PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
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
34528939-0	2021	Bcl-xL inhibits tBid and Bax via distinct mechanisms.	tBID	16-20	BCL2 like 1	Homo sapiens	0-6
34528939-4	2021	Here, we combined quantitative analysis of the interactions and the localization dynamics of the family representatives Bcl-xL, Bax and tBid, in living cells.	tBID	136-140	BCL2 like 1	Homo sapiens	120-126
34528939-6	2021	Bcl-xL clearly stabilized tBid at mitochondria, where they formed tight complexes.	tBID	26-30	BCL2 like 1	Homo sapiens	0-6
34263972-7	2021	Cathepsins in the cytosol cleaved Bid to generate tBid, which subsequently activated Bax to induce mitochondrial outer membrane permeabilization (MOMP).	tBID	50-54	BH3 interacting domain death agonist	Homo sapiens	34-37
34263972-7	2021	Cathepsins in the cytosol cleaved Bid to generate tBid, which subsequently activated Bax to induce mitochondrial outer membrane permeabilization (MOMP).	tBID	50-54	BCL2 associated X, apoptosis regulator	Homo sapiens	85-88
34988150-4	2021	Methods: We incorporated the pro-apoptotic truncated BH3 interacting-domain death agonist (tBID) with the mutant ecDHFR destabilizing domain to form a novel recombinant protein as the major component of an engineered tBID-based safety switch system, which would be unstable and quickly degraded in the absence of trimethoprim (TMP) but, upon TMP treatment, should become stabilized and allow tBID to induce cell death experimentally.	tBID	91-95	BH3 interacting domain death agonist	Homo sapiens	53-89
34988150-4	2021	Methods: We incorporated the pro-apoptotic truncated BH3 interacting-domain death agonist (tBID) with the mutant ecDHFR destabilizing domain to form a novel recombinant protein as the major component of an engineered tBID-based safety switch system, which would be unstable and quickly degraded in the absence of trimethoprim (TMP) but, upon TMP treatment, should become stabilized and allow tBID to induce cell death experimentally.	tBID	217-221	BH3 interacting domain death agonist	Homo sapiens	53-89
34988150-4	2021	Methods: We incorporated the pro-apoptotic truncated BH3 interacting-domain death agonist (tBID) with the mutant ecDHFR destabilizing domain to form a novel recombinant protein as the major component of an engineered tBID-based safety switch system, which would be unstable and quickly degraded in the absence of trimethoprim (TMP) but, upon TMP treatment, should become stabilized and allow tBID to induce cell death experimentally.	tBID	392-396	BH3 interacting domain death agonist	Homo sapiens	53-89
34831043-8	2021	Our findings suggest that Bad is required for (PCD) control, exerting a p53 stress signal on caspase-8/tBid-mediated death signaling and brain development-related gene regulation.	tBID	103-107	tumor protein p53	Danio rerio	72-75
34831043-8	2021	Our findings suggest that Bad is required for (PCD) control, exerting a p53 stress signal on caspase-8/tBid-mediated death signaling and brain development-related gene regulation.	tBID	103-107	caspase 8, apoptosis-related cysteine peptidase	Danio rerio	93-102
34361006-0	2021	Direct Measurement of the Affinity between tBid and Bax in a Mitochondria-Like Membrane.	tBID	43-47	BCL2 associated X, apoptosis regulator	Homo sapiens	52-55
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
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 associated X, apoptosis regulator	Homo sapiens	106-109
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	BH3 interacting domain death agonist	Homo sapiens	158-161
34361006-7	2021	We conclude by proposing an updated molecular model for the activation of Bax by tBid.	tBID	81-85	BCL2 associated X, apoptosis regulator	Homo sapiens	74-77
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
34931711-0	2022	BCL-2-family protein tBID can act as a BAX-like effector of apoptosis.	tBID	21-25	BCL2 associated X, apoptosis regulator	Homo sapiens	39-42
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 associated X, apoptosis regulator	Homo sapiens	102-105
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 antagonist/killer 1	Homo sapiens	110-113
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
34931711-2	2022	Here, we report that tBID can also mediate mitochondrial permeabilization by itself, resulting in release of cytochrome c and mitochondrial DNA, caspase activation and apoptosis even in absence of BAX and BAK.	tBID	21-25	cytochrome c, somatic	Homo sapiens	109-121
34931711-2	2022	Here, we report that tBID can also mediate mitochondrial permeabilization by itself, resulting in release of cytochrome c and mitochondrial DNA, caspase activation and apoptosis even in absence of BAX and BAK.	tBID	21-25	BCL2 associated X, apoptosis regulator	Homo sapiens	197-200
34931711-2	2022	Here, we report that tBID can also mediate mitochondrial permeabilization by itself, resulting in release of cytochrome c and mitochondrial DNA, caspase activation and apoptosis even in absence of BAX and BAK.	tBID	21-25	BCL2 antagonist/killer 1	Homo sapiens	205-208
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 associated X, apoptosis regulator	Homo sapiens	108-111
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 antagonist/killer 1	Homo sapiens	116-119
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
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
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	hexokinase 1	Homo sapiens	78-90
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	hexokinase 2	Homo sapiens	95-107
33843148-0	2021	Evaluating the inhibitory priority of Bcl-xL to Bad, tBid and Bax by using live-cell imaging assay.	tBID	53-57	BCL2 like 1	Homo sapiens	38-44
33843148-3	2021	Based on over-expression model system, we here evaluate the inhibitory priority of Bcl-xL to Bad, tBid and Bax by using live-cell imaging assay on cell viability.	tBID	98-102	BCL2 like 1	Homo sapiens	83-89
33843148-5	2021	In the case of equimolar co-expression of Bad and CFP-Bcl-xL, the inhibition of Bcl-xL on tBid/Bax mediate-apoptosis was completely relieved.	tBID	90-94	complement factor properdin	Homo sapiens	50-53
33843148-5	2021	In the case of equimolar co-expression of Bad and CFP-Bcl-xL, the inhibition of Bcl-xL on tBid/Bax mediate-apoptosis was completely relieved.	tBID	90-94	BCL2 like 1	Homo sapiens	54-60
33843148-5	2021	In the case of equimolar co-expression of Bad and CFP-Bcl-xL, the inhibition of Bcl-xL on tBid/Bax mediate-apoptosis was completely relieved.	tBID	90-94	BCL2 like 1	Homo sapiens	80-86
33843148-5	2021	In the case of equimolar co-expression of Bad and CFP-Bcl-xL, the inhibition of Bcl-xL on tBid/Bax mediate-apoptosis was completely relieved.	tBID	90-94	BCL2 associated X, apoptosis regulator	Homo sapiens	95-98
33843148-6	2021	Moreover, co-expression of tBid-P2A-CFP-Bcl-xL significantly relieved the inhibition of Bcl-xL on the pro-apoptotic ability Bax, suggesting that Bcl-xL preferentially inhibits the pro-apoptotic ability of Bad over tBid, subsequently to Bax.	tBID	27-31	complement factor properdin	Homo sapiens	36-39
33843148-6	2021	Moreover, co-expression of tBid-P2A-CFP-Bcl-xL significantly relieved the inhibition of Bcl-xL on the pro-apoptotic ability Bax, suggesting that Bcl-xL preferentially inhibits the pro-apoptotic ability of Bad over tBid, subsequently to Bax.	tBID	27-31	BCL2 like 1	Homo sapiens	40-46
33843148-6	2021	Moreover, co-expression of tBid-P2A-CFP-Bcl-xL significantly relieved the inhibition of Bcl-xL on the pro-apoptotic ability Bax, suggesting that Bcl-xL preferentially inhibits the pro-apoptotic ability of Bad over tBid, subsequently to Bax.	tBID	27-31	BCL2 like 1	Homo sapiens	88-94
33843148-6	2021	Moreover, co-expression of tBid-P2A-CFP-Bcl-xL significantly relieved the inhibition of Bcl-xL on the pro-apoptotic ability Bax, suggesting that Bcl-xL preferentially inhibits the pro-apoptotic ability of Bad over tBid, subsequently to Bax.	tBID	27-31	BCL2 associated X, apoptosis regulator	Homo sapiens	124-127
33843148-6	2021	Moreover, co-expression of tBid-P2A-CFP-Bcl-xL significantly relieved the inhibition of Bcl-xL on the pro-apoptotic ability Bax, suggesting that Bcl-xL preferentially inhibits the pro-apoptotic ability of Bad over tBid, subsequently to Bax.	tBID	27-31	BCL2 like 1	Homo sapiens	88-94
33843148-6	2021	Moreover, co-expression of tBid-P2A-CFP-Bcl-xL significantly relieved the inhibition of Bcl-xL on the pro-apoptotic ability Bax, suggesting that Bcl-xL preferentially inhibits the pro-apoptotic ability of Bad over tBid, subsequently to Bax.	tBID	27-31	BCL2 associated X, apoptosis regulator	Homo sapiens	236-239
31492967-7	2020	In cytosol of apoptotic cells, Bcl-xL associates with Bax to form hetero-trimer with 1:2 stoichiometry, while Bcl-xL associates with Bad to form hetero-trimer with 2:1 stoichiometry and Bcl-xL associates with tBid to form hetero-dimer.	tBID	209-213	BCL2 like 1	Homo sapiens	110-116
33614474-0	2020	ClC-5 Downregulation Induces Osteosarcoma Cell Apoptosis by Promoting Bax and tBid Complex Formation.	tBID	78-82	chloride voltage-gated channel 5	Homo sapiens	0-5
33614474-10	2020	Immunoprecipitation showed that ClC-5 interacted with Bax and ClC-5 downregulation enhanced Bax and tBid complex formation.	tBID	100-104	chloride voltage-gated channel 5	Homo sapiens	32-37
33614474-10	2020	Immunoprecipitation showed that ClC-5 interacted with Bax and ClC-5 downregulation enhanced Bax and tBid complex formation.	tBID	100-104	BCL2 associated X, apoptosis regulator	Homo sapiens	54-57
33614474-10	2020	Immunoprecipitation showed that ClC-5 interacted with Bax and ClC-5 downregulation enhanced Bax and tBid complex formation.	tBID	100-104	chloride voltage-gated channel 5	Homo sapiens	62-67
33614474-11	2020	Collectively, we demonstrate that ClC-5 downregulation induces osteosarcoma cell apoptosis via mitochondria-dependent apoptotic pathway activation by promoting Bax and tBid association and subsequent Bax translocation.	tBID	168-172	chloride voltage-gated channel 5	Homo sapiens	34-39
32984322-6	2020	The dephosphorylation led to an increased level of the antiapoptotic cis ATR (ATR-H) in the cytoplasm and, thus, its accumulation at mitochondria via binding with tBid.	tBID	163-167	ATR serine/threonine kinase	Homo sapiens	73-76
32984322-6	2020	The dephosphorylation led to an increased level of the antiapoptotic cis ATR (ATR-H) in the cytoplasm and, thus, its accumulation at mitochondria via binding with tBid.	tBID	163-167	ATR serine/threonine kinase	Homo sapiens	78-83
31492967-2	2020	Based on over-expression model system, FRET analysis was used to quantify the protein-protein interactions among Bax, Bcl-xL, Bad and tBid in healthy and apoptotic cells.	tBID	134-138	BCL2 associated X, apoptosis regulator	Homo sapiens	113-116
31492967-5	2020	Bcl-xL binds preferentially to Bad, then to tBid and Bax in mitochondria, whilst Bcl-xL displays higher affinity to Bad or tBid than to itself.	tBID	44-48	BCL2 like 1	Homo sapiens	0-6
31492967-5	2020	Bcl-xL binds preferentially to Bad, then to tBid and Bax in mitochondria, whilst Bcl-xL displays higher affinity to Bad or tBid than to itself.	tBID	123-127	BCL2 like 1	Homo sapiens	81-87
32835867-6	2020	Indeed, the sequential CTSC silencing and curcumin treatment also significantly curtailed tumor volume as well as ameliorated cytosolic cyt c and tBID protein levels in tumor tissues compared to those in control and individual treatments of CTSC targeting and on curcumin treatment in nude mice xenografts.	tBID	146-150	cathepsin C	Mus musculus	23-27
32126227-8	2020	In addition, by a direct comparison with its lipid symmetrical counterpart it is shown that asymmetric models were more resistant to tBid-promoted Bax-permeabilization, suggesting a role played by MOM lipid asymmetry on the mitochondria pathway of apoptosis.	tBID	133-137	BCL2 associated X, apoptosis regulator	Homo sapiens	147-150
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	56-60	BCL2 antagonist/killer 1	Homo sapiens	42-45
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	56-60	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	87-92
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	56-60	BCL2 antagonist/killer 1	Homo sapiens	98-101
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	56-60	BCL2 binding component 3	Homo sapiens	102-106
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	56-60	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	87-92
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	56-60	BCL2 antagonist/killer 1	Homo sapiens	98-101
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	56-60	BCL2 binding component 3	Homo sapiens	102-106
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	112-116	complement factor properdin	Homo sapiens	24-27
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	112-116	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	28-33
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	112-116	BCL2 antagonist/killer 1	Homo sapiens	42-45
32430171-2	2020	The cells co-expressing CFP-Mcl-1 and YFP-Bak/BimL/Puma/tBid showed co-localization of Mcl-1 with Bak/Puma/BimL/tBid and also showed the inhibitory action of Mcl-1 on the Bak-, BimL-, Puma- or tBid-mediated cell death.	tBID	112-116	BCL2 binding component 3	Homo sapiens	51-55
32430171-4	2020	Fluorescence resonance energy transfer (FRET) imaging proved the direct binding of Mcl-1 to Bak, BimL, Puma and tBid, respectively.	tBID	112-116	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	83-88
31492967-7	2020	In cytosol of apoptotic cells, Bcl-xL associates with Bax to form hetero-trimer with 1:2 stoichiometry, while Bcl-xL associates with Bad to form hetero-trimer with 2:1 stoichiometry and Bcl-xL associates with tBid to form hetero-dimer.	tBID	209-213	BCL2 like 1	Homo sapiens	110-116
32426354-9	2020	The cis-ATR, containing an exposed BH3 domain, is anti-apoptotic at mitochondria by binding to tBid, preventing activation of pro-apoptotic Bax.	tBID	95-99	ATR serine/threonine kinase	Homo sapiens	8-11
32345661-5	2020	tBid-induced mitochondrial outer membrane permeabilization was also required to drive SMAC release and relieve inhibitor of apoptosis protein inhibition of caspase-3, thereby allowing caspase-3 auto-processing to the fully active p17/p12 form.	tBID	0-4	diablo IAP-binding mitochondrial protein	Homo sapiens	86-90
32345661-5	2020	tBid-induced mitochondrial outer membrane permeabilization was also required to drive SMAC release and relieve inhibitor of apoptosis protein inhibition of caspase-3, thereby allowing caspase-3 auto-processing to the fully active p17/p12 form.	tBID	0-4	DNA polymerase epsilon 4, accessory subunit	Homo sapiens	234-237
32345661-5	2020	tBid-induced mitochondrial outer membrane permeabilization was also required to drive SMAC release and relieve inhibitor of apoptosis protein inhibition of caspase-3, thereby allowing caspase-3 auto-processing to the fully active p17/p12 form.	tBID	0-4	caspase 3	Homo sapiens	156-165
32345661-5	2020	tBid-induced mitochondrial outer membrane permeabilization was also required to drive SMAC release and relieve inhibitor of apoptosis protein inhibition of caspase-3, thereby allowing caspase-3 auto-processing to the fully active p17/p12 form.	tBID	0-4	caspase 3	Homo sapiens	184-193
32345661-5	2020	tBid-induced mitochondrial outer membrane permeabilization was also required to drive SMAC release and relieve inhibitor of apoptosis protein inhibition of caspase-3, thereby allowing caspase-3 auto-processing to the fully active p17/p12 form.	tBID	0-4	DNA polymerase epsilon 3, accessory subunit	Homo sapiens	230-233
30889542-5	2019	Lysosomal distribution of tBid stimulates cytosolic cathepsin B resulting accumulation of truncated-AIF with induction in scramblase mediated phosphatidylserine exposure in HepG2CR cells.	tBID	26-30	cathepsin B	Homo sapiens	52-63
31558028-4	2019	During the initiation phase of self-assembly, the two central hydrophobic helices (alpha6 and alpha7) of tBid insert halfway into the phospholipid core, while the other helices remain on the surface.	tBID	105-109	immunoglobulin kappa variable 3D-25 (pseudogene)	Homo sapiens	83-100
31558028-5	2019	In oligomerized tBid clusters, alpha6 and alpha7 prefer to float up, and the other helices may sink to the bottom of the membrane and cause the formation of transient two-dimensional, micelle-like pore structures, which are responsible for the permeabilization of membranes and the induction of apoptosis.	tBID	16-20	immunoglobulin kappa variable 3D-25 (pseudogene)	Homo sapiens	31-48
31302316-14	2019	Feq3 also up-regulated tBid, which interacts with the mitochondrial pathway and tumor necrosis factor-alpha (TNF-alpha)/TNF-Rs, FasL/Fas, and TNF-related apoptosis inducing ligand receptors (TRAIL-Rs)/TRAIL-dependent caspases apoptotic signaling pathway in HNSCC cells.	tBID	23-27	tumor necrosis factor	Homo sapiens	80-107
31302316-14	2019	Feq3 also up-regulated tBid, which interacts with the mitochondrial pathway and tumor necrosis factor-alpha (TNF-alpha)/TNF-Rs, FasL/Fas, and TNF-related apoptosis inducing ligand receptors (TRAIL-Rs)/TRAIL-dependent caspases apoptotic signaling pathway in HNSCC cells.	tBID	23-27	Fas ligand	Homo sapiens	128-132
31302316-14	2019	Feq3 also up-regulated tBid, which interacts with the mitochondrial pathway and tumor necrosis factor-alpha (TNF-alpha)/TNF-Rs, FasL/Fas, and TNF-related apoptosis inducing ligand receptors (TRAIL-Rs)/TRAIL-dependent caspases apoptotic signaling pathway in HNSCC cells.	tBID	23-27	TNF superfamily member 10	Homo sapiens	191-196
31302316-14	2019	Feq3 also up-regulated tBid, which interacts with the mitochondrial pathway and tumor necrosis factor-alpha (TNF-alpha)/TNF-Rs, FasL/Fas, and TNF-related apoptosis inducing ligand receptors (TRAIL-Rs)/TRAIL-dependent caspases apoptotic signaling pathway in HNSCC cells.	tBID	23-27	TNF superfamily member 10	Homo sapiens	201-206
30982575-3	2019	In this study, we report that adenovirus-mediated ectopic overexpression of EMC6 (Ad5-EMC6) in BGC823 and SGC7901 gastric cancer cells decreases the activity of ERK1/2, down-regulates the levels of BCL-2 protein and phosphorylated BCL-2, increases the expression of tBID and BAX, and decreases mitochondrial membrane potential and subsequently leading to cell apoptosis.	tBID	266-270	ER membrane protein complex subunit 6	Homo sapiens	76-80
30982575-3	2019	In this study, we report that adenovirus-mediated ectopic overexpression of EMC6 (Ad5-EMC6) in BGC823 and SGC7901 gastric cancer cells decreases the activity of ERK1/2, down-regulates the levels of BCL-2 protein and phosphorylated BCL-2, increases the expression of tBID and BAX, and decreases mitochondrial membrane potential and subsequently leading to cell apoptosis.	tBID	266-270	ER membrane protein complex subunit 6	Homo sapiens	82-90
30810413-0	2019	Polyethyleneimine-polyethylene glycol copolymer targeted by anti-HER2 nanobody for specific delivery of transcriptionally targeted tBid containing construct.	tBID	131-135	erb-b2 receptor tyrosine kinase 2	Homo sapiens	65-69
31250646-9	2019	Astrakurkurol persuaded the expression of death receptor associated proteins (Fas), which triggered caspase-8 activation following tBid cleavage.	tBID	131-135	caspase 8	Homo sapiens	100-109
30889542-5	2019	Lysosomal distribution of tBid stimulates cytosolic cathepsin B resulting accumulation of truncated-AIF with induction in scramblase mediated phosphatidylserine exposure in HepG2CR cells.	tBID	26-30	apoptosis inducing factor mitochondria associated 1	Homo sapiens	100-103
30536001-8	2019	Here, we describe in detail the permeabilization of liposomes induced by the interaction between BAX and BH3-only activator tBID.	tBID	124-128	BCL2 associated X, apoptosis regulator	Homo sapiens	97-100
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	BH3 interacting domain death agonist	Homo sapiens	0-3
29876988-5	2018	Consistently, Tan I cleaved poly (adenosine diphosphate-ribose) polymerase (PARP) and caspase-8, caspase-3, attenuated the expression of Bid and activated tBid as a caspase-8 substrate and activated phosphorylation of p38 MAPK in HCT116and HT29 cells.	tBID	155-159	poly(ADP-ribose) polymerase 1	Homo sapiens	76-80
29876988-5	2018	Consistently, Tan I cleaved poly (adenosine diphosphate-ribose) polymerase (PARP) and caspase-8, caspase-3, attenuated the expression of Bid and activated tBid as a caspase-8 substrate and activated phosphorylation of p38 MAPK in HCT116and HT29 cells.	tBID	155-159	caspase 8	Homo sapiens	86-95
29876988-5	2018	Consistently, Tan I cleaved poly (adenosine diphosphate-ribose) polymerase (PARP) and caspase-8, caspase-3, attenuated the expression of Bid and activated tBid as a caspase-8 substrate and activated phosphorylation of p38 MAPK in HCT116and HT29 cells.	tBID	155-159	caspase 8	Homo sapiens	165-174
30179292-5	2018	Ectopic expression of LGP2 in NB cells significantly enhanced poly (I:C)-induced NB cell death associated with downregulation of MDA5, RIG-I, MAVS and Bcl-2, as well as upregulation of Noxa and tBid.	tBID	194-198	DExH-box helicase 58	Homo sapiens	22-26
30385739-5	2018	We therefore hypothesised that improving caspase-8 activation or sensitising mitochondria to truncated Bid (tBid) could convert non-responder GBM cell lines to responders.	tBID	108-112	BH3 interacting domain death agonist	Homo sapiens	103-106
30035337-9	2018	Using pharmacologic inhibitors, we also find that PN-PDT activates caspase-8/tBid and p38-MAPK, triggering the activation of the apoptotic pathways.	tBID	77-81	caspase 8	Homo sapiens	67-76
30301883-8	2018	By contrast, prolonged EtOH exposure promoted tBid-induced outer mitochondrial membrane permeabilization and cell death only in HepG2 cells, owing to enhanced Bak oligomerization.	tBID	46-50	BCL2 antagonist/killer 1	Homo sapiens	159-162
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	caspase 8	Homo sapiens	12-21
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
30017071-4	2018	Here, we show that tBid is capable of associating with phospholipids to form soluble, nanometer-sized lipoprotein particles that retain binding affinity for the antiapoptotic protein Bcl-xL.	tBID	19-23	BCL2 like 1	Homo sapiens	183-189
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 like 1	Homo sapiens	69-75
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
29567940-5	2018	Systems modeling of the tBid-Bax interplay and their fluxes between cytosol and mitochondrial membranes reproduced experimental data on tBid-triggered Bax activation and oligomerization highly accurately.	tBID	24-28	BCL2 associated X, apoptosis regulator	Homo sapiens	29-32
29706657-8	2018	Deprivation of these mitochondrial safeguards licensed DR-generated truncated BH3-interacting domain death agonist (tBID) to activate BCL-2-associated X protein (BAX) and initiated mitochondrial outer membrane permeabilization (MOMP).	tBID	116-120	BCL2 associated X, apoptosis regulator	Homo sapiens	134-160
29706657-8	2018	Deprivation of these mitochondrial safeguards licensed DR-generated truncated BH3-interacting domain death agonist (tBID) to activate BCL-2-associated X protein (BAX) and initiated mitochondrial outer membrane permeabilization (MOMP).	tBID	116-120	BCL2 associated X, apoptosis regulator	Homo sapiens	162-165
29265109-4	2018	By using single-molecule fluorescence and Forster resonance energy transfer techniques, we showed that Bax was mainly present as monomers, dimers and tetramers in lipid bilayers, while truncated Bid (tBid) enhanced the membrane association and tetramerization of Bax.	tBID	200-204	BH3 interacting domain death agonist	Homo sapiens	195-198
29265109-4	2018	By using single-molecule fluorescence and Forster resonance energy transfer techniques, we showed that Bax was mainly present as monomers, dimers and tetramers in lipid bilayers, while truncated Bid (tBid) enhanced the membrane association and tetramerization of Bax.	tBID	200-204	BCL2 associated X, apoptosis regulator	Homo sapiens	263-266
29265109-5	2018	HN (100 nmol/L) inhibited the self-association and tBid-activated association of Bax with the bilayers, and significantly decreased the proportion of Bax in tetramers.	tBID	51-55	BCL2 associated X, apoptosis regulator	Homo sapiens	81-84
29265109-10	2018	Meanwhile, HN interacts with the membrane-bound Bax and tBid, preventing the recruitment of cytosolic Bax and its oligomerization in the membrane.	tBID	56-60	BCL2 associated X, apoptosis regulator	Homo sapiens	102-105
29022237-8	2018	Moderate release of CTSB cleaves Bax-like BH3 protein (Bid) to become active truncated Bid (tBid).	tBID	92-96	cathepsin B	Homo sapiens	20-24
29022237-8	2018	Moderate release of CTSB cleaves Bax-like BH3 protein (Bid) to become active truncated Bid (tBid).	tBID	92-96	BH3 interacting domain death agonist	Homo sapiens	87-90
