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Science, ISSN 0036-8075, 2/2007, Volume 315, Issue 5813, pp. 856 - 859
A central issue in the regulation of apoptosis by the Bcl-2 family is whether its BH3-only members initiate apoptosis by directly binding to the essential... 
Research fellowships | Protein isoforms | Medical research | Myeloid cells | Antibodies | Cytochromes | Ligands | Reports | Grants | Viability | Apoptosis | RESPONSES | FAMILY-MEMBERS | X-L | MULTIDISCIPLINARY SCIENCES | BIM | HELIX | MITOCHONDRIAL-MEMBRANE | PUMA | DOMAINS | BH3-ONLY PROTEINS | CELL-DEATH | bcl-2-Associated X Protein - chemistry | Humans | BH3 Interacting Domain Death Agonist Protein - genetics | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | Tumor Suppressor Proteins - genetics | BH3 Interacting Domain Death Agonist Protein - chemistry | Apoptosis Regulatory Proteins - genetics | bcl-Associated Death Protein - metabolism | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Proto-Oncogene Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Myeloid Cell Leukemia Sequence 1 Protein | Mice | Mutation | bcl-X Protein - metabolism | Research | Peptides | Analysis
Journal Article
Molecular Cell, ISSN 1097-2765, 2005, Volume 17, Issue 3, pp. 393 - 403
Apoptosis is initiated when Bcl-2 and its prosurvival relatives are engaged by proapoptotic BH3-only proteins via interaction of its BH3 domain with a groove... 
CYTOCHROME-C | COMPLEX | SURVIVAL FACTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIA | BIM | RELEASE | PEPTIDE | CELL-DEATH | FAMILY | MEMBER | CELL BIOLOGY | Humans | Molecular Sequence Data | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | Genetic Complementation Test | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | Carrier Proteins - chemistry | Proto-Oncogene Proteins c-bcl-2 - chemistry | Membrane Proteins - metabolism | Neoplasm Proteins - genetics | Peptide Fragments - genetics | Cell Survival - physiology | Binding, Competitive | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | bcl-X Protein | Peptide Fragments - metabolism | Membrane Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Proto-Oncogene Proteins - genetics | Recombinant Proteins - genetics | Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Peptide Fragments - chemistry | Animals | Apoptosis Regulatory Proteins | Carrier Proteins - metabolism | Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Myeloid Cell Leukemia Sequence 1 Protein | Biosensing Techniques | Ligands | Mice | Apoptosis - physiology | Proteins - chemistry | In Vitro Techniques | Proto-Oncogene Proteins c-bcl-2 - genetics
Journal Article
The FEBS Journal, ISSN 1742-464X, 07/2016, Volume 283, Issue 14, pp. 2690 - 2700
B‐cell lymphoma 2 (BCL‐2) family proteins mediate mitochondrial apoptosis by regulating mitochondrial outer membrane permeabilization (MOMP), which leads to... 
pro‐apoptotic; sensitizer | direct activator | BH3‐only | derepressor | mitochondrial apoptosis | effector | mitochondrial outer membrane permeabilization | anti‐apoptotic | B‐cell lymphoma 2 | Derepressor | Anti-apoptotic | Mitochondrial outer membrane permeabilization | Pro-apoptotic; sensitizer | Mitochondrial apoptosis | Direct activator | Effector | B-cell lymphoma 2 | BH3-only | anti-apoptotic | pro-apoptotic; sensitizer | DNA-BINDING DOMAIN | MITOCHONDRIAL OUTER-MEMBRANE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROMOTE APOPTOSIS | DIRECT ACTIVATION | sensitizer | CELL-DEATH | BAX ACTIVATION | CHANGES CONFORMATION | pro-apoptotic | PROLYL ISOMERASE PIN1 | PEPTIDE COMPLEX | Signal Transduction | Tumor Suppressor Protein p53 - antagonists & inhibitors | Humans | Protein Multimerization | Tumor Suppressor Protein p53 - metabolism | bcl-2-Associated X Protein - metabolism | Models, Molecular | Permeability | Mitochondrial Membranes - metabolism | bcl-X Protein - chemistry | Proto-Oncogene Proteins c-bcl-2 - metabolism | Animals | Models, Biological | Protein Conformation | Proto-Oncogene Proteins c-bcl-2 - chemistry | Protein Interaction Domains and Motifs | Tumor Suppressor Protein p53 - chemistry | Apoptosis - physiology | bcl-X Protein - metabolism | Tumor proteins | Protein-protein interactions | Protein binding | Apoptosis | Proteins | Lymphomas
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2011, Volume 286, Issue 1, pp. 491 - 501
Bcl-2 family proteins regulate a critical step in apoptosis referred to as mitochondrial outer membrane permeabilization (MOMP). Members of a subgroup of the... 
