Protein Bcl Xl
Mostrando 13-24 de 53 artigos, teses e dissertações.
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13. c-Myc Augments Gamma Irradiation-Induced Apoptosis by Suppressing Bcl-XL
Alterations in MYC and p53 are hallmarks of cancer. p53 coordinates the response to gamma irradiation (γ-IR) by either triggering apoptosis or cell cycle arrest. c-Myc activates the p53 apoptotic checkpoint, and thus tumors overexpressing MYC often harbor p53 mutations. Nonetheless, many of these cancers are responsive to therapy, suggesting that Myc may se
American Society for Microbiology.
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14. An essential role for Bruton's [corrected] tyrosine kinase in the regulation of B-cell apoptosis.
Mutations of the Bruton's tyrosine kinase (btk) gene cause X-linked agammaglobulinemia (XLA) in humans and X-linked immune deficiency (Xid) in mice. To establish the BTK role in B-cell activation we examined the responses of wild-type and Xid B cells to stimulation through surface IgM and CD40, the transducers of thymus independent-type 2 and thymus-dependen
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15. BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins
Two major pathways for induction of apoptosis have been identified—intrinsic and extrinsic. The extrinsic pathway is represented by tumor necrosis factor family receptors, which utilize protein interaction modules known as death domains and death effector domains (DEDs) to assemble receptor signaling complexes that recruit and activate certain caspase-fami
The National Academy of Sciences.
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16. MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death
Activation of the cascade of proteolytic caspases has been identified as the final common pathway of apoptosis in diverse biological systems. We have isolated a gene, termed MRIT, that possesses overall sequence homology to FLICE (MACH), a large prodomain caspase that links the aggregated complex of the death domain receptors of the tumor necrosis factor rec
The National Academy of Sciences of the USA.
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17. Xenopus Bcl-XL selectively protects Rohon-Beard neurons from metamorphic degeneration
Amphibian metamorphosis involves extensive, but selective, neuronal death and turnover, thus sharing many features with mammalian postnatal development. The antiapoptotic protein Bcl-XL plays an important role in postnatal mammalian neuronal survival. It is therefore of interest that accumulation of the mRNA encoding the Xenopus Bcl-XL homologue, termed xR11
The National Academy of Sciences.
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18. Coupling of Cell Growth Control and Apoptosis Functions of Id Proteins
The Id family of helix-loop-helix proteins function as negative regulators of cell differentiation and as positive regulators of G1 cell cycle control. We report here that enforced overexpression of the Id3 gene suppresses the colony-forming efficiency of primary rat embryo fibroblasts. Cotransfection with the antiapoptotic Bcl2 or BclXL gene alleviates this
American Society for Microbiology.
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19. ABT-737 Synergizes with Chemotherapy to Kill Head and Neck Squamous Cell Carcinoma Cells via a Noxa-Mediated PathwayS⃞
Overexpression of Bcl-XL, an antiapoptotic Bcl-2 family member, occurs in a majority of head and neck squamous cell carcinomas (HNSCCs) and correlates with chemotherapy resistance in this disease. Overexpression of Bcl-2 is also observed in HNSCC, albeit less frequently. We have previously shown that peptides derived from the BH3 domains of proapoptotic
American Society for Pharmacology and Experimental Therapeutics.
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20. Channel formation by antiapoptotic protein Bcl-2
Bcl-2 is the prototypical member of a large family of apoptosis-regulating proteins, consisting of blockers and promoters of cell death. The three-dimensional structure of a Bcl-2 homologue, Bcl-XL, suggests striking similarity to the pore-forming domains of diphtheria toxin and the bacterial colicins, prompting exploration of whether Bcl-2 is capable of for
The National Academy of Sciences of the USA.
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21. Identification of Novel Isoforms of the BH3 Domain Protein Bim Which Directly Activate Bax To Trigger Apoptosis
Bim (Bcl-2-interacting mediator of cell death) is a member of the BH3 domain-only subgroup of Bcl-2 family members, for which three splice variants have been described. Bim is expressed in many healthy cell types, where it is maintained in an inactive conformation through binding to the microtubule-associated dynein motor complex. Upon certain apoptotic stim
American Society for Microbiology.
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22. Suppression of Mitochondrial Function by Oxidatively Truncated Phospholipids Is Reversible, Aided by Bid, and Suppressed by Bcl-XL*
Oxidatively truncated phospholipids are present in atherosclerotic lesions, apoptotic cells, and oxidized low density lipoproteins. Some of these lipids rapidly enter cells to induce apoptosis by the intrinsic pathway, but how such lipids initiate this process is unknown. We show the truncated phospholipid hexadecyl azelaoyl glycerophosphocholine (Az-LPAF),
American Society for Biochemistry and Molecular Biology.
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23. Bax- and Bak-induced cell death in the fission yeast Schizosaccharomyces pombe.
The effects of the expression of the human Bcl-2 family proteins Bax, Bak, Bcl-2, and Bcl-XL were examined in the fission yeast Schizosaccharomyces pombe and compared with Bax-induced cell death in mammalian cells. Expression of the proapoptotic proteins Bax and Bak conferred a lethal phenotype in this yeast, which was strongly suppressed by coexpression of
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24. Mutagenesis of the BH3 Domain of BAX Identifies Residues Critical for Dimerization and Killing
The BCL-2 family of proteins is comprised of proapoptotic as well as antiapoptotic members (S. N. Farrow and R. Brown, Curr. Opin. Genet. Dev. 6:45–49, 1996). A prominent death agonist, BAX, forms homodimers and heterodimerizes with multiple antiapoptotic members. Death agonists have an amphipathic α helix, called BH3; however, the initial assessment of B
American Society for Microbiology.