29022237-9	2018	Active tBid is then translocated to the mitochondrial outer membrane, resulting in oligomerization of BCL2-associated X protein (Bax) forming the mitochondrial outer membrane pores, and releasing mitochondrial intramembranous proteins.	tBID	7-11	BCL2 associated X, apoptosis regulator	Homo sapiens	102-127
29022237-9	2018	Active tBid is then translocated to the mitochondrial outer membrane, resulting in oligomerization of BCL2-associated X protein (Bax) forming the mitochondrial outer membrane pores, and releasing mitochondrial intramembranous proteins.	tBID	7-11	BCL2 associated X, apoptosis regulator	Homo sapiens	129-132
29567940-5	2018	Systems modeling of the tBid-Bax interplay and their fluxes between cytosol and mitochondrial membranes reproduced experimental data on tBid-triggered Bax activation and oligomerization highly accurately.	tBID	24-28	BCL2 associated X, apoptosis regulator	Homo sapiens	151-154
29567940-5	2018	Systems modeling of the tBid-Bax interplay and their fluxes between cytosol and mitochondrial membranes reproduced experimental data on tBid-triggered Bax activation and oligomerization highly accurately.	tBID	136-140	BCL2 associated X, apoptosis regulator	Homo sapiens	29-32
29567940-5	2018	Systems modeling of the tBid-Bax interplay and their fluxes between cytosol and mitochondrial membranes reproduced experimental data on tBid-triggered Bax activation and oligomerization highly accurately.	tBID	136-140	BCL2 associated X, apoptosis regulator	Homo sapiens	151-154
29407584-6	2018	Apoptosis correlated with a decrease of phospho-ERK1/2, the accumulation of Bim and translocation of truncated Bid (tBid) and jBid.	tBID	116-120	BH3 interacting domain death agonist	Homo sapiens	111-114
29167312-7	2018	Investigations into the underlying molecular mechanisms reveal that bortezomib and ketoconazole act in concert to cause the accumulation of truncated Bid (tBid).	tBID	155-159	BH3 interacting domain death agonist	Homo sapiens	150-153
29193479-5	2017	BCL-XL also traps tBID, a proapoptotic activator BH3-only protein, and sequesters p53.	tBID	18-22	BCL2 like 1	Homo sapiens	0-6
30246563-6	2018	Gene expression analysis showed a significant rise in the expression of tBid in both MDA-MB-231/HER2+ and MDA-MB-231 compared to the two other cell lines.	tBID	72-76	erb-b2 receptor tyrosine kinase 2	Homo sapiens	96-100
28888620-7	2017	In a cell-free reconstitution system, caspase-8-mediated Bid cleavage and recombinant tBid induced mitochondrial cytochrome c release and ROS generation, which were blocked by Bcl-xL and antioxidant enzymes.	tBID	86-90	cytochrome c, somatic	Homo sapiens	113-125
28888620-5	2017	Moreover, Bid knockdown abrogated TNF-alpha- or TRAIL-induced ROS generation, whereas overexpression of truncated Bid (tBid) or knockdown of cytochrome c spontaneously elevated ROS production.	tBID	119-123	BH3 interacting domain death agonist	Homo sapiens	114-117
28888620-7	2017	In a cell-free reconstitution system, caspase-8-mediated Bid cleavage and recombinant tBid induced mitochondrial cytochrome c release and ROS generation, which were blocked by Bcl-xL and antioxidant enzymes.	tBID	86-90	BCL2 like 1	Homo sapiens	176-182
29039326-6	2017	The two flavonoids activated caspase-8, which cleaved Bid into tBid; simultaneously, Bax transferred from cytosol into mitochondria to decrease MMP; consequentially, cytochrome c released from mitochondria activated caspase-9, and then caspase-9 activated caspase-3, which executed the apoptosis.	tBID	63-67	caspase 8	Homo sapiens	29-38
28529067-3	2017	Here we designed a dual-target therapeutic system in which MSCs were engineered to produce and deliver scFv-Fdt-tBid, a novel gamma-SM-targeted immunoproapoptotic molecule.	tBID	112-116	immunglobulin heavy chain variable region	Homo sapiens	103-107
28529067-3	2017	Here we designed a dual-target therapeutic system in which MSCs were engineered to produce and deliver scFv-Fdt-tBid, a novel gamma-SM-targeted immunoproapoptotic molecule.	tBID	112-116	kallikrein related peptidase 3	Homo sapiens	126-134
28529067-4	2017	Such engineered MSCs (MSC.scFv-Fdt-tBid) would home to tumor sites and release the fusion protein to induce the apoptosis of prostate cancer cells.	tBID	35-39	immunglobulin heavy chain variable region	Homo sapiens	26-30
28529067-6	2017	Importantly, MSC.scFv-Fdt-tBid caused cell death through an apoptosis-dependent manner.	tBID	26-30	immunglobulin heavy chain variable region	Homo sapiens	17-21
28529067-8	2017	Finally, the in vivo experiments demonstrated that MSC.scFv-Fdt-tBid significantly inhibited gamma-SM-positive tumor growth without toxic side effects.	tBID	64-68	immunglobulin heavy chain variable region	Homo sapiens	55-59
28529067-8	2017	Finally, the in vivo experiments demonstrated that MSC.scFv-Fdt-tBid significantly inhibited gamma-SM-positive tumor growth without toxic side effects.	tBID	64-68	kallikrein related peptidase 3	Homo sapiens	93-101
28529067-9	2017	Collectively, this study represented a novel immunoproapoptotic molecule scFv-Fdt-tBid for gamma-SM-positive tumors and demonstrated the therapeutic efficiency and safety of scFv-Fdt-tBid-modified MSCs against prostate cancers.	tBID	82-86	immunglobulin heavy chain variable region	Homo sapiens	73-77
28529067-9	2017	Collectively, this study represented a novel immunoproapoptotic molecule scFv-Fdt-tBid for gamma-SM-positive tumors and demonstrated the therapeutic efficiency and safety of scFv-Fdt-tBid-modified MSCs against prostate cancers.	tBID	82-86	kallikrein related peptidase 3	Homo sapiens	91-99
28529067-9	2017	Collectively, this study represented a novel immunoproapoptotic molecule scFv-Fdt-tBid for gamma-SM-positive tumors and demonstrated the therapeutic efficiency and safety of scFv-Fdt-tBid-modified MSCs against prostate cancers.	tBID	82-86	immunglobulin heavy chain variable region	Homo sapiens	174-178
28529067-9	2017	Collectively, this study represented a novel immunoproapoptotic molecule scFv-Fdt-tBid for gamma-SM-positive tumors and demonstrated the therapeutic efficiency and safety of scFv-Fdt-tBid-modified MSCs against prostate cancers.	tBID	183-187	immunglobulin heavy chain variable region	Homo sapiens	73-77
28529067-9	2017	Collectively, this study represented a novel immunoproapoptotic molecule scFv-Fdt-tBid for gamma-SM-positive tumors and demonstrated the therapeutic efficiency and safety of scFv-Fdt-tBid-modified MSCs against prostate cancers.	tBID	183-187	kallikrein related peptidase 3	Homo sapiens	91-99
28529067-9	2017	Collectively, this study represented a novel immunoproapoptotic molecule scFv-Fdt-tBid for gamma-SM-positive tumors and demonstrated the therapeutic efficiency and safety of scFv-Fdt-tBid-modified MSCs against prostate cancers.	tBID	183-187	immunglobulin heavy chain variable region	Homo sapiens	174-178
28337703-4	2017	Combination of UMI-77 and TRAIL in glioma cells led to the activation of caspase-8 and Bid, cleavage of caspase-3 and poly-ADP ribose polymerase (PARP), accumulation of tBid in the mitochondria and release of cytochrome c into the cytosol.	tBID	169-173	TNF superfamily member 10	Homo sapiens	26-31
29039326-6	2017	The two flavonoids activated caspase-8, which cleaved Bid into tBid; simultaneously, Bax transferred from cytosol into mitochondria to decrease MMP; consequentially, cytochrome c released from mitochondria activated caspase-9, and then caspase-9 activated caspase-3, which executed the apoptosis.	tBID	63-67	BH3 interacting domain death agonist	Homo sapiens	54-57
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
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
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	prominin 1	Mus musculus	169-174
27760587-6	2017	The results demonstrated that the coinfection of Ad-CD133-Cre and Ad-CMV-LoxP-Neo-LoxP-tBid significantly increased tBid expression in CD133+ ovarian CSCs.	tBID	87-91	prominin 1	Mus musculus	135-140
27760587-6	2017	The results demonstrated that the coinfection of Ad-CD133-Cre and Ad-CMV-LoxP-Neo-LoxP-tBid significantly increased tBid expression in CD133+ ovarian CSCs.	tBID	116-120	prominin 1	Mus musculus	52-57
27760587-6	2017	The results demonstrated that the coinfection of Ad-CD133-Cre and Ad-CMV-LoxP-Neo-LoxP-tBid significantly increased tBid expression in CD133+ ovarian CSCs.	tBID	116-120	prominin 1	Mus musculus	135-140
27760587-7	2017	Moreover, the tBid overexpression induced by a recombinant adenovirus Cre/loxP system dramatically inhibited cell proliferation and invasion, significantly elevated cell apoptosis, and activated the mitochondrial apoptosis pathway in CD133+ ovarian CSCs.	tBID	14-18	prominin 1	Mus musculus	234-239
27760587-8	2017	Additionally, recombinant adenovirus Cre/loxP system-mediated tBid overexpression suppressed the tumorigenic potential of CD133+ ovarian CSCs in a xenograft mouse model.	tBID	62-66	prominin 1	Mus musculus	122-127
27760587-9	2017	In conclusion, our study successfully constructed a recombinant adenovirus Cre/loxP system and induced tBid overexpression in CD133+ ovarian CSCs, providing a new therapeutic approach for ovarian cancer treatment.	tBID	103-107	prominin 1	Mus musculus	126-131
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
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	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	62-67
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 like 1	Homo sapiens	69-75
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 like 2	Homo sapiens	77-82
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 related protein A1	Homo sapiens	88-93
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	phorbol-12-myristate-13-acetate-induced protein 1	Homo sapiens	244-248
28004114-7	2017	The knockdown of miR-20a inhibited the translocation of tBID to the mitochondria, which induced the mitochondrial pathway of apoptosis.	tBID	56-60	microRNA 20a	Homo sapiens	17-24
27878291-7	2017	The co-infection of Ad-CMV-LoxP-Neo-LoxP-tBid and Ad-CD133-Cre selectively induced tBid overexpression, which inhibited cell growth and triggered the cell apoptosis of CD133+ ovarian cancer stem cells.	tBID	41-45	prominin 1	Homo sapiens	168-173
28004114-8	2017	Notably, we found that the knockdown of miR-20a also reversed the resistance of TRAIL in established TRAIL-resistant SW480 cells by tBID-mitochondria pathway.	tBID	132-136	microRNA 20a	Homo sapiens	40-47
27878291-7	2017	The co-infection of Ad-CMV-LoxP-Neo-LoxP-tBid and Ad-CD133-Cre selectively induced tBid overexpression, which inhibited cell growth and triggered the cell apoptosis of CD133+ ovarian cancer stem cells.	tBID	83-87	prominin 1	Homo sapiens	53-58
27878291-7	2017	The co-infection of Ad-CMV-LoxP-Neo-LoxP-tBid and Ad-CD133-Cre selectively induced tBid overexpression, which inhibited cell growth and triggered the cell apoptosis of CD133+ ovarian cancer stem cells.	tBID	83-87	prominin 1	Homo sapiens	168-173
28004114-8	2017	Notably, we found that the knockdown of miR-20a also reversed the resistance of TRAIL in established TRAIL-resistant SW480 cells by tBID-mitochondria pathway.	tBID	132-136	TNF superfamily member 10	Homo sapiens	80-85
27878291-8	2017	The Cre/LoxP system-mediated tBid overexpression activated the pro-apoptotic signaling pathway and augmented the cytotoxic effect of cisplatin in CD133+ ovarian cancer stem cells.	tBID	29-33	prominin 1	Homo sapiens	146-151
27878291-10	2017	Taken together, the present study provides evidence that the adenovirus-mediated tBid overexpression induced by the Cre/LoxP system can effectively eliminate CD133+ ovarian cancer stem cells, representing a novel therapeutic strategy for the treatment of ovarian cancer.	tBID	81-85	prominin 1	Homo sapiens	158-163
28004114-8	2017	Notably, we found that the knockdown of miR-20a also reversed the resistance of TRAIL in established TRAIL-resistant SW480 cells by tBID-mitochondria pathway.	tBID	132-136	TNF superfamily member 10	Homo sapiens	101-106
26794447-2	2016	BH3-only proteins such as tBID, together with lipids of the MOM, are thought to play a key role in BAX and BAK activation.	tBID	26-30	BCL2 associated X, apoptosis regulator	Homo sapiens	99-102
27716614-2	2016	Earlier studies showed that the lysosomal aspartic protease Cathepsin D (CtsD) cleaves Bid to tBid, resulting in the amplification of the initial apoptotic cascade via mitochondrial outer membrane permeabilization (MOMP).The goal of this study was to identify further targets for CtsD that might be involved in activation upon death receptor ligation.	tBID	94-98	cathepsin D	Homo sapiens	60-71
27716614-2	2016	Earlier studies showed that the lysosomal aspartic protease Cathepsin D (CtsD) cleaves Bid to tBid, resulting in the amplification of the initial apoptotic cascade via mitochondrial outer membrane permeabilization (MOMP).The goal of this study was to identify further targets for CtsD that might be involved in activation upon death receptor ligation.	tBID	94-98	cathepsin D	Homo sapiens	73-77
27716614-2	2016	Earlier studies showed that the lysosomal aspartic protease Cathepsin D (CtsD) cleaves Bid to tBid, resulting in the amplification of the initial apoptotic cascade via mitochondrial outer membrane permeabilization (MOMP).The goal of this study was to identify further targets for CtsD that might be involved in activation upon death receptor ligation.	tBID	94-98	BH3 interacting domain death agonist	Homo sapiens	87-90
27716614-2	2016	Earlier studies showed that the lysosomal aspartic protease Cathepsin D (CtsD) cleaves Bid to tBid, resulting in the amplification of the initial apoptotic cascade via mitochondrial outer membrane permeabilization (MOMP).The goal of this study was to identify further targets for CtsD that might be involved in activation upon death receptor ligation.	tBID	94-98	cathepsin D	Homo sapiens	280-284
26794447-3	2016	In particular, cardiolipin (CL) has been shown to stimulate tBID-induced BAX activation in vitro.	tBID	60-64	BCL2 associated X, apoptosis regulator	Homo sapiens	73-76
26794447-4	2016	However, it is still unclear whether this process also relies on CL in the cell, or whether it is more dependent on MTCH2, a proposed receptor for tBID present in the MOM.	tBID	147-151	mitochondrial carrier 2	Homo sapiens	116-121
26794447-9	2016	However, when both CL and MTCH2 were depleted, a significant reduction in tBID recruitment was observed, suggesting that in HCT116 cells, CL and MTCH2 can have redundant functions in this process.	tBID	74-78	mitochondrial carrier 2	Homo sapiens	26-31
26794447-9	2016	However, when both CL and MTCH2 were depleted, a significant reduction in tBID recruitment was observed, suggesting that in HCT116 cells, CL and MTCH2 can have redundant functions in this process.	tBID	74-78	mitochondrial carrier 2	Homo sapiens	145-150
27120618-6	2016	The Cat B inhibitor (leu) and Cat D inhibitor (pepA) inhibited Rh2-O-induced HepG2 apoptosis as well as tBid production and Deltaphim depolarization, indicating that lysosomal permeabilization occurred upstream of mitochondrial dysfunction.	tBID	104-108	carnosine dipeptidase 2	Homo sapiens	47-51
26943324-3	2016	We observed that apoptotic cell death induced by expression of the truncated form of BH3 interacting-domain death agonist (tBid) and a constitutively active form of caspase 3 (revC3), respectively, showed higher immunogenicity than cell death induced by expression of the tuberculosis-necrotizing toxin (TNT).	tBID	123-127	caspase 3	Homo sapiens	165-174
27053107-7	2016	By generating Bid/Bax/Bak-deficient (TKO) cells, we demonstrated that Bid is primarily cleaved by caspase 8, not by effector caspases, to give rise to truncated Bid (tBid) upon TRAIL treatment.	tBID	166-170	BH3 interacting domain death agonist	Homo sapiens	70-73
27053107-7	2016	By generating Bid/Bax/Bak-deficient (TKO) cells, we demonstrated that Bid is primarily cleaved by caspase 8, not by effector caspases, to give rise to truncated Bid (tBid) upon TRAIL treatment.	tBID	166-170	caspase 8	Homo sapiens	98-107
27053107-7	2016	By generating Bid/Bax/Bak-deficient (TKO) cells, we demonstrated that Bid is primarily cleaved by caspase 8, not by effector caspases, to give rise to truncated Bid (tBid) upon TRAIL treatment.	tBID	166-170	BH3 interacting domain death agonist	Homo sapiens	70-73
27053107-7	2016	By generating Bid/Bax/Bak-deficient (TKO) cells, we demonstrated that Bid is primarily cleaved by caspase 8, not by effector caspases, to give rise to truncated Bid (tBid) upon TRAIL treatment.	tBID	166-170	TNF superfamily member 10	Homo sapiens	177-182
26674343-6	2016	Further, a high degree of ILz(6):TRAIL multimerization triggered rapid signaling events such as activation of caspases, tBid generation, and chromatin condensation.	tBID	120-124	TNF superfamily member 10	Homo sapiens	33-38
27320914-0	2016	MOAP-1 Mediates Fas-Induced Apoptosis in Liver by Facilitating tBid Recruitment to Mitochondria.	tBID	63-67	modulator of apoptosis 1	Mus musculus	0-6
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
27320914-4	2016	Subsequent tBid recruitment to mitochondria, which is facilitated by its receptor MTCH2 at the outer mitochondrial membrane (OMM), is a critical step for commitment to apoptosis via the effector proteins Bax or Bak.	tBID	11-15	mitochondrial carrier 2	Mus musculus	82-87
27320914-4	2016	Subsequent tBid recruitment to mitochondria, which is facilitated by its receptor MTCH2 at the outer mitochondrial membrane (OMM), is a critical step for commitment to apoptosis via the effector proteins Bax or Bak.	tBID	11-15	BCL2-associated X protein	Mus musculus	204-207
27320914-4	2016	Subsequent tBid recruitment to mitochondria, which is facilitated by its receptor MTCH2 at the outer mitochondrial membrane (OMM), is a critical step for commitment to apoptosis via the effector proteins Bax or Bak.	tBID	11-15	BCL2-antagonist/killer 1	Mus musculus	211-214
27320914-7	2016	In the absence of MOAP-1, mitochondrial accumulation of tBid is markedly impaired.	tBID	56-60	modulator of apoptosis 1	Mus musculus	18-24
27320914-8	2016	MOAP-1 binds to MTCH2, and this interaction appears necessary for MTCH2 to engage tBid.	tBID	82-86	modulator of apoptosis 1	Mus musculus	0-6
27320914-8	2016	MOAP-1 binds to MTCH2, and this interaction appears necessary for MTCH2 to engage tBid.	tBID	82-86	mitochondrial carrier 2	Mus musculus	66-71
27320914-9	2016	These findings reveal a role for MOAP-1 in Fas signaling in the liver by promoting MTCH2-mediated tBid recruitment to mitochondria.	tBID	98-102	modulator of apoptosis 1	Mus musculus	33-39
27320914-9	2016	These findings reveal a role for MOAP-1 in Fas signaling in the liver by promoting MTCH2-mediated tBid recruitment to mitochondria.	tBID	98-102	mitochondrial carrier 2	Mus musculus	83-88
26769704-6	2016	Moreover, the expression of tBid, DR5, and Fas proteins was enhanced by FBRA extract, and the pretreatment with caspase-8 inhibitor, but not caspase-9 inhibitor, restored the reduction of the cell viability induced by FBRA extract.	tBID	28-32	caspase 8	Homo sapiens	112-121
26699404-4	2016	Based on apparently contradictory experimental evidence, two distinct molecular mechanisms have been proposed to underlie the propagation of MOMP signals, namely a reaction-diffusion mechanism governed by anisotropies in the production of the MOMP-inducer truncated Bid (tBid), or a process that drives the spatial propagation of MOMP by sequential bursts of reactive oxygen species.	tBID	271-275	BH3 interacting domain death agonist	Homo sapiens	266-269
26854628-7	2016	Upon H2O2-induced apoptosis, the association of EndoII with Bax were significantly decreased, while the interaction of Bax/tBid were increased, accompanied by a translocation of Bax from cytosol to mitochondria.	tBID	123-127	BCL2 associated X, apoptosis regulator	Rattus norvegicus	119-122
26854628-7	2016	Upon H2O2-induced apoptosis, the association of EndoII with Bax were significantly decreased, while the interaction of Bax/tBid were increased, accompanied by a translocation of Bax from cytosol to mitochondria.	tBID	123-127	BCL2 associated X, apoptosis regulator	Rattus norvegicus	119-122
26854628-8	2016	Knockdown of EndoII did not affect the expression of Bax, but further promoted the binding of Bax with tBid and favored the accumulation of Bax to mitochondria as well as Bax activation; whereas EndoII overexpression produced the opposite effects.	tBID	103-107	SH3 domain containing GRB2 like 1, endophilin A2	Rattus norvegicus	13-19
26854628-8	2016	Knockdown of EndoII did not affect the expression of Bax, but further promoted the binding of Bax with tBid and favored the accumulation of Bax to mitochondria as well as Bax activation; whereas EndoII overexpression produced the opposite effects.	tBID	103-107	BCL2 associated X, apoptosis regulator	Rattus norvegicus	94-97
26854628-8	2016	Knockdown of EndoII did not affect the expression of Bax, but further promoted the binding of Bax with tBid and favored the accumulation of Bax to mitochondria as well as Bax activation; whereas EndoII overexpression produced the opposite effects.	tBID	103-107	BCL2 associated X, apoptosis regulator	Rattus norvegicus	94-97
26854628-8	2016	Knockdown of EndoII did not affect the expression of Bax, but further promoted the binding of Bax with tBid and favored the accumulation of Bax to mitochondria as well as Bax activation; whereas EndoII overexpression produced the opposite effects.	tBID	103-107	BCL2 associated X, apoptosis regulator	Rattus norvegicus	94-97
26417093-4	2015	Recently, a specific V2 requirement was demonstrated for mitochondrial Bak import and truncated Bid (tBid)-induced apoptosis.	tBID	101-105	BH3 interacting domain death agonist	Homo sapiens	96-99
26223015-8	2015	Cathepsin B process BID to active tBID which induces the release of cytochrome C from mitochondria.	tBID	34-38	cathepsin B	Homo sapiens	0-11
26223015-8	2015	Cathepsin B process BID to active tBID which induces the release of cytochrome C from mitochondria.	tBID	34-38	BH3 interacting domain death agonist	Homo sapiens	20-23
26223015-8	2015	Cathepsin B process BID to active tBID which induces the release of cytochrome C from mitochondria.	tBID	34-38	cytochrome c, somatic	Homo sapiens	68-80
27509965-9	2016	There was an increased expression of truncated Bid (tBid), which indicated caspase8 proteolysis activity in Bid cleavage as its substrate in the extrinsic pathway.	tBID	52-56	BH3 interacting domain death agonist	Homo sapiens	47-50
27509965-9	2016	There was an increased expression of truncated Bid (tBid), which indicated caspase8 proteolysis activity in Bid cleavage as its substrate in the extrinsic pathway.	tBID	52-56	caspase 8	Homo sapiens	75-83
26417093-0	2015	Motifs of VDAC2 required for mitochondrial Bak import and tBid-induced apoptosis.	tBID	58-62	voltage-dependent anion channel 2	Mus musculus	10-15
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	BCL2 binding component 3	Mus musculus	9-13
26387736-4	2015	ATR contains a BH3-like domain that allows ATR-tBid interaction at mitochondria, suppressing cytochrome c release and apoptosis.	tBID	47-51	ATR serine/threonine kinase	Homo sapiens	0-3
26387736-4	2015	ATR contains a BH3-like domain that allows ATR-tBid interaction at mitochondria, suppressing cytochrome c release and apoptosis.	tBID	47-51	ATR serine/threonine kinase	Homo sapiens	43-46
26387736-4	2015	ATR contains a BH3-like domain that allows ATR-tBid interaction at mitochondria, suppressing cytochrome c release and apoptosis.	tBID	47-51	cytochrome c, somatic	Homo sapiens	93-105
25714678-0	2015	Distinct lipid effects on tBid and Bim activation of membrane permeabilization by pro-apoptotic Bax.	tBID	26-30	BCL2 associated X, apoptosis regulator	Homo sapiens	96-99
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	68-72	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	75-80
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	68-72	BCL2 antagonist/killer 1	Homo sapiens	83-86
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	68-72	BCL2 like 1	Homo sapiens	120-126
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	68-72	BCL2 associated X, apoptosis regulator	Homo sapiens	129-132
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	113-117	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	75-80
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	113-117	BCL2 antagonist/killer 1	Homo sapiens	83-86
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	113-117	BCL2 like 1	Homo sapiens	120-126
26231047-6	2015	RESULTS: We show that regulation of bilayer permeabilization by the tBid - Mcl-1 - Bak axis closely resemblesthe tBid - Bcl-XL - Bax model.	tBID	113-117	BCL2 associated X, apoptosis regulator	Homo sapiens	129-132
26231047-9	2015	A 2.5 molar excess of obatoclax relative to Mcl-1 overcame Mcl-1-mediated inhibition of tBid-Bak activation.	tBID	88-92	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	44-49
