Small-molecule FRET probes for protein kinase activity monitoring in living cells

2010 ◽  
Vol 397 (4) ◽  
pp. 750-755 ◽  
Author(s):  
Angela Vaasa ◽  
Marje Lust ◽  
Anna Terrin ◽  
Asko Uri ◽  
Manuela Zaccolo
Keyword(s):  
Protein Kinase ◽  
Small Molecule ◽  
Kinase Activity ◽  
Living Cells ◽  
Activity Monitoring ◽  
Protein Kinase Activity

scholarly journals Real Time Visualization of Protein Kinase Activity in Living Cells

2002 ◽  
Vol 277 (13) ◽  
pp. 11527-11532 ◽  
Author(s):  
Ren-Hwa Yeh ◽  
Xiongwei Yan ◽  
Michael Cammer ◽  
Anne R. Bresnick ◽  
David S. Lawrence
Keyword(s):  
Protein Kinase ◽  
Real Time ◽  
Kinase Activity ◽  
Living Cells ◽  
Protein Kinase Activity ◽  
Real Time Visualization

Effect of Thrombin on Phosphorylation of Platelet Membrane Proteins

1976 ◽  
Vol 35 (03) ◽  
pp. 635-642 ◽  
Author(s):  
M Steiner
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Qualitative Change ◽  
Protein Kinase Activity ◽  
Protein Substrates ◽  
Phosphoprotein Phosphatase ◽  
Progressive Loss ◽  
Platelet Membranes ◽  
Endogenous Protein ◽  
Considerable Loss

SummaryThe effect of thrombin on the phosphorylating activity of platelet membranes was compared to that of trypsin. Preincubation of non-32P phosphorylated platelet membranes with or without either of these two enzymes resulted in a considerable loss of membrane protein kinase activity which was most severe when trypsin was used. Protein kinase activity and endogenous protein acceptors decreased in parallel. 32P-phosphorylated membranes showed a slow but progressive loss of label which was accelerated by trypsin. Thrombin under these conditions prevented the loss of 32P-phosphate. These results are interpreted to indicate a thrombin-induced destruction of a phosphoprotein phosphatase. The protein kinase activity of phosphorylated platelet membranes using endogenous or exogenous protein substrates showed a significant reduction compared to non-phosphorylated membranes suggesting a deactivation of protein kinase by phosphorylation of platelet membranes. Neither thrombin nor trypsin caused a qualitative change in the membrane polypeptides accepting 32P-phosphate but resulted in quantitative alterations of their ability to become phosphorylated.

scholarly journals Evidence for Ecto-Protein Kinase Activity That Phosphorylates Kemptide in a Cyclic AMP-dependent Mode

1989 ◽  
Vol 264 (24) ◽  
pp. 14549-14555 ◽  
Author(s):  
D Kübler ◽  
W Pyerin ◽  
O Bill ◽  
A Hotz ◽  
J Sonka ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Protein Kinase Activity

scholarly journals Gradual Loss of a DNA-Inducible Protein Kinase Activity From the Cytoplasmic Extracts of Arbacia Embryos

1996 ◽  
Vol 191 (2) ◽  
pp. 281-282 ◽  
Author(s):  
J. Kanungo ◽  
B. Calhoun ◽  
Y. Takeda ◽  
J. A. Hardin ◽  
H. Rasmussen
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Gradual Loss ◽  
Inducible Protein
Sign in / Sign up

Export Citation Format

Share Document