The pro-apoptotic BH3-protein Bim contains two distinct binding sites for anti-apoptotic proteins that together confer resistance of Bim/Bcl-2 and Bim/Bcl-XL complexes to BH3-mimetic drugs under development for use in humans.

Replicating experimental evolution from ancestral proteins shows that historical contingency steadily overwhelms chance and necessity as the primary cause of evolutionary variation in molecular sequences on long phylogenetic timescales.

Using mice expressing a Bcl-2 mutant protein to suppress multiple central tolerance pathways, it is shown that central tolerance is crucial for preventing autoimmunity.

IRBIT and the Bcl-2 homolog Bcl2l10 form a complex at the endoplasmic reticulum that controls Ca²⁺ signaling, however IRBIT turns into an apoptosis facilitator following stress and inhibits anti-apoptotic activity of Bcl2l10.

Six computationally designed and in vitro optimized protein inhibitors serve as molecular probes to reveal BCL2 profiles of different human cancers.

An integrative approach, combining genetic mouse and large-scale human genetics studies, was used to reveal a novel role for the Bcl-2 protein Bid in maintenance of mitochondrial function that alters susceptibility to myocardial infarction.

The C-terminal membrane binding domain of Bim is shown to interact with and activate Bim enabling it to kill cells not dependent on anti-apoptotic proteins for survival.

Short peptides that bind tightly to anti-apoptotic protein Bfl-1 but not other Bcl-2 family members provide a tool for diagnosing cancer cell survival mechanisms and a lead for developing new therapeutics.

Dimers of Bak assemble into clusters without using a distinct protein-protein interface, which may explain the apparent difficulties in obtaining high resolution structures of the pore complex and in targeting dimer-dimer interactions to regulate apoptosis.

Epstein-Barr virus hijacks host anti-apoptotic machinery to ensure survival during latent infection.