Cragg, Mark S., Kuroda, Junya, Puthalakath, Hamsa, Huang, David C.S., Strasser, Andreas
Background: The epidermal growth factor receptor (EGFR) plays a critical role in the control of cellular proliferation, differentiation, and survival. Abnormalities in EGF-EGFR signaling, such as...
Kuroda, Junya, Puthalakath, Hamsa, Cragg, Mark S., Kelly, Priscilla N., Bouillet, Philippe, Huang, David C.S., ...
Cell killing is a critical pharmacological activity of imatinib to eradicate Bcr/Abl+ leukemias. We found that imatinib kills Bcr/Abl+ leukemic cells by triggering the Bcl-2-regulated apoptotic...
Willis, Simon N., Chen, Lin, Dewson, Grant, Wei, Andrew, Naik, Edwina, Fletcher, Jamie I., ...
Commitment of cells to apoptosis is governed largely by the interaction between members of the Bcl-2 protein family. Its three subfamilies have distinct roles: The BH3-only proteins trigger apoptosis...
Willis, Simon N., Chen, Lin, Dewson, Grant, Wei, Andrew, Naik, Edwina, Fletcher, Jamie I., ...
Commitment of cells to apoptosis is governed largely by the interaction between members of the Bcl-2 protein family. Its three subfamilies have distinct roles: The BH3-only proteins trigger apoptosis...
Willis, Simon N., Chen, Lin, Dewson, Grant, Wei, Andrew, Naik, Edwina, Fletcher, Jamie I., ...
Commitment of cells to apoptosis is governed largely by the interaction between members of the Bcl-2 protein family. Its three subfamilies have distinct roles: The BH3-only proteins trigger apoptosis...
Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1
Moriishi, Kohji, Huang, David C. S., Cory, Suzanne, Adams, Jerry M.
The Bcl-2 family of proteins regulates apoptosis, the cell death program triggered by activation of certain proteases (caspases). An attractive model for how Bcl-2 and its closest relatives prevent...
Activation of Fas by FasL induces apoptosis by a mechanism that cannot be blocked by Bcl-2 or Bcl-xL
Huang, David C. S., Hahne, Michael, Schroeter, Michael, Frei, Karl, Fontana, Adriano, Villunger, Andreas, ...
Fas activation triggers apoptosis in many cell types. Studies with anti-Fas antibodies have produced conflicting results on Fas signaling, particularly the role of the Bcl-2 family in this process....
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
Hinds, Mark G., Lackmann, Martin, Skea, Gretchen L., Harrison, Penny J., Huang, David C.S., Day, Catherine L.
Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the pro-apoptotic BH3-only proteins. The solution...
Willis, Simon N., Chen, Lin, Dewson, Grant, Wei, Andrew, Naik, Edwina, Fletcher, Jamie I., ...
Commitment of cells to apoptosis is governed largely by the interaction between members of the Bcl-2 protein family. Its three subfamilies have distinct roles: The BH3-only proteins trigger apoptosis...
Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.
Day, Catherine L, Puthalakath, Hamsa, Skea, Gretchen, Strasser, Andreas, Barsukov, Igor, Lian, Lu-Yun, ...
The dynein and myosin V motor complexes are multi-protein structures that function to transport molecules and organelles within the cell. DLC (dynein light-chain) proteins, found as components of...
Silke, John, Kratina, Tobias, Chu, Diep, Ekert, Paul G., Day, Catherine L., Pakusch, Miha, ...
Inhibitor of apoptosis (IAP) proteins, which bind to caspases via their baculoviral IAP repeat domains, also bear RING domains that enable them to promote ubiquitylation of themselves and other...
Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1
Moriishi, Kohji, Huang, David C. S., Cory, Suzanne, Adams, Jerry M.
The Bcl-2 family of proteins regulates apoptosis, the cell death program triggered by activation of certain proteases (caspases). An attractive model for how Bcl-2 and its closest relatives prevent...
Activation of Fas by FasL induces apoptosis by a mechanism that cannot be blocked by Bcl-2 or Bcl-xL
Huang, David C. S., Hahne, Michael, Schroeter, Michael, Frei, Karl, Fontana, Adriano, Villunger, Andreas, ...
Fas activation triggers apoptosis in many cell types. Studies with anti-Fas antibodies have produced conflicting results on Fas signaling, particularly the role of the Bcl-2 family in this process....
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
Hinds, Mark G., Lackmann, Martin, Skea, Gretchen L., Harrison, Penny J., Huang, David C.S., Day, Catherine L.
Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the pro-apoptotic BH3-only proteins. The solution...
Willis, Simon N., Chen, Lin, Dewson, Grant, Wei, Andrew, Naik, Edwina, Fletcher, Jamie I., ...
Commitment of cells to apoptosis is governed largely by the interaction between members of the Bcl-2 protein family. Its three subfamilies have distinct roles: The BH3-only proteins trigger apoptosis...
Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.
Day, Catherine L, Puthalakath, Hamsa, Skea, Gretchen, Strasser, Andreas, Barsukov, Igor, Lian, Lu-Yun, ...
