PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19701793-0 2009 Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid. tBID 85-89 BCL2 apoptosis regulator Homo sapiens 34-39 19228691-6 2009 CypD enhances the limiting effect of Bcl2 on the tBid-induced release of cytochrome c from mitochondria, which is not mediated via the MPT. tBID 49-53 BCL2 apoptosis regulator Homo sapiens 37-41 19228717-4 2009 It is controversial whether some BH3-domain proteins (Bim or tBid) directly activate multidomain pro-apoptotic proteins (e.g., Bax and Bak) or act via inhibition of those anti-apoptotic Bcl-2 proteins (Bcl-2, Bcl-XL, Bcl-w, Mcl-1, Bfl1/A-1, and Bcl-B) that stabilize pro-apoptotic proteins. tBID 61-65 BCL2 apoptosis regulator Homo sapiens 186-191 19228717-4 2009 It is controversial whether some BH3-domain proteins (Bim or tBid) directly activate multidomain pro-apoptotic proteins (e.g., Bax and Bak) or act via inhibition of those anti-apoptotic Bcl-2 proteins (Bcl-2, Bcl-XL, Bcl-w, Mcl-1, Bfl1/A-1, and Bcl-B) that stabilize pro-apoptotic proteins. tBID 61-65 BCL2 apoptosis regulator Homo sapiens 202-207 18547146-9 2008 However, the addition of tBid recruited molar excesses of either protein to membranes, indicating that tBid activates both pro- and antiapoptotic members of the Bcl-2 family. tBID 103-107 BCL2 apoptosis regulator Homo sapiens 161-166 18358005-10 2008 PLS3 and tBid may form a bidirectional positive feedback loop that is antagonized by Bcl-2. tBID 9-13 BCL2 apoptosis regulator Homo sapiens 85-90 18195012-1 2008 BIM and tBID are two BCL-2 homology 3 (BH3)-only proteins with a particularly strong capacity to trigger BAX-driven mitochondrial outer membrane permeabilization, a crucial event in mammalian apoptosis. tBID 8-12 BCL2 apoptosis regulator Homo sapiens 21-26 17825286-9 2007 However, in the presence of tBid, co-incubation of apoptosis-competent mitochondria with Bcl-2 microsomes, but not with Bcl-2 mitochondria, diminished the Bax-binding to Bcl-2 significantly, suggesting that Bcl-2 in ER is readily inactivated by tBid. tBID 28-32 BCL2 apoptosis regulator Homo sapiens 89-94 17825286-9 2007 However, in the presence of tBid, co-incubation of apoptosis-competent mitochondria with Bcl-2 microsomes, but not with Bcl-2 mitochondria, diminished the Bax-binding to Bcl-2 significantly, suggesting that Bcl-2 in ER is readily inactivated by tBid. tBID 245-249 BCL2 apoptosis regulator Homo sapiens 89-94 17825286-10 2007 Co-incubation assay further confirmed that Bcl-2 in the ER, but not Bcl-2 in the mitochondria, is potentially inactivated by tBid. tBID 125-129 BCL2 apoptosis regulator Homo sapiens 43-48 17825286-11 2007 Our quantitative in vitro studies indicate that Bcl-2 in mitochondria and ER are similarly potent in inhibiting Bax-associated apoptosis of other mitochondria, but are regulated by tBid differently. tBID 181-185 BCL2 apoptosis regulator Homo sapiens 48-53 16987815-2 2006 Among the "BCL-2 homology (BH) 3-only" members of pro-apoptotic proteins, truncated BID (tBID) has been implicated in direct BAX activation, although an explicit molecular mechanism remains elusive. tBID 89-93 BCL2 apoptosis regulator Homo sapiens 11-16 17005564-0 2006 tBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formation. tBID 0-4 BCL2 apoptosis regulator Homo sapiens 59-64 17005564-3 2006 tBid also activates anti-apoptotic Bcl-2 in the mitochondrial outer membrane, changing it from a single-spanning to a multispanning conformation that binds the active Bax and inhibits cytochrome c release. tBID 0-4 BCL2 apoptosis regulator Homo sapiens 