26231047-9	2015	A 2.5 molar excess of obatoclax relative to Mcl-1 overcame Mcl-1-mediated inhibition of tBid-Bak activation.	tBID	88-92	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	59-64
26231047-9	2015	A 2.5 molar excess of obatoclax relative to Mcl-1 overcame Mcl-1-mediated inhibition of tBid-Bak activation.	tBID	88-92	BCL2 antagonist/killer 1	Homo sapiens	93-96
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	caspase 8	Mus musculus	143-152
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
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	BCL2-associated X protein	Mus musculus	194-197
25623406-5	2015	ELISA analyses were also made of Bax:tBid heterodimers, a process which activates Bax, essential for its apoptotic functioning.	tBID	37-41	BCL2 associated X, apoptosis regulator	Rattus norvegicus	33-36
25633293-12	2015	BAX mediated the release of mitochondrial cytochrome c, activation of caspase-3 and cell death partially through the lysosome-cathepsin B-tBid pathway.	tBID	138-142	BCL2 associated X, apoptosis regulator	Homo sapiens	0-3
25633293-12	2015	BAX mediated the release of mitochondrial cytochrome c, activation of caspase-3 and cell death partially through the lysosome-cathepsin B-tBid pathway.	tBID	138-142	cathepsin B	Homo sapiens	126-137
26097873-7	2015	The sorafenib-increased cathepsin B activity induced the proteolysis of Bid into tBid that stimulates the intrinsic pathway of apoptosis characterized by mitochondrial membrane depolarization, oxygen radical generation and cytochrome c release.	tBID	81-85	cathepsin B	Homo sapiens	24-35
26097873-7	2015	The sorafenib-increased cathepsin B activity induced the proteolysis of Bid into tBid that stimulates the intrinsic pathway of apoptosis characterized by mitochondrial membrane depolarization, oxygen radical generation and cytochrome c release.	tBID	81-85	BH3 interacting domain death agonist	Homo sapiens	72-75
26097873-7	2015	The sorafenib-increased cathepsin B activity induced the proteolysis of Bid into tBid that stimulates the intrinsic pathway of apoptosis characterized by mitochondrial membrane depolarization, oxygen radical generation and cytochrome c release.	tBID	81-85	cytochrome c, somatic	Homo sapiens	223-235
25623406-5	2015	ELISA analyses were also made of Bax:tBid heterodimers, a process which activates Bax, essential for its apoptotic functioning.	tBID	37-41	BCL2 associated X, apoptosis regulator	Rattus norvegicus	82-85
25623406-9	2015	Bax:tBid heterodimers were markedly increased by EtOH exposure on P4, an increase which persisted even 2 hours after termination of treatment.	tBID	4-8	BCL2 associated X, apoptosis regulator	Rattus norvegicus	0-3
25233093-8	2014	Besides, TNFalpha was released in this hyperglycemic condition, which in turn activated caspase 8, cleaved Bid to tBid and finally the mitochorndia-dependent apoptotic pathway.	tBID	114-118	tumor necrosis factor	Rattus norvegicus	9-17
25233093-8	2014	Besides, TNFalpha was released in this hyperglycemic condition, which in turn activated caspase 8, cleaved Bid to tBid and finally the mitochorndia-dependent apoptotic pathway.	tBID	114-118	BH3 interacting domain death agonist	Rattus norvegicus	107-110
24616078-9	2014	These results suggest that inhibition of the cysteine cathepsin B and cathepsin L activation in ischemic astrocytes contributes to neuroprotection via blocking the tBid-mitochondrial apoptotic signaling pathway.	tBID	164-168	cathepsin B	Rattus norvegicus	54-65
25077544-2	2014	Its function in apoptosis is associated with the proteolytic cleavage to the truncated form tBid, mainly by caspase-8.	tBID	92-96	caspase 8	Homo sapiens	108-117
25077544-3	2014	tBid translocates to mitochondria and assists Bax and Bak in induction of apoptosis.	tBID	0-4	BCL2 associated X, apoptosis regulator	Homo sapiens	46-49
25077544-3	2014	tBid translocates to mitochondria and assists Bax and Bak in induction of apoptosis.	tBID	0-4	BCL2 antagonist/killer 1	Homo sapiens	54-57
24616078-0	2014	Inhibition of cysteine cathepsin B and L activation in astrocytes contributes to neuroprotection against cerebral ischemia via blocking the tBid-mitochondrial apoptotic signaling pathway.	tBID	140-144	cathepsin B	Rattus norvegicus	23-34
24616078-2	2014	Here, we test the hypothesis that activation of cathepsin B and L contributes to the ischemic astrocyte injury via the tBid-mitochondrial apoptotic signaling pathways.	tBID	119-123	cathepsin B	Rattus norvegicus	48-59
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
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 like 1	Homo sapiens	134-140
25288797-7	2014	The activated Bax triggered by tBid or BH3 domain peptide integrates on bilayers and tends to form tetramers, which are termed as pre-pore.	tBID	31-35	BCL2 associated X, apoptosis regulator	Homo sapiens	14-17
24973666-6	2014	Cordycepin-induced cell death was also associated with induction of Fas and death receptor 5, activation of caspase-8, and truncation of Bid (tBid), suggesting that tBid might serve to connect activation of both the mitochondrial-mediated intrinsic and death receptor-mediated extrinsic apoptotic pathways.	tBID	165-169	BH3 interacting domain death agonist	Homo sapiens	137-140
24726886-0	2014	Therapeutic efficacy of improved alpha-fetoprotein promoter-mediated tBid delivered by folate-PEI600-cyclodextrin nanopolymer vector in hepatocellular carcinoma.	tBID	69-73	alpha fetoprotein	Homo sapiens	33-50
24726886-4	2014	EA4D was fused with tBid and coupled with nano-particle vector (H1) to form pGL3-EA4D-tBid/H1.	tBID	86-90	succinate dehydrogenase complex subunit C	Homo sapiens	76-80
24726886-5	2014	pGL3-EA4D-tBid/H1 could express a high level of tBid while retain the specificity to AFP-producing cells.	tBID	10-14	succinate dehydrogenase complex subunit C	Homo sapiens	0-4
24726886-5	2014	pGL3-EA4D-tBid/H1 could express a high level of tBid while retain the specificity to AFP-producing cells.	tBID	10-14	alpha fetoprotein	Homo sapiens	85-88
24726886-5	2014	pGL3-EA4D-tBid/H1 could express a high level of tBid while retain the specificity to AFP-producing cells.	tBID	48-52	succinate dehydrogenase complex subunit C	Homo sapiens	0-4
24726886-6	2014	In a HCC tumor model, application of pGL3-EA4D-tBid/H1 significantly inhibited the growth of AFP-producing-implanted tumors with minimal side-effects, but had no effect on non-AFP-producing tumors.	tBID	47-51	succinate dehydrogenase complex subunit C	Homo sapiens	37-41
24726886-6	2014	In a HCC tumor model, application of pGL3-EA4D-tBid/H1 significantly inhibited the growth of AFP-producing-implanted tumors with minimal side-effects, but had no effect on non-AFP-producing tumors.	tBID	47-51	alpha fetoprotein	Homo sapiens	93-96
24901048-0	2014	Multiple partners can kiss-and-run: Bax transfers between multiple membranes and permeabilizes those primed by tBid.	tBID	111-115	BCL2 associated X, apoptosis regulator	Homo sapiens	36-39
24901048-3	2014	Binding to membranes is regulated by cleavage of Bid to truncated Bid (tBid), by conformation changes in tBid and Bax, and by interactions with other proteins.	tBID	71-75	BH3 interacting domain death agonist	Homo sapiens	49-52
24901048-3	2014	Binding to membranes is regulated by cleavage of Bid to truncated Bid (tBid), by conformation changes in tBid and Bax, and by interactions with other proteins.	tBID	71-75	BH3 interacting domain death agonist	Homo sapiens	66-69
24901048-10	2014	In the case of tBid, the process of transfer is synergetic with Bax in the sense that tBid "runs" faster if it has been "kissed" by Bax.	tBID	15-19	BCL2 associated X, apoptosis regulator	Homo sapiens	64-67
24901048-10	2014	In the case of tBid, the process of transfer is synergetic with Bax in the sense that tBid "runs" faster if it has been "kissed" by Bax.	tBID	15-19	BCL2 associated X, apoptosis regulator	Homo sapiens	132-135
24901048-10	2014	In the case of tBid, the process of transfer is synergetic with Bax in the sense that tBid "runs" faster if it has been "kissed" by Bax.	tBID	86-90	BCL2 associated X, apoptosis regulator	Homo sapiens	64-67
24901048-10	2014	In the case of tBid, the process of transfer is synergetic with Bax in the sense that tBid "runs" faster if it has been "kissed" by Bax.	tBID	86-90	BCL2 associated X, apoptosis regulator	Homo sapiens	132-135
24901048-11	2014	Furthermore, Mtch2 accelerates the re-localization of tBid at the mitochondria.	tBID	54-58	mitochondrial carrier 2	Homo sapiens	13-18
24901048-12	2014	In contrast, binding to Bcl-XL dramatically impedes tBid re-localization by lowering the off-rate threefold.	tBID	52-56	BCL2 like 1	Homo sapiens	24-30
24853737-2	2014	Here, we characterized the interaction of fluorescently labeled truncated Bid (tBid) with a mitochondria-like supported lipid bilayer at the single-molecule level.	tBID	79-83	BH3 interacting domain death agonist	Homo sapiens	74-77
24616078-9	2014	These results suggest that inhibition of the cysteine cathepsin B and cathepsin L activation in ischemic astrocytes contributes to neuroprotection via blocking the tBid-mitochondrial apoptotic signaling pathway.	tBID	164-168	cathepsin L	Rattus norvegicus	70-81
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	BCL2 antagonist/killer 1	Homo sapiens	196-199
24333953-0	2014	Involvement of cardiolipin in tBID-induced activation of BAX during apoptosis.	tBID	30-34	BCL2 associated X, apoptosis regulator	Homo sapiens	57-60
24333953-4	2014	Cooperation between tBID and the mitochondrial-specific phospholipid cardiolipin has been suggested to promote BAX or BAK oligomerization.	tBID	20-24	BCL2 associated X, apoptosis regulator	Homo sapiens	111-114
24333953-4	2014	Cooperation between tBID and the mitochondrial-specific phospholipid cardiolipin has been suggested to promote BAX or BAK oligomerization.	tBID	20-24	BCL2 antagonist/killer 1	Homo sapiens	118-121
24586573-4	2014	One of these, TBID, displays toward HIPK2 unprecedented efficacy (IC50 = 0.33 microM) and selectivity (Gini coefficient 0.592 out of a panel of 76 kinases).	tBID	14-18	homeodomain interacting protein kinase 2	Homo sapiens	36-41
24586573-5	2014	The two other members of the HIPK family, HIPK1 and HIPK3, are also inhibited by TBID albeit less efficiently than HIPK2.	tBID	81-85	homeodomain interacting protein kinase 1	Homo sapiens	42-47
24586573-5	2014	The two other members of the HIPK family, HIPK1 and HIPK3, are also inhibited by TBID albeit less efficiently than HIPK2.	tBID	81-85	homeodomain interacting protein kinase 3	Homo sapiens	52-57
24586573-5	2014	The two other members of the HIPK family, HIPK1 and HIPK3, are also inhibited by TBID albeit less efficiently than HIPK2.	tBID	81-85	homeodomain interacting protein kinase 2	Homo sapiens	115-120
24586573-7	2014	We also provide evidence that TBID is cell permeable by showing that HIPK2 activity is reduced in cells treated with TBID, although with an IC50 two orders of magnitude higher (about 50 microM) than in vitro.	tBID	30-34	homeodomain interacting protein kinase 2	Homo sapiens	69-74
24586573-7	2014	We also provide evidence that TBID is cell permeable by showing that HIPK2 activity is reduced in cells treated with TBID, although with an IC50 two orders of magnitude higher (about 50 microM) than in vitro.	tBID	117-121	homeodomain interacting protein kinase 2	Homo sapiens	69-74
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	BCL2 associated X, apoptosis regulator	Homo sapiens	44-47
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	translocase of outer mitochondrial membrane 40	Homo sapiens	57-62
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	translocase of outer mitochondrial membrane 22	Homo sapiens	63-68
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	BCL2 associated X, apoptosis regulator	Homo sapiens	74-77
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	BCL2 associated X, apoptosis regulator	Homo sapiens	74-77
24464226-2	2014	Truncated Bid (tBid) induces Bax/Bak-dependent mitochondrial outer membrane permeability and the release of cytochrome c and Smac/Diablo.	tBID	15-19	BH3 interacting domain death agonist	Homo sapiens	10-13
24464226-2	2014	Truncated Bid (tBid) induces Bax/Bak-dependent mitochondrial outer membrane permeability and the release of cytochrome c and Smac/Diablo.	tBID	15-19	BCL2 associated X, apoptosis regulator	Homo sapiens	29-32
24464226-2	2014	Truncated Bid (tBid) induces Bax/Bak-dependent mitochondrial outer membrane permeability and the release of cytochrome c and Smac/Diablo.	tBID	15-19	BCL2 antagonist/killer 1	Homo sapiens	33-36
24464226-2	2014	Truncated Bid (tBid) induces Bax/Bak-dependent mitochondrial outer membrane permeability and the release of cytochrome c and Smac/Diablo.	tBID	15-19	cytochrome c, somatic	Homo sapiens	108-120
24464226-2	2014	Truncated Bid (tBid) induces Bax/Bak-dependent mitochondrial outer membrane permeability and the release of cytochrome c and Smac/Diablo.	tBID	15-19	diablo IAP-binding mitochondrial protein	Homo sapiens	125-129
24464226-2	2014	Truncated Bid (tBid) induces Bax/Bak-dependent mitochondrial outer membrane permeability and the release of cytochrome c and Smac/Diablo.	tBID	15-19	diablo IAP-binding mitochondrial protein	Homo sapiens	130-136
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	voltage dependent anion channel 2	Homo sapiens	209-214
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	69-73	BCL2 antagonist/killer 1	Homo sapiens	215-218
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	BCL2 associated X, apoptosis regulator	Homo sapiens	44-47
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	translocase of outer mitochondrial membrane 40	Homo sapiens	57-62
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	translocase of outer mitochondrial membrane 22	Homo sapiens	63-68
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	BCL2 associated X, apoptosis regulator	Homo sapiens	74-77
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	BCL2 associated X, apoptosis regulator	Homo sapiens	74-77
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	BCL2 antagonist/killer 1	Homo sapiens	196-199
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	voltage dependent anion channel 2	Homo sapiens	209-214
24269536-7	2014	Our simulations predict the displacement of Bax from the TOM40/TOM22/tBid/Bax complex by another Bax in auto-catalytic manner and explain, in terms of structure, the tBid-mediated displacement of Bak from the VDAC2/Bak complex.	tBID	166-170	BCL2 antagonist/killer 1	Homo sapiens	215-218
25292102-4	2014	Our findings indicated that IFN-gamma treatment caused a time-dependent reduction in cell viability and induced apoptosis through a FADD-mediated caspase-8/tBid/mitochondria-dependent pathway in both cell lines.	tBID	156-160	interferon gamma	Homo sapiens	28-37
25292102-4	2014	Our findings indicated that IFN-gamma treatment caused a time-dependent reduction in cell viability and induced apoptosis through a FADD-mediated caspase-8/tBid/mitochondria-dependent pathway in both cell lines.	tBID	156-160	Fas associated via death domain	Homo sapiens	132-136
25292102-4	2014	Our findings indicated that IFN-gamma treatment caused a time-dependent reduction in cell viability and induced apoptosis through a FADD-mediated caspase-8/tBid/mitochondria-dependent pathway in both cell lines.	tBID	156-160	caspase 8	Homo sapiens	146-155
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	37-41	arrestin beta 1	Homo sapiens	0-10
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	37-41	arrestin beta 1	Homo sapiens	76-86
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	37-41	cytochrome c, somatic	Homo sapiens	140-152
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	110-114	arrestin beta 1	Homo sapiens	0-10
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	110-114	arrestin beta 1	Homo sapiens	76-86
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	110-114	cytochrome c, somatic	Homo sapiens	140-152
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	110-114	arrestin beta 1	Homo sapiens	0-10
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	110-114	arrestin beta 1	Homo sapiens	76-86
24141717-10	2014	Arrestin-2-(1-380) action depends on tBID: at physiological concentrations, arrestin-2-(1-380) directly binds tBID and doubles tBID-induced cytochrome C release from isolated mitochondria.	tBID	110-114	cytochrome c, somatic	Homo sapiens	140-152
24141717-12	2014	Thus, arrestin-2-(1-380) cooperates with another product of caspase activity, tBID, and their concerted action significantly contributes to cell death.	tBID	78-82	arrestin beta 1	Homo sapiens	6-16
24158446-2	2013	One of the pro-apoptotic proteins, tBid, can induce apoptosis by promoting Bax activation, Bax homo-oligomerization, and mitochondrial outer membrane permeabilization.	tBID	35-39	BCL2 associated X, apoptosis regulator	Homo sapiens	75-78
24292837-6	2014	Generated fragment actively participates in the core mechanism of apoptosis: it assists another product of caspase activity, tBID, in releasing cytochrome C from mitochondria.	tBID	125-129	cytochrome c, somatic	Homo sapiens	144-156
24158446-2	2013	One of the pro-apoptotic proteins, tBid, can induce apoptosis by promoting Bax activation, Bax homo-oligomerization, and mitochondrial outer membrane permeabilization.	tBID	35-39	BCL2 associated X, apoptosis regulator	Homo sapiens	91-94
24158446-10	2013	Of note, the BH3-containing helix alpha3, which was previously believed to be exposed above the membrane surface, is also membrane associated, suggesting an "on the membrane" binding mode for tBid interaction with Bax.	tBID	192-196	BCL2 associated X, apoptosis regulator	Homo sapiens	214-217
23173725-6	2013	The activated forms of caspase-3 (revCasp-3) and Bid (tBid) were very effective and, therefore, analyzed after stable integration into human leukemia and murine melanoma cell lines.	tBID	54-58	BH3 interacting domain death agonist	Homo sapiens	49-52
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 antagonist/killer 1	Homo sapiens	82-85
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
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	BH3 interacting domain death agonist	Homo sapiens	153-156
24139803-6	2013	The recruitment of Bcl-2 to the BAP31-CDIP1 complex, as well as CDIP1-dependent truncated Bid (tBid) and caspase-8 activation, contributes to BAX oligomerization.	tBID	95-99	cell death inducing Trp53 target 1	Mus musculus	64-69
24139803-6	2013	The recruitment of Bcl-2 to the BAP31-CDIP1 complex, as well as CDIP1-dependent truncated Bid (tBid) and caspase-8 activation, contributes to BAX oligomerization.	tBID	95-99	BCL2-associated X protein	Mus musculus	142-145
24062605-0	2013	Mithramycin A induces apoptosis by regulating the mTOR/Mcl-1/tBid pathway in androgen-independent prostate cancer cells.	tBID	61-65	mechanistic target of rapamycin kinase	Homo sapiens	50-54
24062605-5	2013	Mith significantly induced truncated Bid (tBid) and siRNA-mediated knock-down of Mcl-1 increased tBid protein levels.	tBID	97-101	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	81-86
24062605-7	2013	Thus, Mith acts as an effective tumor growth inhibitor in prostate cancer cells through the mTOR/Mcl-1/tBid signaling pathway.	tBID	103-107	mechanistic target of rapamycin kinase	Homo sapiens	92-96
23782464-7	2013	The Y110E mutant also showed decreased release of cytochrome c from isolated mitochondria challenged with tBid protein, resulting in a failure to activate caspase 3.	tBID	106-110	cytochrome c, somatic	Homo sapiens	50-62
22890322-4	2013	RIP1 is required for the formation of a RIP1/FADD/caspase-8 complex that drives caspase-8 activation, cleavage of Bid into tBid, mitochondrial outer membrane permeabilization, full activation of caspase-3 and caspase-dependent apoptosis.	tBID	123-127	receptor interacting serine/threonine kinase 1	Homo sapiens	0-4
22890322-4	2013	RIP1 is required for the formation of a RIP1/FADD/caspase-8 complex that drives caspase-8 activation, cleavage of Bid into tBid, mitochondrial outer membrane permeabilization, full activation of caspase-3 and caspase-dependent apoptosis.	tBID	123-127	receptor interacting serine/threonine kinase 1	Homo sapiens	40-44
22890322-4	2013	RIP1 is required for the formation of a RIP1/FADD/caspase-8 complex that drives caspase-8 activation, cleavage of Bid into tBid, mitochondrial outer membrane permeabilization, full activation of caspase-3 and caspase-dependent apoptosis.	tBID	123-127	Fas associated via death domain	Homo sapiens	45-49
22890322-4	2013	RIP1 is required for the formation of a RIP1/FADD/caspase-8 complex that drives caspase-8 activation, cleavage of Bid into tBid, mitochondrial outer membrane permeabilization, full activation of caspase-3 and caspase-dependent apoptosis.	tBID	123-127	caspase 8	Homo sapiens	50-59
23744079-0	2013	tBid undergoes multiple conformational changes at the membrane required for Bax activation.	tBID	0-4	BCL2 associated X, apoptosis regulator	Homo sapiens	76-79
23744079-2	2013	Full-length Bid is cleaved in response to apoptotic stimuli into two fragments, p7 and tBid (p15), that are held together by strong hydrophobic interactions until the complex binds to membranes.	tBID	87-91	BH3 interacting domain death agonist	Homo sapiens	12-15
23744079-2	2013	Full-length Bid is cleaved in response to apoptotic stimuli into two fragments, p7 and tBid (p15), that are held together by strong hydrophobic interactions until the complex binds to membranes.	tBID	87-91	cyclin dependent kinase inhibitor 2B	Homo sapiens	93-96
23744079-6	2013	The conformational change of tBid is a prerequisite for interaction with Bax and is, therefore, a novel step that can be modulated to promote or inhibit MOMP.	tBID	29-33	BCL2 associated X, apoptosis regulator	Homo sapiens	73-76
23744079-7	2013	Using automated high-throughput image analysis in cells, we show that down-regulation of Mtch2 causes a significant delay between tBid and Bax relocalization in cells.	tBID	130-134	mitochondrial carrier 2	Homo sapiens	89-94
23744079-8	2013	We propose that by promoting insertion of tBid via a conformational change at the mitochondrial outer membrane, Mtch2 accelerates tBid-mediated Bax activation and MOMP.	tBID	42-46	mitochondrial carrier 2	Homo sapiens	112-117
23744079-8	2013	We propose that by promoting insertion of tBid via a conformational change at the mitochondrial outer membrane, Mtch2 accelerates tBid-mediated Bax activation and MOMP.	tBID	42-46	BCL2 associated X, apoptosis regulator	Homo sapiens	144-147
23744079-8	2013	We propose that by promoting insertion of tBid via a conformational change at the mitochondrial outer membrane, Mtch2 accelerates tBid-mediated Bax activation and MOMP.	tBID	130-134	mitochondrial carrier 2	Homo sapiens	112-117
23744079-8	2013	We propose that by promoting insertion of tBid via a conformational change at the mitochondrial outer membrane, Mtch2 accelerates tBid-mediated Bax activation and MOMP.	tBID	130-134	BCL2 associated X, apoptosis regulator	Homo sapiens	144-147
23834359-5	2013	We show that caspase-9 can cleave Bid into tBid at amino acid 59 and that this cleavage of Bid is required for ROS production following serum withdrawal.	tBID	43-47	caspase 9	Homo sapiens	13-22
23834359-5	2013	We show that caspase-9 can cleave Bid into tBid at amino acid 59 and that this cleavage of Bid is required for ROS production following serum withdrawal.	tBID	43-47	BH3 interacting domain death agonist	Homo sapiens	34-37
23834359-8	2013	CONCLUSIONS: Taken together, these data suggest that caspase-9 is required for mitochondrial morphological changes and ROS production by cleaving and activating Bid into tBid.	tBID	170-174	caspase 9	Homo sapiens	53-62
23834359-8	2013	CONCLUSIONS: Taken together, these data suggest that caspase-9 is required for mitochondrial morphological changes and ROS production by cleaving and activating Bid into tBid.	tBID	170-174	BH3 interacting domain death agonist	Homo sapiens	161-164
23660334-3	2013	Sanguinarine also promoted the activation of caspase-8 and truncation of Bid (tBid).	tBID	78-82	BH3 interacting domain death agonist	Homo sapiens	73-76
23494744-3	2013	We found that, in Bcl-3-silenced cells, caspase-3, caspase-8 and caspase-9 activation is accelerated and tBid mitochondrial content is increased.	tBID	105-109	BCL3 transcription coactivator	Homo sapiens	18-23
23333919-7	2013	The p62/LC3b complex interacts with Fas and truncated BID (tBID) physically.	tBID	59-63	sequestosome 1	Homo sapiens	4-7
23333919-13	2013	Subsequently, the LC3b-mediated lysosomal degradation of tBID is eliminated.	tBID	57-61	microtubule associated protein 1 light chain 3 beta	Homo sapiens	18-22
23186154-12	2013	P188"s neuroprotection appears to involve a relationship between cathepsin B and tBid-mediated mitochondrial initiation of cell death.	tBID	81-85	cathepsin B	Homo sapiens	65-76
