The rheostat in the membrane: BCL-2 family proteins and apoptosis von Volkmann, N, Marassi, F M, Newmeyer, D D, Hanein, D

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Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis von Chipuk, Jerry E., Kuwana, Tomomi, Bouchier-Hayes, Lisa, Droin, Nathalie M., Newmeyer, Donald D., Schuler, Martin, Green, Douglas R.

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Bcl-2-family proteins and the role of mitochondria in apoptosis von Kuwana, Tomomi, Newmeyer, Donald D

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Mitochondrial Shape Governs BAX-Induced Membrane Permeabilization and Apoptosis von Renault, Thibaud T., Floros, Konstantinos V., Elkholi, Rana, Corrigan, Kelly-Ann, Kushnareva, Yulia, Wieder, Shira Y., Lindtner, Claudia, Serasinghe, Madhavika N., Asciolla, James J., Buettner, Christoph, Newmeyer, Donald D., Chipuk, Jerry E.

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Mitochondria: Releasing Power for Life and Unleashing the Machineries of Death von Newmeyer, Donald D, Ferguson-Miller, Shelagh

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BH3 Domains of BH3-Only Proteins Differentially Regulate Bax-Mediated Mitochondrial Membrane Permeabilization Both Directly and Indirectly von Kuwana, Tomomi, Bouchier-Hayes, Lisa, Chipuk, Jerry E., Bonzon, Christine, Sullivan, Barbara A., Green, Douglas R., Newmeyer, Donald D.

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Mitochondrial residence of the apoptosis inducer BAX is more important than BAX oligomerization in promoting membrane permeabilization von Kuwana, Tomomi, King, Louise E., Cosentino, Katia, Suess, Julian, Garcia-Saez, Ana J., Gilmore, Andrew P., Newmeyer, Donald D.

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PUMA Couples the Nuclear and Cytoplasmic Proapoptotic Function of p53 von Chipuk, Jerry E, Bouchier-Hayes, Lisa, Kuwana, Tomomi, Newmeyer, Donald D, Green, Douglas R

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The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis von Kluck, Ruth M., Bossy-Wetzel, Ella, Green, Douglas R., Newmeyer, Donald D.

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Bax activation initiates the assembly of a multimeric catalyst that facilitates Bax pore formation in mitochondrial outer membranes von Kushnareva, Yulia, Andreyev, Alexander Y, Kuwana, Tomomi, Newmeyer, Donald D

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Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane von Kuwana, Tomomi, Mackey, Mason R., Perkins, Guy, Ellisman, Mark H., Latterich, Martin, Schneiter, Roger, Green, Douglas R., Newmeyer, Donald D.

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Phenotypic selection with an intrabody library reveals an anti-apoptotic function of PKM2 requiring Mitofusin-1 von Liu, Tong, Kuwana, Tomomi, Zhang, Hongkai, Vander Heiden, Matthew G, Lerner, Richard A, Newmeyer, Donald D

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Opa1-Mediated Cristae Opening Is Bax/Bak and BH3 Dependent, Required for Apoptosis, and Independent of Bak Oligomerization von Yamaguchi, Ryuji, Lartigue, Lydia, Perkins, Guy, Scott, Ray T., Dixit, Amruta, Kushnareva, Yulia, Kuwana, Tomomi, Ellisman, Mark H., Newmeyer, Donald D.

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Mitochondria: pharmacological manipulation of cell death von Bouchier-Hayes, Lisa, Lartigue, Lydia, Newmeyer, Donald D

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Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes von Gillies, Laura A, Du, Han, Peters, Bjoern, Knudson, C Michael, Newmeyer, Donald D, Kuwana, Tomomi

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The Multidomain Proapoptotic Molecules Bax and Bak Are Directly Activated by Heat von Lisa J. Pagliari, Kuwana, Tomomi, Christine Bonzon, Newmeyer, Donald D., Shine Tu, Helen M. Beere, Green, Douglas R.

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Cytochrome c Maintains Mitochondrial Transmembrane Potential and ATP Generation after Outer Mitochondrial Membrane Permeabilization during the Apoptotic Process von Waterhouse, Nigel J., Goldstein, Joshua C., von Ahsen, Oliver, Schuler, Martin, Newmeyer, Donald D., Green, Douglas R.

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Caspase-2-induced apoptosis requires bid cleavage: a physiological role for bid in heat shock-induced death von Bonzon, Christine, Bouchier-Hayes, Lisa, Pagliari, Lisa J, Green, Douglas R, Newmeyer, Donald D

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Different Mitochondrial Intermembrane Space Proteins Are Released during Apoptosis in a Manner That Is Coordinately Initiated but Can Vary in Duration von Muñoz-Pinedo, Cristina, Guío-Carrimón, Ana, Goldstein, Joshua C., Fitzgerald, Patrick, Newmeyer, Donald D., Green, Douglas R.

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Apoptosis Induction by Caspase-8 Is Amplified through the Mitochondrial Release of Cytochrome c von Kuwana, T, Smith, J J, Muzio, M, Dixit, V, Newmeyer, D D, Kornbluth, S

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