Results 211 to 220 of about 45,804 (237)
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Kinase crosstalk through beclin 1
Nature Reviews Molecular Cell Biology, 2013Katharine H Wrighton
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The Beclin 1 network regulates autophagy and apoptosis [PDF]
Beclin 1, the mammalian orthologue of yeast Atg6, has a central role in autophagy, a process of programmed cell survival, which is increased during periods of cell stress and extinguished during the cell cycle. It interacts with several cofactors (Atg14L, UVRAG, Bif-1, Rubicon, Ambra1, HMGB1, nPIST, VMP1, SLAM, IP(3)R, PINK and survivin) to regulate ...
Daolin Tang
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BAC-mediated transgenic expression of fluorescent autophagic protein Beclin 1 reveals a role for Beclin 1 in lymphocyte development [PDF]
Beclin 1/Atg6 is an essential component of the evolutionary conserved PtdIns(3)-kinase (Vps34) protein complex that regulates macroautophagy (autophagy) in eukaryotic cells and also interacts with antiapoptotic Bcl-2 family members, Bcl-2, and Bcl-x(L).
Eric J Nestler
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Beclin-1-Dependent Autophagy Protects the Heart During Sepsis [PDF]
Background: Cardiac dysfunction is a major component of sepsis-induced multiorgan failure in critical care units. Changes in cardiac autophagy and its role during sepsis pathogenesis have not been clearly defined. Targeted autophagy-based therapeutic approaches for sepsis are not yet developed.
Qing-jun Zhang, Zhi-Ping Liu, Bo Ci
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Beclin-1 and LC3A expression in cutaneous malignant melanomas
Melanoma Research, 2011Autophagy is an intracellular pathway for the degradation of long-lived proteins and damaged organelles. It is, in essence, a recycling process allowing cells to survive oxygen and nutrient depletion. The expression of two autophagy-related proteins, beclin 1 and light chain 3A (LC3A) was investigated in 79 nodular cutaneous melanomas. The results were
Efthimios, Sivridis +6 more
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2019
Beclin 1 is the first mammalian autophagy protein identified as a novel Bcl-2-interacting protein. Subsequent studies have demonstrated that this landmark protein is essential for autophagy. By investigating the interaction between Bcl-2 and Beclin 1, key molecular mechanisms of mammalian autophagy regulation have been discovered.
Hai-Dong, Xu, Zheng-Hong, Qin
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Beclin 1 is the first mammalian autophagy protein identified as a novel Bcl-2-interacting protein. Subsequent studies have demonstrated that this landmark protein is essential for autophagy. By investigating the interaction between Bcl-2 and Beclin 1, key molecular mechanisms of mammalian autophagy regulation have been discovered.
Hai-Dong, Xu, Zheng-Hong, Qin
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Beclin 1 Complex and Neurodegenerative Disorders
2020Beclin1 is the mammalian orthologue of yeast Atg6/vacuolar protein sorting-30 (VPS30). Beclin1 interacts with various biological macromolecules like ATG14, BIF-1, NRBF2, RUBICON, UVRAG, AMBRA1, HMGB1, PINK1, and PARKIN. Such interactions promote Beclin1-PI3KC3 complex formation.
Ozaifa Kareem +5 more
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Regulation of autophagy by Beclin 1 in the heart [PDF]
Dysregulation of autophagy in cardiomyocytes is implicated in various heart disease conditions. Beclin 1, a mammalian ortholog of yeast Atg6 and a core component of the autophagy machinery, plays a central role in the regulation of autophagy through activation of Vps34.
Yasuhiro Maejima +2 more
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Regulation of macroautophagy by mTOR and Beclin 1 complexes
Biochimie, 2008Macroautophagy or autophagy is a vacuolar degradative pathway terminating in the lysosomal compartment after forming a cytoplasmic vacuole or autophagosome that engulfs macromolecules and organelles. The original discovery that ATG (AuTophaGy related) genes in yeast are involved in the formation of autophagosomes has greatly increased our knowledge of ...
Sophie, Pattingre +3 more
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Beclin-1: Autophagic regulator and therapeutic target in cancer
The International Journal of Biochemistry & Cell Biology, 2013Beclin-1 (the mammalian ortholog of yeast ATG6) has been well-characterized to play a pivotal role in autophagy that is a major catabolic pathway in which the cell degrades macromolecules and damaged organelles. Beclin-1 structure has been identified to contain three identifiable domains, including a short Bcl-2-homology-3 (BH3) motif, a central coiled-
Lei-lei, Fu, Yan, Cheng, Bo, Liu
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