Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy.
By S. Pattingre, Amina T Tassa, X. Qu, R. Garuti, X. H. Liang, N. Mizushima, M. Packer, M. Schneider, Beth Levine. Cell, 2005
3,670 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology, Plant Science
View Paper: https://www.semanticscholar.org/paper/3debe65157b7b1fdc4c00bc3ffd365bd36921290
How researchers see this paper
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In Epidemiology
- Beth Levine
- I. Slaninová
- Guido Kroemer
- D. Klionsky
- N. Mizushima
- Alec C. Kimmelman
- V. Deretic
- E. White
In Molecular Biology
- Guido Kroemer
- Beth Levine
- D. Klionsky
- I. Slaninová
- N. Mizushima
- E. White
- Douglas R. Green
- Alec C. Kimmelman
In Plant Science
- I. Slaninová
- Beth Levine
- Guido Kroemer
- N. Mizushima
- Douglas R. Green
- D. Klionsky
- L. Galluzzi
- Eric H. Baehrecke
Citations in the corpus
- Autophagy, Immunity, and Microbial Adaptations (2009, background): “…murine γ-HV68 Viral Bcl-2-like proteins inhibit autophagy Unknown KSHV vBcl-2 and γ-HV68 M11 inhibit autophagy by binding to Beclin 1 Ku et al., 2008b; Pattingre et al., 2005; Sinha et al., 2008 Epstein-Barr virus (EBV) EBV LMP1 protein induces autophagy Proposed mechanism to decrease LMP1 levels…”
- Autophagy-Dependent Ferroptosis: Machinery and Regulation (2020, positive): “In addition to Ubdependent receptors, Ub-independent receptors (e.g., BCL2 interacting protein 3 like [BNIP3L/NIX] (Sandoval et al., 2008), FUN14 domain containing 1 [FUNDC1] (Liu et al., 2012), BCL2 interacting protein 3 [BNIP3] (O'Sullivan et al., 2015), nipsnap homolog 1 [NIPSNAP1] (Princely Abud”
- Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (2012, positive): “Although a population of BECN1 may localize in proximity to the trans-Golgi network,(574) it is also present at the ER and mitochondria.(566) In keeping with these observations, in cerebellar organotypic cultures BECN1 co-immunoprecipitates with BCL2 that is primarily localized at the mitochondria a”
- Molecular definitions of autophagy and related processes (2017, positive): “…autophagy and beclin 1 regulator 1 (AMBRA1, originally “activating molecule in Beclin 1-regulated autophagy”), as well as the BECN1 inhibitor BCL2, which also interacts with ATG12 (Liang et al , 1999; Pattingre et al , 2005; Fimia et al , 2007; Zalckvar et al , 2009; Rubinstein et al , 2011).”
- Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, neutral): “Conversely, ER-targeted BCL-X L suppresses autophag”
- ER stress-induced cell death mechanisms. (2013, background): “Recently, it was reported that JNK-mediated phosphorylation of Bcl-2 causes its release of Beclin-1, thereby allowing autophagy to proceed [50].”
- Regulation of Autophagy by Reactive Oxygen Species (ROS): Implications for Cancer Progression and Treatment (2009, positive): “The class III PI3 kinase complex, including Beclin-1 = Atg6, is required for generation of preautophagosome structures (106).”
- Cardiac autophagy is a maladaptive response to hemodynamic stress. (2007, background): “As noted earlier, prior studies have demonstrated that GFP-LC3 overexpression, both in vitro and in vivo, does not alter basal or starvation-induced autophagy (15, 19).”
- Autophagic cell death: the story of a misnomer (2008, background): “and interacts with apoptosis-regulatory proteins, such as BCL2 and BCL-x L (Ref”
- Biological functions of antioxidants in plant transformation (2008, background): “ever, examination of the function of ATG genes in other higher eukaryotes indicates that autophagy might have a dual role: pro- and/or anti-cell death (Yu et al. 2004; Boya et al. 2005; Pattingre et al. 2005).”
- Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “This effect is mediated through the ability of Bcl-2 to interact with Beclin 1, a key protein in autophagosome formation [52].”
- Role of autophagy in cancer (2007, background): “Although BCL2 localized to the endoplasmic reticulum can interact with BECN1 and inhibit autophag”