MITOCHONDRIAL-MEMBRANE PERMEABILIZATION | ANTAGONIST ABT-737 | MCL-1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | MIMETIC ABT-737 | APOPTOTIC PROTEIN BAK | SENSITIVITY | OLIGOMERIZATION | BCL-2 FAMILY-MEMBERS | BH3-ONLY PROTEINS | CELL-DEATH | bcl-2-Associated X Protein - chemistry | Humans | Protein Multimerization | Cell Membrane Permeability | Molecular Sequence Data | Proto-Oncogene Proteins - chemistry | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | BH3 Interacting Domain Death Agonist Protein - chemistry | HEK293 Cells | Protein Structure, Quaternary | Cell Membrane - metabolism | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Peptide Fragments - metabolism | Cytochromes c - secretion | Apoptosis Regulatory Proteins - chemistry | bcl-2-Associated X Protein - metabolism | Apoptosis Regulatory Proteins - metabolism | Animals | Membrane Proteins - chemistry | Liposomes - metabolism | Mice | Adaptor Proteins, Signal Transducing - metabolism | bcl-X Protein - metabolism | bcl-2 Homologous Antagonist-Killer Protein - chemistry | Apoptosis | Cytochrome c | BH3 Peptides | Mitochondria | Cell Death | Liposomes | Cell Biology | Bcl-2 Family Proteins
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 09/2014, Volume 289, Issue 38, pp. 26481 - 26491
The B cell lymphoma-2 (BCL-2) family is the key mediator of cellular sensitivity to apoptosis during pharmacological interventions for numerous human... 
POTENT | OLIGOMERIZES BAK | CANCERS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEATH | MITOCHONDRIAL-MEMBRANE | INHIBITORS | CYTOCHROME-C RELEASE | DISCOVERY | ADDICTION | MEMBRANE PERMEABILIZATION | bcl-2-Associated X Protein - chemistry | Nitriles - pharmacology | Apoptosis - drug effects | Mitochondria, Liver - metabolism | Humans | Unilamellar Liposomes - chemistry | bcl-2-Associated X Protein - physiology | Piperazines - chemistry | Proto-Oncogene Proteins - chemistry | Sulfones - pharmacology | Nitrophenols - chemistry | Benzopyrans - chemistry | bcl-X Protein - chemistry | Molecular Mimicry | Bcl-2-Like Protein 11 | Biphenyl Compounds - pharmacology | Nitrophenols - pharmacology | Membrane Proteins - physiology | Sulfones - chemistry | BH3 Interacting Domain Death Agonist Protein - chemistry | Myeloid Cell Leukemia Sequence 1 Protein - chemistry | Benzamides - pharmacology | Protein Interaction Domains and Motifs | Biphenyl Compounds - chemistry | Benzopyrans - pharmacology | Benzamides - chemistry | Aniline Compounds - pharmacology | BH3 Interacting Domain Death Agonist Protein - physiology | Sulfonamides - chemistry | Apoptosis Regulatory Proteins - chemistry | Permeability | Sulfonamides - pharmacology | Piperazines - pharmacology | Mitochondrial Membranes - metabolism | Mitochondria, Liver - drug effects | Myeloid Cell Leukemia Sequence 1 Protein - physiology | Pyrroles - pharmacology | Animals | Membrane Proteins - chemistry | bcl-X Protein - physiology | Nitriles - chemistry | Proto-Oncogene Proteins - physiology | Pyrroles - chemistry | Apoptosis Regulatory Proteins - physiology | Mice | Aniline Compounds - chemistry | HeLa Cells | BH3 Mimetics | MOMP | Mitochondria | Bcl-2 Proteins | Bax | Anticancer Drug | Cell Biology | Apoptosis
Journal Article
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 09/2014, Volume 111, Issue 39, pp. E4076 - E4085
Journal Article
Journal of Medicinal Chemistry, ISSN 0022-2623, 07/2007, Volume 50, Issue 15, pp. 3457 - 3464
A new pocket detection protocol successfully identified transient pockets on the protein surfaces of BCL-XL, IL-2, and MDM2. Because the native inhibitor... 
MOLECULAR-DYNAMICS | CHEMISTRY, MEDICINAL | LIGAND DOCKING | FLEXIBILITY | FORCE-FIELD | SIMULATIONS | BINDING-SITES | ANTAGONISTS | INHIBITOR | P53 | PREDICTION | bcl-X Protein - chemistry | Computer Simulation | Drug Design | Models, Molecular | Protein Binding | Interleukin-2 - chemistry | Ligands | Protein Conformation | Proto-Oncogene Proteins c-mdm2 - chemistry | Binding Sites
Journal Article
Journal Article