23243310-3	2013	TGF-beta directly induces transcription of the BH3-only protein BIK and represses expression of the pro-survival factor BCL-X(L) but has no effect on the direct BAX/BAK "activators" BIM or BID (tBID).	tBID	194-198	transforming growth factor, beta 1	Mus musculus	0-8
22806078-2	2013	In so-called type II cells, an additional mechanism involving tBid-mediated caspase-9 activation is required to efficiently trigger cell death.	tBID	62-66	caspase 9	Homo sapiens	76-85
23333919-7	2013	The p62/LC3b complex interacts with Fas and truncated BID (tBID) physically.	tBID	59-63	microtubule associated protein 1 light chain 3 beta	Homo sapiens	8-12
23333919-7	2013	The p62/LC3b complex interacts with Fas and truncated BID (tBID) physically.	tBID	59-63	BH3 interacting domain death agonist	Homo sapiens	54-57
23333919-9	2013	The deletion of p62 robustly increases tBID and cleaved caspase-3, implying an antiapoptotic effect.	tBID	39-43	sequestosome 1	Homo sapiens	16-19
23333919-11	2013	The deletion of the p62 PBI domain or the ubiquitin-associated domain both lead to elevated tBID, cleaved caspase-3, and significantly more cell death after hyperoxia.	tBID	92-96	sequestosome 1	Homo sapiens	20-23
23190604-0	2012	ABT-737 promotes tBid mitochondrial accumulation to enhance TRAIL-induced apoptosis in glioblastoma cells.	tBID	17-21	TNF superfamily member 10	Homo sapiens	60-65
23476680-5	2013	Furthermore, our results present for the first time that baicalein triggers a convergence of the intrinsic and extrinsic apoptotic pathways via the death receptor-caspase 8-tBid signaling cascade in CCRF-CEM cells.	tBID	173-177	caspase 8	Homo sapiens	163-172
23190604-10	2012	In conclusion, the rational combination of ABT-737 and TRAIL cooperates to trigger tBid mitochondrial accumulation and apoptosis.	tBID	83-87	TNF superfamily member 10	Homo sapiens	55-60
23190604-3	2012	Interestingly, the concerted action of ABT-737 and TRAIL to trigger the accumulation of truncated Bid (tBid) at mitochondrial membranes is identified as a key underlying mechanism.	tBID	103-107	TNF superfamily member 10	Homo sapiens	51-56
23190604-3	2012	Interestingly, the concerted action of ABT-737 and TRAIL to trigger the accumulation of truncated Bid (tBid) at mitochondrial membranes is identified as a key underlying mechanism.	tBID	103-107	BH3 interacting domain death agonist	Homo sapiens	98-101
23190604-4	2012	ABT-737 and TRAIL cooperate to cleave BH3-interacting domain death agonist (Bid) into its active fragment tBid, leading to increased accumulation of tBid at mitochondrial membranes.	tBID	106-110	TNF superfamily member 10	Homo sapiens	12-17
23190604-4	2012	ABT-737 and TRAIL cooperate to cleave BH3-interacting domain death agonist (Bid) into its active fragment tBid, leading to increased accumulation of tBid at mitochondrial membranes.	tBID	106-110	BH3 interacting domain death agonist	Homo sapiens	76-79
23190604-4	2012	ABT-737 and TRAIL cooperate to cleave BH3-interacting domain death agonist (Bid) into its active fragment tBid, leading to increased accumulation of tBid at mitochondrial membranes.	tBID	149-153	TNF superfamily member 10	Homo sapiens	12-17
23190604-4	2012	ABT-737 and TRAIL cooperate to cleave BH3-interacting domain death agonist (Bid) into its active fragment tBid, leading to increased accumulation of tBid at mitochondrial membranes.	tBID	149-153	BH3 interacting domain death agonist	Homo sapiens	76-79
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 like 1	Homo sapiens	126-132
23058921-6	2012	In vitro cytochrome c release experiments further confirmed that, compared with the control group, tBid treatment led to an increase in cytochrome c release from mitofilin-deficient mitochondria.	tBID	99-103	cytochrome c, somatic	Homo sapiens	9-21
23058921-6	2012	In vitro cytochrome c release experiments further confirmed that, compared with the control group, tBid treatment led to an increase in cytochrome c release from mitofilin-deficient mitochondria.	tBID	99-103	cytochrome c, somatic	Homo sapiens	136-148
23058921-6	2012	In vitro cytochrome c release experiments further confirmed that, compared with the control group, tBid treatment led to an increase in cytochrome c release from mitofilin-deficient mitochondria.	tBID	99-103	inner membrane mitochondrial protein	Homo sapiens	162-171
23019260-6	2012	Bid in the PD temporal cortex could be further cleaved into tBid in the cytosol, which is translocated into the mitochondria, where cytochrome c is then released and caspase-3 is subsequently activated.	tBID	60-64	BH3 interacting domain death agonist	Homo sapiens	0-3
23019260-6	2012	Bid in the PD temporal cortex could be further cleaved into tBid in the cytosol, which is translocated into the mitochondria, where cytochrome c is then released and caspase-3 is subsequently activated.	tBID	60-64	cytochrome c, somatic	Homo sapiens	132-144
23019260-6	2012	Bid in the PD temporal cortex could be further cleaved into tBid in the cytosol, which is translocated into the mitochondria, where cytochrome c is then released and caspase-3 is subsequently activated.	tBID	60-64	caspase 3	Homo sapiens	166-175
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
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
22761256-3	2012	We found that caspase 8-cleaved Bid (tBid) could result in LMP directly.	tBID	37-41	caspase 8	Homo sapiens	14-23
22761256-3	2012	We found that caspase 8-cleaved Bid (tBid) could result in LMP directly.	tBID	37-41	BH3 interacting domain death agonist	Homo sapiens	32-35
22761256-4	2012	Although Bax or Bak might modestly enhance tBid-triggered LMP, they are not necessary for LMP.	tBID	43-47	BCL2 associated X, apoptosis regulator	Homo sapiens	9-12
22761256-4	2012	Although Bax or Bak might modestly enhance tBid-triggered LMP, they are not necessary for LMP.	tBID	43-47	BCL2 antagonist/killer 1	Homo sapiens	16-19
22761256-10	2012	We further noted that chymotrypsin-cleaved Bid is more potent than tBid at binding to PA, inserting into the lipid bilayer, and promoting LMP.	tBID	67-71	BH3 interacting domain death agonist	Homo sapiens	43-46
22513214-7	2012	Importantly, tBid plays a major role in Bax activation, and Bik indirectly activates Bak by displacing it from Mcl-1 and Bcl-X(L), pointing to the synergistic mechanism of the combination treatment.	tBID	13-17	BCL2 associated X, apoptosis regulator	Homo sapiens	40-43
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	tumor necrosis factor	Homo sapiens	86-113
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	tumor necrosis factor	Homo sapiens	115-124
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	Fas ligand	Homo sapiens	130-140
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	Fas ligand	Homo sapiens	142-146
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	TNF receptor superfamily member 1A	Homo sapiens	183-189
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	TNF receptor superfamily member 1B	Homo sapiens	191-197
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	TNF receptor superfamily member 1A	Homo sapiens	227-233
22348919-9	2012	5-epi-Sinuleptolide also up-regulated tBid, which is associated with up-regulation of tumor necrosis factor-alpha (TNF-alpha) and Fas ligand (FasL) and their cognate receptors (i.e., TNF-RI, TNF-R2 and Fas), downstream adaptor TNF-R1-associated death domain (TRADD) and Fas-associated death domain (FADD), and activated caspase-8 in SCC25 cells.	tBID	38-42	caspase 8	Homo sapiens	320-329
22487998-12	2012	Furthermore, calpain inhibition also prevented the activation of caspase-9 and caspase-12, along with the cleavage of Bid to tBid, all upstream signals for caspase-3 activation.	tBID	125-129	BH3 interacting domain death agonist	Rattus norvegicus	118-121
22487998-12	2012	Furthermore, calpain inhibition also prevented the activation of caspase-9 and caspase-12, along with the cleavage of Bid to tBid, all upstream signals for caspase-3 activation.	tBID	125-129	caspase 3	Rattus norvegicus	156-165
22416135-1	2012	The molecular basis of the interaction between mitochondrial carrier homologue 2 (MTCH2) and truncated BID (tBID) was characterized.	tBID	108-112	mitochondrial carrier 2	Homo sapiens	47-80
22416135-1	2012	The molecular basis of the interaction between mitochondrial carrier homologue 2 (MTCH2) and truncated BID (tBID) was characterized.	tBID	108-112	mitochondrial carrier 2	Homo sapiens	82-87
22416135-1	2012	The molecular basis of the interaction between mitochondrial carrier homologue 2 (MTCH2) and truncated BID (tBID) was characterized.	tBID	108-112	BH3 interacting domain death agonist	Homo sapiens	103-106
22416135-3	2012	In response to apoptotic signals, MTCH2 recruits tBID to the mitochondria, where it activates apoptosis.	tBID	49-53	mitochondrial carrier 2	Homo sapiens	34-39
22416135-4	2012	A combination of peptide arrays screening with biochemical and biophysical techniques was used to characterize the mechanism of the interaction between tBID and MTCH2 at the structural and molecular levels.	tBID	152-156	mitochondrial carrier 2	Homo sapiens	161-166
22416135-6	2012	The two specific binding sites between the proteins were determined to be tBID residues 59-73 that bind MTCH2 residues 140-161, and tBID residues 111-125 that bind MTCH2 residues 240-290.	tBID	74-78	mitochondrial carrier 2	Homo sapiens	104-109
22416135-6	2012	The two specific binding sites between the proteins were determined to be tBID residues 59-73 that bind MTCH2 residues 140-161, and tBID residues 111-125 that bind MTCH2 residues 240-290.	tBID	74-78	mitochondrial carrier 2	Homo sapiens	164-169
22416135-6	2012	The two specific binding sites between the proteins were determined to be tBID residues 59-73 that bind MTCH2 residues 140-161, and tBID residues 111-125 that bind MTCH2 residues 240-290.	tBID	132-136	mitochondrial carrier 2	Homo sapiens	164-169
22388349-4	2012	Drp1 siRNA and small molecule inhibitors of Drp1 prevented mitochondrial fission, loss of mitochondrial membrane potential (MMP), and cell death induced by glutamate or tBid overexpression in immortalized hippocampal HT-22 neuronal cells.	tBID	169-173	dynamin 1-like	Mus musculus	0-4
22388349-4	2012	Drp1 siRNA and small molecule inhibitors of Drp1 prevented mitochondrial fission, loss of mitochondrial membrane potential (MMP), and cell death induced by glutamate or tBid overexpression in immortalized hippocampal HT-22 neuronal cells.	tBID	169-173	dynamin 1-like	Mus musculus	44-48
22683989-2	2012	It was also shown that recruitment of mitochondria in IFN-alpha induced apoptosis involves the cleavage of BH3 interacting domain death agonist (Bid) to truncated Bid (tBid).	tBID	168-172	interferon alpha 2	Homo sapiens	54-63
22683989-2	2012	It was also shown that recruitment of mitochondria in IFN-alpha induced apoptosis involves the cleavage of BH3 interacting domain death agonist (Bid) to truncated Bid (tBid).	tBID	168-172	BH3 interacting domain death agonist	Homo sapiens	145-148
22683989-2	2012	It was also shown that recruitment of mitochondria in IFN-alpha induced apoptosis involves the cleavage of BH3 interacting domain death agonist (Bid) to truncated Bid (tBid).	tBID	168-172	BH3 interacting domain death agonist	Homo sapiens	163-166
22683989-3	2012	In the present study, we demonstrate that tBid induced by IFN-alpha2a activates mitochondrial Bak to trigger the loss of mitochondrial membrane integrity, consequently causing release of apoptosis-inducing factor (AIF) in ovarian cancer cells, OVCAR3.	tBID	42-46	interferon alpha 2	Homo sapiens	58-68
22683989-3	2012	In the present study, we demonstrate that tBid induced by IFN-alpha2a activates mitochondrial Bak to trigger the loss of mitochondrial membrane integrity, consequently causing release of apoptosis-inducing factor (AIF) in ovarian cancer cells, OVCAR3.	tBID	42-46	BCL2 antagonist/killer 1	Homo sapiens	94-97
22507272-11	2012	Apoptosis occurred with activation of caspase-8 and cleavage of Bid to tBid, increase in Bax:Bcl-2 ratio, mitochondrial release of cytochrome c, and increases in the expression and activity of calpain and caspase-3.	tBID	71-75	BH3 interacting domain death agonist	Homo sapiens	64-67
22513214-0	2012	The proteasome inhibitor MG132 potentiates TRAIL receptor agonist-induced apoptosis by stabilizing tBid and Bik in human head and neck squamous cell carcinoma cells.	tBID	99-103	TNF superfamily member 10	Homo sapiens	43-48
22513214-3	2012	Combination treatment of HNSCC cells synergistically induced apoptotic cell death accompanied by caspase-8, caspase-9, and caspase-3 activation and Bid cleavage into truncated Bid (tBid).	tBID	181-185	BH3 interacting domain death agonist	Homo sapiens	176-179
22513214-4	2012	Generation and accumulation of tBid through the cooperative action of MG132 with TRAIL or AY4 and Bik accumulation through MG132-mediated proteasome inhibition are critical to the synergistic apoptosis.	tBID	31-35	TNF superfamily member 10	Homo sapiens	81-86
22513214-4	2012	Generation and accumulation of tBid through the cooperative action of MG132 with TRAIL or AY4 and Bik accumulation through MG132-mediated proteasome inhibition are critical to the synergistic apoptosis.	tBID	31-35	BCL2 interacting killer	Homo sapiens	98-101
22326460-1	2012	Recent studies report mitochondrial carrier homolog 2 (MTCH2) as a novel and uncharacterized protein that acts as a receptor-like protein for the truncated BH3-interacting domain death agonist (tBID) protein in the outer membrane of mitochondria.	tBID	194-198	mitochondrial carrier 2	Mus musculus	22-53
22326460-1	2012	Recent studies report mitochondrial carrier homolog 2 (MTCH2) as a novel and uncharacterized protein that acts as a receptor-like protein for the truncated BH3-interacting domain death agonist (tBID) protein in the outer membrane of mitochondria.	tBID	194-198	mitochondrial carrier 2	Mus musculus	55-60
22326460-2	2012	These studies, using mouse embryonic stem cells and fibroblasts as well as mice with a conditional knockout of MTCH2 in the liver, showed that deletion of MTCH2 hindered recruitment of tBID to the mitochondria with subsequent reductions in the activation of pro-apoptotic proteins, mitochondrial outer membrane permeabilization and apoptosis.	tBID	185-189	mitochondrial carrier 2	Mus musculus	155-160
22326460-5	2012	There are extensive differences between the protein sequences of MTCH2 and other mitochondrial carriers that may explain the ability of MTCH2 to associate with tBID and thus its role in apoptosis.	tBID	160-164	mitochondrial carrier 2	Mus musculus	65-70
22326460-5	2012	There are extensive differences between the protein sequences of MTCH2 and other mitochondrial carriers that may explain the ability of MTCH2 to associate with tBID and thus its role in apoptosis.	tBID	160-164	mitochondrial carrier 2	Mus musculus	136-141
21738214-11	2012	Once processed, tBID localizes in the mitochondria of MNNG-treated cells, where it can facilitate BAX activation and PCD.	tBID	16-20	BCL2-associated X protein	Mus musculus	98-101
22019693-7	2012	Moreover, the BH3-only protein Bid was cleaved into a truncated Bid (tBid) after cinobufacini treatment.	tBID	69-73	BH3 interacting domain death agonist	Homo sapiens	31-34
22019693-7	2012	Moreover, the BH3-only protein Bid was cleaved into a truncated Bid (tBid) after cinobufacini treatment.	tBID	69-73	BH3 interacting domain death agonist	Homo sapiens	64-67
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	BH3 interacting domain death agonist	Homo sapiens	10-13
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
21986059-6	2012	Interestingly, Bcl-2 family member Bid was cleaved during the course of infection, and the truncated Bid (tBid) appeared to play a role in the initiation of the intrinsic apoptosis with increased release of cytochrome c in cytosol.	tBID	106-110	BH3 interacting domain death agonist	Homo sapiens	101-104
21986059-6	2012	Interestingly, Bcl-2 family member Bid was cleaved during the course of infection, and the truncated Bid (tBid) appeared to play a role in the initiation of the intrinsic apoptosis with increased release of cytochrome c in cytosol.	tBID	106-110	cytochrome c, somatic	Homo sapiens	207-219
21787858-8	2011	The mechanism involves inhibition of intracellular ROS generation and JNK activation, and modulating the balance between the expression of Mcl-1 and its binding partners, Bim, Noxa and tBid.	tBID	185-189	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	139-144
21786169-6	2011	Combination therapy caused activation of caspase-8 and cleavage of Bid to tBid and increased Bax:Bcl-2 ratio and mitochondrial release of cytochrome c and apoptosis-inducing factor (AIF).	tBID	74-78	BH3 interacting domain death agonist	Homo sapiens	67-70
21382479-4	2011	Truncated BID (tBID) translocates to the mitochondria, facilitates the release of cytochrome c, and activates the intrinsic pathways.	tBID	15-19	BH3 interacting domain death agonist	Homo sapiens	10-13
21704663-3	2011	The anti-MUC1 nanobody was covalently linked to the distal end of poly(ethylene glycol)(3500) (PEG(3500)) in PEG(3500)-25kDa polyethylenimine (PEI) conjugates and the resultant macromolecular entity successfully condensed plasmids coding a transcriptionally targeted truncated-Bid (tBid) killer gene under the control of the cancer-specific MUC1 promoter.	tBID	282-286	mucin 1, cell surface associated	Homo sapiens	9-13
21704663-4	2011	The engineered polyplexes exhibited favourable physicochemical characteristics for transfection and dramatically elevated the level of Bid/tBid expression in both MUC1 over-expressing caspase 3-deficient (MCF7 cells) and caspase 3-positive (T47D and SKBR3) tumour cell lines and, concomitantly, induced considerable cell death.	tBID	139-143	mucin 1, cell surface associated	Homo sapiens	163-167
21704663-4	2011	The engineered polyplexes exhibited favourable physicochemical characteristics for transfection and dramatically elevated the level of Bid/tBid expression in both MUC1 over-expressing caspase 3-deficient (MCF7 cells) and caspase 3-positive (T47D and SKBR3) tumour cell lines and, concomitantly, induced considerable cell death.	tBID	139-143	caspase 3	Homo sapiens	184-193
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 associated X, apoptosis regulator	Homo sapiens	139-142
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
21519916-5	2011	The treatment with cryptotanshinone further suppressed TNF-alpha-mediated expression of c-FLIP(L), Bcl-x(L), but the increased level of tBid (a caspase-8 substrate).	tBID	136-140	caspase 8	Homo sapiens	144-153
21525171-0	2011	Bortezomib primes glioblastoma, including glioblastoma stem cells, for TRAIL by increasing tBid stability and mitochondrial apoptosis.	tBID	91-95	TNF superfamily member 10	Homo sapiens	71-76
21525171-4	2011	Investigations into the underlying molecular mechanisms reveal that bortezomib and TRAIL act in concert to cause accumulation of tBid, the active cleavage product of Bid.	tBID	129-133	TNF superfamily member 10	Homo sapiens	83-88
21525171-5	2011	Also, the stability of TRAIL-derived tBid markedly increases on proteasome inhibition.	tBID	37-41	TNF superfamily member 10	Homo sapiens	23-28
21525171-8	2011	Coinciding with tBid accumulation, the activation of Bax/Bak and loss of mitochondrial membrane potential are strongly increased in cotreated cells.	tBID	16-20	BCL2 associated X, apoptosis regulator	Homo sapiens	53-56
21525171-8	2011	Coinciding with tBid accumulation, the activation of Bax/Bak and loss of mitochondrial membrane potential are strongly increased in cotreated cells.	tBID	16-20	BCL2 antagonist/killer 1	Homo sapiens	57-60
21419123-7	2011	Cleavage of Bid into truncated Bid (tBid), as well as increased cytotoxic potential, were also observed.	tBID	36-40	BH3 interacting domain death agonist	Homo sapiens	12-15
21355080-6	2011	Combined treatment with PI103 and TRAIL enhances cleavage of Bid and the insertion of tBid into mitochondrial membranes, and reduces phosphorylation of Bim(EL).	tBID	86-90	TNF superfamily member 10	Homo sapiens	34-39
21382479-4	2011	Truncated BID (tBID) translocates to the mitochondria, facilitates the release of cytochrome c, and activates the intrinsic pathways.	tBID	15-19	cytochrome c, somatic	Homo sapiens	82-94
21382479-10	2011	Mutation of Cav-1 Y14 tyrosine to phenylalanine (Y14F) disrupted the hyperoxia-induced interaction between BID and Cav-1 and subsequently yielded a decreased level of tBID and resistance to hyperoxia-induced apoptosis.	tBID	167-171	caveolin 1	Homo sapiens	12-17
21459798-4	2011	Mechanistic studies reveal that bortezomib profoundly enhances TRAIL-induced cleavage of Bid into tBid, accumulation of tBid in the cytosol, and its insertion into mitochondrial membranes, pointing to a concerted effect on Bid cleavage (TRAIL) and stabilization of tBid (bortezomib), which links the death receptor to the mitochondrial pathway.	tBID	98-102	TNF superfamily member 10	Homo sapiens	63-68
21382479-10	2011	Mutation of Cav-1 Y14 tyrosine to phenylalanine (Y14F) disrupted the hyperoxia-induced interaction between BID and Cav-1 and subsequently yielded a decreased level of tBID and resistance to hyperoxia-induced apoptosis.	tBID	167-171	BH3 interacting domain death agonist	Homo sapiens	107-110
21459798-4	2011	Mechanistic studies reveal that bortezomib profoundly enhances TRAIL-induced cleavage of Bid into tBid, accumulation of tBid in the cytosol, and its insertion into mitochondrial membranes, pointing to a concerted effect on Bid cleavage (TRAIL) and stabilization of tBid (bortezomib), which links the death receptor to the mitochondrial pathway.	tBID	98-102	BH3 interacting domain death agonist	Homo sapiens	89-92
21382479-12	2011	Deletion of glutathione peroxidase-2 using siRNA aggravated the BID-Cav-1 interaction and tBID formation.	tBID	90-94	glutathione peroxidase 2	Homo sapiens	12-36
21459798-4	2011	Mechanistic studies reveal that bortezomib profoundly enhances TRAIL-induced cleavage of Bid into tBid, accumulation of tBid in the cytosol, and its insertion into mitochondrial membranes, pointing to a concerted effect on Bid cleavage (TRAIL) and stabilization of tBid (bortezomib), which links the death receptor to the mitochondrial pathway.	tBID	120-124	TNF superfamily member 10	Homo sapiens	63-68
21459798-4	2011	Mechanistic studies reveal that bortezomib profoundly enhances TRAIL-induced cleavage of Bid into tBid, accumulation of tBid in the cytosol, and its insertion into mitochondrial membranes, pointing to a concerted effect on Bid cleavage (TRAIL) and stabilization of tBid (bortezomib), which links the death receptor to the mitochondrial pathway.	tBID	120-124	TNF superfamily member 10	Homo sapiens	63-68
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
20539308-5	2011	In addition, Bax and truncated-Bid (tBid) mediate a global increase in ER membrane permeability to ER luminal proteins in vitro.	tBID	36-40	BH3 interacting domain death agonist	Homo sapiens	31-34
21223573-5	2011	We tested truncated Bid (tBid), a human pro-apoptotic protein that induces apoptosis very rapidly and efficiently, as suicide gene for gene therapy against HIV-1 infection.	tBID	25-29	BH3 interacting domain death agonist	Homo sapiens	20-23
21223573-6	2011	RESULTS: When tBid was introduced into the HIV-1 LTR-based, Tat- and Rev-dependent transgene expression vector pLRed(INS)2R, very efficient induction of apoptosis was observed within 24 hours, but only in the presence of both HIV-1 regulatory proteins Tat and Rev.	tBID	14-18	Rev	Human immunodeficiency virus 1	69-72
21223573-6	2011	RESULTS: When tBid was introduced into the HIV-1 LTR-based, Tat- and Rev-dependent transgene expression vector pLRed(INS)2R, very efficient induction of apoptosis was observed within 24 hours, but only in the presence of both HIV-1 regulatory proteins Tat and Rev.	tBID	14-18	Rev	Human immunodeficiency virus 1	260-263
21789791-0	2011	Novel insights into the synergistic interaction of Bortezomib and TRAIL: tBid provides the link.	tBID	73-77	TNF superfamily member 10	Homo sapiens	66-71
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
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 like 1	Homo sapiens	216-222
21310911-6	2011	The level of active caspase-3 was similar in both groups; however, more activated proteins for genes involved in the mitochondrial pathway (cleaved caspase-8, tBid) and endoplasmic reticulum (ER) stress (cleaved caspase-12) and, though less active, NF-kappaB subunits and antiapoptotic proteins (XIAP and cFlip) were detected in the TNF-alpha(-/-) eyes compared with wild-type mice.	tBID	159-163	caspase 3	Mus musculus	20-29
21072056-4	2011	In this study, we have identified a native complex containing caspase-8 and BID on the mitochondrial membrane, and showed that death receptor activation by Fas or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induced the cleavage of BID (tBID formation) within this complex.	tBID	256-260	caspase 8	Homo sapiens	62-71
