The BCL-2 protein family: opposing activities that mediate cell death

By R. Youle, A. Strasser. Nature reviews. Molecular cell biology, 2008

4,739 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/23a3782a4540cbdf96c67b53628cd40ff4551c65

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

Mitochondrial dynamics and apoptosis. (2008, background): “Bax translocates to mitochondria during apoptosis and concentrates into foci on the mitochondrial surface when cells become committed to die (Youle and Strasser 2008).”
The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. (2012, neutral): “Antiapoptotic members of the Bcl-2 family, such as Bcl-2, Bcl-xL, and Mcl-1, bind and antagonize the homologous proapoptotic members of the family, including Bax and Bak, and the ‘‘BH3-only’’ members such as Bim, Bad, and Puma (which share homology with Bcl-2 only at the BH3 region) (Youle and Stras”
Copper metabolism in cell death and autophagy (2023, background): “The release of mitochondrial proteins is determined by the mitochondrial membrane potential, which is tightly regulated by the BCL2 protein family [78].”
Role of Bcl-2 family proteins and caspases in the regulation of apoptosis (2011, background): “The antiapoptotic member of Bcl-2 family, including Bcl-2 itself, decreases apoptosis mainly by preventing mitochondrial outer membrane permeabilization (MOMP) either by neutralizing the activity of both pro-apoptotic members (BH3 only protein and multidomain members) [48].”
Mitochondria in Apoptosis: Bcl-2 family Members and Mitochondrial Dynamics (2011, background): “Bcl-2 Family Members Bcl-2 family proteins are subdivided into three groups on the basis of their pro-or antiapoptotic action and the Bcl-2 Homology (BH) domains they possess (Figure 1A)(Schinzel et al., 2004; Youle and Strasser, 2008).”
Cellular and molecular mechanisms of mitochondrial function (2012, background): “74 A second conformational change occurs when the a 5 and a 6 helices insert directly into the outer membrane, culminating in mitochondrial outer membrane permeabilization (MOMP) and cytochrome c release.”
BCL-2 family antagonists for cancer therapy (2008, background): “In mammalian cells, five pro-survival proteins — BCL-2, BCL-X L , BCL-w, MCL1 and A1 — antagonize the pro-apoptotic function of BAK and BAX”
Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production (2014, neutral): “Apoptosis comprises two convergent pathways: the intrinsic and extrinsic (Youle and Strasser, 2008).”
Understanding MAPK Signaling Pathways in Apoptosis (2020, background): “The C-terminal truncated form of Bid (tBid) translocates to mitochondria and induces the release of cytochrome c, which in turn induces further caspase activation (caspase-9 and the effector caspases-3, -6, and -7) through the intrinsic pathway [31].”
GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death (2016, neutral): “The placement and function of GSDMD in the canonical and non-canonical inflammasome pathway strongly resembles the placement and function of Bax (Bcl-2-associated X protein) in the apoptotic cell death pathways (Youle & Strasser, 2008).”
Cytochrome c: functions beyond respiration (2008, background): “and thereby regulate cytochrome c release and intrinsic apoptosi”
Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA (2014, background): “Bax/Bak-Dependent Induction of Type I IFNs The intrinsic pathway of apoptosis is activated upon MOMP by the Bax/Bak channel (Jiang and Wang, 2004).”
Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies (2016, background): “BH-domains (BH1, BH2 and BH3); and the proapoptotic BH3-only proteins group includes Bid (BH3 interacting-domain death agonist), Bim (Bcl-2-like protein 11), Bad (Bcl-2-associated death promoter), Puma (p53 upregulated modulator of apoptosis), Noxa, BMF, HRK and BIK (Figure 3) [33].”