Results 311 to 320 of about 221,308 (340)
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BAXing in the hypersensitive response
Trends in Plant Science, 1999Most of the cell death pathways that have been characterized in animal systems require caspase activation as a deterministic step. In some cases, this might involve mitochondria participation, whereas others by-pass this organelle and activate caspases using protein–protein interactions. In organisms such as C.
Eric Lam+2 more
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Characterisation of the Bax-nucleophosmin interaction: the importance of the Bax C-terminus
Apoptosis, 2008The molecular chaperone nucleophosmin has been identified as a novel Bax binding protein with this interaction proposed to be a key event in the activation and translocation of Bax in mitochondrial dysfunction and apoptotic cell death. Using a proximity assay, we have quantitatively defined the high affinity and saturable interaction between Bax and ...
Jane Thompson+7 more
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Characterization of Bax-ς, a Cell Death-Inducing Isoform of Bax
Biochemical and Biophysical Research Communications, 2000The Ced-9/Bcl-like family of genes codes for proteins that have antiapoptotic and proapoptotic activity. Several Bax isoproteins have been detected by 2-D gel electrophoresis, and a novel human member, designated as Bax-sigma, has been identified and cloned from human cancer promyelocytic cells. Bax-sigma contains BH-3, BH-1, and BH-2 domains, putative
Myriam Beauchemin+4 more
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RACK1 promotes Bax oligomerization and dissociates the interaction of Bax and Bcl-XL
Cellular Signalling, 2010Bax, a member of Bcl-2 family, plays an essential role in apoptotic pathways induced by a number of apoptotic stimulus. In a search for new potential binding partners of Bax, we identified the receptor for activated C-kinase 1 (RACK1) by a yeast two-hybrid assay.
Wu, Yinyuan+8 more
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ASC is a Bax adaptor and regulates the p53–Bax mitochondrial apoptosis pathway
Nature Cell Biology, 2004The apoptosis-associated speck-like protein (ASC) is an unusual adaptor protein that contains the Pyrin/PAAD death domain in addition to the CARD protein-protein interaction domain. Here, we present evidence that ASC can function as an adaptor molecule for Bax and regulate a p53-Bax mitochondrial pathway of apoptosis.
Ohtsuka, T.+7 more
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Proceedings of the Royal Musical Association, 1977
On 27 July 1913 Colin Taylor, a music master at Eton and confidant of the young Philip Heseltine, wrote to his protégé: By the way I was introduced to Bax at the Russian Ballet the other night – do you know him? I have always pictured him as a slow speaking dreamy man – dreamy he may be, but in his speech he is short, dry and quite unpoetical.
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On 27 July 1913 Colin Taylor, a music master at Eton and confidant of the young Philip Heseltine, wrote to his protégé: By the way I was introduced to Bax at the Russian Ballet the other night – do you know him? I have always pictured him as a slow speaking dreamy man – dreamy he may be, but in his speech he is short, dry and quite unpoetical.
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Bax to the wall: Bax- and Bak-induced mitochondrial dysfunction in apoptosis
Trends in Biochemical Sciences, 2001The functionally divergent Bcl-2 homologues share homology in four regions, the Bcl-2 homology (BH) domains 1–4, and control apoptosis by regulating the integrity of the outer mitochondrial membrane, either promoting (as is the case for Bax and Bak) or inhibiting (Bcl-2, Bcl-xL) the release of apoptogenic factors such as cytochrome c.
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ACS Applied Materials and Interfaces, 2016
B-cell lymphoma 2 (Bcl-2) and Bcl-2-associated X protein (Bax) are often used to monitor the apoptosis of tumor cells and evaluate cancer drug effect.
Shiwei Zhou+2 more
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B-cell lymphoma 2 (Bcl-2) and Bcl-2-associated X protein (Bax) are often used to monitor the apoptosis of tumor cells and evaluate cancer drug effect.
Shiwei Zhou+2 more
semanticscholar +1 more source
Allostery in BAX protein activation
Journal of Biomolecular Structure and Dynamics, 2016BAX is a member of the proapoptotic BCL-2 family of proteins, which is involved in the regulation of the intrinsic pathway of apoptosis. In the process of apoptosis, BH3-only molecules activate cytosolic BAX. Activated BAX molecules insert into the mitochondrial outer membrane with their [Formula: see text]-helix and form oligomers that lead to ...
Hansi Zhang+2 more
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HSP60, Bax, and Cardiac Apoptosis
Cardiovascular Toxicology, 2003HSP60 has long been known as an important chaperonin and as having key folding functions within the mitochondria. However, it has now become evident that significant amounts of HSP60 are found in extra-mitochondrial locations. This extra-mitochondrial HSP60 in the heart has key anti-apoptotic functions. Extra-mitochondrial HSP60 complexes with both bax
Anne A Knowlton, Sanjiv Gupta
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