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Lana Bozulic

Researcher at Friedrich Miescher Institute for Biomedical Research

Publications -  6
Citations -  961

Lana Bozulic is an academic researcher from Friedrich Miescher Institute for Biomedical Research. The author has contributed to research in topics: AKT1 & Protein kinase B. The author has an hindex of 6, co-authored 6 publications receiving 902 citations.

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Journal ArticleDOI

PKBα/Akt1 Acts Downstream of DNA-PK in the DNA Double-Strand Break Response and Promotes Survival

TL;DR: This work reports a route by which activated PKB promotes survival in response to DNA insults in vivo, and places PKB downstream of DNA-PK in the DNA damage response signaling cascade, where it provides a prosurvival signal.
Book ChapterDOI

Protein kinase B (PKB/Akt), a key mediator of the PI3K signaling pathway.

TL;DR: The remarkable complexity in the regulation of PKB signaling downstream of PI3K could be attributed to the specific roles of the PKB isoforms, their expression pattern, subcellular localization, targets, phosphorylation by upstream kinases in a stimulus- and context-dependent manner and by phosphatases, and interaction with binding partners.
Journal ArticleDOI

PIKKing on PKB: regulation of PKB activity by phosphorylation.

TL;DR: PKB regulation by mTORC2 and DNA-PK in a stimulus-dependent and context-dependent manner and the possible implications of this for PKB activity, substrate specificity and therapeutic intervention are reviewed.
Journal ArticleDOI

In vivo analysis of protein kinase B (PKB)/Akt regulation in DNA-PKcs-null mice reveals a role for PKB/Akt in DNA damage response and tumorigenesis.

TL;DR: It is revealed that DNA-PK is required for DNA damage-induced phosphorylation but dispensable for insulin- and growth factor-induced PKB Ser-473 phosphorylated, and genetic evidence of PKB deregulation in DNA- PKcs-/- mice is provided.
Journal ArticleDOI

Carboxy-Terminal Modulator Protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis.

TL;DR: The Carboxy-Terminal Modulator Protein (CTMP) protein was identified as a PKB inhibitor that binds to its hydrophobic motif as mentioned in this paper, and it exhibits a dual sub-mitochondrial localization as a membrane bound pool and a free pool of mature CTMP in the inter-membrane space.