BH3 profiling--measuring integrated function of the mitochondrial apoptotic pathway to predict cell fate decisions.

[1]  A. Letai,et al.  Heightened mitochondrial priming is the basis for apoptotic hypersensitivity of CD4+ CD8+ thymocytes , 2010, Proceedings of the National Academy of Sciences.

[2]  Derek W. Yecies,et al.  MCL-1–dependent leukemia cells are more sensitive to chemotherapy than BCL-2–dependent counterparts , 2009, The Journal of cell biology.

[3]  A. Letai,et al.  Control of mitochondrial apoptosis by the Bcl-2 family , 2009, Journal of Cell Science.

[4]  N. Tjandra,et al.  BAX Activation is Initiated at a Novel Interaction Site , 2008, Nature.

[5]  D. Lauffenburger,et al.  Quantitative analysis of pathways controlling extrinsic apoptosis in single cells. , 2008, Molecular cell.

[6]  S. Armstrong,et al.  BCL-2 dependence and ABT-737 sensitivity in acute lymphoblastic leukemia. , 2008, Blood.

[7]  A. Letai,et al.  Diagnosing and exploiting cancer's addiction to blocks in apoptosis , 2008, Nature Reviews Cancer.

[8]  A. Letai,et al.  BH3 profiling identifies three distinct classes of apoptotic blocks to predict response to ABT-737 and conventional chemotherapeutic agents. , 2007, Cancer cell.

[9]  Mark Ellisman,et al.  Mitochondria frozen with trehalose retain a number of biological functions and preserve outer membrane integrity , 2007, Cell Death and Differentiation.

[10]  Michael T. Certo,et al.  Chronic lymphocytic leukemia requires BCL2 to sequester prodeath BIM, explaining sensitivity to BCL2 antagonist ABT-737. , 2007, The Journal of clinical investigation.

[11]  S. Armstrong,et al.  Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. , 2006, Cancer cell.

[12]  T. Kuwana,et al.  BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. , 2005, Molecular cell.

[13]  Brian J. Smith,et al.  Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. , 2005, Molecular cell.

[14]  Philippe Juin,et al.  The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA. , 2004, Molecular cell.

[15]  S. Korsmeyer,et al.  Antiapoptotic BCL-2 is required for maintenance of a model leukemia. , 2004, Cancer cell.

[16]  A. Petros,et al.  Structural biology of the Bcl-2 family of proteins. , 2004, Biochimica et biophysica acta.

[17]  S. Korsmeyer,et al.  Development and maintenance of B and T lymphocytes requires antiapoptotic MCL-1 , 2003, Nature.

[18]  S. Korsmeyer,et al.  Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. , 2002, Cancer cell.

[19]  S. Cory,et al.  The Bcl2 family: regulators of the cellular life-or-death switch , 2002, Nature Reviews Cancer.

[20]  J. Chin,et al.  A view to a kill: ligands for Bcl-2 family proteins. , 2002, Current opinion in chemical biology.

[21]  S. Korsmeyer,et al.  BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. , 2001, Molecular cell.

[22]  M. Minden,et al.  The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2 , 2001, Cell Death and Differentiation.

[23]  W. Zong,et al.  BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. , 2001, Genes & development.

[24]  S. Korsmeyer,et al.  Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death , 2001, Science.

[25]  S. Korsmeyer,et al.  The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. , 2000, Molecular cell.

[26]  S. Fesik,et al.  Three-dimensional structures of proteins involved in programmed cell death. , 1997, Journal of molecular biology.

[27]  R. Meadows,et al.  Structure of Bcl-xL-Bak Peptide Complex: Recognition Between Regulators of Apoptosis , 1997, Science.

[28]  S. Korsmeyer,et al.  Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death , 1993, Cell.

[29]  Gerard I. Evan,et al.  Induction of apoptosis in fibroblasts by c-myc protein , 1992, Cell.

[30]  J. Sklar,et al.  Nucleotide sequence of a t(14;18) chromosomal breakpoint in follicular lymphoma and demonstration of a breakpoint-cluster region near a transcriptionally active locus on chromosome 18. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[31]  C. Croce,et al.  The t(14;18) chromosome translocations involved in B-cell neoplasms result from mistakes in VDJ joining. , 1985, Science.

[32]  S. Korsmeyer,et al.  Cloning the chromosomal breakpoint of t(14;18) human lymphomas: clustering around Jh on chromosome 14 and near a transcriptional unit on 18 , 1985, Cell.

[33]  Victoria Del Gaizo Moore,et al.  Rational design of therapeutics targeting the BCL-2 family: are some cancer cells primed for death but waiting for a final push? , 2008, Advances in experimental medicine and biology.

[34]  J Salvage,et al.  A matter of life and death. , 1981, Nursing times.