A Unified Model of Mammalian BCL-2 Protein Family Interactions at the Mitochondria

An inhibitor of Bcl-2 family proteins induces regression of solid tumours

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Mobility measurement by analysis of fluorescence photobleaching recovery kinetics

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Differential Targeting of Prosurvival Bcl-2 Proteins by Their BH3-Only Ligands Allows Complementary Apoptotic Function

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The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis

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Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics

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Bid, Bax, and Lipids Cooperate to Form Supramolecular Openings in the Outer Mitochondrial Membrane

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Structure of Bcl-x _L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis

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The BCL-2 Family Reunion

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Mitochondria in Apoptosis: Bcl-2 Family Members and Mitochondrial Dynamics

Martinou, J., & Youle, R. J. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.06.017 · Cited by 1,366 · see citing works

Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members

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tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cPreprint

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Proapoptotic Bak is sequestered by Mcl-1 and Bcl-x L , but not Bcl-2, until displaced by BH3-only proteinsPreprint

Willis, S. N., Chen, L., Dewson, G., Wei, A. H., Naik, E., Fletcher, J. I., Adams, J. M., & Huang, D. C. S. (2005) · Genes & Development · doi:10.1101/gad.1304105 · Cited by 1,236 · see citing works

Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane

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BH3 Domains of BH3-Only Proteins Differentially Regulate Bax-Mediated Mitochondrial Membrane Permeabilization Both Directly and Indirectly

Kuwana, T., Bouchier-Hayes, L., Chipuk, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., & Newmeyer, D. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.003 · Cited by 1,185 · see citing works

Cytosol-to-membrane redistribution of Bax and Bcl-X L during apoptosis

Hsu, Y., Wolter, K. G., & Youle, R. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3668 · Cited by 1,134 · see citing works

Apoptosis Initiated When BH3 Ligands Engage Multiple Bcl-2 Homologs, Not Bax or Bak

Willis, S. N., Fletcher, J. I., Kaufmann, T., van Delft, M. F., Chen, L., Czabotar, P. E., Ierino, H., Lee, E. F., Fairlie, W. D., Bouillet, P., et al. (2007) · Science · doi:10.1126/science.1133289 · Cited by 1,125 · see citing works

Structure of Bax

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Quantifying colocalization by correlation: The Pearson correlation coefficient is superior to the Mander's overlap coefficient

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Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies

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Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis

Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846 · see citing works

Structural biology of the Bcl-2 family of proteins

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Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol

Edlich, F., Banerjee, S., Suzuki, M., Cleland, M. M., Arnoult, D., Wang, C., Neutzner, A., Tjandra, N., & Youle, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.02.034 · Cited by 630 · see citing works

Role of Bax and Bak in mitochondrial morphogenesis

Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625 · see citing works

Stepwise Activation of BAX and BAK by tBID, BIM, and PUMA Initiates Mitochondrial Apoptosis

Kim, H., Tu, H.-C., Ren, D., Takeuchi, O., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.030 · Cited by 600 · see citing works

Nonionic Detergents Induce Dimerization among Members of the Bcl-2 Family

Hsu, Y., & Youle, R. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13829 · Cited by 591 · see citing works

Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes

Leber, B. F., Lin, J., & Andrews, D. W. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0746-4 · Cited by 378 · see citing works

Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins

Brooks, C., Wei, Q., Feng, L., Dong, G., Tao, Y., Mei, L., Xie, Z.-J., & Dong, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703976104 · Cited by 351 · see citing works

To Trigger Apoptosis, Bak Exposes Its BH3 Domain and Homodimerizes via BH3:Groove Interactions

Dewson, G., Kratina, T., Sim, H. W., Puthalakath, H., Adams, J. M., Colman, P. M., & Kluck, R. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.005 · Cited by 348 · see citing works

BH3-Triggered Structural Reorganization Drives the Activation of Proapoptotic BAX

Gavathiotis, E., Reyna, D. E., Davis, M. L., Bird, G. H., & Walensky, L. D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.019 · Cited by 310 · see citing works

Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX

Ku, B., Liang, C., Jung, J. U., & Oh, B. (2010) · Cell Research · doi:10.1038/cr.2010.149 · Cited by 307 · see citing works

Bax- or Bak-Induced Mitochondrial Fission Can Be Uncoupled from Cytochrome c Release

Sheridan, C., Delivani, P., Cullen, S. P., & Martin, S. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.002 · Cited by 264 · see citing works