35-40 17005564-4 2006 However, it is not known whether other mitochondrial proteins are required to elicit the tBid-induced Bcl-2 conformational alteration. tBID 89-93 BCL2 apoptosis regulator Homo sapiens 102-107 17005564-6 2006 We found that purified tBid was sufficient to induce a conformational alteration in the liposome-tethered, but not cytosolic Bcl-2, resulting in a multispanning form that is similar to the one found in the mitochondrial outer membrane of drug-treated cells. tBID 23-27 BCL2 apoptosis regulator Homo sapiens 125-130 17005564-7 2006 Mutations that abolished tBid/Bcl-2 interaction also abolished the conformational alteration, demonstrating that a direct tBid/Bcl-2 interaction at the membrane is both required and sufficient to elicit the conformational alteration. tBID 25-29 BCL2 apoptosis regulator Homo sapiens 127-132 17005564-7 2006 Mutations that abolished tBid/Bcl-2 interaction also abolished the conformational alteration, demonstrating that a direct tBid/Bcl-2 interaction at the membrane is both required and sufficient to elicit the conformational alteration. tBID 122-126 BCL2 apoptosis regulator Homo sapiens 30-35 17005564-7 2006 Mutations that abolished tBid/Bcl-2 interaction also abolished the conformational alteration, demonstrating that a direct tBid/Bcl-2 interaction at the membrane is both required and sufficient to elicit the conformational alteration. tBID 122-126 BCL2 apoptosis regulator Homo sapiens 127-132 17005564-10 2006 Thus, there is a strong correlation between the direct interaction of membrane-bound Bcl-2 and tBid with activation of Bcl-2 in vitro and in vivo. tBID 95-99 BCL2 apoptosis regulator Homo sapiens 85-90 17005564-10 2006 Thus, there is a strong correlation between the direct interaction of membrane-bound Bcl-2 and tBid with activation of Bcl-2 in vitro and in vivo. tBID 95-99 BCL2 apoptosis regulator Homo sapiens 119-124 16485030-8 2006 Steady state tBid mitochondrial localization was prohibited by activation of the MAPK pathway, also when the Bcl-2 homology domain 3 (BH3) domain of tBid was disrupted. tBID 13-17 BCL2 apoptosis regulator Homo sapiens 109-114 16485030-8 2006 Steady state tBid mitochondrial localization was prohibited by activation of the MAPK pathway, also when the Bcl-2 homology domain 3 (BH3) domain of tBid was disrupted. tBID 149-153 BCL2 apoptosis regulator Homo sapiens 109-114 16642033-3 2006 In transfected cells and isolated mitochondria, Bcl-2, but not the inactive point mutants Bcl-2-G145A and Bcl-2-V159D, undergoes a conformation change in the mitochondrial membrane in response to apoptotic agonists such as tBid and Bax. tBID 223-227 BCL2 apoptosis regulator Homo sapiens 48-53 16642033-5 2006 Thus, Bcl-2 must change the conformation to inhibit tBid-induced oligomerization of integral membrane Bax monomers and small oligomers. tBID 52-56 BCL2 apoptosis regulator Homo sapiens 6-11 16380381-3 2006 Here, we have identified the anti-apoptotic Bcl-2 family member Mcl-1 as a potent tBid-binding partner. tBID 82-86 BCL2 apoptosis regulator Homo sapiens 44-49 16380381-4 2006 Site-directed mutagenesis reveals that the Bcl-2 homology (BH)3 domain of tBid is essential for binding to Mcl-1, whereas all three BH domains (BH1, BH2, and BH3) of Mcl-1 are required for interaction with tBid. tBID 74-78 BCL2 apoptosis regulator Homo sapiens 43-48 16380381-4 2006 Site-directed mutagenesis reveals that the Bcl-2 homology (BH)3 domain of tBid is essential for binding to Mcl-1, whereas all three BH domains (BH1, BH2, and BH3) of Mcl-1 are required for interaction with tBid. tBID 