The dynein and myosin V motor complexes are multi-protein structures that function to transport molecules and organelles within the cell. DLC (dynein light-chain) proteins, found as components of...
Silke, John, Kratina, Tobias, Chu, Diep, Ekert, Paul G., Day, Catherine L., Pakusch, Miha, ...
Inhibitor of apoptosis (IAP) proteins, which bind to caspases via their baculoviral IAP repeat domains, also bear RING domains that enable them to promote ubiquitylation of themselves and other...
Kuroda, Junya, Puthalakath, Hamsa, Cragg, Mark S., Kelly, Priscilla N., Bouillet, Philippe, Huang, David C. S., ...
Cell killing is a critical pharmacological activity of imatinib to eradicate Bcr/Abl+ leukemias. We found that imatinib kills Bcr/Abl+ leukemic cells by triggering the Bcl-2-regulated apoptotic...
O’Reilly, Lorraine A., Cullen, Leonie, Visvader, Jane, Lindeman, Geoffrey J., Print, Cris, Bath, Mary L., ...
Proapoptotic Bcl-2 family members activate cell death by neutralizing their anti-apoptotic relatives, which in turn maintain cell viability by regulating the activation of the cell death effectors,...
FADD and caspase-8 are required for cytokine-induced proliferation of hemopoietic progenitor cells
Pellegrini, Marc, Bath, Sue, Marsden, Vanessa S., Huang, David C. S., Metcalf, Donald, Harris, Alan W., ...
The role of caspase-8 and its adaptor Fas-associated death domain (FADD) in lymphocyte apoptosis is well defined, but their functions in other hemopoietic lineages are not clear. We were unable to...
Structural insights into the degradation of Mcl-1 induced by BH3 domains
Czabotar, Peter E., Lee, Erinna F., Van Delft, Mark F., Day, Catherine L., Smith, Brian J., Huang, David C. S., ...
Apoptosis is held in check by prosurvival proteins of the Bcl-2 family. The distantly related BH3-only proteins bind to and antagonize them, thereby promoting apoptosis. Whereas binding of the...
Cragg, Mark S, Kuroda, Junya, Puthalakath, Hamsa, Huang, David C. S, Strasser, Andreas
Andreas Strasser and colleagues demonstrate that activation of the proapoptotic BH3-only protein BIM is essential for tumor cell killing and that shutdown of the EGFR−MEK−ERK signaling cascade is...
Uren, Rachel T., Dewson, Grant, Chen, Lin, Coyne, Stephanie C., Huang, David C.S., Adams, Jerry M., ...
The Bcl-2 family regulates apoptosis by controlling mitochondrial integrity. To clarify whether its prosurvival members function by sequestering their Bcl-2 homology 3 (BH3)–only ligands or their...
Colussi, Paul A., Quinn, Leonie M., Huang, David C.S., Coombe, Michelle, Read, Stuart H., Richardson, Helena, ...
Bcl-2 family of proteins are key regulators of apoptosis. Both proapoptotic and antiapoptotic members of this family are found in mammalian cells, but no such proteins have been described in insects....
Wilson-Annan, Julie, O'Reilly, Lorraine A., Crawford, Simon A., Hausmann, George, Beaumont, Jennifer G., Parma, Loes P., ...
Prosurvival Bcl-2–like proteins, like Bcl-w, are thought to function on organelles such as the mitochondrion and to be targeted to them by their hydrophobic COOH-terminal domain. We unexpectedly...
Hausmann, George, O'Reilly, Lorraine A., Van Driel, Rosemary, Beaumont, Jennifer G., Strasser, Andreas, Adams, Jerry M., ...
How Bcl-2 and its pro-survival relatives prevent activation of the caspases that mediate apoptosis is unknown, but they appear to act through the caspase activator apoptosis protease–activating...
Lee, Erinna F., Czabotar, Peter E., Van Delft, Mark F., Michalak, Ewa M., Boyle, Michelle J., Willis, Simon N., ...
Like Bcl-2, Mcl-1 is an important survival factor for many cancers, its expression contributing to chemoresistance and disease relapse. However, unlike other prosurvival Bcl-2–like proteins, Mcl-1...
In vivo efficacy of the Bcl-2 antagonist ABT-737 against aggressive Myc-driven lymphomas
Mason, Kylie D., Vandenberg, Cassandra J., Scott, Clare L., Wei, Andrew H., Cory, Suzanne, Huang, David C. S., ...
Deregulated Myc expression drives many human cancers, including Burkitt's lymphoma and a highly aggressive subset of diffuse large cell lymphomas. Myc-driven tumors often display resistance to...
Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax
Fletcher, Jamie I., Meusburger, Sarina, Hawkins, Christine J., Riglar, David T., Lee, Erinna F., Fairlie, W. Douglas, ...
A central issue in the control of apoptosis is whether its essential mediators Bax and Bak must be restrained by Bcl-2-like prosurvival relatives to prevent their damaging mitochondria and unleashing...