◽  
Vol 14 (2) ◽  
pp. 1315-1329 ◽  
Author(s):  
Nina C. Hubner ◽  
Luan N. Nguyen ◽  
Nadine C. Hornig ◽  
Hendrik G. Stunnenberg

ChemBioChem ◽  
2012 ◽  
Vol 13 (13) ◽  
pp. 1829-1829
Author(s):  
Lalit Kumar Sharma ◽  
Na-Ra Lee ◽  
Eun Ryoung Jang ◽  
Beilei Lei ◽  
Chang-Guo Zhan ◽  
...  

ChemBioChem ◽  
2012 ◽  
Vol 13 (13) ◽  
pp. 1899-1903 ◽  
Author(s):  
Lalit Kumar Sharma ◽  
Na-Ra Lee ◽  
Eun Ryoung Jang ◽  
Beilei Lei ◽  
Chang-Guo Zhan ◽  
...  

2010 ◽  
Vol 38 (4) ◽  
pp. 1006-1011 ◽  
Author(s):  
Isabelle Landrieu ◽  
Arnaud Leroy ◽  
Caroline Smet-Nocca ◽  
Isabelle Huvent ◽  
Laziza Amniai ◽  
...  

NMR spectroscopy was used to explore the different aspects of the normal and pathological functions of tau, but proved challenging because the protein contains 441 amino acids and has poor signal dispersion. We have set out to dissect the phosphorylation patterns of tau in order to understand better its role in the aggregation process and microtubule-binding regulation. Our current knowledge on the functional consequences of specific phosphorylations is still limited, mainly because producing and assessing quantitatively phosphorylated tau samples is far from straightforward, even in vitro. We use NMR spectroscopy as a proteomics tool to characterize the phosphorylation patterns of tau, after in vitro phosphorylation by recombinant kinases. The phosphorylated tau can next be use for functional assays or interaction assays with phospho-dependent protein partners, such as the prolyl cis–trans isomerase Pin1.


Sign in / Sign up

Export Citation Format

Share Document