206-210 BCL2 apoptosis regulator Homo sapiens 43-48 15846373-5 2005 Overexpression of Bcl-2, which is able to interact with CPT-1, counteracts the effects exerted by tBid on beta-oxidation. tBID 98-102 BCL2 apoptosis regulator Homo sapiens 18-23 16167175-2 2005 Bcl-2 inhibition of apoptosis is mediated by its binding to pro-apoptotic proteins, e.g., Bax and tBid, inhibition of their oligomerization, and thus inhibition of mitochondrial outer membrane pore formation, through which other pro-apoptotic proteins, e.g., cytochrome c, are released to the cytosol. tBID 98-102 BCL2 apoptosis regulator Homo sapiens 0-5 15324812-5 2004 These compounds represent the first antiapoptotic small molecules targeting a Bcl-2 protein as shown by their ability to inhibit tBid-induced SMAC release, caspase-3 activation, and cell death. tBID 129-133 BCL2 apoptosis regulator Homo sapiens 78-83 15148322-5 2004 p15 tBid is potently apoptotic and activates the multidomain Bcl-2 protein, Bax, resulting in release of cytochrome c from mitochondria. tBID 4-8 BCL2 apoptosis regulator Homo sapiens 61-66 15138279-1 2004 BCL-2 homology 3 (BH3)-only proteins of the BCL-2 family such as tBID and BIM(EL) assist BAX-type proteins to breach the permeability barrier of the outer mitochondrial membrane, thereby allowing cytoplasmic release of cytochrome c and other active inducers of cell death normally confined to the mitochondrial inter-membrane space. tBID 65-69 BCL2 apoptosis regulator Homo sapiens 0-5 15138279-1 2004 BCL-2 homology 3 (BH3)-only proteins of the BCL-2 family such as tBID and BIM(EL) assist BAX-type proteins to breach the permeability barrier of the outer mitochondrial membrane, thereby allowing cytoplasmic release of cytochrome c and other active inducers of cell death normally confined to the mitochondrial inter-membrane space. tBID 65-69 BCL2 apoptosis regulator Homo sapiens 44-49 15123718-1 2004 The proapoptotic Bcl-2 family protein Bid is cleaved by caspase-8 to release the C-terminal fragment tBid, which translocates to the outer mitochondrial membrane and induces massive cytochrome c release and cell death. tBID 101-105 BCL2 apoptosis regulator Homo sapiens 17-22 14701745-4 2004 Here we show that growth factor deprivation induced proteolytic cleavage of the proapoptotic Bcl-2 family member BID to yield its active truncated form, tBID. tBID 153-157 BCL2 apoptosis regulator Homo sapiens 93-98 12721291-6 2003 This mechanism of inhibition by BCL-2 also occurs in intact cells stimulated with Fas or expressing tBID. tBID 100-104 BCL2 apoptosis regulator Homo sapiens 32-37 12721291-8 2003 This model suggests that the primary mechanism for BCL-2 blockade targets activated BAK rather than sequestering tBID. tBID 113-117 BCL2 apoptosis regulator Homo sapiens 51-56 12624108-10 2003 Alkaline treatment stripped off tBid from the membrane-bound organellar fraction of Bid plus Bcl-2-co-transfected cells, but not from cells transfected with only Bid, suggesting inhibition of tBid insertion into mitochondrial membranes by Bcl-2. tBID 32-36 BCL2 apoptosis regulator Homo sapiens 93-98 12624108-14 2003 Critical steps blocked by Bcl-2 included tBid insertion, Bax translocation, and Bax/Bak oligomerization in the mitochondrial membranes. tBID 41-45 BCL2 apoptosis regulator Homo sapiens 26-31 11326099-2 2001 tBID, the caspase-activated form of a "BH3-domain-only" BCL-2 family member, triggers the homooligomerization of "multidomain" conserved proapoptotic family members BAK or BAX, resulting in the release of cytochrome c from mitochondria. tBID 0-4 BCL2 apoptosis regulator