21072056-4	2011	In this study, we have identified a native complex containing caspase-8 and BID on the mitochondrial membrane, and showed that death receptor activation by Fas or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induced the cleavage of BID (tBID formation) within this complex.	tBID	256-260	BH3 interacting domain death agonist	Homo sapiens	76-79
21072056-4	2011	In this study, we have identified a native complex containing caspase-8 and BID on the mitochondrial membrane, and showed that death receptor activation by Fas or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induced the cleavage of BID (tBID formation) within this complex.	tBID	256-260	TNF superfamily member 10	Homo sapiens	163-218
21072056-4	2011	In this study, we have identified a native complex containing caspase-8 and BID on the mitochondrial membrane, and showed that death receptor activation by Fas or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induced the cleavage of BID (tBID formation) within this complex.	tBID	256-260	TNF superfamily member 10	Homo sapiens	220-225
21072056-4	2011	In this study, we have identified a native complex containing caspase-8 and BID on the mitochondrial membrane, and showed that death receptor activation by Fas or tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induced the cleavage of BID (tBID formation) within this complex.	tBID	256-260	BH3 interacting domain death agonist	Homo sapiens	251-254
21072056-5	2011	tBID then shifted to separate mitochondria-associated complexes that contained other BCL-2 family members, such as BAK and BCL-X(L).	tBID	0-4	BCL2 like 1	Homo sapiens	123-131
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 antagonist/killer 1	Homo sapiens	125-128
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
21130780-4	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	173-177	BCL2 associated X, apoptosis regulator	Homo sapiens	191-194
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	173-177	BCL2 associated X, apoptosis regulator	Homo sapiens	196-222
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
21130780-5	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 like 1	Homo sapiens	281-287
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 antagonist/killer 1	Homo sapiens	113-120
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	100-104	BCL2 like 1	Homo sapiens	166-172
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 antagonist/killer 1	Homo sapiens	113-120
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
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 like 1	Homo sapiens	166-172
21130780-11	2011	The presented work, however, reveals that the balance between BAD phosphorylation and dephosphorylation modulates the degree to which BAD influences the signaling from tBID to BAK/BAX.	tBID	168-172	BCL2 antagonist/killer 1	Homo sapiens	176-183
21130780-14	2011	Nonetheless, our model serves to evaluate BAD and its sensitizing effects on the tBID-induction of BAK/BAX and thus aid in predicting when the incorporation of BAD in an apoptosis signaling model is important and when it is not.	tBID	81-85	BCL2 antagonist/killer 1	Homo sapiens	99-106
21152867-0	2011	A novel recombinant immuno-tBid with a furin site effectively suppresses the growth of HER2-positive osteosarcoma cells in vitro.	tBID	27-31	furin, paired basic amino acid cleaving enzyme	Homo sapiens	39-44
21152867-0	2011	A novel recombinant immuno-tBid with a furin site effectively suppresses the growth of HER2-positive osteosarcoma cells in vitro.	tBID	27-31	erb-b2 receptor tyrosine kinase 2	Homo sapiens	87-91
21152867-2	2011	Previously, we constructed an immuno-carboxy terminal fragment of Bid (immuno-tBid) and reported its specific and effective destruction of HER2-positive tumor cells.	tBID	78-82	BH3 interacting domain death agonist	Homo sapiens	66-69
21152867-2	2011	Previously, we constructed an immuno-carboxy terminal fragment of Bid (immuno-tBid) and reported its specific and effective destruction of HER2-positive tumor cells.	tBID	78-82	erb-b2 receptor tyrosine kinase 2	Homo sapiens	139-143
21152867-3	2011	In this study, in order to further reduce the immunogenicity of the previous immuno-proapoptotic protein, we constructed a novel immuno-tBid by replacing domain II of Pseudomonas exotoxin A with a short furin cleavage sequence from the diphtheria toxin.	tBID	136-140	furin, paired basic amino acid cleaving enzyme	Homo sapiens	203-208
21152867-7	2011	We demonstrate here that this novel immuno-tBid induces the specific destruction of HER2-overexpressing SOSP-9607-E10 cells through the release of cytochrome C.	tBID	43-47	erb-b2 receptor tyrosine kinase 2	Homo sapiens	84-88
21152867-7	2011	We demonstrate here that this novel immuno-tBid induces the specific destruction of HER2-overexpressing SOSP-9607-E10 cells through the release of cytochrome C.	tBID	43-47	cytochrome c, somatic	Homo sapiens	147-159
21980415-4	2011	Apoptosis upon knockdown of C9orf82 was associated with increased caspase-10 expression and activation, which was required for the generation of an 11 kDa tBid fragment and activation of Caspase-9.	tBID	155-159	caspase activity and apoptosis inhibitor 1	Homo sapiens	28-35
21980415-4	2011	Apoptosis upon knockdown of C9orf82 was associated with increased caspase-10 expression and activation, which was required for the generation of an 11 kDa tBid fragment and activation of Caspase-9.	tBID	155-159	caspase 10	Homo sapiens	66-76
20978129-7	2010	Cells lacking Apaf-1 or the pro-apoptotic BH3-only protein Bid exhibited lower levels of heat-induced Bak activation, cytochrome c release, and loss of mitochondrial membrane potential, although cleavage of Bid to truncated Bid (tBid) occurred downstream of caspase-9 activation.	tBID	229-233	apoptotic peptidase activating factor 1	Homo sapiens	14-20
20978129-7	2010	Cells lacking Apaf-1 or the pro-apoptotic BH3-only protein Bid exhibited lower levels of heat-induced Bak activation, cytochrome c release, and loss of mitochondrial membrane potential, although cleavage of Bid to truncated Bid (tBid) occurred downstream of caspase-9 activation.	tBID	229-233	BH3 interacting domain death agonist	Homo sapiens	59-62
20978129-8	2010	Combined, the data suggest that caspase-9 is the critical initiator caspase activated during heat-induced apoptosis and that tBid may function to promote cytochrome c release during this process as part of a feed-forward amplification loop.	tBID	125-129	cytochrome c, somatic	Homo sapiens	154-166
21368876-2	2010	These platforms may be at the mitochondrial contact sites in which truncated Bid (tBid) has been demonstrated to be located.	tBID	82-86	BH3 interacting domain death agonist	Homo sapiens	77-80
20833157-6	2010	We further demonstrated that knockdown of caspase-8 using its siRNA inhibited the mitochondrial translocation of tBid, the activations of caspase-9 and caspase-3, and subsequent DNA fragmentation by haplophytin-A.	tBID	113-117	caspase 8	Homo sapiens	42-51
20833157-8	2010	During haplophytin-A-induced apoptosis, caspase-8-stimulated tBid provide a link between the death receptor-mediated extrinsic pathway and the mitochondria- mediated intrinsic pathway.	tBID	61-65	caspase 8	Homo sapiens	40-49
20655869-1	2010	BAX cooperates with truncated BID (tBID) and Ca(2+) in permeabilizing the outer mitochondrial membrane (OMM) and releasing mitochondrial apoptogenic proteins.	tBID	35-39	BCL2 associated X, apoptosis regulator	Homo sapiens	0-3
19777160-8	2010	Combination therapy showed activation of caspase-8, cleavage of Bid to tBid, increase in p53 and p21 expression, down regulation of anti-apoptotic Mcl-1, and increase in Bax:Bcl-2 ratio to trigger apoptosis.	tBID	71-75	BH3 interacting domain death agonist	Homo sapiens	64-67
20655869-8	2010	Altogether, these data suggest that in brain mitochondria, BAX insertion/oligomerization can be dissociated from OMM permeabilization and that tBID and Ca(2+) stimulate BAX insertion/oligomerization and BAX-mediated OMM permeabilization by different mechanisms involving mPT induction and modulation of the SH-redox state.	tBID	143-147	BCL2 associated X, apoptosis regulator	Homo sapiens	169-172
20655869-8	2010	Altogether, these data suggest that in brain mitochondria, BAX insertion/oligomerization can be dissociated from OMM permeabilization and that tBID and Ca(2+) stimulate BAX insertion/oligomerization and BAX-mediated OMM permeabilization by different mechanisms involving mPT induction and modulation of the SH-redox state.	tBID	143-147	BCL2 associated X, apoptosis regulator	Homo sapiens	169-172
20886583-3	2010	DR5/TRAIL induced apoptosis involves downregulation of c-FLIP (L), caspase-8 activation, activated proapoptotic mediators tBid and Bax, mitochondrial permeability transition, and activation of caspase-9.	tBID	122-126	TNF receptor superfamily member 10b	Homo sapiens	0-3
20886583-3	2010	DR5/TRAIL induced apoptosis involves downregulation of c-FLIP (L), caspase-8 activation, activated proapoptotic mediators tBid and Bax, mitochondrial permeability transition, and activation of caspase-9.	tBID	122-126	TNF superfamily member 10	Homo sapiens	4-9
20850011-4	2010	Here we show that Drp1 stimulates tBid-induced Bax oligomerization and cytochrome c release by promoting tethering and hemifusion of membranes in vitro.	tBID	34-38	dynamin 1 like	Homo sapiens	18-22
20850011-4	2010	Here we show that Drp1 stimulates tBid-induced Bax oligomerization and cytochrome c release by promoting tethering and hemifusion of membranes in vitro.	tBID	34-38	BCL2 associated X, apoptosis regulator	Homo sapiens	47-50
20850011-4	2010	Here we show that Drp1 stimulates tBid-induced Bax oligomerization and cytochrome c release by promoting tethering and hemifusion of membranes in vitro.	tBID	34-38	cytochrome c, somatic	Homo sapiens	71-83
20655869-1	2010	BAX cooperates with truncated BID (tBID) and Ca(2+) in permeabilizing the outer mitochondrial membrane (OMM) and releasing mitochondrial apoptogenic proteins.	tBID	35-39	BH3 interacting domain death agonist	Homo sapiens	30-33
20655869-4	2010	Ca(2+) in a mitochondrial permeability transition (mPT)-dependent and recombinant tBID in an mPT-independent manner promoted BAX insertion/ oligomerization in the OMM and augmented cytochrome c release.	tBID	82-86	BCL2 associated X, apoptosis regulator	Homo sapiens	125-128
20655869-4	2010	Ca(2+) in a mitochondrial permeability transition (mPT)-dependent and recombinant tBID in an mPT-independent manner promoted BAX insertion/ oligomerization in the OMM and augmented cytochrome c release.	tBID	82-86	cytochrome c, somatic	Homo sapiens	181-193
20655869-7	2010	On the other hand, a reducing agent, dithiothreitol (DTT), inhibited BAX insertion/oligomerization augmented by tBID or Ca(2+) and suppressed the BAX-mediated release of cytochrome c and Smac/DIABLO but failed to inhibit Ca(2+)-induced swelling.	tBID	112-116	BCL2 associated X, apoptosis regulator	Homo sapiens	69-72
20168333-4	2010	TRAIL alone triggered robust formation of the "death-inducing signaling complex" (DISC), activation of the initiator caspase-8, and truncation of the BH3-only protein BID (tBID).	tBID	172-176	TNF superfamily member 10	Homo sapiens	0-5
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	mitogen-activated protein kinase 14	Homo sapiens	45-48
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	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	87-92
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
20361227-7	2010	Our data also suggest that LMP occurs earlier than mitochondrial outer membrane permeabilization; Bid activation initiated by caspase-8 might be reinforced by CtrB in consequence of LMP, which causes a positive feedback loop leading to the accumulation of tBid, and results in lysosome- and mitochondrion-dependent apoptosis.	tBID	256-260	BH3 interacting domain death agonist	Rattus norvegicus	98-101
20083086-7	2010	Assembly of MAC from Bax or Bak was monitored in real time by directly patch-clamping mitochondria with micropipettes containing the sentinel tBid, a direct activator of Bax and Bak.	tBID	142-146	BCL2 associated X, apoptosis regulator	Homo sapiens	21-24
20361227-7	2010	Our data also suggest that LMP occurs earlier than mitochondrial outer membrane permeabilization; Bid activation initiated by caspase-8 might be reinforced by CtrB in consequence of LMP, which causes a positive feedback loop leading to the accumulation of tBid, and results in lysosome- and mitochondrion-dependent apoptosis.	tBID	256-260	caspase 8	Rattus norvegicus	126-135
20361227-7	2010	Our data also suggest that LMP occurs earlier than mitochondrial outer membrane permeabilization; Bid activation initiated by caspase-8 might be reinforced by CtrB in consequence of LMP, which causes a positive feedback loop leading to the accumulation of tBid, and results in lysosome- and mitochondrion-dependent apoptosis.	tBID	256-260	chymotrypsinogen B1	Rattus norvegicus	159-163
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
20336154-0	2010	Therapeutic effect of alpha-fetoprotein promoter-mediated tBid and chemotherapeutic agents on orthotopic liver tumor in mice.	tBID	58-62	alpha fetoprotein	Mus musculus	22-39
21666767-5	2010	ATRA plus IFN-gamma induced extrinsic pathway of apoptosis by activation of caspase-8 and cleavage of Bid to tBid and also down regulation of hTERT, c-IAP2, and survivin and upregulation of Smac/Diablo to promote apoptosis.	tBID	109-113	interferon gamma	Homo sapiens	10-19
21666767-5	2010	ATRA plus IFN-gamma induced extrinsic pathway of apoptosis by activation of caspase-8 and cleavage of Bid to tBid and also down regulation of hTERT, c-IAP2, and survivin and upregulation of Smac/Diablo to promote apoptosis.	tBID	109-113	BH3 interacting domain death agonist	Homo sapiens	102-105
20083086-7	2010	Assembly of MAC from Bax or Bak was monitored in real time by directly patch-clamping mitochondria with micropipettes containing the sentinel tBid, a direct activator of Bax and Bak.	tBID	142-146	BCL2 antagonist/killer 1	Homo sapiens	28-31
20083086-7	2010	Assembly of MAC from Bax or Bak was monitored in real time by directly patch-clamping mitochondria with micropipettes containing the sentinel tBid, a direct activator of Bax and Bak.	tBID	142-146	BCL2 associated X, apoptosis regulator	Homo sapiens	170-173
20083086-7	2010	Assembly of MAC from Bax or Bak was monitored in real time by directly patch-clamping mitochondria with micropipettes containing the sentinel tBid, a direct activator of Bax and Bak.	tBID	142-146	BCL2 antagonist/killer 1	Homo sapiens	178-181
20436477-0	2010	MTCH2/MIMP is a major facilitator of tBID recruitment to mitochondria.	tBID	37-41	mitochondrial carrier 2	Mus musculus	0-5
20436477-2	2010	Here we show that MTCH2/MIMP (mitochondrial carrier homologue 2/Met-induced mitochondrial protein), a novel truncated BID (tBID)-interacting protein, is a surface-exposed outer mitochondrial membrane protein that facilitates the recruitment of tBID to mitochondria.	tBID	123-127	mitochondrial carrier 2	Mus musculus	18-23
20436477-2	2010	Here we show that MTCH2/MIMP (mitochondrial carrier homologue 2/Met-induced mitochondrial protein), a novel truncated BID (tBID)-interacting protein, is a surface-exposed outer mitochondrial membrane protein that facilitates the recruitment of tBID to mitochondria.	tBID	244-248	mitochondrial carrier 2	Mus musculus	18-23
20436477-3	2010	Knockout of MTCH2/MIMP in embryonic stem cells and in mouse embryonic fibroblasts hinders the recruitment of tBID to mitochondria, the activation of Bax/Bak, MOMP, and apoptosis.	tBID	109-113	mitochondrial carrier 2	Mus musculus	12-17
20436477-4	2010	Moreover, conditional knockout of MTCH2/MIMP in the liver decreases the sensitivity of mice to Fas-induced hepatocellular apoptosis and prevents the recruitment of tBID to liver mitochondria both in vivo and in vitro.	tBID	164-168	mitochondrial carrier 2	Mus musculus	34-39
20436477-6	2010	These loss-of-function models indicate that MTCH2/MIMP has a critical function in liver apoptosis by regulating the recruitment of tBID to mitochondria.	tBID	131-135	mitochondrial carrier 2	Mus musculus	44-49
19820711-0	2009	Membrane promotes tBID interaction with BCL(XL).	tBID	18-22	BCL2 like 1	Homo sapiens	40-47
20404718-9	2010	Additionally, Vpr-induced cleavage of BID to tBID and suppression of BID expression prevented Vpr-induced apoptosis.	tBID	45-49	BH3 interacting domain death agonist	Homo sapiens	38-41
20404718-13	2010	CONCLUSIONS: These studies delineate a novel pathway of Vpr-induced apoptosis in RTEC, which is mediated by sustained ERK activation, resulting in caspase 8-mediated cleavage of BID to tBID, thereby facilitating Bax-mediated mitochondrial injury and apoptosis.	tBID	185-189	mitogen-activated protein kinase 1	Homo sapiens	118-121
20404718-13	2010	CONCLUSIONS: These studies delineate a novel pathway of Vpr-induced apoptosis in RTEC, which is mediated by sustained ERK activation, resulting in caspase 8-mediated cleavage of BID to tBID, thereby facilitating Bax-mediated mitochondrial injury and apoptosis.	tBID	185-189	caspase 8	Homo sapiens	147-156
20404718-13	2010	CONCLUSIONS: These studies delineate a novel pathway of Vpr-induced apoptosis in RTEC, which is mediated by sustained ERK activation, resulting in caspase 8-mediated cleavage of BID to tBID, thereby facilitating Bax-mediated mitochondrial injury and apoptosis.	tBID	185-189	BH3 interacting domain death agonist	Homo sapiens	178-181
20404718-13	2010	CONCLUSIONS: These studies delineate a novel pathway of Vpr-induced apoptosis in RTEC, which is mediated by sustained ERK activation, resulting in caspase 8-mediated cleavage of BID to tBID, thereby facilitating Bax-mediated mitochondrial injury and apoptosis.	tBID	185-189	BCL2 associated X, apoptosis regulator	Homo sapiens	212-215
19942342-8	2010	In addition, suppression of caspase-8 with the specific inhibitor Z-IETD-FMK inhibited AE-induced the activation of Bax, the cleavage of Bid, the translocation of tBid to the mitochondria and the release of cytochrome c, apoptosis-inducing factor (AIF) and Endo G from the mitochondria and subsequent apoptosis.	tBID	163-167	caspase 8	Homo sapiens	28-37
20371697-3	2010	EXPERIMENTAL DESIGN: Recombinant e23sFv-TD-tBID, consisting of a single-chain anti-HER2 antibody fragment linked to a human active truncated Bid by a 10-amino acid residue furin cleavage sequence, was bacterially expressed.	tBID	43-47	erb-b2 receptor tyrosine kinase 2	Homo sapiens	83-87
20371697-3	2010	EXPERIMENTAL DESIGN: Recombinant e23sFv-TD-tBID, consisting of a single-chain anti-HER2 antibody fragment linked to a human active truncated Bid by a 10-amino acid residue furin cleavage sequence, was bacterially expressed.	tBID	43-47	BH3 interacting domain death agonist	Homo sapiens	141-144
20371697-3	2010	EXPERIMENTAL DESIGN: Recombinant e23sFv-TD-tBID, consisting of a single-chain anti-HER2 antibody fragment linked to a human active truncated Bid by a 10-amino acid residue furin cleavage sequence, was bacterially expressed.	tBID	43-47	furin, paired basic amino acid cleaving enzyme	Homo sapiens	172-177
20371697-5	2010	RESULTS: e23sFv-TD-tBID selectively binds to HER2-positive cells and induces apoptotic cell death in vitro and in vivo.	tBID	19-23	erb-b2 receptor tyrosine kinase 2	Homo sapiens	45-49
20371697-6	2010	An investigation of its mechanism of action has revealed that e23sFv-TD-tBID was internalized on binding to the surface of HER2-positive tumor cells, proteolytically cleaved and transported directly to cytosol.	tBID	72-76	erb-b2 receptor tyrosine kinase 2	Homo sapiens	123-127
20371697-12	2010	CONCLUSION: These data suggest that recombinant e23sFv-TD-tBID has therapeutic potential for HER2-positive tumors and warrant further testing for clinical applications.	tBID	58-62	erb-b2 receptor tyrosine kinase 2	Homo sapiens	93-97
19640637-6	2010	Bax was translocated from the cytosol to mitochondria and Bid was cleaved into its truncated form, tBid.	tBID	99-103	BCL2 associated X, apoptosis regulator	Homo sapiens	0-3
19640637-6	2010	Bax was translocated from the cytosol to mitochondria and Bid was cleaved into its truncated form, tBid.	tBID	99-103	BH3 interacting domain death agonist	Homo sapiens	58-61
19937732-2	2010	Degradation of procaspases, production of tBid, loss of mitochondrial membrane potential, Bcl-2 degradation, mitochondrial translocation of Bax, and cytochrome c release were observed in PLA(2)-treated cells.	tBID	42-46	phospholipase A2 group IB	Homo sapiens	187-193
19766591-5	2009	A bystander effect was also observed after exogenous expression of tBid, which facilitates MAC formation and cytochrome c release.	tBID	67-71	cytochrome c, somatic	Homo sapiens	109-121
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
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	B cell leukemia/lymphoma 2	Mus musculus	37-41
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	BCL2-antagonist/killer 1	Mus musculus	66-69
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	BCL2-associated X protein	Mus musculus	70-73
19820692-6	2009	tBID sensitivity of BAK(-/-) MEFs is also reduced, although not to the same extent as V2(-/-) MEFs, which might result from their strong overexpression of BAX.	tBID	0-4	BCL2-antagonist/killer 1	Mus musculus	20-23
19820692-6	2009	tBID sensitivity of BAK(-/-) MEFs is also reduced, although not to the same extent as V2(-/-) MEFs, which might result from their strong overexpression of BAX.	tBID	0-4	BCL2-associated X protein	Mus musculus	155-158
19820692-7	2009	Indeed, addition of recombinant BAX also sensitized V2(-/-) MEFs to tBID.	tBID	68-72	BCL2-associated X protein	Mus musculus	32-35
19820692-8	2009	Thus, VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK, thereby controlling tBID-induced OMM permeabilization and cell death.	tBID	137-141	voltage-dependent anion channel 2	Mus musculus	6-11
19820692-8	2009	Thus, VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK, thereby controlling tBID-induced OMM permeabilization and cell death.	tBID	137-141	BCL2-antagonist/killer 1	Mus musculus	112-115
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	B cell leukemia/lymphoma 2	Mus musculus	12-17
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
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	caspase 8	Mus musculus	93-102
19839062-7	2009	tBid was capable of binding to Bcl-xL and displacing Bak and Bax from Bcl-xL, leading to release of cytochrome c from wild-type mitochondria.	tBID	0-4	BCL2-like 1	Mus musculus	31-37
19839062-7	2009	tBid was capable of binding to Bcl-xL and displacing Bak and Bax from Bcl-xL, leading to release of cytochrome c from wild-type mitochondria.	tBID	0-4	BCL2-antagonist/killer 1	Mus musculus	53-56
19839062-7	2009	tBid was capable of binding to Bcl-xL and displacing Bak and Bax from Bcl-xL, leading to release of cytochrome c from wild-type mitochondria.	tBID	0-4	BCL2-associated X protein	Mus musculus	61-64
19839062-7	2009	tBid was capable of binding to Bcl-xL and displacing Bak and Bax from Bcl-xL, leading to release of cytochrome c from wild-type mitochondria.	tBID	0-4	BCL2-like 1	Mus musculus	70-76
19839062-8	2009	Bcl-xL-deficient mitochondria were more susceptible to tBid-induced cytochrome c release.	tBID	55-59	BCL2-like 1	Mus musculus	0-6
19758996-2	2009	Although it is well established that recruitment of mitochondria in this context involves the cleavage of Bid to truncated Bid (tBid), the precise post-mitochondrial signaling responsible for executioner caspase activation is controversial.	tBID	128-132	BH3 interacting domain death agonist	Homo sapiens	106-109
19758996-2	2009	Although it is well established that recruitment of mitochondria in this context involves the cleavage of Bid to truncated Bid (tBid), the precise post-mitochondrial signaling responsible for executioner caspase activation is controversial.	tBID	128-132	BH3 interacting domain death agonist	Homo sapiens	123-126
19761754-5	2009	Co-immunoprecipitation experiments showed that the membrane-bound Bcl-x(L) sequestered tBid by direct interaction at physiological pH.	tBID	87-91	BCL2 like 1	Homo sapiens	66-71
19761754-6	2009	If Bcl-x(L) behaves similarly at low pH as it does at physiological pH, the membrane-bound Bcl-x(L) should bind to tBid through protein regions other than the BH3 domain of tBid and the hydrophobic pocket of Bcl-x(L).	tBID	115-119	BCL2 like 1	Homo sapiens	3-8
19761754-6	2009	If Bcl-x(L) behaves similarly at low pH as it does at physiological pH, the membrane-bound Bcl-x(L) should bind to tBid through protein regions other than the BH3 domain of tBid and the hydrophobic pocket of Bcl-x(L).	tBID	115-119	BCL2 like 1	Homo sapiens	3-10
