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An inhibitor of Bcl-2 family proteins induces regression of solid tumours
TLDR
Mechanistic studies reveal that ABT-737 does not directly initiate the apoptotic process, but enhances the effects of death signals, displaying synergistic cytotoxicity with chemotherapeutics and radiation. Expand
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
TLDR
Overexpressed Bax accelerates apoptotic death induced by cytokine deprivation in an IL-3-dependent cell line and counters the death repressor activity of B cl-2, suggesting a model in which the ratio of Bcl-2 to Bax determines survival or death following an apoptotic stimulus. Expand
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Multiple death signals influence mitochondria during apoptosis, yet the critical initiating event for mitochondrial dysfunction in vivo has been unclear. tBID, the caspase-activated form of aExpand
Serine Phosphorylation of Death Agonist BAD in Response to Survival Factor Results in Binding to 14-3-3 Not BCL-XL
TLDR
The rapid phosphorylation of BAD following IL-3 connects a proximal survival signal with the BCL-2 family, modulating this checkpoint for apoptosis and enhanced BAD's death-promoting activity. Expand
BCL-2 family members and the mitochondria in apoptosis.
TLDR
As the BCL-2 family members reside upstream of irreversible cellular damage and focus much of their efforts at the level of mitochondria, they play a pivotal role in deciding whether a cell will live or die, and it is argued that the amphipathic a-helical BH3 domain serves as a critical death domain in the pro-apoptotic members. Expand
Cell Death Critical Control Points
TLDR
The identification of critical control points in the cell death pathway has yielded fundamental insights for basic biology, as well as provided rational targets for new therapeutics. Expand
Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics.
TLDR
A two-class model for BH3 domains is supported: BID-like domains that "activate" BAX, BAK and BAD-like domain that "sensitize" by occupying the pocket of antiapoptotic members. Expand
MLL translocations specify a distinct gene expression profile that distinguishes a unique leukemia
TLDR
It is proposed that MLL constitute a distinct disease, denoted here as MLL, and it is shown that the differences in gene expression are robust enough to classify leukemias correctly as M LL, acute lymphoblastic leukemia or acute myelogenous leukemia. Expand
BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis.
TLDR
In mammals, BH3 domain-only molecules activate multidomain proapoptotic members to trigger a mitochondrial pathway, which both releases cytochrome c to activate caspases and initiates caspase-independent mitochondrial dysfunction. Expand
Bad, a heterodimeric partner for Bcl-xL and Bcl-2, displaces bax and promotes cell death
TLDR
A novel interacting protein, Bad, whose homology to Bcl-2 is limited to the BH1 and BH2 domains is identified, whose role in the mammalian cell death pathway is determined by these competing dimerizations in which levels of Bad influence the effectiveness of BCl-2 versus B cl-xL in repressing death. Expand
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