Homo sapiens 56-61 11716782-0 2001 The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites. tBID 38-42 BCL2 apoptosis regulator Homo sapiens 18-23 11716782-9 2001 These findings link these sites with cardiolipin in tBid targeting and suggest a role for Bcl-2 family members in regulating the activity of contact sites in relation to apoptosis. tBID 52-56 BCL2 apoptosis regulator Homo sapiens 90-95 34931711-0 2022 BCL-2-family protein tBID can act as a BAX-like effector of apoptosis. tBID 21-25 BCL2 apoptosis regulator Homo sapiens 0-5 34931711-1 2022 During apoptosis, the BCL-2-family protein tBID promotes mitochondrial permeabilization by activating BAX and BAK and by blocking anti-apoptotic BCL-2 members. tBID 43-47 BCL2 apoptosis regulator Homo sapiens 145-150 34931711-3 2022 This previously unrecognized activity of tBID depends on helix 6, homologous to the pore-forming regions of BAX and BAK, and can be blocked by pro-survival BCL-2 proteins. tBID 41-45 BCL2 apoptosis regulator Homo sapiens 156-161 34931711-6 2022 Our findings define tBID as an effector of mitochondrial permeabilization in apoptosis and provide a new paradigm for BCL-2 proteins, with implications for anti-bacterial immunity and cancer therapy. tBID 20-24 BCL2 apoptosis regulator Homo sapiens 118-123 34361006-4 2021 Here we focus on the interaction between two core Bcl-2 family members, the executor pore-forming protein Bax and the truncated form of the activator protein Bid (tBid), which we imaged at the single particle level in a mitochondria-like planar supported lipid bilayer. tBID 163-167 BCL2 apoptosis regulator Homo sapiens 50-55 35336786-5 2022 Although the BCL-2 proteins are controlled by a complex regulatory network, a specific mechanism for the inhibition of tBID remained unknown. tBID 119-123 BCL2 apoptosis regulator Homo sapiens 13-18 35336786-8 2022 In contrast to general apoptosis inhibition by anti-apoptotic BCL-2 proteins, hexokinase I and hexokinase 2 specifically inhibit tBID and thus the mitochondrial apoptosis pathway in response to death receptor signaling. tBID 129-133 BCL2 apoptosis regulator Homo sapiens 62-67 30017071-2 2018 Bid and its caspase-8 cleavage product, tBid, promote the permeabilization of the mitochondrial outer membrane and sequester antiapoptotic Bcl-2 proteins to counter their cytoprotective activity. tBID 40-44 BCL2 apoptosis regulator Homo sapiens 139-144 30017071-6 2018 Lipoparticle-bound tBid retains an alpha-helical structure and binds Bcl-xL through its third Bcl-2 homology motif, forming a soluble, lipid-associated heteroprotein complex. tBID 19-23 BCL2 apoptosis regulator Homo sapiens 94-99 28026162-2 2017 Members of the antiapoptotic Bcl-2 proteins, including Bcl-2, Mcl-1, Bcl-xL, Bcl-w, and Bfl-1, inhibit apoptosis by selectively binding to conserved alpha-helical regions, named BH3 domains, of pro-apoptotic proteins such as Bim, tBid, Bad, or NOXA. tBID 230-234 BCL2 apoptosis regulator Homo sapiens 29-34 28026162-2 2017 Members of the antiapoptotic Bcl-2 proteins, including Bcl-2, Mcl-1, Bcl-xL, Bcl-w, and Bfl-1, inhibit apoptosis by selectively binding to conserved alpha-helical regions, named BH3 domains, of pro-apoptotic proteins such as Bim, tBid, Bad, or NOXA. tBID 230-234 BCL2 apoptosis regulator Homo sapiens 55-60 25288797-3 2014 This process requires the BH3-only activator protein (i.e. tBid) and can be inhibited by anti-apoptotic Bcl-2 family proteins such as Bcl-xL. tBID 59-63 BCL2 apoptosis regulator Homo sapiens 104-109 23893415-9 2013 Mutagenesis of the alpha6 helix disrupted apoptotic function