scispace - formally typeset
D

Daniela Brodbeck

Researcher at Friedrich Miescher Institute for Biomedical Research

Publications -  5
Citations -  1165

Daniela Brodbeck is an academic researcher from Friedrich Miescher Institute for Biomedical Research. The author has contributed to research in topics: Protein kinase A & Phosphorylation. The author has an hindex of 5, co-authored 5 publications receiving 1126 citations.

Papers
More filters
Journal ArticleDOI

Protein Kinase Bα/Akt1 Regulates Placental Development and Fetal Growth

TL;DR: It is shown that PKBα is widely expressed in placenta including all types of trophoblast and vascular endothelial cells and shows significant hypotrophy, with marked reduction of the decidual basalis and nearly complete loss of glycogen-containing cells in the spongiotrophoblast, and exhibit decreased vascularization.
Journal ArticleDOI

A Human Protein Kinase Bγ with Regulatory Phosphorylation Sites in the Activation Loop and in the C-terminal Hydrophobic Domain

TL;DR: Cloned human protein kinase Bγ (PKBγ) is found that it contains two regulatory phosphorylation sites, Thr305 and Ser472, which correspond to Thr308 and Ser473 of PKBα, which differs significantly from the previously published rat PKBγ.
Journal ArticleDOI

Mechanism of Protein Kinase B Activation by Insulin/Insulin-Like Growth Factor-1 Revealed by Specific Inhibitors of Phosphoinositide 3-Kinase—Significance for Diabetes and Cancer

TL;DR: Stimulation of PKB activity protects cells from apoptosis by phosphorylation and inactivation of the pro-apoptotic protein BAD, which could explain why PKB is overexpressed in some ovarian, breast, and pancreatic carcinomas.
Journal ArticleDOI

Two Splice Variants of Protein Kinase Bγ Have Different Regulatory Capacity Depending on the Presence or Absence of the Regulatory Phosphorylation Site Serine 472 in the Carboxyl-terminal Hydrophobic Domain

TL;DR: Results suggest that phosphorylation of the hydrophobic motif at the extreme C terminus of PKBγ may facilitate translocation of the kinase to the membrane and/or its phosphorylated on the activation loop site by phosphoinositide-dependent protein kinase-1.