PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20023601-4 2010 Our results show that after the onset of sepsis, tBid (the active form of Bid) is significantly increased in mitochondrial fractions of the thymus, spleen, Peyer patches, and liver, and that Fas or FasL deficiency blocks Bid activation in various tissues after septic challenge. tBID 49-53 BH3 interacting domain death agonist Mus musculus 74-77 27320914-3 2016 Upon Fas receptor stimulation, the BH3-only protein Bid is cleaved into the active form, tBid. tBID 89-93 BH3 interacting domain death agonist Mus musculus 52-55 21738214-9 2012 We also demonstrate that, after MNNG treatment, BID is directly processed into tBID by calpains. tBID 79-83 BH3 interacting domain death agonist Mus musculus 48-51 27760587-5 2017 In the current study, we constructed a recombinant adenovirus Cre/loxP regulation system to selectively introduce truncated Bid (tBid) expression specifically targeting CD133+ in ovarian CSCs. tBID 129-133 BH3 interacting domain death agonist Mus musculus 124-127 25457551-8 2015 Notably, PUMA contributed to neuronal apoptosis through competitive binding of apoptosis repressor with caspase recruitment domain to activate caspase-8 that cleaved Bid into tBid to accelerate Bax mitochondrial translocation, revealing a novel pathway of Bax activation by PUMA to mediate Abeta-induced neuronal apoptosis. tBID 175-179 BH3 interacting domain death agonist Mus musculus 166-169 20179769-2 2010 In response to death receptors activation, Bid is cleaved by caspase-8 into its active form, tBid (truncated Bid), which then translocates to the mitochondria to trigger cytochrome c release and subsequent apoptosis. tBID 93-97 BH3 interacting domain death agonist Mus musculus 43-46 11805084-1 2002 Activation of the tumor necrosis factor R1/Fas receptor results in the cleavage of cytosolic BID to truncated tBID. tBID 110-114 BH3 interacting domain death agonist Mus musculus 93-96 19820692-1 2009 Truncated BID (tBID), a proapoptotic BCL2 family protein, induces BAK/BAX-dependent release of cytochrome c and other mitochondrial intermembrane proteins to the cytosol to induce apoptosis. tBID 15-19 BH3 interacting domain death agonist Mus musculus 10-13 19839062-1 2009 UNLABELLED: Bcl-2 homology domain 3 (BH3)-only protein Bid is posttranslationally cleaved by caspase-8 into its truncated form (tBid) and couples with stress signals to the mitochondrial cell death pathway. tBID 128-132 BH3 interacting domain death agonist Mus musculus 55-58 16600192-9 2006 Activation of caspase-8 and cleavage of Bid to tBid in RGC-5 cells following exposure to IFN-gamma indicated co-operation between extrinsic and intrinsic pathways of apoptosis. tBID 47-51 BH3 interacting domain death agonist Mus musculus 40-43 15899861-2 2005 Activation of the TNF-R1 receptor results in the cleavage of BID into truncated BID (tBID), which translocates to the mitochondria and induces the activation of BAX or BAK. tBID 85-89 BH3 interacting domain death agonist Mus musculus 61-64 15899861-2 2005 Activation of the TNF-R1 receptor results in the cleavage of BID into truncated BID (tBID), which translocates to the mitochondria and induces the activation of BAX or BAK. tBID 85-89 BH3 interacting domain death agonist Mus musculus 80-83 15650755-2 2005 MtDNA-depleted cells show a 3-4-fold increased proapoptotic proteins (Bax, BAD and Bid), markedly increased antiapoptotic Bcl-2, and reduced processing of p21 Bid to active tBid. tBID 173-177 BH3 interacting domain death agonist Mus musculus 159-162 12946648-3 2003 AAP-induced loss of mitochondrial cytochrome c coincided with the appearance in the cytosol of a fragment corresponding to truncated Bid (tBid). tBID 138-142 BH3 interacting domain death agonist Mus musculus 133-136 12946648-7 2003 This correlated with the inhibition of the processing of Bid to tBid. tBID 64-68 BH3 interacting domain death agonist Mus musculus 57-60 12598529-1 2003 Bid is instrumental in death receptor-mediated apoptosis where it is cleaved by caspase 8 at aspartate 60 and aspartate 75 to generate truncated Bid (tBID) forms that facilitate release of mitochondrial cytochrome c. Bid is also cleaved at these sites by caspase 3 that is activated downstream of cytochrome c release after diverse apoptotic stimuli. tBID 150-154 BH3 interacting domain death agonist Mus musculus 0-3 12598529-1 2003 Bid is instrumental in death receptor-mediated apoptosis where it is cleaved by caspase 8 at aspartate 60 and aspartate 75 to generate truncated Bid (tBID) forms that facilitate release of mitochondrial cytochrome c. Bid is also cleaved at these sites by caspase 3 that is activated downstream of cytochrome c release after diverse apoptotic stimuli. tBID 150-154 BH3 interacting domain death agonist Mus musculus 145-148 12598529-1 2003 Bid is instrumental in death receptor-mediated apoptosis where it is cleaved by caspase 8 at aspartate 60 and aspartate 75 to generate truncated Bid (tBID) forms that facilitate release of mitochondrial cytochrome c. Bid is also cleaved at these sites by caspase 3 that is activated downstream of cytochrome c release after diverse apoptotic stimuli. tBID 150-154 BH3 interacting domain death agonist Mus musculus 145-148 11859412-1 2002 A crucial event in the process of apoptosis is caspase-dependent generation of truncated Bid (tBid), inducing release of cytochrome c. In an in vitro reconstitution system we combined purified recombinant tBid with isolated liver mitochondria and identified the released proteins using a proteomic matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) approach. tBID 94-98 BH3 interacting domain death agonist Mus musculus 89-92 11753562-3 2001 Here we report on the ability of truncated Bid (tBid) to induce the release of a DNAse activity from mitochondria. tBID 48-52 BH3 interacting domain death agonist Mus musculus 43-46 10982793-2 2000 The p15 form of truncated Bid (tBid) translocates to mitochondria and induces cytochrome c release, leading to the activation of downstream caspases and apoptosis. tBID 31-35 BH3 interacting domain death agonist Mus musculus 26-29 11175253-0 2000 Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. We review data supporting a model in which activated tBID results in an allosteric activation of BAK, inducing its intramembranous oligomerization into a proposed pore for cytochrome c efflux. tBID 175-179 BH3 interacting domain death agonist Mus musculus 32-35