TY  -  
T1  - Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling 
SN  -  /  
UR  - http://hdl.handle.net/10138/162434 
T3  -  
A1  - Kauko, Otto; Laajala, Teemu Daniel; Jumppanen, Mikael; Hintsanen, Petteri; Suni, Veronika; Haapaniemi, Pekka; Corthals, Garry; Aittokallio, Tero; Westermarck, Jukka; Imanishi, Susumu Y. 
A2  -  
PB  -  
Y1  - 2015 
LA  - eng 
AB  - Hyperactivated RAS drives progression of many human malignancies. However, oncogenic activity of RAS is dependent on simultaneous inactivation of protein phosphatase 2A (PP2A) activity. Although PP2A is known to regulate some of the RAS effector pathways, it has not been systematically assessed how these proteins functionally interact. Here we have analyzed phosphoproteomes regulated by either RAS or PP2A, by phosphopeptide enrichment followed by mass-spectrometry-based label-free quantification... 
VO  -  
IS  -  
SP  -  
OP  -  
KW  - PROTEIN PHOSPHATASE 2A; CANCER GENOMICS BROWSER; CELL-TRANSFORMATION; H-RAS; K-RAS; PHOSPHORYLATION DYNAMICS; PROTEOMICS ANALYSIS; TUMOR-SUPPRESSOR; OVARIAN-CANCER; IN-VIVO; 3111 Biomedicine 
N1  -   
PP  -  
ER  -