scholarly journals Cytoplasmic activated protein kinase Akt regulates lipid-droplet accumulation in Drosophila nurse cells

Development ◽  
2006 ◽  
Vol 133 (23) ◽  
pp. 4731-4735 ◽  
Author(s):  
N. Vereshchagina ◽  
C. Wilson
Keyword(s):  
Protein Kinase ◽  
Lipid Droplet ◽  
Nurse Cells ◽  
Protein Kinase Akt

scholarly journals The HMG-CoA reductase inhibitor simvastatin activates the protein kinase Akt and promotes angiogenesis in normocholesterolemic animals.

10.1038/79510 ◽  
2000 ◽  
Vol 6 (9) ◽  
pp. 1004-1010 ◽  
Author(s):  
Yasuko Kureishi ◽  
Zhengyu Luo ◽  
Ichiro Shiojima ◽  
Ann Bialik ◽  
David Fulton ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Reductase Inhibitor ◽  
Hmg Coa Reductase ◽  
Hmg Coa Reductase Inhibitor ◽  
Coa Reductase ◽  
Protein Kinase Akt

Activation of the serine/threonine protein kinase Akt during the progression of Barrett neoplasia

2007 ◽  
Vol 38 (10) ◽  
pp. 1526-1531 ◽  
Author(s):  
Elizabeth Sagatys ◽  
Christopher R. Garrett ◽  
David Boulware ◽  
Scott Kelley ◽  
Mokenge Malafa ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Akt

scholarly journals Development and characterization of Protein Kinase B/AKT isoform-specific Nanobodies

2020 ◽  
Author(s):  
Tijs Merckaert ◽  
Olivier Zwaenepoel ◽  
Kris Gevaert ◽  
Jan Gettemans
Keyword(s):  
Protein Kinase ◽  
Mammalian Cells ◽  
Specific Inhibitor ◽  
Akt Inhibitor ◽  
Different Types ◽  
Approaches To Study ◽  
Complex Target ◽  
Protein Kinase Akt ◽  
Prime Target

Abstract Background The serine/threonine protein kinase AKT is frequently over-activated in cancer and is associated with poor prognosis. As a central node in the PI3K/AKT/mTOR pathway, which regulates various processes considered to be hallmarks of cancer, this kinase has become a prime target for cancer therapy. However, AKT has proven to be a highly complex target as it comes in three isoforms (AKT1, AKT2 and AKT3) which are highly homologous, yet non-redundant. The isoform-specific functions of the AKT kinases can be dependent on context (i.e. different types of cancer) and even opposed to one another. To date, there is no isoform-specific inhibitor available and no alternative to genetic approaches to study the function of a single AKT isoform. Results We have developed and characterized nanobodies that specifically interact with the AKT1 or AKT2 isoforms. These new tools should enable future studies of AKT1 and AKT2 isoform-specific functions. Furthermore, for both isoforms we obtained a nanobody that interferes with the AKT-PIP3-interaction, an essential step in the activation of the kinase. Conclusions The nanobodies characterized in this study, which can be expressed in mammalian cells, are a new stepping stone towards unravelling AKT isoform-specific signalling and can lead to the first isoform-specific AKT inhibitor.

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