Ask about this productRelated genes to: Bcl-G antibody
- Gene:
- BCL2 NIH gene
- Name:
- BCL2 apoptosis regulator
- Previous symbol:
- -
- Synonyms:
- Bcl-2, PPP1R50
- Chromosome:
- 18q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2019-04-23
- Gene:
- BCL2L1 NIH gene
- Name:
- BCL2 like 1
- Previous symbol:
- -
- Synonyms:
- BCLX, BCL2L, Bcl-X, bcl-xL, bcl-xS, PPP1R52
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1997-10-30
- Date modifiied:
- 2016-01-13
- Gene:
- BCL9L NIH gene
- Name:
- BCL9 like
- Previous symbol:
- -
- Synonyms:
- DLNB11, B9L, Bcl9-2
- Chromosome:
- 11q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-09
- Date modifiied:
- 2018-11-16
Related products to: Bcl-G antibody
Related articles to: Bcl-G antibody
- Cytotoxic chemotherapy is intended to eliminate transformed cells but can also provoke therapy-induced senescence, a persistent and pro-inflammatory cell state that can promote tumor progression. The molecular mechanisms that govern the apoptosis-senescence fate decision remain incompletely understood. Here, we show that the mitochondrial pore-forming proteins BAX and BAK function as a critical checkpoint that restricts entry to therapy-induced senescence. Genetic ablation of BAX and BAK markedly enhanced entry to senescence in response to multiple DNA-damaging agents, whereas loss of the BAX/BAK antagonists Bcl-xL or Mcl-1 suppressed entry to senescence and promoted cell death. Mechanistically, genotoxic stress induced BH3-only proteins, including Noxa, Bid, and Puma, creating a dependence on Bcl-xL and Mcl-1 to restrain BAX/BAK activation and maintain survival. These findings identify the Bcl-2 family network as a central regulator of entry to therapy-induced senescence, a pro-inflammatory cell state that goes beyond the mere avoidance of apoptosis. - Source: PubMed
Publication date: 2026/08/03
Gallagher Aldave AislinnVenugopalan VaishnaviGunay GokhanHamsici SerenRibeiro Ronaldo RodriguesCostigan AoifeGabrielyan AnnaEfe-Cicek HandeMartin Seamus J - Bisphenol A (BPA) is a potential risk factor for pancreatic ductal adenocarcinoma (PDAC). This study integrated network toxicology, molecular docking, molecular dynamics (MD) simulations, and TCGA clinical data analysis to explore the potential molecular mechanisms linking BPA exposure to PDAC risk. BPA-PDAC intersection targets were identified through multi-database screening, followed by protein-protein interaction (PPI) network construction to screen core hub genes. A total of 10 core hub genes were identified via PPI analysis combined with the Maximal Clique Centrality (MCC) algorithm. Molecular docking demonstrated that ESR1 exhibited one of the strongest binding affinities for BPA (-8.2 kcal/mol), and MD simulations confirmed favorable thermodynamic stability of the BPA-ESR1 complex. TCGA analysis revealed stage-dependent expression patterns: early stages showed downregulation of TP53 and BCL2, whereas advanced stages showed upregulation of BCL2L1, HSP90AA1, and HSP90AB1, while ESR1, HIF1A, and PARP1 remained consistently low. These findings suggest that BPA may promote PDAC progression by disrupting ERα-mediated endocrine signaling and impairing DNA repair through PARP1 interference, providing candidate molecular targets and a hypothesis-generating foundation for pancreatic cancer risk assessment, warranting further experimental validation. - Source: PubMed
Publication date: 2026/07/20
Li XueruWu FanZhang ZunhanAn JiayiZhou GuoqiangWang YangZhao DandanChen Xiaolu - Carbon nanotubes (CNTs) are carbon-based nanomaterials. They have been widely used in environmental technologies and in biomedical fields. - Source: PubMed
Publication date: 2026/07/01
Lotfipanah ShirinSaremi LeilaRafieitabatabaei YasaminsadatAsgari MasoudHajebrahimi Zahra - Mg and Ca are involved in nearly every aspect of cellular function. These divalent cations can bind to the same protein binding sites, often with significantly binding affinities, resulting in distinct conformational changes in proteins. Recent studies demonstrated that both Mg and Ca can influence lipid-dependent folding and insertion of various membrane-active peptides and non-constitutive membrane proteins and peptides. Specifically, cardiolipin, can recruit various apoptotic regulators of the Bcl-2 family (e.g., pro-apoptotic BAX and anti-apoptotic Bcl-xL) to the model membranes in the absence of canonical protein activators, like the BH3-only proteins. This interaction can only occur in the presence of divalent cations, such as Mg which is constantly present outside of the targeted mitochondrial membrane in the cell, or Ca, which is released from the mitochondria at the early stages of apoptosis. Here, we use all-atom molecular dynamics simulations to provide the first atomistic-level characterization of the dynamic protein-lipid-cation interaction of the Bcl-xL, anchored to the cardiolipin-containing lipid bilayer, in the presence of either Mg or Ca. Our results show that both ions interact with Bcl-xL and membrane lipids in the membrane-anchored state, but through distinct modes. Whereas Mg primarily forms water-mediated interactions with both the protein and the lipids, Ca establishes direct contacts with both. These differences led to more constrained conformational dynamics of Bcl-xL in the presence of Ca, particularly in the α1-α2 loop and the BH3-binding groove involved in inhibitory interactions with pro-apoptotic BAX. - Source: PubMed
Publication date: 2026/06/29
Nguyen QuynhFreites J AlfredoLadokhin Alexey STobias Douglas J - Myeloproliferative neoplasms (MPNs) are frequently accompanied by bone marrow fibrosis and leukemic transformation, yet the cellular and molecular mechanisms that sustain apoptosis resistance and fibrotic progression remain unclear. - Source: PubMed
Publication date: 2026/06/02
Wu ChunyanWang YitingZhang QuanchaoLi ChanChen YuanzhongWu Yong