because a chimera of Bak with the alpha6 derived from Bcl-2 could be activated by truncated Bid (tBid) and could form BH3:groove homodimers but could not form high molecular weight oligomers or mediate cell death. tBID 158-162 BCL2 apoptosis regulator Homo sapiens 115-120 22895112-7 2012 Furthermore, we show that mutation of a conserved residue in the BH3 region in Bad and tBid disrupted their interactions with Bcl-XL and Bcl-2, while the corresponding BimEL mutant showed no decrease in binding to these anti-apoptotic proteins. tBID 87-91 BCL2 apoptosis regulator Homo sapiens 137-142 22994712-8 2012 Truncated-Bid (tBid) translocated to mitochondria and activated the mitochondrial pathway in conjunction with down-regulation of Bcl-2 protein expression. tBID 15-19 BCL2 apoptosis regulator Homo sapiens 129-134 22454688-3 2012 Both intracellular and mitochondrial reactive oxygen species were increased to lead to alterations of mitochondrial membrane permeability and Bcl-2 family including upregulation of Bid, tBid, and Bax and downregulation of Bcl-2. tBID 186-190 BCL2 apoptosis regulator Homo sapiens 142-147 22036586-2 2011 We employed chimeric proteins composed of exogenous BH3 domains inserted into a tBID backbone that can activate the proapoptotic effectors BAX and BAK to permeabilize membranes without being universally sequestered by all antiapoptotic BCL-2 proteins. tBID 80-84 BCL2 apoptosis regulator Homo sapiens 236-241 21459798-8 2011 By comparison, overexpression of Bcl-2, which simultaneously antagonizes tBid and p53, significantly inhibits bortezomib- and TRAIL-induced apoptosis and even rescues clonogenic survival. tBID 73-77 BCL2 apoptosis regulator Homo sapiens 33-38 21439939-7 2011 The antiapoptotic activity of M11 was suppressed by coexpression of proapoptotic BH3-only protein tBid, indicating that M11 inhibits apoptosis likely by the same mechanism as cellular antiapoptotic proteins Bcl-2 or Bcl-XL. tBID 98-102 BCL2 apoptosis regulator Homo sapiens 207-212 21130780-4 2011 The work presented here considers the incorporation of BAD and its various modifications in a model of the tBID-induction of BAK (Bcl-2 homologous antagonist killer) or the tBID-induction of BAX (Bcl-2-associated X protein). tBID 107-111 BCL2 apoptosis regulator Homo sapiens 130-135 21130780-5 2011 Steady state equations are used to develop an explicit formula describing the total concentration level of tBID, guaranteed to trigger apoptosis, as a bilinear function of the total BAD concentration level and the total anti-apoptotic protein concentration level (usually Bcl-2 or Bcl-xL). tBID 107-111 BCL2 apoptosis regulator Homo sapiens 272-277 21130780-6 2011 In particular, the formula explains how the pro-apoptotic protein BAD lowers the threshold at which tBID induces BAK/BAX activation-reducing the level of total Bcl-2/Bcl-xL available to inhibit tBID signaling in the mitochondria. tBID 100-104 BCL2 apoptosis regulator Homo sapiens 160-165 21130780-6 2011 In particular, the formula explains how the pro-apoptotic protein BAD lowers the threshold at which tBID induces BAK/BAX activation-reducing the level of total Bcl-2/Bcl-xL available to inhibit tBID signaling in the mitochondria. tBID 194-198 BCL2 apoptosis regulator Homo sapiens 160-165 20168333-5 2010 Nevertheless, simultaneous disruption of the p38 MAPK pathway was required to suppress MCL-1 expression, thereby allowing tBID to activate the proapoptotic BCL-2 family member BAK and stimulate mitochondrial outer membrane permeabilization (MOMP). tBID 122-126 BCL2 apoptosis regulator Homo sapiens 156-161