Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax.

By J. Lovell, Lieven P. Billen, Scott Bindner, A. Shamas-Din, Cecile Fradin, B. Leber, David W. Andrews. Cell, 2008

601 citations recorded by the source corpus.

Subfields: Biomedical Engineering, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/f4dc47dbf2a95b82b9356d7c5cc74dfa19df581a

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In Biomedical Engineering

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Citations in the corpus

• Bax, Bak and beyond — mitochondrial performance in apoptosis (2018, background): “conditions, Bax and Bak are activated and accumulate at the MOM, where they oligomerize and mediate MOMP, which leads to the release of proapoptotic factors, such as cytochrome c [11, 12].”
• Mitochondria in Apoptosis: Bcl-2 family Members and Mitochondrial Dynamics (2011, background): “In contrast to the stapled Bim peptide, tBid is unable to interact with full-length Bax or Bcl-x L in solution (Lovell et al., 2008) begging the question of where in the cell do interactions between BH3-only proteins and Bax or Bak occur.”
• Making heads or tails of phospholipids in mitochondria (2011, background): “Similarly, membrane insertion of Bax and its oligomerization were found to proceed more efficiently in the presence of CL (Lutter et al., 2000; Lucken-Ardjomande et al., 2008; Sani et al., 2009).”
• Targeting mitochondria for cancer therapy (2010, background): “BCL-2 and BCL-X L can also interact with activated BH3-only proteins, thereby blocking the pro-apoptotic cascade before BAX activatio”
• Mitochondria and cell death: outer membrane permeabilization and beyond (2010, background): “FRET -based analysis of BAX-mediated liposome permeabilization has provided compelling, real-time evidence for direct and dynamic interactions between truncated BID (tBID) and BAX, which precede BAX membrane insertion and liposome permeabilizatio”
• Mechanisms of action of Bcl-2 family proteins. (2013, background): “However, the consequences of this interaction incorporate the features of both the displacement and direct activation models, because the sensitizer BH3 proteins neutralize the dual function of the antiapoptotic proteins by displacing both the activator BH3 proteins and Bax or Bak from the membrane-”
• The BCL-2 Family Reunion (2010, background): “Binding between BID and BAX has been difficult to study, but FRET analysis revealed the interaction in vitro (Lovell et al., 2008).”
• Multiple Functions of BCL-2 Family Proteins (2013, background): “tBID then activates the intrinsic pathway by well-studied mechanisms in which tBID transiently binds and induces BAX activation on mitochondrial membranes in vitro and in cells (Kuwana et al. 2002; Billen et al. 2008; Lovell et al. 2008).”
• Control of mitochondrial apoptosis by the Bcl-2 family (2009, background): “Studies using full-length proteins, lipid membranes and real-time fluorescence resonance energy transfer (FRET) analyses has provided convincing evidence of such an interaction and for its role in membrane permeabilization (Lovell et al., 2008).”