Apoptosis and oncogenesis: give and take in the BCL-2 family

Llambi, F., & Green, D. R. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.12.001 · Cited by 261 · see citing works

The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes

Hoppins, S. C., Edlich, F., Harwig, M. C., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.11.030 · Cited by 243 · see citing works

The X-Ray Structure of a BAK Homodimer Reveals an Inhibitory Zinc Binding Site

Moldoveanu, T., Liu, Q., Tocilj, A., Watson, M., Shore, G. C., & Gehring, K. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.10.014 · Cited by 239 · see citing works

Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands

Kvansakul, M., Yang, H. J., Fairlie, W. D., Czabotar, P. E., Fischer, S. F., Perugini, M. A., Huang, D. C. S., & Colman, P. M. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.83 · Cited by 235 · see citing works

Resistance to Caspase-Independent Cell Death Requires Persistence of Intact Mitochondria

Tait, S. W. G., Parsons, M. J., Llambi, F., Bouchier‐Hayes, L., Connell, S., Muñoz‐Pinedo, C., & Green, D. R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.014 · Cited by 204 · see citing works

Interaction with a Membrane Surface Triggers a Reversible Conformational Change in Bax Normally Associated with Induction of Apoptosis

Yethon, J. A., Epand, R. F., Leber, B. F., Epand, R. M., & Andrews, D. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306289200 · Cited by 203 · see citing works

Role for CED-9 and Egl-1 as Regulators of Mitochondrial Fission and Fusion Dynamics

Delivani, P., Adrain, C., Taylor, R. C., Duriez, P. J., & Martin, S. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.034 · Cited by 193 · see citing works

The role of BH3-only protein Bim extends beyond inhibiting Bcl-2–like prosurvival proteins

Mérino, D., Giam, M., Hughes, P., Siggs, O. M., Heger, K., O’Reilly, L. A., Adams, J. M., Strasser, A., Lee, E. F., Fairlie, W. D., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200905153 · Cited by 186 · see citing works

Still embedded together binding to membranes regulates Bcl-2 protein interactions

Leber, B. F., Lin, J., & Andrews, D. W. (2010) · Oncogene · doi:10.1038/onc.2010.283 · Cited by 167 · see citing works

Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains

Moldoveanu, T., Gehring, K., & Green, D. R. (2008) · Nature · doi:10.1038/nature07353 · Cited by 143 · see citing works

Differential Regulation of Bax and Bak by Anti-apoptotic Bcl-2 Family Proteins Bcl-B and Mcl-1

Zhai, D., Jin, C., Huang, Z., Satterthwait, A. C., & Reed, J. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708426200 · Cited by 138 · see citing works

Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak

Uren, R. T., Dewson, G., Chen, L., Coyne, S. C., Huang, D. C. S., Adams, J. M., & Kluck, R. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606065 · Cited by 123 · see citing works

Bcl-2 and Bax Interact via the BH1–3 Groove-BH3 Motif Interface and a Novel Interface Involving the BH4 Motif

Ding, J., Zhang, Z., Roberts, G. J., Falcone, M., Miao, Y., Shao, Y., Zhang, X. C., Andrews, D. W., & Lin, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.148361 · Cited by 77 · see citing works

Apoptotic Regulation by MCL-1 through Heterodimerization

Liu, Q., Moldoveanu, T., Sprules, T. J., Matta‐Camacho, E., Mansur‐Azzam, N., & Gehring, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105452 · Cited by 74 · see citing works

Perturbation of the Bcl-2 Network and an Induced Noxa/Bcl-xL Interaction Trigger Mitochondrial Dysfunction after DNA Damage

López-Bertoni, H., Zhang, L., George, N. M., Liu, X., Pang, X., Evans, J. J. D., Targy, N. M., & Luo, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.086231 · Cited by 57 · see citing works

Digestive versus regulatory proteases: on calpain action in vivo

Friedrich, P., & Bozóky, Z. (2005) · Biological Chemistry · doi:10.1515/bc.2005.071 · Cited by 40 · see citing works

Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018.

Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works

Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy

Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219 · see citing works

BCL-2 family proteins: changing partners in the dance towards death

Kale, J., Osterlund, E. J., & Andrews, D. W. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.186 · Cited by 1,574 · see citing works

Recent advances in 2D and 3D in vitro systems using primary hepatocytes, alternative hepatocyte sources and non-parenchymal liver cells and their use in investigating mechanisms of hepatotoxicity, cell signaling and ADME

Godoy, P., Hewitt, N. J., Albrecht, U., Andersen, M. E., Ansari, N., Bhattacharya, S., Bode, J. G., Bolleyn, J., Borner, C., Böttger, J., et al. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1078-5 · Cited by 1,280 · see citing works

The role of BCL-2 family proteins in regulating apoptosis and cancer therapy

Qian, S., Wei, Z., Yang, W., Huang, J., Yang, Y., & Wang, J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.985363 · Cited by 1,011 · see citing works

Mechanisms of Action of Bcl-2 Family Proteins

Shamas-Din, A., Kale, J., Leber, B., & Andrews, D. W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008714 · Cited by 705 · see citing works

Bax Crystal Structures Reveal How BH3 Domains Activate Bax and Nucleate Its Oligomerization to Induce Apoptosis

Czabotar, P. E., Westphal, D., Dewson, G., Ma, S., Hockings, C., Fairlie, W. D., Lee, E. F., Yao, S., Robin, A. Y., Smith, B. J., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.031 · Cited by 573 · see citing works

A fate worse than death: apoptosis as an oncogenic process

Ichim, G., & Tait, S. W. G. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.58 · Cited by 451 · see citing works

Many players in BCL-2 family affairs

Moldoveanu, T., Follis, A. V., Kriwacki, R. W., & Green, D. R. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.006 · Cited by 421 · see citing works

Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane

O'Neill, K. L., Huang, K., Zhang, J., Chen, Y., & Luo, X. (2016) · Genes & Development · doi:10.1101/gad.276725.115 · Cited by 323 · see citing works

The clearance of dying cells: table for two

Green, D. R., Oguin, T. H., & Martinez, J. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2015.172 · Cited by 314 · see citing works

BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation

Llambi, F., Wang, Y.-M., Victor, B., Yang, M., Schneider, D. M., Gingras, S., Parsons, M. J., Zheng, J. H., Brown, S. A., Pelletier, S., et al. (2016) · Cell · doi:10.1016/j.cell.2016.02.026 · Cited by 261 · see citing works

Bax Exists in a Dynamic Equilibrium between the Cytosol and Mitochondria to Control Apoptotic Priming

Schellenberg, B., Wang, P., Keeble, J. A., Rodriguez-Enriquez, R., Walker, S., Owens, T. W., Foster, F., Tanianis-Hughes, J., Brennan, K., Streuli, C. H., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.022 · Cited by 237 · see citing works

The BCL-2 family of proteins and mitochondrial outer membrane permeabilisation

Birkinshaw, R. W., & Czabotar, P. E. (2017) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2017.04.001 · Cited by 229 · see citing works

Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species

Subburaj, Y., Cosentino, K., Axmann, M., Pedrueza-Villalmanzo, E., Hermann, E., Bleicken, S., Spatz, J., & García-Sáez, A. J. (2015) · Nature Communications · doi:10.1038/ncomms9042 · Cited by 181 · see citing works

Differential retrotranslocation of mitochondrial Bax and Bak

Todt, F., Cakir, Z., Reichenbach, F., Emschermann, F., Lauterwasser, J., Kaiser, A., Ichim, G., Tait, S. W., Frank, S., Langer, H. F., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201488806 · Cited by 172 · see citing works

Bak Core and Latch Domains Separate during Activation, and Freed Core Domains Form Symmetric Homodimers

Brouwer, J. M., Westphal, D., Dewson, G., Robin, A. Y., Uren, R. T., Bartolo, R., Thompson, G. V., Colman, P. M., Kluck, R. M., & Czabotar, P. E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.07.016 · Cited by 161 · see citing works

Physiological and Pharmacological Control of BAK, BAX, and Beyond

Luna-Vargas, M. P. A., & Chipuk, J. E. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.07.002 · Cited by 142 · see citing works

Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: a requirement for VDAC2 or Bak for efficient Bax apoptotic function

Ma, S. B., Nguyen, T. N., Tan, I., Ninnis, R., Iyer, S., Stroud, D. A., Menard, M., Kluck, R. M., Ryan, M. T., & Dewson, G. (2014) · Cell Death & Differentiation · doi:10.1038/cdd.2014.119 · Cited by 138 · see citing works

An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway

Garner, T. P., Reyna, D. E., Priyadarshi, A., Chen, H.-C., Li, S., Wu, Y., Ganesan, Y. T., Malashkevich, V. N., Cheng, E. H., & Gavathiotis, E. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.010 · Cited by 108 · see citing works

Systems analysis of BCL2 protein family interactions establishes a model to predict responses to chemotherapy

