Structure of Bax: coregulation of dimer formation and intracellular localization.
By Motoshi Suzuki, R. Youle, N. Tjandra. Cell, 2000
1,145 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/c4aa798cb1e6b129e042b88b48f976dfcabf637f
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In Molecular Biology
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Citations in the corpus
- Mechanisms of cytochrome c release from mitochondria (2006, background): “In support of this model, BCL-2, BCL-XL and BAX share structural similarities with the pore-forming domain of bacterial toxins.(55)”
- Ways of dying: multiple pathways to apoptosis. (2003, background): “The “multi-BH domain” Bax, Bak, and Bok share three domains (BH1, BH2, and BH3) with Bcl-2 and, judging by Bax, also have a similar 3D structure, namely a globular bundle of -helices with a hydrophobic surface groove (Fesik 2000; Suzuki et al. 2000).”
- Subcellular location prediction of apoptosis proteins (2002, neutral): “12, 15, 16).”
- Mechanisms of action of Bcl-2 family proteins. (2013, background): “NMR studies indicate that in the initial step of activation, helix 9 of Bax is bound to the hydrophobic pocket in “cis,” preventing helix 9 from inserting into the MOM (Suzuki et al. 2000).”
- Life in the balance: how BH3-only proteins induce apoptosis. (2005, background): “The structural similarity of Bax to pro-survival proteins [35 ,40] has encouraged the view that certain BH3-only proteins directly engage Bax.”
- Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins (2002, background): “Mammalian Bax, Bak, Bok/Mtd, Bcl-xS (a splice variant of the bcl-x gene) and Bcl-GL have two or three BH regions (Figure 1) and appear to be structurally very similar to their pro-survival relatives.(8,9,16) In contrast, mammalian Bik/Nbk, Blk, Bad, Hrk/DP5, Bid, Bim/Bod, Noxa, Puma/Bbc3, BclGs (a s”
- Bcl-2 family members: intracellular targeting, membrane-insertion, and changes in subcellular localization (2004, background): “Therefore, contrary to the suggestions made for Bax, BH3-only proteins appear to be able to displace the C-terminus of Bcl-w from the hydrophobic groove without any additional energetic input [50,51].”