19761754-6	2009	If Bcl-x(L) behaves similarly at low pH as it does at physiological pH, the membrane-bound Bcl-x(L) should bind to tBid through protein regions other than the BH3 domain of tBid and the hydrophobic pocket of Bcl-x(L).	tBID	115-119	BCL2 like 1	Homo sapiens	91-96
19761754-6	2009	If Bcl-x(L) behaves similarly at low pH as it does at physiological pH, the membrane-bound Bcl-x(L) should bind to tBid through protein regions other than the BH3 domain of tBid and the hydrophobic pocket of Bcl-x(L).	tBID	173-177	BCL2 like 1	Homo sapiens	91-96
19796174-2	2009	The active C-terminal fragment of Bid (tBid) translocates to the mitochondria where it interacts with cardiolipins at contact sites and induces the release of cytochrome c by a mechanism that is not yet fully understood.	tBID	39-43	BH3 interacting domain death agonist	Homo sapiens	34-37
19796174-2	2009	The active C-terminal fragment of Bid (tBid) translocates to the mitochondria where it interacts with cardiolipins at contact sites and induces the release of cytochrome c by a mechanism that is not yet fully understood.	tBID	39-43	cytochrome c, somatic	Homo sapiens	159-171
19796174-3	2009	It has been shown that the alpha-helices alphaH6 and alphaH7 (which create the hairpin-forming domain of tBid) mediate the insertion of Bid into mitochondrial membranes and are essential for the cytochrome c-releasing activity.	tBID	105-109	cytochrome c, somatic	Homo sapiens	195-207
19918914-2	2010	Introducing truncated Bid (tBid), a recently known member of the Bcl-2 family, eradicates cancer cells efficiently.	tBID	27-31	BH3 interacting domain death agonist	Homo sapiens	22-25
19918914-4	2010	These two core promoter modules contained cancer specific promoters of MUC1 and Survivin genes accompanied by hypoxia-responsive elements and estrogen responsive elements (microenvironment condition of breast cancer cells) which were employed to achieve a higher and more specific level of tBid expression in breast cancer cells.	tBID	290-294	mucin 1, cell surface associated	Homo sapiens	71-75
20392206-1	2010	The truncated C-terminal portion of Bid (tBid) is an important intermediate in ligand-induced apoptosis.	tBID	41-45	BH3 interacting domain death agonist	Homo sapiens	36-39
20392206-2	2010	tBid has been shown to be sensitive to proteasomal inhibitors and downregulated by activation of the epidermal growth factor (EGF) pathway.	tBID	0-4	epidermal growth factor	Homo sapiens	101-124
20392206-2	2010	tBid has been shown to be sensitive to proteasomal inhibitors and downregulated by activation of the epidermal growth factor (EGF) pathway.	tBID	0-4	epidermal growth factor	Homo sapiens	126-129
20392206-3	2010	Here, we provide evidence that tBid is a substrate of the ubiquitin ligase Itch, which can specifically interact with and ubiquitinate tBid, but not intact Bid.	tBID	31-35	itchy E3 ubiquitin protein ligase	Homo sapiens	75-79
20392206-3	2010	Here, we provide evidence that tBid is a substrate of the ubiquitin ligase Itch, which can specifically interact with and ubiquitinate tBid, but not intact Bid.	tBID	135-139	itchy E3 ubiquitin protein ligase	Homo sapiens	75-79
20392206-3	2010	Here, we provide evidence that tBid is a substrate of the ubiquitin ligase Itch, which can specifically interact with and ubiquitinate tBid, but not intact Bid.	tBID	135-139	BH3 interacting domain death agonist	Homo sapiens	32-35
20392206-6	2010	Our findings identify Itch as a key molecule between EGF signalling and resistance to apoptosis through downregulation of tBid, providing further details on how EGF receptor and proteasome inhibitors can contribute to the induction of apoptosis and the treatment of cancer.	tBID	122-126	itchy E3 ubiquitin protein ligase	Homo sapiens	22-26
20392206-6	2010	Our findings identify Itch as a key molecule between EGF signalling and resistance to apoptosis through downregulation of tBid, providing further details on how EGF receptor and proteasome inhibitors can contribute to the induction of apoptosis and the treatment of cancer.	tBID	122-126	epidermal growth factor	Homo sapiens	53-56
20392206-6	2010	Our findings identify Itch as a key molecule between EGF signalling and resistance to apoptosis through downregulation of tBid, providing further details on how EGF receptor and proteasome inhibitors can contribute to the induction of apoptosis and the treatment of cancer.	tBID	122-126	epidermal growth factor	Homo sapiens	161-164
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
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	caspase 8	Mus musculus	61-70
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	55-59	BCL2-associated X protein	Mus musculus	144-147
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	55-59	BCL2-antagonist/killer 1	Mus musculus	152-155
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	55-59	BCL2-associated X protein	Mus musculus	379-382
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	55-59	BCL2-antagonist/killer 1	Mus musculus	390-393
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	161-165	BCL2-associated X protein	Mus musculus	144-147
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	161-165	BCL2-antagonist/killer 1	Mus musculus	152-155
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	161-165	BCL2-associated X protein	Mus musculus	144-147
20179769-3	2010	Accumulating evidence now indicate that the binding of tBid initiates an ordered sequences of events that prime mitochondria from the action of Bax and Bak: (1) tBid interacts with mitochondria via a specific binding to cardiolipin (CL) and immediately disturbs mitochondrial structure and function idependently of its BH3 domain; (2) Then, tBid activates through its BH3 domain Bax and/or Bak and induces their subsequent oligomerization in mitochondrial membranes.	tBID	161-165	BCL2-antagonist/killer 1	Mus musculus	152-155
20179769-11	2010	These support the notion that tBid acts as a bifunctional molecule: first, it binds to mitochondrial CL via its helix alphaH6 and destabilizes mitochondrial structure and function, and then it promotes through its BH3 domain the activation and oligomerization of Bax and/or Bak, leading to cytochrome c release and execution of apoptosis.	tBID	30-34	BCL2-associated X protein	Mus musculus	263-266
20179769-11	2010	These support the notion that tBid acts as a bifunctional molecule: first, it binds to mitochondrial CL via its helix alphaH6 and destabilizes mitochondrial structure and function, and then it promotes through its BH3 domain the activation and oligomerization of Bax and/or Bak, leading to cytochrome c release and execution of apoptosis.	tBID	30-34	BCL2-antagonist/killer 1	Mus musculus	274-277
19695221-8	2009	Western blotting revealed that combination therapy downregulated angiogenic factors and also induced extrinsic pathway of apoptosis with activation of caspase-8 for Bid cleavage to tBid.	tBID	181-185	caspase 8	Homo sapiens	151-160
19695221-8	2009	Western blotting revealed that combination therapy downregulated angiogenic factors and also induced extrinsic pathway of apoptosis with activation of caspase-8 for Bid cleavage to tBid.	tBID	181-185	BH3 interacting domain death agonist	Homo sapiens	165-168
19820711-2	2009	We used fluorescence correlation spectroscopy to quantify the molecular interactions of BH3-interacting domain death agonist (BID) and its truncated form tBID with the B cell lymphoma extra-large protein truncated at the C terminus (BCL(XL)DeltaCt) in solution and in membranes, and we found that (i) only the active form tBID binds to BCL(XL)DeltaCt and (ii) that the membrane strongly promotes binding between them.	tBID	322-326	BH3 interacting domain death agonist	Homo sapiens	126-129
19820711-3	2009	Particularly, a BH3 peptide from BID disrupts the tBID-BCL(XL) complex in solution, but only partially in lipid bilayers.	tBID	50-54	BH3 interacting domain death agonist	Homo sapiens	33-36
19820711-3	2009	Particularly, a BH3 peptide from BID disrupts the tBID-BCL(XL) complex in solution, but only partially in lipid bilayers.	tBID	50-54	BCL2 like 1	Homo sapiens	55-62
19820711-4	2009	These data indicate that tBID-BCL(XL) interactions in solution and lipid membranes are distinct, and they support a model in which BCL(XL) inhibition of tBID takes place predominantly at the membrane.	tBID	25-29	BCL2 like 1	Homo sapiens	30-37
19820711-4	2009	These data indicate that tBID-BCL(XL) interactions in solution and lipid membranes are distinct, and they support a model in which BCL(XL) inhibition of tBID takes place predominantly at the membrane.	tBID	25-29	BCL2 like 1	Homo sapiens	131-138
19820711-4	2009	These data indicate that tBID-BCL(XL) interactions in solution and lipid membranes are distinct, and they support a model in which BCL(XL) inhibition of tBID takes place predominantly at the membrane.	tBID	153-157	BCL2 like 1	Homo sapiens	30-37
19820711-4	2009	These data indicate that tBID-BCL(XL) interactions in solution and lipid membranes are distinct, and they support a model in which BCL(XL) inhibition of tBID takes place predominantly at the membrane.	tBID	153-157	BCL2 like 1	Homo sapiens	131-138
19450542-4	2009	Targeting of tBid to the mitochondria, which is necessary for Bax/Bak oligomerization and cristae remodelling, is dependent on the exposure of CL at contact sites between the inner and outer mitochondrial membranes.	tBID	13-17	BCL2 associated X, apoptosis regulator	Homo sapiens	62-65
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
19450542-4	2009	Targeting of tBid to the mitochondria, which is necessary for Bax/Bak oligomerization and cristae remodelling, is dependent on the exposure of CL at contact sites between the inner and outer mitochondrial membranes.	tBID	13-17	BCL2 antagonist/killer 1	Homo sapiens	66-69
19450542-7	2009	Deficiencies in CL inhibit the formation of tBid and prevent apoptosis by removing an essential activation platform for the autoprocessing of caspase-8.	tBID	44-48	caspase 8	Homo sapiens	142-151
19466402-0	2009	Activation of Bax by joint action of tBid and mitochondrial outer membrane: Monte Carlo simulations.	tBID	37-41	BCL2 associated X, apoptosis regulator	Homo sapiens	14-17
19670908-4	2009	In this study, we characterize the molecular interactions between full-length tBID and BCL-XL using NMR spectroscopy and isothermal titration calorimetry (ITC).	tBID	78-82	BCL2 like 1	Homo sapiens	87-93
19670908-0	2009	Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL.	tBID	41-45	BCL2 like 1	Homo sapiens	64-70
19670908-3	2009	The pro-apoptotic activity of tBID is regulated by its interactions with pro-survival BCL-XL and pro-death BAX, both in the cytosol and at the mitochondrial membrane.	tBID	30-34	BCL2 like 1	Homo sapiens	86-92
19670908-3	2009	The pro-apoptotic activity of tBID is regulated by its interactions with pro-survival BCL-XL and pro-death BAX, both in the cytosol and at the mitochondrial membrane.	tBID	30-34	BCL2 associated X, apoptosis regulator	Homo sapiens	107-110
19670908-5	2009	In aqueous solution, tBID adopts an alpha-helical but dynamically disordered conformation; however, the three-dimensional conformation is stabilized when tBID engages its BH3 domain in the BH3-binding hydrophobic groove of BCL-XL to form a stable heterodimeric complex.	tBID	21-25	BCL2 like 1	Homo sapiens	223-229
19670908-5	2009	In aqueous solution, tBID adopts an alpha-helical but dynamically disordered conformation; however, the three-dimensional conformation is stabilized when tBID engages its BH3 domain in the BH3-binding hydrophobic groove of BCL-XL to form a stable heterodimeric complex.	tBID	154-158	BCL2 like 1	Homo sapiens	223-229
19670908-6	2009	Characterization of the binding thermodynamics by ITC reveals that the interaction between tBID and BCL-XL is driven by enthalpy but disfavored by the entropy associated with the conformational order induced in tBID upon binding BCL-XL.	tBID	91-95	BCL2 like 1	Homo sapiens	100-106
19670908-6	2009	Characterization of the binding thermodynamics by ITC reveals that the interaction between tBID and BCL-XL is driven by enthalpy but disfavored by the entropy associated with the conformational order induced in tBID upon binding BCL-XL.	tBID	91-95	BCL2 like 1	Homo sapiens	229-235
19670908-6	2009	Characterization of the binding thermodynamics by ITC reveals that the interaction between tBID and BCL-XL is driven by enthalpy but disfavored by the entropy associated with the conformational order induced in tBID upon binding BCL-XL.	tBID	211-215	BCL2 like 1	Homo sapiens	100-106
19670908-6	2009	Characterization of the binding thermodynamics by ITC reveals that the interaction between tBID and BCL-XL is driven by enthalpy but disfavored by the entropy associated with the conformational order induced in tBID upon binding BCL-XL.	tBID	211-215	BCL2 like 1	Homo sapiens	229-235
19557009-2	2009	Although some data support a role for certain BH3-only proteins, such as Bim or tBid, to directly activate Bax, others have led to the conclusion that BH3-only proteins act indirectly by antagonizing the prosurvival Bcl-2 proteins, thereby allowing Bax activation to proceed.	tBID	80-84	BCL2 associated X, apoptosis regulator	Homo sapiens	107-110
19643600-4	2009	Consequently SAHA/TRAIL combination induced many apoptotic events, such as a cleavage of Bid into tBid, dissipation of mitochondrial membrane potential, activation of caspase-3 with the consequent cleavage of both NF-kB and Akt.	tBID	98-102	TNF superfamily member 10	Homo sapiens	18-23
19466402-4	2009	The pro-death action of Bax is regulated by interactions with both other prosurvival proteins, such as tBid, and the MOM, but the exact mechanisms remain largely unclear.	tBID	103-107	BCL2 associated X, apoptosis regulator	Homo sapiens	24-27
19466402-5	2009	Here, the mechanisms of integration of Bax into a model membrane mimicking the MOM were studied by Monte Carlo simulations preceded by a computer prediction of the docking of tBid with Bax.	tBID	175-179	BCL2 associated X, apoptosis regulator	Homo sapiens	39-42
19466402-5	2009	Here, the mechanisms of integration of Bax into a model membrane mimicking the MOM were studied by Monte Carlo simulations preceded by a computer prediction of the docking of tBid with Bax.	tBID	175-179	BCL2 associated X, apoptosis regulator	Homo sapiens	185-188
19466402-6	2009	A novel model of Bax activation by tBid was predicted by the simulations.	tBID	35-39	BCL2 associated X, apoptosis regulator	Homo sapiens	17-20
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	15-19	BCL2 associated X, apoptosis regulator	Homo sapiens	29-32
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	15-19	BCL2 associated X, apoptosis regulator	Homo sapiens	66-69
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	15-19	adrenoceptor alpha 1D	Homo sapiens	78-84
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	15-19	BCL2 associated X, apoptosis regulator	Homo sapiens	66-69
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	189-193	BCL2 associated X, apoptosis regulator	Homo sapiens	29-32
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	189-193	BCL2 associated X, apoptosis regulator	Homo sapiens	66-69
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	189-193	adrenoceptor alpha 1D	Homo sapiens	78-84
19466402-7	2009	In this model, tBid binds to Bax at an interaction site formed by Bax helices alpha1, alpha2, alpha3 and alpha5 leading, due to interaction of the positively charged N-terminal fragment of tBid with anionic lipid headgroups, to Bax reorientation such that a hydrogen-bonded pair of residues, Asp98 and Ser184, is brought into close proximity with negatively charged lipid headgroups.	tBID	189-193	BCL2 associated X, apoptosis regulator	Homo sapiens	66-69
19712588-6	2009	Together, these data suggest that the cleaved DOBI may acquire a new function, possibly by cooperating with tBid in the mitochondrial event of cell death caused by TRAIL.	tBID	108-112	TNF superfamily member 10	Homo sapiens	164-169
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	peptidylprolyl isomerase D	Homo sapiens	0-4
19180563-2	2009	Degradation of procaspases, production of tBid, loss of mitochondrial membrane potential, and cytochrome c release were observed in PLA(2)-treated cells.	tBID	42-46	phospholipase A2 group IIA	Homo sapiens	132-138
19423619-7	2009	The presence of z-IETD-fmk, a caspase-8 inhibitor, markedly reversed tBid formation and caspase activation and partially reversed the dissipation of platelet DeltaPsim stimulated by resveratrol.	tBID	69-73	caspase 8	Homo sapiens	30-39
19381674-2	2009	The aim of this study was to investigate whether gal-1 induced activation of the death-receptor pathway in Jurkat T lymphocytes mediates apoptosis via the mitochondrial pathway linked by truncated Bid (tBid).	tBID	202-206	galectin 1	Homo sapiens	49-54
19381674-2	2009	The aim of this study was to investigate whether gal-1 induced activation of the death-receptor pathway in Jurkat T lymphocytes mediates apoptosis via the mitochondrial pathway linked by truncated Bid (tBid).	tBID	202-206	BH3 interacting domain death agonist	Homo sapiens	197-200
19454696-6	2009	Relocalized lysosomal cathepsin B can process Bid to active tBid to cause cytochrome c and apoptosis-activating factor release from mitochondria.	tBID	60-64	cathepsin B	Homo sapiens	22-33
19454696-6	2009	Relocalized lysosomal cathepsin B can process Bid to active tBid to cause cytochrome c and apoptosis-activating factor release from mitochondria.	tBID	60-64	BH3 interacting domain death agonist	Homo sapiens	46-49
19454696-6	2009	Relocalized lysosomal cathepsin B can process Bid to active tBid to cause cytochrome c and apoptosis-activating factor release from mitochondria.	tBID	60-64	cytochrome c, somatic	Homo sapiens	74-86
19233849-5	2009	Reconstitution experiments using recombinant proteins and permeabilized Bid-deficient cells demonstrated that truncated Bid (tBid), but not full-length Bid, potently induced Bak activation and the release of cytochrome c.	tBID	125-129	BH3 interacting domain death agonist	Homo sapiens	72-75
19233849-5	2009	Reconstitution experiments using recombinant proteins and permeabilized Bid-deficient cells demonstrated that truncated Bid (tBid), but not full-length Bid, potently induced Bak activation and the release of cytochrome c.	tBID	125-129	BH3 interacting domain death agonist	Homo sapiens	120-123
19233849-5	2009	Reconstitution experiments using recombinant proteins and permeabilized Bid-deficient cells demonstrated that truncated Bid (tBid), but not full-length Bid, potently induced Bak activation and the release of cytochrome c.	tBID	125-129	BH3 interacting domain death agonist	Homo sapiens	120-123
19233849-5	2009	Reconstitution experiments using recombinant proteins and permeabilized Bid-deficient cells demonstrated that truncated Bid (tBid), but not full-length Bid, potently induced Bak activation and the release of cytochrome c.	tBID	125-129	cytochrome c, somatic	Homo sapiens	208-220
19233849-8	2009	These data suggest that tBid plays an important regulatory role in the execution of DNA damage-induced cytochrome c release and apoptosis.	tBID	24-28	cytochrome c, somatic	Homo sapiens	103-115
19233849-9	2009	However, the fact that cleavage of Bid to tBid is mediated by executioner caspases suggests that a self-amplifying feed forward loop involving caspases, Bid, and mitochondria may help determine irreversible commitment to apoptosis.	tBID	42-46	BH3 interacting domain death agonist	Homo sapiens	35-38
19233849-9	2009	However, the fact that cleavage of Bid to tBid is mediated by executioner caspases suggests that a self-amplifying feed forward loop involving caspases, Bid, and mitochondria may help determine irreversible commitment to apoptosis.	tBID	42-46	caspase 8	Homo sapiens	74-82
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
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	cytochrome c, somatic	Homo sapiens	73-85
19062087-0	2008	Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax.	tBID	20-24	BCL2 associated X, apoptosis regulator	Homo sapiens	107-110
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 associated X, apoptosis regulator	Homo sapiens	127-130
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 antagonist/killer 1	Homo sapiens	135-138
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
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 like 1	Homo sapiens	209-215
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 like 2	Homo sapiens	217-222
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	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	224-229
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 related protein A1	Homo sapiens	231-235
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 related protein A1	Homo sapiens	236-239
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 like 10	Homo sapiens	245-250
19550122-10	2009	After mDRA-6 exposure, the proenzymes of Caspase-8, -9 and -3 were reduced and their active cleavage products were increased along with the increase of exposure time, the cleavage products of PARP were also increased, Bid was degraded to tBid, and an abundance of Cyto c was released from mitochondria, but the proenzyme of Caspase-10 showed no change and no cleavage products of Caspase-10 were detectable.	tBID	238-242	caspase 8	Homo sapiens	41-61
19038292-7	2009	Further studies revealed that heart mitochondria overexpressing Glrx2 released less cytochrome c than did controls in response to treatment with tBid or a peptide encompassing the BH3 domain of Bid.	tBID	145-149	glutaredoxin 2 (thioltransferase)	Mus musculus	64-69
19120440-7	2009	The neutralization of Fas ligand (FasL) protected against traumatically induced or Fas-mediated caspase-3 activation and the loss of mitochondrial membrane potential and tBid expression in wild-type spinal cord cultures.	tBID	170-174	Fas ligand (TNF superfamily, member 6)	Mus musculus	22-32
19120440-7	2009	The neutralization of Fas ligand (FasL) protected against traumatically induced or Fas-mediated caspase-3 activation and the loss of mitochondrial membrane potential and tBid expression in wild-type spinal cord cultures.	tBID	170-174	Fas ligand (TNF superfamily, member 6)	Mus musculus	34-38
18368485-7	2009	Also, IFN-gamma activated caspase-8 and cleaved Bid to truncated Bid (tBid) for translocation to mitochondria.	tBID	70-74	BH3 interacting domain death agonist	Homo sapiens	65-68
19062087-5	2008	Simultaneous measurements of these interactions revealed an ordered series of steps required for outer membrane permeabilization: (1) tBid rapidly binds to membranes, where (2) tBid interacts with Bax, causing (3) Bax insertion into membranes and (4) oligomerization, culminating in (5) membrane permeabilization.	tBID	134-138	BCL2 associated X, apoptosis regulator	Homo sapiens	214-217
19062087-5	2008	Simultaneous measurements of these interactions revealed an ordered series of steps required for outer membrane permeabilization: (1) tBid rapidly binds to membranes, where (2) tBid interacts with Bax, causing (3) Bax insertion into membranes and (4) oligomerization, culminating in (5) membrane permeabilization.	tBID	177-181	BCL2 associated X, apoptosis regulator	Homo sapiens	197-200
19062087-6	2008	Bcl-XL prevents membrane-bound tBid from binding Bax.	tBID	31-35	BCL2 like 1	Homo sapiens	0-6
19062087-6	2008	Bcl-XL prevents membrane-bound tBid from binding Bax.	tBID	31-35	BCL2 associated X, apoptosis regulator	Homo sapiens	49-52
19062087-7	2008	Bad releases tBid from Bcl-XL, restoring both tBid binding to Bax and membrane permeabilization.	tBID	13-17	BCL2 like 1	Homo sapiens	23-29
19062087-7	2008	Bad releases tBid from Bcl-XL, restoring both tBid binding to Bax and membrane permeabilization.	tBID	13-17	BCL2 associated X, apoptosis regulator	Homo sapiens	62-65
19062087-7	2008	Bad releases tBid from Bcl-XL, restoring both tBid binding to Bax and membrane permeabilization.	tBID	46-50	BCL2 like 1	Homo sapiens	23-29
19062087-7	2008	Bad releases tBid from Bcl-XL, restoring both tBid binding to Bax and membrane permeabilization.	tBID	46-50	BCL2 associated X, apoptosis regulator	Homo sapiens	62-65
19070569-3	2008	(2008) now describe the reconstitution and regulation in liposomes of tBid-mediated membrane penetration and oligomerization of Bax.	tBID	70-74	BCL2 associated X, apoptosis regulator	Homo sapiens	128-131
18388575-9	2008	Hsp70 overexpression inhibited burn serum-induced apoptosis of cardiomyocytes; and burn serum-induced activation of caspases-3, -8, and -9; and Bid cleavage into tBid.	tBID	162-166	heat shock protein family A (Hsp70) member 1B	Rattus norvegicus	0-5
18591962-6	2008	However, cells treated with Actinomycin D (ActD) become susceptible to TNF-alpha-induced cell death through the activation of caspase-8, generation of tBid and activation of caspase-9 and -3.	tBID	151-155	tumor necrosis factor	Rattus norvegicus	71-80
