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Human Beclin 1 Protein expressed in HEK-293 Cells - ABIN2715218
Zhu, Messer, Wang, Lin, Cham, Chang, Billiar, Lotze, Boone, Chang: Cytosolic HMGB1 controls the cellular autophagy/apoptosis checkpoint during inflammation. in The Journal of clinical investigation 2015
Human Beclin 1 Protein expressed in Wheat germ - ABIN1346622
Giatromanolaki, Koukourakis, Koutsopoulos, Chloropoulou, Liberis, Sivridis: High Beclin 1 expression defines a poor prognosis in endometrial adenocarcinomas. in Gynecologic oncology 2011
Show all 3 Pubmed References
Beclin1 plays an important role in vincristine-induced dopaminergic neurons toxicity.
Data suggest that BECN1 exhibits a helical region that transitions between packing (folding/unfolding) as part of either one of two conserved domains; packing of this helical region appears to have important implications for relative stability of autophagy-inactive and autophagy-active BECN1 complexes.
downregulation of HOXC9 (show HOXC9 Proteins) releases its transcriptional inhibition of DAPK1 (show DAPK1 Proteins), resulting in the activation of the DAPK1 (show DAPK1 Proteins)-Beclin1 pathway, which induces autophagy in glioblastoma cells
ASPP2 (show TP53BP2 Proteins) is a key regulator of BECN1-dependent autophagy.
the polyQ domain enables wild-type ataxin 3 (show ATXN3 Proteins) to interact with beclin 1, a key initiator of autophagy; this interaction allows the deubiquitinase activity of ataxin 3 (show ATXN3 Proteins) to protect beclin 1 from proteasome-mediated degradation and thereby enables autophagy
findings suggest that expression of cFLIPL regulates the basal interaction of Bcl-2 (show BCL2 Proteins) with Beclin-1 and substantiates p53 (show TP53 Proteins) dependent ubiquitination of Beclin-1 during autophagic stress to determine the fate of cell death or survival.
Here, sequence analyses, structural modeling, mutagenesis combined with pull-down assays, X-ray crystal structure determination and small-angle X-ray scattering were used to investigate the Beclin 1-GAPR-1 interaction. changes in the structure of the equatorial groove combined with the improved dimerization of pentad mutant GAPR-1 are likely to abrogate binding to Beclin 1.
Acetylated PGK1 (show PGK1 Proteins) binds to and phosphorylates Beclin1 at S30 (show FAU Proteins), leading to activation of the VPS34 (show PIK3C3 Proteins)-Beclin1 complex to initiate autophagosomal formation.
reactive oxygen species (ROS (show ROS1 Proteins)) production was induced, which increased RelA (show NFkBP65 Proteins) transcriptional activity and beclin 1 (BECN1) expression in oral cancer cells irradiated with LPL (show LCP1 Proteins)
Further data showed that reactive oxygen species-c-Jun (show JUN Proteins) activation by HBx resulted in the release of beclin-1 from its association with beclin-2 to form a complex with VPS34 (show PIK3C3 Proteins), thus enhancing autophagosome formation.
Beclin1 interacts with both the N- and C-termini of LAPTM4B. Beclin1 competes with EGFR for LAPTM4B binding.
proteostasis regulator cysteamine, which rescues the function of the most common F508del-CFTR (show CFTR Proteins) mutant and hence reduces lung inflammation in CF patients, can also repair the defects of CF macrophages, thus restoring both bacterial internalization and clearance through a process that involves upregulation of the pro-autophagic protein Beclin 1 and re-establishment of the autophagic pathway.
Genetically disrupting BECN1-BCL2 (show BCL2 Proteins) binding hyperactivates autophagy in vivo, which sequestrates amyloid oligomers and prevents Alzheimer's disease progression.
Data show that 1-month of oral treatment with beta-asarone reduces AChE, Abeta42, APP (show APP Proteins) and Beclin-1 levels and alleviates some behavioral impairments by inhibiting the autophagy via regulating the PI3K/Akt (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) pathway in APP (show APP Proteins)/PS1 (show PSEN1 Proteins) transgenic mice. The results further support the exploration of beta-asarone as a possible disease-modifying agent for the treatment of Alzheimer's disease.
identify FAK (show PTK2 Proteins) as a novel negative regulator of Beclin1-mediated autophagy and indicate that this pathway can facilitate the promotion of compensatory hypertrophic growth
The results not only demonstrate that BECN1 as a PI3K-III component is essential for cytokinesis, but also suggest that BECN1 is not associated with autophagy pathway in mouse oocytes.
this study shows that knockdown of beclin1 enhances macrophage-associated (show CD163 Proteins) phagocytosis and intracellular killing of Pseudomonas aeruginosa
provide the novel evidence that GADD45A (show GADD45A Proteins) inhibits autophagy via impairing the BECN1-PIK3C3 (show PIK3C3 Proteins) complex formation
in-vitro genetic depletion of beclin-1 in high glucose treated adult rat cardiomyocytes markedly inhibited the level of autophagy and subsequent apoptotic cell death.
suggest that neuronal death induced by decreased beclin 1 levels may also be due to impaired trophic factor signaling
FBG1 (show FBXO2 Proteins) degrades A1AT (show SERPINA1 Proteins)-Z through a Beclin1-dependent arm of autophagy.
Data indicate that the expression of MAP1LC3A (show MAP1LC3A Proteins), B and autophagy-associated genes (ATG5 (show ATG5 Proteins), mTOR (show FRAP1 Proteins), Beclin-1) was increased in normal pigs, while decreased in miniature pigs.
Beclin-1 participates in the regulation of autophagy and has an important role in development, tumorigenesis, and neurodegeneration (Zhong et al., 2009
beclin 1 (coiled-coil, myosin-like BCL2 interacting protein)
, beclin 1
, beclin 1 proteinBeclin-1-like protein
, myosin-like BCL2 interacting protein
, ATG6 autophagy related 6 homolog
, beclin 1 (coiled-coil, moesin-like BCL2 interacting protein)
, beclin 1 (coiled-coil, moesin-like BCL2-interacting protein)
, coiled-coil myosin-like BCL2-interacting protein
, Bcl-2-interacting protein beclin
, coiled-coil, myosin-like BCL2-interacting protein
, beclin 1 (coiled-coil, myosin-like BCL2-interacting protein)
, autophagy-related protein 6