Induction of autophagy promotes the growth of early preneoplastic rat liver nodules.
Cagliari, Italy. In Oncotarget, Jan 2016
The ultrastructural and immunohistochemical analyses of KRT-19-positive preneoplastic hepatocytes showed the presence of autophagic vacuoles which was associated with p62, Ambra1 and Beclin1 protein accumulation suggesting that a differential modulation of autophagy occurs at early stages of the oncogenesis in KRT-19-positive vs negative lesions.
Ambra1 at a glance.
Roma, Italy. In J Cell Sci, Jul 2015
The activating molecule in Beclin-1-regulated autophagy (Ambra1), also known as autophagy/Beclin-1 regulator 1, is a highly intrinsically disordered and vertebrate-conserved adapter protein that is part of the autophagy signaling network.
Enhanced Autophagy of Adipose-Derived Stem Cells Grown on Chitosan Substrates.
Taipei, Taiwan. In Biores Open Access, 2014
The upstream components of autophagy signal pathway-UNC51-like kinase 1 (Ulk1), autophagy-related protein 13 (Atg13), and autophagy/beclin-1 regulator 1 (Ambra1) genes were more highly expressed in ADSC spheroids before and after adding H2O2 than those in the conventional culture.
Beclin-1 and its role as a target for anticancer therapy.
Poznań, Poland. In J Physiol Pharmacol, 2014
Beclin-1 is a protein that plays a central role in autophagy; it interacts with multiple cofactors (Atg14L, UVRAG, Bif-1, Rubicon, Ambra1, HMGB1, IP3R, PINK and survivin) to promote the formation of the Beclin-1-Vps34-Vps15 complex which triggers the autophagy protein cascade.
Ambra1 at the crossroad between autophagy and cell death.
Roma, Italy. In Oncogene, 2013
This review is focused on the role that Ambra1, a central component of the autophagosome formation machinery, has in the switch between autophagy and apoptosis and its implication in cancer development and chemotherapy resistance.
Beclin-1: autophagic regulator and therapeutic target in cancer.
Chengdu, China. In Int J Biochem Cell Biol, 2013
Recent data indicate that Beclin-1 may interact with some co-factors such as Class III phosphatidylinositol 3-kinase (PI3KCIII)/Vps34, Vps15, ATG14L/Barkor, UVRAG, Bif-1, Rubicon, Ambra1, HMGB1, Survivin, Akt and Bcl-2/Bcl-XL to positively or negatively orchestrate the Beclin-1 interactome, thereby co-regulating the autophagy process.
The Beclin 1 network regulates autophagy and apoptosis.
Pittsburgh, United States. In Cell Death Differ, 2011
It interacts with several cofactors (Atg14L, UVRAG, Bif-1, Rubicon, Ambra1, HMGB1, nPIST, VMP1, SLAM, IP(3)R, PINK and survivin) to regulate the lipid kinase Vps-34 protein and promote formation of Beclin 1-Vps34-Vps15 core complexes, thereby inducing autophagy.