18602901-6	2008	We found that 4-HPR caused apoptosis with activation of caspase-8 and cleavage of Bid to truncated Bid (tBid).	tBID	104-108	BH3 interacting domain death agonist	Homo sapiens	99-102
18374914-11	2008	Caspase 8 inhibitor significantly inhibited the amyloid beta protein-mediated increase in mitochondrial tBid and the release of cytochrome c. Therefore, TAB blocked the overload of calcium in mitochondria and impaired the amyloid beta protein-mediated activation of the caspase 8-tBid-cytochrome c pathway, thereby conferring its neuroprotective effects on amyloid beta protein-mediated neurotoxicity.	tBID	104-108	caspase 8	Rattus norvegicus	0-9
18259190-4	2008	When isolated mitochondria were incubated with phospholipase A2, which led to phosphatidylethanolamine and cardiolipin hydrolysis, tBid and Bax insertion were hindered.	tBID	131-135	phospholipase A2 group IB	Homo sapiens	47-63
18368485-7	2009	Also, IFN-gamma activated caspase-8 and cleaved Bid to truncated Bid (tBid) for translocation to mitochondria.	tBID	70-74	interferon gamma	Homo sapiens	6-15
18368485-7	2009	Also, IFN-gamma activated caspase-8 and cleaved Bid to truncated Bid (tBid) for translocation to mitochondria.	tBID	70-74	BH3 interacting domain death agonist	Homo sapiens	48-51
18602901-6	2008	We found that 4-HPR caused apoptosis with activation of caspase-8 and cleavage of Bid to truncated Bid (tBid).	tBID	104-108	haptoglobin-related protein	Homo sapiens	16-19
18644999-2	2008	Herein, we describe experiments conducted with a fusion protein, which was generated by fusing a human epidermal growth factor receptor-2 (HER2)-specific single-chain antibody with domain II of Pseudomonas exotoxin A and the truncated active BID (tBID).	tBID	247-251	erb-b2 receptor tyrosine kinase 2	Homo sapiens	97-137
18644999-2	2008	Herein, we describe experiments conducted with a fusion protein, which was generated by fusing a human epidermal growth factor receptor-2 (HER2)-specific single-chain antibody with domain II of Pseudomonas exotoxin A and the truncated active BID (tBID).	tBID	247-251	erb-b2 receptor tyrosine kinase 2	Homo sapiens	139-143
18644999-4	2008	Specifically, by excluding cells with undetectable HER2, we showed that the secreted immuno-tBID molecule selectively recognized and killed HER2-overexpressing tumor cells in vitro by attacking their mitochondria and inducing their apoptotic death.	tBID	92-96	erb-b2 receptor tyrosine kinase 2	Homo sapiens	51-55
18644999-4	2008	Specifically, by excluding cells with undetectable HER2, we showed that the secreted immuno-tBID molecule selectively recognized and killed HER2-overexpressing tumor cells in vitro by attacking their mitochondria and inducing their apoptotic death.	tBID	92-96	erb-b2 receptor tyrosine kinase 2	Homo sapiens	140-144
18644999-11	2008	Our data showed that, compared with the toxins employed before, the chimeric immuno-tBID molecule can not only specifically recognize HER2-positive tumor cells but also certainly induce apoptosis even in the presence of zVAD and TAT-BH4, thereby suggesting an alternative approach to treating HER2/neu-positive tumors.	tBID	84-88	erb-b2 receptor tyrosine kinase 2	Homo sapiens	134-138
18644999-11	2008	Our data showed that, compared with the toxins employed before, the chimeric immuno-tBID molecule can not only specifically recognize HER2-positive tumor cells but also certainly induce apoptosis even in the presence of zVAD and TAT-BH4, thereby suggesting an alternative approach to treating HER2/neu-positive tumors.	tBID	84-88	erb-b2 receptor tyrosine kinase 2	Homo sapiens	293-297
18246124-4	2008	In addition, 2-ME exposure resulted in an increase in mitochondrial membrane potential, increased apoptosis, accompanied by higher activation of caspase-3, -9, cleavage of Bid to tBid and protein poly(ADP-ribose) polymerase (PARP) cleavage in HeLa cells lacking MTS-hOGG1.	tBID	179-183	BH3 interacting domain death agonist	Homo sapiens	172-175
18547146-6	2008	We examined the mechanism of Bax activation by tBid and its inhibition by Bcl-XL using full-length recombinant proteins and measuring permeabilization of liposomes and mitochondria in vitro.	tBID	47-51	BCL2 associated X, apoptosis regulator	Homo sapiens	29-32
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
18547146-10	2008	Bcl-XL competes with Bax for the activation of soluble, monomeric Bax through interaction with membranes, tBid, or t-Bid-activated Bax, thereby inhibiting Bax binding to membranes, oligomerization, and membrane permeabilization.	tBID	106-110	BCL2 like 1	Homo sapiens	0-6
18547146-10	2008	Bcl-XL competes with Bax for the activation of soluble, monomeric Bax through interaction with membranes, tBid, or t-Bid-activated Bax, thereby inhibiting Bax binding to membranes, oligomerization, and membrane permeabilization.	tBID	106-110	BCL2 associated X, apoptosis regulator	Homo sapiens	21-24
18547146-10	2008	Bcl-XL competes with Bax for the activation of soluble, monomeric Bax through interaction with membranes, tBid, or t-Bid-activated Bax, thereby inhibiting Bax binding to membranes, oligomerization, and membrane permeabilization.	tBID	106-110	BCL2 associated X, apoptosis regulator	Homo sapiens	66-69
18547146-10	2008	Bcl-XL competes with Bax for the activation of soluble, monomeric Bax through interaction with membranes, tBid, or t-Bid-activated Bax, thereby inhibiting Bax binding to membranes, oligomerization, and membrane permeabilization.	tBID	106-110	BCL2 associated X, apoptosis regulator	Homo sapiens	66-69
18547146-10	2008	Bcl-XL competes with Bax for the activation of soluble, monomeric Bax through interaction with membranes, tBid, or t-Bid-activated Bax, thereby inhibiting Bax binding to membranes, oligomerization, and membrane permeabilization.	tBID	106-110	BCL2 associated X, apoptosis regulator	Homo sapiens	66-69
18547146-12	2008	By out-competing Bax for the interactions leading to membrane permeabilization, Bcl-XL ties up both tBid and Bax in nonproductive interactions and inhibits Bax binding to membranes.	tBID	100-104	BCL2 associated X, apoptosis regulator	Homo sapiens	17-20
18547146-12	2008	By out-competing Bax for the interactions leading to membrane permeabilization, Bcl-XL ties up both tBid and Bax in nonproductive interactions and inhibits Bax binding to membranes.	tBID	100-104	BCL2 like 1	Homo sapiens	80-86
18358005-1	2008	In tumor necrosis factor-alpha (TNF-alpha)-induced apoptosis, tBid is targeted to mitochondria and causes cytochrome c release.	tBID	62-66	tumor necrosis factor	Homo sapiens	3-30
18358005-1	2008	In tumor necrosis factor-alpha (TNF-alpha)-induced apoptosis, tBid is targeted to mitochondria and causes cytochrome c release.	tBID	62-66	tumor necrosis factor	Homo sapiens	32-41
18358005-1	2008	In tumor necrosis factor-alpha (TNF-alpha)-induced apoptosis, tBid is targeted to mitochondria and causes cytochrome c release.	tBID	62-66	cytochrome c, somatic	Homo sapiens	106-118
18358005-2	2008	We investigated the regulation of tBid-induced cytochrome c release and apoptosis by phospholipid scramblase 3 (PLS3).	tBID	34-38	cytochrome c, somatic	Homo sapiens	47-59
18358005-2	2008	We investigated the regulation of tBid-induced cytochrome c release and apoptosis by phospholipid scramblase 3 (PLS3).	tBID	34-38	phospholipid scramblase 3	Homo sapiens	85-110
18358005-2	2008	We investigated the regulation of tBid-induced cytochrome c release and apoptosis by phospholipid scramblase 3 (PLS3).	tBID	34-38	phospholipid scramblase 3	Homo sapiens	112-116
18358005-3	2008	Overexpression of PLS3 enhanced, whereas downregulation of PLS3 delayed, TNF-alpha-induced apoptosis and targeting of tBid to mitochondria.	tBID	118-122	phospholipid scramblase 3	Homo sapiens	18-22
18358005-4	2008	On the basis of the theory that tBid targets mitochondrial cardiolipin, we hypothesize that PLS3 enhances translocation of cardiolipin to the mitochondrial surface to facilitate tBid targeting.	tBID	32-36	phospholipid scramblase 3	Homo sapiens	92-96
18358005-4	2008	On the basis of the theory that tBid targets mitochondrial cardiolipin, we hypothesize that PLS3 enhances translocation of cardiolipin to the mitochondrial surface to facilitate tBid targeting.	tBID	178-182	phospholipid scramblase 3	Homo sapiens	92-96
18358005-7	2008	Determination of the tBid binding capacity on the mitochondrial surface by FITC-labeled tBid(G94E) also confirmed that tBid binding capacity increased upon PLS3 overexpression and decreased with downregulation of PLS3.	tBID	21-25	phospholipid scramblase 3	Homo sapiens	156-160
18358005-7	2008	Determination of the tBid binding capacity on the mitochondrial surface by FITC-labeled tBid(G94E) also confirmed that tBid binding capacity increased upon PLS3 overexpression and decreased with downregulation of PLS3.	tBID	21-25	phospholipid scramblase 3	Homo sapiens	213-217
18358005-7	2008	Determination of the tBid binding capacity on the mitochondrial surface by FITC-labeled tBid(G94E) also confirmed that tBid binding capacity increased upon PLS3 overexpression and decreased with downregulation of PLS3.	tBID	88-92	phospholipid scramblase 3	Homo sapiens	156-160
18358005-7	2008	Determination of the tBid binding capacity on the mitochondrial surface by FITC-labeled tBid(G94E) also confirmed that tBid binding capacity increased upon PLS3 overexpression and decreased with downregulation of PLS3.	tBID	88-92	phospholipid scramblase 3	Homo sapiens	156-160
18358005-8	2008	PLS3 activity, determined by a lipid flip-flop assay, was activated by calcium and tBid but inhibited by Bcl-2.	tBID	83-87	phospholipid scramblase 3	Homo sapiens	0-4
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
18358005-12	2008	These studies thus establish PLS3 as an important downstream effector of Bcl-2 and tBid in apoptosis.	tBID	83-87	phospholipid scramblase 3	Homo sapiens	29-33
18084240-4	2008	Using this assay, we studied how the lipid composition of membranes affects tBid-induced Bax activation in vitro with pure liposomes.	tBID	76-80	BCL2 associated X, apoptosis regulator	Homo sapiens	89-92
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
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 associated X, apoptosis regulator	Homo sapiens	105-108
18195012-7	2008	In contrast, tBID alone potently assisted BAX to permeabilize membranes at least in part by producing a structural distortion in the lipid bilayer via BH3-independent interaction of tBID with cardiolipin.	tBID	13-17	BCL2 associated X, apoptosis regulator	Homo sapiens	42-45
18195012-7	2008	In contrast, tBID alone potently assisted BAX to permeabilize membranes at least in part by producing a structural distortion in the lipid bilayer via BH3-independent interaction of tBID with cardiolipin.	tBID	182-186	BCL2 associated X, apoptosis regulator	Homo sapiens	42-45
18195012-8	2008	Together, these results support the notion that BIM and tBID follow different strategies to trigger BAX-driven mitochondrial outer membrane permeabilization with strong potency.	tBID	56-60	BCL2 associated X, apoptosis regulator	Homo sapiens	100-103
18191430-8	2008	Diclofenac also induced early Bid activation (tBid formation, 6 h), which is an upstream mechanism that initiates Bax activation and mitochondrial translocation.	tBID	46-50	BH3 interacting domain death agonist	Homo sapiens	30-33
18191430-8	2008	Diclofenac also induced early Bid activation (tBid formation, 6 h), which is an upstream mechanism that initiates Bax activation and mitochondrial translocation.	tBID	46-50	BCL2 associated X, apoptosis regulator	Homo sapiens	114-117
18084240-7	2008	When incubated with tBid, mitochondria isolated from U18666A-treated cells showed a delay in the release of Smac/Diablo and Cytochrome c, as well as in Bax oligomerization.	tBID	20-24	diablo IAP-binding mitochondrial protein	Homo sapiens	108-112
18084240-7	2008	When incubated with tBid, mitochondria isolated from U18666A-treated cells showed a delay in the release of Smac/Diablo and Cytochrome c, as well as in Bax oligomerization.	tBID	20-24	diablo IAP-binding mitochondrial protein	Homo sapiens	113-119
18084240-7	2008	When incubated with tBid, mitochondria isolated from U18666A-treated cells showed a delay in the release of Smac/Diablo and Cytochrome c, as well as in Bax oligomerization.	tBID	20-24	cytochrome c, somatic	Homo sapiens	124-136
18084240-7	2008	When incubated with tBid, mitochondria isolated from U18666A-treated cells showed a delay in the release of Smac/Diablo and Cytochrome c, as well as in Bax oligomerization.	tBID	20-24	BCL2 associated X, apoptosis regulator	Homo sapiens	152-155
18252800-1	2008	Truncated Bid (tBid) releases cytochrome c from mitochondria by inducing Bak (and Bax) pore formation in the outer membrane.	tBID	15-19	BH3 interacting domain death agonist	Homo sapiens	10-13
18252800-1	2008	Truncated Bid (tBid) releases cytochrome c from mitochondria by inducing Bak (and Bax) pore formation in the outer membrane.	tBID	15-19	cytochrome c, somatic	Homo sapiens	30-42
18252800-1	2008	Truncated Bid (tBid) releases cytochrome c from mitochondria by inducing Bak (and Bax) pore formation in the outer membrane.	tBID	15-19	BCL2 antagonist/killer 1	Homo sapiens	73-76
18252800-1	2008	Truncated Bid (tBid) releases cytochrome c from mitochondria by inducing Bak (and Bax) pore formation in the outer membrane.	tBID	15-19	BCL2 associated X, apoptosis regulator	Homo sapiens	82-85
18252800-2	2008	An important issue is whether a second tBid action, independent of Bak and Bax, is also required to enhance cytochrome c mobility in the intermembrane spaces.	tBID	39-43	cytochrome c, somatic	Homo sapiens	108-120
18252800-4	2008	Cytochrome c diffusibility in the intermembrane spaces was unaffected by changes in [tBid] over the range 0.5-19.0 pmol per mg of mitochondrial protein, when tBid-dependent Bak activation was increased several-thousand fold.	tBID	158-162	BCL2 antagonist/killer 1	Homo sapiens	173-176
18252800-7	2008	Basal cytochrome c diffusibility in the intermembrane spaces in the absence of tBid was determined to be approximately 0.2 minute(-1), which is sufficient to support cytochrome c release with a half-time of 3.4 minutes.	tBID	79-83	cytochrome c, somatic	Homo sapiens	6-18
18252800-8	2008	It is concluded that tBid has a monofunctional action at low concentrations and, more generally, that the basal cytochrome c diffusibility in the intermembrane spaces is adequate for rapid and complete cytochrome c release irrespective of the mode of outer membrane permeabilisation.	tBID	21-25	cytochrome c, somatic	Homo sapiens	112-124
18252800-8	2008	It is concluded that tBid has a monofunctional action at low concentrations and, more generally, that the basal cytochrome c diffusibility in the intermembrane spaces is adequate for rapid and complete cytochrome c release irrespective of the mode of outer membrane permeabilisation.	tBID	21-25	cytochrome c, somatic	Homo sapiens	202-214
17724464-0	2008	Bfl-1/A1 functions, similar to Mcl-1, as a selective tBid and Bak antagonist.	tBID	53-57	BCL2 related protein A1	Homo sapiens	0-8
17724464-3	2008	We demonstrate that in living cells Bfl-1 selectively interacts with Bak and tBid, but not with Bax or Bid.	tBID	77-81	BCL2 related protein A1	Homo sapiens	36-41
17724464-5	2008	We also show that Bfl-1 blocks tumor necrosis factor-alpha (TNFalpha)-induced activation of Bax indirectly, via association with tBid.	tBID	129-133	BCL2 related protein A1	Homo sapiens	18-23
17724464-5	2008	We also show that Bfl-1 blocks tumor necrosis factor-alpha (TNFalpha)-induced activation of Bax indirectly, via association with tBid.	tBID	129-133	tumor necrosis factor	Homo sapiens	31-58
17724464-5	2008	We also show that Bfl-1 blocks tumor necrosis factor-alpha (TNFalpha)-induced activation of Bax indirectly, via association with tBid.	tBID	129-133	tumor necrosis factor	Homo sapiens	60-68
17724464-5	2008	We also show that Bfl-1 blocks tumor necrosis factor-alpha (TNFalpha)-induced activation of Bax indirectly, via association with tBid.	tBID	129-133	BCL2 associated X, apoptosis regulator	Homo sapiens	92-95
17724464-6	2008	C-terminal deletion decreased Bfl-1"s interaction with Bak and tBid and reduced its ability to suppress Bak- and tBid-mediated cell death.	tBID	63-67	BCL2 related protein A1	Homo sapiens	30-35
17724464-6	2008	C-terminal deletion decreased Bfl-1"s interaction with Bak and tBid and reduced its ability to suppress Bak- and tBid-mediated cell death.	tBID	113-117	BCL2 related protein A1	Homo sapiens	30-35
17724464-8	2008	Bfl-1 associates with tBid to prevent activation of proapoptotic Bax and Bak, and it also interacts directly with Bak to antagonize Bak-mediated cell death, similar to Mcl-1.	tBID	22-26	BCL2 related protein A1	Homo sapiens	0-5
18667818-8	2008	Sanguinarine also promoted the activation of caspase-8 and truncation of Bid (tBid).	tBID	78-82	BH3 interacting domain death agonist	Homo sapiens	73-76
18098270-9	2008	Combination therapy activated the receptor-mediated pathway of apoptosis with induction of TNF-alpha, activation of caspase-8, and cleavage of Bid to tBid.	tBID	150-154	BH3 interacting domain death agonist	Homo sapiens	143-146
17765974-8	2008	Moreover, GzmH directly processes Bid to produce the active form tBid leading to cytochrome c release.	tBID	65-69	granzyme H	Homo sapiens	10-14
17765974-8	2008	Moreover, GzmH directly processes Bid to produce the active form tBid leading to cytochrome c release.	tBID	65-69	BH3 interacting domain death agonist	Homo sapiens	34-37
17765974-8	2008	Moreover, GzmH directly processes Bid to produce the active form tBid leading to cytochrome c release.	tBID	65-69	cytochrome c, somatic	Homo sapiens	81-93
18173728-6	2008	The Bid cleavage coincided with a translocation of tBid from cytoplasm to mitochondria.	tBID	51-55	BH3 interacting domain death agonist	Homo sapiens	4-7
17767197-5	2008	Cotreatment with TAM and TRAIL in breast cancer cells decreased the levels of antiapoptotic proteins including FLIPs and Bcl-2, and enhanced the levels of proapoptotic proteins such as FADD, caspase 8, tBid, Bax and caspase 9.	tBID	202-206	TNF superfamily member 10	Homo sapiens	25-30
17633456-12	2007	Bax and tBid then agregate on mitochondrial membrane, which in turn causes a decrease of mitochondrial transmembrane potential and release of cytochrome C into cytoplasm.	tBID	8-12	cytochrome c, somatic	Homo sapiens	142-154
18166654-3	2007	We found that, upon Bid cleavage, the N-terminal fragment (tBid-N) is ubiquitinated and degraded, thus freeing the BH3 domain in the C-terminal fragment (tBid-C).	tBID	59-63	BH3 interacting domain death agonist	Homo sapiens	20-23
18166654-3	2007	We found that, upon Bid cleavage, the N-terminal fragment (tBid-N) is ubiquitinated and degraded, thus freeing the BH3 domain in the C-terminal fragment (tBid-C).	tBID	154-158	BH3 interacting domain death agonist	Homo sapiens	20-23
17375293-3	2007	Proteolysis of the N-terminus (encompassing H1 and H2) of Bid by caspase 8 in apoptosis yields activated "tBid" (truncated Bid), which translocates to the mitochondria and induces the efflux of cytochrome c.	tBID	106-110	BH3 interacting domain death agonist	Homo sapiens	58-61
17375293-3	2007	Proteolysis of the N-terminus (encompassing H1 and H2) of Bid by caspase 8 in apoptosis yields activated "tBid" (truncated Bid), which translocates to the mitochondria and induces the efflux of cytochrome c.	tBID	106-110	caspase 8	Homo sapiens	65-74
17375293-3	2007	Proteolysis of the N-terminus (encompassing H1 and H2) of Bid by caspase 8 in apoptosis yields activated "tBid" (truncated Bid), which translocates to the mitochondria and induces the efflux of cytochrome c.	tBID	106-110	cytochrome c, somatic	Homo sapiens	194-206
17375293-4	2007	The release of cytochrome c from mitochondria to the cytosol constitutes a critical control point in apoptosis that is regulated by interaction of tBid protein with mitochondrial membrane.	tBID	147-151	cytochrome c, somatic	Homo sapiens	15-27
17698840-1	2007	Previous studies have suggested that Mcl-1, an antiapoptotic Bcl-2 homolog that does not exhibit appreciable affinity for the caspase 8-generated C-terminal Bid fragment (tBid), diminishes sensitivity to tumor necrosis factor-alpha-related apoptosis-inducing ligand (TRAIL).	tBID	171-175	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	37-42
17698840-3	2007	Affinity purification/immunoblotting assays using K562 human leukemia cells, which contain Mcl-1 and Bcl-x(L) as the predominant antiapoptotic Bcl-2 homologs, demonstrated that TRAIL treatment resulted in binding of tBid to Bcl-x(L) but not Mcl-1.	tBID	216-220	TNF superfamily member 10	Homo sapiens	177-182
17893612-3	2007	Bid is a proapoptotic Bcl-2 family member that is cleaved to its active form, tBid, by caspase 8 and granzyme B.	tBID	78-82	granzyme B	Rattus norvegicus	101-111
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	28-32	BCL2 associated X, apoptosis regulator	Homo sapiens	155-158
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
17825286-9	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 associated X, apoptosis regulator	Homo sapiens	155-158
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
17893612-3	2007	Bid is a proapoptotic Bcl-2 family member that is cleaved to its active form, tBid, by caspase 8 and granzyme B.	tBID	78-82	BH3 interacting domain death agonist	Rattus norvegicus	0-3
17893612-3	2007	Bid is a proapoptotic Bcl-2 family member that is cleaved to its active form, tBid, by caspase 8 and granzyme B.	tBID	78-82	BCL2, apoptosis regulator	Rattus norvegicus	22-27
17893612-3	2007	Bid is a proapoptotic Bcl-2 family member that is cleaved to its active form, tBid, by caspase 8 and granzyme B.	tBID	78-82	caspase 8	Rattus norvegicus	87-96
17520191-1	2007	Bid, a member of the pro-apoptotic Bcl-2 protein family, is activated through caspase-8-mediated cleavage into a truncated form (p15 tBid) during TNF-alpha(tumor necrosis factor alpha)-induced apoptosis.	tBID	133-137	BH3 interacting domain death agonist	Homo sapiens	0-3
17520191-1	2007	Bid, a member of the pro-apoptotic Bcl-2 protein family, is activated through caspase-8-mediated cleavage into a truncated form (p15 tBid) during TNF-alpha(tumor necrosis factor alpha)-induced apoptosis.	tBID	133-137	caspase 8	Homo sapiens	78-87
17520191-1	2007	Bid, a member of the pro-apoptotic Bcl-2 protein family, is activated through caspase-8-mediated cleavage into a truncated form (p15 tBid) during TNF-alpha(tumor necrosis factor alpha)-induced apoptosis.	tBID	133-137	cyclin dependent kinase inhibitor 2B	Homo sapiens	129-132
17520191-1	2007	Bid, a member of the pro-apoptotic Bcl-2 protein family, is activated through caspase-8-mediated cleavage into a truncated form (p15 tBid) during TNF-alpha(tumor necrosis factor alpha)-induced apoptosis.	tBID	133-137	tumor necrosis factor	Homo sapiens	146-183
17520191-2	2007	Activated tBid can induce Bax oligomerization and translocation to mitochondria, triggering the release of cytochrome c, caspase-3 activation and cell apoptosis.	tBID	10-14	BCL2 associated X, apoptosis regulator	Homo sapiens	26-29
17520191-2	2007	Activated tBid can induce Bax oligomerization and translocation to mitochondria, triggering the release of cytochrome c, caspase-3 activation and cell apoptosis.	tBID	10-14	cytochrome c, somatic	Homo sapiens	107-119
17520191-2	2007	Activated tBid can induce Bax oligomerization and translocation to mitochondria, triggering the release of cytochrome c, caspase-3 activation and cell apoptosis.	tBID	10-14	caspase 3	Homo sapiens	121-130
17520191-3	2007	However, it is debatable that whether Bid and tBid can interact directly with Bax in living cells.	tBID	46-50	BCL2 associated X, apoptosis regulator	Homo sapiens	78-81
17308307-6	2007	Moreover GzmK targets mitochondria by cleaving Bid to generate its active form tBid, which disrupts the outer mitochondrial membrane leading to the release of cytochrome c and endonuclease G.	tBID	79-83	granzyme K	Homo sapiens	9-13
17308307-6	2007	Moreover GzmK targets mitochondria by cleaving Bid to generate its active form tBid, which disrupts the outer mitochondrial membrane leading to the release of cytochrome c and endonuclease G.	tBID	79-83	BH3 interacting domain death agonist	Homo sapiens	47-50
17308307-6	2007	Moreover GzmK targets mitochondria by cleaving Bid to generate its active form tBid, which disrupts the outer mitochondrial membrane leading to the release of cytochrome c and endonuclease G.	tBID	79-83	cytochrome c, somatic	Homo sapiens	159-171
17308307-6	2007	Moreover GzmK targets mitochondria by cleaving Bid to generate its active form tBid, which disrupts the outer mitochondrial membrane leading to the release of cytochrome c and endonuclease G.	tBID	79-83	endonuclease G	Homo sapiens	176-190
17762183-8	2007	These results show that the alkaline sondition (pH=8.0) induces cell apoptosis by activating caspase-8, which cleaves Bid to tBid, tBid translocation to mitochondria, and then activating the caspase-3 in the ASTC-a-1 cells.	tBID	125-129	caspase 8	Homo sapiens	93-102
