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- Publications
- Influence
Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics.
- A. Letai, M. Bassik, L. Walensky, Mia D Sorcinelli, S. Weiler, S. Korsmeyer
- Biology, Medicine
- Cancer cell
- 1 September 2002
The "BH3-only" proteins of the BCL-2 family require "multidomain" proapoptotic members BAX and BAK to release cytochrome c from mitochondria and kill cells. We find short peptides representing the… Expand
Genome-Scale CRISPR-Mediated Control of Gene Repression and Activation
- L. Gilbert, Max A. Horlbeck, +10 authors J. Weissman
- Biology, Medicine
- Cell
- 1 October 2014
While the catalog of mammalian transcripts and their expression levels in different cell types and disease states is rapidly expanding, our understanding of transcript function lags behind. We… Expand
JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy.
- Yongjie Wei, S. Pattingre, S. Sinha, M. Bassik, B. Levine
- Biology, Medicine
- Molecular cell
- 20 June 2008
Starvation induces autophagy to preserve cellular homeostasis in virtually all eukaryotic organisms. However, the mechanisms by which starvation induces autophagy are not completely understood. In… Expand
Exercise-induced BCL2-regulated autophagy is required for muscle glucose homeostasis
Exercise has beneficial effects on human health, including protection against metabolic disorders such as diabetes. However, the cellular mechanisms underlying these effects are incompletely… Expand
Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum.
- S. Oakes, L. Scorrano, +4 authors S. Korsmeyer
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 4 January 2005
Proapoptotic BCL-2 family members BAX and BAK are required for the initiation of mitochondrial dysfunction during apoptosis and for maintaining the endoplasmic reticulum (ER) Ca(2+) stores necessary… Expand
Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
- C. Hetz, P. Bernasconi, +8 authors S. Korsmeyer
- Biology, Medicine
- Science
- 28 April 2006
Accumulation of misfolded protein in the endoplasmic reticulum (ER) triggers an adaptive stress response—termed the unfolded protein response (UPR)—mediated by the ER transmembrane protein kinase and… Expand
A Systematic Mammalian Genetic Interaction Map Reveals Pathways Underlying Ricin Susceptibility
- M. Bassik, M. Kampmann, +11 authors J. Weissman
- Biology, Medicine
- Cell
- 14 February 2013
Genetic interaction (GI) maps, comprising pairwise measures of how strongly the function of one gene depends on the presence of a second, have enabled the systematic exploration of gene function in… Expand
Phosphorylation of BCL‐2 regulates ER Ca2+ homeostasis and apoptosis
- M. Bassik, L. Scorrano, S. Oakes, T. Pozzan, S. Korsmeyer
- Biology, Medicine
- The EMBO journal
- 10 March 2004
Phosphorylation of BCL‐2 within an unstructured loop inhibits its antiapoptotic effect. We found that phosphorylated BCL‐2 predominantly localized to the endoplasmic reticulum (ER) and tested whether… Expand
Selective silencing of euchromatic L1s revealed by genome-wide screens for L1 regulators
- Nian Liu, C. H. Lee, +4 authors J. Wysocka
- Biology, Medicine
- Nature
- 6 December 2017
Transposable elements, also known as transposons, are now recognized not only as parasitic DNA, the spread of which in the genome must be controlled by the host, but also as major players in genome… Expand
Biochemical and Genetic Analysis of the Mitochondrial Response of Yeast to BAX and BCL-XL
- A. Gross, K. Pilcher, +5 authors M. Forte
- Biology, Medicine
- Molecular and Cellular Biology
- 1 May 2000
ABSTRACT The BCL-2 family includes both proapoptotic (e.g., BAX and BAK) and antiapoptotic (e.g., BCL-2 and BCL-XL) molecules. The cell death-regulating activity of BCL-2 members appears to depend on… Expand