Lindner, A. U., Concannon, C. G., Boukes, G. J., Cannon, M. D., Llambi, F., Ryan, D., Boland, K., Kehoe, J., McNamara, D. A., Murray, F., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2269 · Cited by 105 · see citing works

Crosstalk between apoptosis and autophagy signaling pathways

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Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation

Bleicken, S., Hantusch, A., Das, K. K., Frickey, T., & Garcia-Saez, A. J. (2017) · Nature Communications · doi:10.1038/s41467-017-00086-6 · Cited by 70 · see citing works

Consequences of the combined loss of BOK and BAK or BOK and BAX

Ke, F., Bouillet, P., Kaufmann, T., Strasser, A., Kerr, J., & Voss, A. K. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.176 · Cited by 72 · see citing works

Assembly of the Bak Apoptotic Pore

Ma, S., Hockings, C., Anwari, K., Kratina, T., Fennell, S., Lazarou, M., Ryan, M. T., Kluck, R. M., & Dewson, G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490094 · Cited by 71 · see citing works

Organization of the Mitochondrial Apoptotic BAK Pore

Aluvila, S., Mandal, T., Hustedt, E., Fajer, P., Choe, J. Y., & Oh, K. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526806 · Cited by 71 · see citing works

Bok is a genuine multi-BH-domain protein that triggers apoptosis in the absence of Bax and Bak

Einsele-Scholz, S., Malmsheimer, S., Bertram, K., Stehle, D., Johänning, J., Manz, M., Daniel, P. T., Gillissen, B. F., Schulze-Osthoff, K., & Essmann, F. (2016) · Journal of Cell Science · doi:10.1242/jcs.181727 · Cited by 65 · see citing works

Diminished apoptotic priming and ATM signalling confer a survival advantage onto aged haematopoietic stem cells in response to DNA damage

Gutierrez-Martinez, P., Hogdal, L., Nagai, M., Kruta, M., Singh, R., Sarosiek, K., Nussenzweig, A., Beerman, I., Letai, A., & Rossi, D. J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0054-y · Cited by 60 · see citing works

The Incomplete Puzzle of the BCL2 Proteins

Flores-Romero, H., & García-Sáez, A. J. (2019) · Cells · doi:10.3390/cells8101176 · Cited by 38 · see citing works

Epigenetic silencing of Bim transcription by Spi-1/PU.1 promotes apoptosis resistance in leukaemia

Ridinger-Saison, M., Evanno, E., Gallais, I., Rimmelé, P., Selimoglu-Buet, D., Sapharikas, E., Moreau-Gachelin, F., & Guillouf, C. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.88 · Cited by 34 · see citing works

Apoptotic priming is defined by the dynamic exchange of Bcl-2 proteins between mitochondria and cytosol

King, L. E., Rodriguez-Enriquez, R., Pedley, R., Mellor, C. E. L., Wang, P., Zindy, E., White, M. R. H., Brennan, K., & Gilmore, A. P. (2022) · Cell Death & Differentiation · doi:10.1038/s41418-022-01013-z · Cited by 26 · see citing works

Differential mechanisms involved in RG-7388 and Nutlin-3 induced cell death in SJSA-1 osteosarcoma cells

Natarajan, U., Venkatesan, T., Dhandayuthapani, S., Dondapatti, P., & Rathinavelu, A. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109742 · Cited by 11 · see citing works

ИСПОЛЬЗОВAНИЕ ПОТЕНЦИAЛA СОЦИAЛЬНЫХ ПAРТНЕРОВ В ПОДГОТОВКЕ БУДУЩИХ ПЕДAГОГОВ

Атабекова, Б. Б. (2024) · Habaršy. Pedagogika ġylymdary seriâsy · doi:10.51889/2959-5762.2023.80.4.019

Cloning and Characterization of Rat BAT3 cDNA

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EFFECT OF THE NEMATODE PHASMARHABDITIS HERMAPHRODITA ON YOUNG STAGES OF THE PEST SLUG ARION LUSITANICUS

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HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53Preprint

Sasaki, T., Gan, E. C., Wakeham, A. C., Kornbluth, S. A., Mak, T. W., & Okada, H. (2007) · Genes & Development · doi:10.1101/gad.1534107 · Cited by 127 · see citing works

Anthoxanthum Mosaic Virus

Catherall, P. L. (1970) · Plant Pathology · doi:10.1111/j.1365-3059.1970.tb00999.x · Cited by 6 · see citing works