17440103-3	2007	Our data show that sanguinarine treatment of PEL cells results in up-regulation of death receptor 5 (DR5) expression via generation of reactive oxygen species (ROS) and causes activation of caspase-8 and truncation of Bid (tBid).	tBID	223-227	BH3 interacting domain death agonist	Homo sapiens	218-221
17440103-4	2007	Subsequently, tBid translocates to the mitochondria causing conformational changes in Bax, leading to loss of mitochondrial membrane potential and release of cytochrome c to the cytosol.	tBID	14-18	BCL2 associated X, apoptosis regulator	Homo sapiens	86-89
17440103-4	2007	Subsequently, tBid translocates to the mitochondria causing conformational changes in Bax, leading to loss of mitochondrial membrane potential and release of cytochrome c to the cytosol.	tBID	14-18	cytochrome c, somatic	Homo sapiens	158-170
16888643-8	2007	Apoptosis is thought to progress via binding of truncated Bid (tBid) to mitochondrial CL, followed by CL oxidation which results in <protein-id="54205">cyt.	tBID	63-67	BH3 interacting domain death agonist	Homo sapiens	58-61
17130128-10	2007	In isolated mitochondria, Nutlin-3 inhibited cytochrome c release induced by Ca2+, Bim peptide, and recombinant tBid.	tBID	112-116	cytochrome c, somatic	Homo sapiens	45-57
17762183-8	2007	These results show that the alkaline sondition (pH=8.0) induces cell apoptosis by activating caspase-8, which cleaves Bid to tBid, tBid translocation to mitochondria, and then activating the caspase-3 in the ASTC-a-1 cells.	tBID	125-129	BH3 interacting domain death agonist	Homo sapiens	118-121
17762183-8	2007	These results show that the alkaline sondition (pH=8.0) induces cell apoptosis by activating caspase-8, which cleaves Bid to tBid, tBid translocation to mitochondria, and then activating the caspase-3 in the ASTC-a-1 cells.	tBID	125-129	caspase 3	Homo sapiens	191-200
17762183-8	2007	These results show that the alkaline sondition (pH=8.0) induces cell apoptosis by activating caspase-8, which cleaves Bid to tBid, tBid translocation to mitochondria, and then activating the caspase-3 in the ASTC-a-1 cells.	tBID	131-135	caspase 8	Homo sapiens	93-102
17762183-8	2007	These results show that the alkaline sondition (pH=8.0) induces cell apoptosis by activating caspase-8, which cleaves Bid to tBid, tBid translocation to mitochondria, and then activating the caspase-3 in the ASTC-a-1 cells.	tBID	131-135	caspase 3	Homo sapiens	191-200
17154276-4	2007	In mammalian cells, cross-talk between the main apoptotic pathways (the mitochondrial and the death domain protein pathways) involve the pro-death protein BID, the active form of which, tBID, results from protease truncation and translocation to mitochondria.	tBID	186-190	BH3 interacting domain death agonist	Homo sapiens	155-158
16826547-3	2006	In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID"s transformation to tBID by cleavage with caspase 8, required for tBID"s pro-apoptotic action on mitochondria, thereby releasing cytochrome c.	tBID	185-189	cytochrome c, somatic	Homo sapiens	294-306
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
17005564-0	2006	tBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formation.	tBID	0-4	BCL2 associated X, apoptosis regulator	Homo sapiens	87-90
16708390-0	2006	Adenovirus-mediated tBid overexpression results in therapeutic effects on p53-resistant hepatocellular carcinoma.	tBID	20-24	tumor protein p53	Homo sapiens	74-77
16708390-4	2006	The aim of our study is to evaluate the possibility of using truncated Bid (tBid) as a novel therapy for HCC treatment.	tBID	76-80	BH3 interacting domain death agonist	Homo sapiens	71-74
16787424-5	2006	Regulation of this tBid- and Bax-induced increase in pore size of VDAC is a significant step to control cell death induced by cytochrome c. In this work, we have shown, through bilayer electrophysiological experiments, that the increase in VDAC conductance as a result of its interaction with Bax and tBid is reduced because of the action of cyclic AMP-dependent protein kinase A (PKA) in the presence of ATP.	tBID	19-23	BCL2 associated X, apoptosis regulator	Rattus norvegicus	293-296
16787424-5	2006	Regulation of this tBid- and Bax-induced increase in pore size of VDAC is a significant step to control cell death induced by cytochrome c. In this work, we have shown, through bilayer electrophysiological experiments, that the increase in VDAC conductance as a result of its interaction with Bax and tBid is reduced because of the action of cyclic AMP-dependent protein kinase A (PKA) in the presence of ATP.	tBID	301-305	BCL2 associated X, apoptosis regulator	Rattus norvegicus	29-32
16787424-5	2006	Regulation of this tBid- and Bax-induced increase in pore size of VDAC is a significant step to control cell death induced by cytochrome c. In this work, we have shown, through bilayer electrophysiological experiments, that the increase in VDAC conductance as a result of its interaction with Bax and tBid is reduced because of the action of cyclic AMP-dependent protein kinase A (PKA) in the presence of ATP.	tBID	301-305	BCL2 associated X, apoptosis regulator	Rattus norvegicus	293-296
17030378-5	2007	SC-1 also activated intrinsic pathway via increase of pro-apoptotic (tBid, Bak and Bax) and decrease of anti-apoptotic (Bcl-2 and Bcl-x(L)) proteins on mitochondria, disruption of mitochondrial membrane potential, release of cytochrome c and Smac (second mitochondria-derived activator of caspase/direct IAP binding protein with low PI) from mitochondria, and activation of caspase 9.	tBID	69-73	transcription factor 19	Homo sapiens	0-4
16988947-8	2006	Activation of caspase-8 cleaved Bid to truncated Bid (tBid) in cells treated with EGC and EGCG.	tBID	54-58	caspase 8	Homo sapiens	14-23
16988947-8	2006	Activation of caspase-8 cleaved Bid to truncated Bid (tBid) in cells treated with EGC and EGCG.	tBID	54-58	BH3 interacting domain death agonist	Homo sapiens	32-35
16988947-8	2006	Activation of caspase-8 cleaved Bid to truncated Bid (tBid) in cells treated with EGC and EGCG.	tBID	54-58	BH3 interacting domain death agonist	Homo sapiens	49-52
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
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	BH3 interacting domain death agonist	Homo sapiens	84-87
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 associated X, apoptosis regulator	Homo sapiens	125-128
16987815-6	2006	Strikingly, nanomolar concentrations of a synthetic BID BH3 peptide that is chemically tethered to the liposomal membrane activated BAX almost as efficiently as tBID itself.	tBID	161-165	BH3 interacting domain death agonist	Homo sapiens	52-55
16987815-7	2006	These results highlight the importance of membrane targeting of the BID BH3 domain in tBID-mediated BAX activation and support a model in which tBID engages BAX to trigger its pro-apoptotic activity.	tBID	86-90	BH3 interacting domain death agonist	Homo sapiens	68-71
16987815-7	2006	These results highlight the importance of membrane targeting of the BID BH3 domain in tBID-mediated BAX activation and support a model in which tBID engages BAX to trigger its pro-apoptotic activity.	tBID	86-90	BCL2 associated X, apoptosis regulator	Homo sapiens	100-103
16987815-7	2006	These results highlight the importance of membrane targeting of the BID BH3 domain in tBID-mediated BAX activation and support a model in which tBID engages BAX to trigger its pro-apoptotic activity.	tBID	86-90	BCL2 associated X, apoptosis regulator	Homo sapiens	157-160
16987815-7	2006	These results highlight the importance of membrane targeting of the BID BH3 domain in tBID-mediated BAX activation and support a model in which tBID engages BAX to trigger its pro-apoptotic activity.	tBID	144-148	BH3 interacting domain death agonist	Homo sapiens	68-71
16987815-7	2006	These results highlight the importance of membrane targeting of the BID BH3 domain in tBID-mediated BAX activation and support a model in which tBID engages BAX to trigger its pro-apoptotic activity.	tBID	144-148	BCL2 associated X, apoptosis regulator	Homo sapiens	100-103
16987815-7	2006	These results highlight the importance of membrane targeting of the BID BH3 domain in tBID-mediated BAX activation and support a model in which tBID engages BAX to trigger its pro-apoptotic activity.	tBID	144-148	BCL2 associated X, apoptosis regulator	Homo sapiens	157-160
17005564-2	2006	BH3-only protein, tBid, activates pro-apoptotic Bax to release cytochrome c from mitochondria.	tBID	18-22	BCL2 associated X, apoptosis regulator	Homo sapiens	48-51
17005564-2	2006	BH3-only protein, tBid, activates pro-apoptotic Bax to release cytochrome c from mitochondria.	tBID	18-22	cytochrome c, somatic	Homo sapiens	63-75
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
17005564-3	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 associated X, apoptosis regulator	Homo sapiens	167-170
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	cytochrome c, somatic	Homo sapiens	184-196
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
16485030-9	2006	We conclude that the MAPK pathway inhibits TRAIL-induced apoptosis in MCF-7 cells by prohibiting anchoring of tBid to the mitochondrial membrane.	tBID	110-114	TNF superfamily member 10	Homo sapiens	43-48
17002876-0	2006	Differential efflux of mitochondrial endonuclease G by hNoxa and tBid.	tBID	65-69	endonuclease G	Homo sapiens	23-51
17002876-5	2006	We have demonstrated that endonuclease G activities are not detectable among the proteins released from isolated mitochondria by hNoxa but are detectable in that by tBid.	tBID	165-169	endonuclease G	Homo sapiens	26-40
16741989-5	2006	The cleavage product of Bid, tBid, appeared in the cytosol and to a lesser extent in the mitochondria.	tBID	29-33	BH3 interacting domain death agonist	Homo sapiens	24-27
16826547-3	2006	In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID"s transformation to tBID by cleavage with caspase 8, required for tBID"s pro-apoptotic action on mitochondria, thereby releasing cytochrome c.	tBID	185-189	BH3 interacting domain death agonist	Homo sapiens	15-18
16826547-3	2006	In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID"s transformation to tBID by cleavage with caspase 8, required for tBID"s pro-apoptotic action on mitochondria, thereby releasing cytochrome c.	tBID	185-189	BH3 interacting domain death agonist	Homo sapiens	161-164
16826547-3	2006	In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID"s transformation to tBID by cleavage with caspase 8, required for tBID"s pro-apoptotic action on mitochondria, thereby releasing cytochrome c.	tBID	185-189	caspase 8	Homo sapiens	207-216
16826547-3	2006	In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID"s transformation to tBID by cleavage with caspase 8, required for tBID"s pro-apoptotic action on mitochondria, thereby releasing cytochrome c.	tBID	231-235	BH3 interacting domain death agonist	Homo sapiens	15-18
16826547-3	2006	In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID"s transformation to tBID by cleavage with caspase 8, required for tBID"s pro-apoptotic action on mitochondria, thereby releasing cytochrome c.	tBID	231-235	BH3 interacting domain death agonist	Homo sapiens	161-164
16826547-3	2006	In full-length BID, the putative hydrophobic binding surface of its BH3 motif is substantially occluded by intramolecular contacts, many of which are removed on BID"s transformation to tBID by cleavage with caspase 8, required for tBID"s pro-apoptotic action on mitochondria, thereby releasing cytochrome c.	tBID	231-235	caspase 8	Homo sapiens	207-216
16681997-5	2006	The continuing reduction of Bid protein and the gradual increase of tBid protein also indicated that a time-dependent increased turn-over of Bid protein into tBid.	tBID	158-162	BH3 interacting domain death agonist	Homo sapiens	69-72
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
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 associated X, apoptosis regulator	Homo sapiens	102-105
16684533-3	2006	In this study, justicidin A activated caspase-8 to increase tBid, disrupted mitochondrial membrane potential (Delta psi(m)), and caused the release of cytochrome c and Smac/DIABLO in Hep 3B and Hep G2 cells.	tBID	60-64	caspase 8	Homo sapiens	38-47
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
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	interferon gamma	Mus musculus	89-98
16092941-1	2005	Cleaved or truncated BID (tBID) is known to oligomerize both BAK and BAX.	tBID	26-30	BH3 interacting domain death agonist	Rattus norvegicus	21-24
16380381-1	2006	Engagement of death receptors such as tumor necrosis factor-R1 and Fas brings about the cleavage of cytosolic Bid to truncated Bid (tBid), which translocates to mitochondria to activate Bax/Bak, resulting in the release of cytochrome c.	tBID	132-136	BH3 interacting domain death agonist	Homo sapiens	110-113
16380381-1	2006	Engagement of death receptors such as tumor necrosis factor-R1 and Fas brings about the cleavage of cytosolic Bid to truncated Bid (tBid), which translocates to mitochondria to activate Bax/Bak, resulting in the release of cytochrome c.	tBID	132-136	BH3 interacting domain death agonist	Homo sapiens	127-130
16380381-1	2006	Engagement of death receptors such as tumor necrosis factor-R1 and Fas brings about the cleavage of cytosolic Bid to truncated Bid (tBid), which translocates to mitochondria to activate Bax/Bak, resulting in the release of cytochrome c.	tBID	132-136	BCL2 associated X, apoptosis regulator	Homo sapiens	186-189
16380381-1	2006	Engagement of death receptors such as tumor necrosis factor-R1 and Fas brings about the cleavage of cytosolic Bid to truncated Bid (tBid), which translocates to mitochondria to activate Bax/Bak, resulting in the release of cytochrome c.	tBID	132-136	BCL2 antagonist/killer 1	Homo sapiens	190-193
16380381-1	2006	Engagement of death receptors such as tumor necrosis factor-R1 and Fas brings about the cleavage of cytosolic Bid to truncated Bid (tBid), which translocates to mitochondria to activate Bax/Bak, resulting in the release of cytochrome c.	tBID	132-136	cytochrome c, somatic	Homo sapiens	223-235
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
16380381-3	2006	Here, we have identified the anti-apoptotic Bcl-2 family member Mcl-1 as a potent tBid-binding partner.	tBID	82-86	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	64-69
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	74-78	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	107-112
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	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	166-171
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
16380381-5	2006	In vitro studies using isolated mitochondria and recombinant proteins demonstrate that Mcl-1 strongly inhibits tBid-induced cytochrome c release.	tBID	111-115	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	87-92
16380381-5	2006	In vitro studies using isolated mitochondria and recombinant proteins demonstrate that Mcl-1 strongly inhibits tBid-induced cytochrome c release.	tBID	111-115	cytochrome c, somatic	Homo sapiens	124-136
16380381-6	2006	In addition to its ability to interact directly with Bax and Bak, tBid also binds Mcl-1 and displaces Bak from the Mcl-1-Bak complex.	tBID	66-70	BCL2 associated X, apoptosis regulator	Homo sapiens	53-56
16380381-6	2006	In addition to its ability to interact directly with Bax and Bak, tBid also binds Mcl-1 and displaces Bak from the Mcl-1-Bak complex.	tBID	66-70	BCL2 antagonist/killer 1	Homo sapiens	61-64
16380381-6	2006	In addition to its ability to interact directly with Bax and Bak, tBid also binds Mcl-1 and displaces Bak from the Mcl-1-Bak complex.	tBID	66-70	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	82-87
16380381-6	2006	In addition to its ability to interact directly with Bax and Bak, tBid also binds Mcl-1 and displaces Bak from the Mcl-1-Bak complex.	tBID	66-70	BCL2 antagonist/killer 1	Homo sapiens	102-105
16380381-6	2006	In addition to its ability to interact directly with Bax and Bak, tBid also binds Mcl-1 and displaces Bak from the Mcl-1-Bak complex.	tBID	66-70	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	115-120
16380381-6	2006	In addition to its ability to interact directly with Bax and Bak, tBid also binds Mcl-1 and displaces Bak from the Mcl-1-Bak complex.	tBID	66-70	BCL2 antagonist/killer 1	Homo sapiens	102-105
16380381-8	2006	Therefore, our study demonstrates a novel regulation of tBid by Mcl-1 through protein-protein interaction in apoptotic signaling from death receptors to mitochondria.	tBID	56-60	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	64-69
16407197-2	2006	Caspase 8-mediated cleavage of the BH3-only protein Bid into a truncated protein (tBid) and subsequent translocation of tBid to mitochondria has been implicated in death receptor signaling.	tBID	82-86	caspase 8	Homo sapiens	0-9
16407197-2	2006	Caspase 8-mediated cleavage of the BH3-only protein Bid into a truncated protein (tBid) and subsequent translocation of tBid to mitochondria has been implicated in death receptor signaling.	tBID	82-86	BH3 interacting domain death agonist	Homo sapiens	52-55
16407197-2	2006	Caspase 8-mediated cleavage of the BH3-only protein Bid into a truncated protein (tBid) and subsequent translocation of tBid to mitochondria has been implicated in death receptor signaling.	tBID	120-124	caspase 8	Homo sapiens	0-9
16407197-2	2006	Caspase 8-mediated cleavage of the BH3-only protein Bid into a truncated protein (tBid) and subsequent translocation of tBid to mitochondria has been implicated in death receptor signaling.	tBID	120-124	BH3 interacting domain death agonist	Homo sapiens	52-55
16407197-3	2006	We utilized a recombinant fluorescence resonance energy transfer (FRET) Bid probe to determine the kinetics of Bid cleavage and tBid translocation during death receptor-induced apoptosis in caspase 3-deficient MCF-7 cells.	tBID	128-132	caspase 3	Homo sapiens	190-199
16407197-5	2006	Cleavage of the Bid-FRET probe coincided with a translocation of tBid to the mitochondria and a collapse of the mitochondrial membrane potential (DeltaPsim).	tBID	65-69	BH3 interacting domain death agonist	Homo sapiens	16-19
16254338-12	2005	In addition, the expression of F1L was essential to inhibit tBid-induced cytochrome c release in both wild-type murine embryonic fibroblasts (MEFs) and Bax-deficient MEFs, indicating that F1L could inhibit apoptosis in the presence and absence of Bax.	tBID	60-64	Hypothetical protein	Vaccinia virus	31-34
16254338-12	2005	In addition, the expression of F1L was essential to inhibit tBid-induced cytochrome c release in both wild-type murine embryonic fibroblasts (MEFs) and Bax-deficient MEFs, indicating that F1L could inhibit apoptosis in the presence and absence of Bax.	tBID	60-64	cytochrome c, somatic	Homo sapiens	73-85
16254338-12	2005	In addition, the expression of F1L was essential to inhibit tBid-induced cytochrome c release in both wild-type murine embryonic fibroblasts (MEFs) and Bax-deficient MEFs, indicating that F1L could inhibit apoptosis in the presence and absence of Bax.	tBID	60-64	BCL2-associated X protein	Mus musculus	152-155
16254338-12	2005	In addition, the expression of F1L was essential to inhibit tBid-induced cytochrome c release in both wild-type murine embryonic fibroblasts (MEFs) and Bax-deficient MEFs, indicating that F1L could inhibit apoptosis in the presence and absence of Bax.	tBID	60-64	Hypothetical protein	Vaccinia virus	188-191
16254338-12	2005	In addition, the expression of F1L was essential to inhibit tBid-induced cytochrome c release in both wild-type murine embryonic fibroblasts (MEFs) and Bax-deficient MEFs, indicating that F1L could inhibit apoptosis in the presence and absence of Bax.	tBID	60-64	BCL2-associated X protein	Mus musculus	247-250
16254338-13	2005	tBid-induced Bak oligomerization and N-terminal exposure of Bak in Bax-deficient MEFs were inhibited during virus infection, as assessed by cross-linking and limited trypsin proteolysis.	tBID	0-4	BCL2-antagonist/killer 1	Mus musculus	13-16
16254338-13	2005	tBid-induced Bak oligomerization and N-terminal exposure of Bak in Bax-deficient MEFs were inhibited during virus infection, as assessed by cross-linking and limited trypsin proteolysis.	tBID	0-4	BCL2-antagonist/killer 1	Mus musculus	60-63
16254338-13	2005	tBid-induced Bak oligomerization and N-terminal exposure of Bak in Bax-deficient MEFs were inhibited during virus infection, as assessed by cross-linking and limited trypsin proteolysis.	tBID	0-4	BCL2-associated X protein	Mus musculus	67-70
16254338-14	2005	Infection with the F1L deletion virus no longer provided protection from tBid-induced Bak activation and apoptosis.	tBID	73-77	Hypothetical protein	Vaccinia virus	19-22
16254338-14	2005	Infection with the F1L deletion virus no longer provided protection from tBid-induced Bak activation and apoptosis.	tBID	73-77	BCL2 antagonist/killer 1	Homo sapiens	86-89
16199525-10	2005	Remarkably, recombinant Bax- or tBid-mediated release of cytochrome c from isolated mitochondria is significantly compromised in the MAP-1 knockdown cells.	tBID	32-36	cytochrome c, somatic	Homo sapiens	57-69
16199525-10	2005	Remarkably, recombinant Bax- or tBid-mediated release of cytochrome c from isolated mitochondria is significantly compromised in the MAP-1 knockdown cells.	tBID	32-36	modulator of apoptosis 1	Homo sapiens	133-138
16179951-5	2005	The pro-apoptotic proteins Bax and tBid antagonize this effect by blocking the biochemical interaction of Bcl-X(L) with the InsP(3)R. These data support a novel model in which Bcl-X(L) is a direct effector of the InsP(3)R, increasing its sensitivity to InsP(3) and enabling ER Ca(2+) release to be more sensitively coupled to extracellular signals.	tBID	35-39	BCL2 like 1	Homo sapiens	106-114
16179951-5	2005	The pro-apoptotic proteins Bax and tBid antagonize this effect by blocking the biochemical interaction of Bcl-X(L) with the InsP(3)R. These data support a novel model in which Bcl-X(L) is a direct effector of the InsP(3)R, increasing its sensitivity to InsP(3) and enabling ER Ca(2+) release to be more sensitively coupled to extracellular signals.	tBID	35-39	BCL2 like 1	Homo sapiens	176-184
16110313-1	2006	We studied the efficiency of the proapoptotic factor tBid, targeted to tumor cells using the promoters of the hTERT, Survivin and Muc1 genes, in killing breast cancer cells.	tBID	53-57	telomerase reverse transcriptase	Homo sapiens	110-115
16110313-1	2006	We studied the efficiency of the proapoptotic factor tBid, targeted to tumor cells using the promoters of the hTERT, Survivin and Muc1 genes, in killing breast cancer cells.	tBID	53-57	mucin 1, cell surface associated	Homo sapiens	130-134
16092941-1	2005	Cleaved or truncated BID (tBID) is known to oligomerize both BAK and BAX.	tBID	26-30	BCL2-antagonist/killer 1	Rattus norvegicus	61-64
16092941-1	2005	Cleaved or truncated BID (tBID) is known to oligomerize both BAK and BAX.	tBID	26-30	BCL2 associated X, apoptosis regulator	Rattus norvegicus	69-72
16092941-2	2005	Previously, BAK and BAX lacing the C-terminal fragment (BAXDeltaC) were shown to induce modest cytochrome c (Cyt c) release from rat brain mitochondria when activated by tBID.	tBID	170-174	BCL2-antagonist/killer 1	Rattus norvegicus	12-15
16092941-2	2005	Previously, BAK and BAX lacing the C-terminal fragment (BAXDeltaC) were shown to induce modest cytochrome c (Cyt c) release from rat brain mitochondria when activated by tBID.	tBID	170-174	BCL2 associated X, apoptosis regulator	Rattus norvegicus	20-23
16092941-3	2005	We now show that tBID plus monomeric full-length BAX induce extensive release of Cyt c, Smac/DIABLO, and Omi/HtrA2 (but not endonuclease G and the apoptosis inducing factor) comparable to the release induced by alamethicin.	tBID	17-21	diablo, IAP-binding mitochondrial protein	Rattus norvegicus	88-92
16092941-3	2005	We now show that tBID plus monomeric full-length BAX induce extensive release of Cyt c, Smac/DIABLO, and Omi/HtrA2 (but not endonuclease G and the apoptosis inducing factor) comparable to the release induced by alamethicin.	tBID	17-21	diablo, IAP-binding mitochondrial protein	Rattus norvegicus	93-99
16092941-3	2005	We now show that tBID plus monomeric full-length BAX induce extensive release of Cyt c, Smac/DIABLO, and Omi/HtrA2 (but not endonuclease G and the apoptosis inducing factor) comparable to the release induced by alamethicin.	tBID	17-21	HtrA serine peptidase 2	Rattus norvegicus	109-114
16092941-9	2005	We propose that tBID plus BAX activate ROS generation, which subsequently augments iPLA(2) activity leading to changes in the OMM that allow translocation of certain mitochondrial proteins from the intermembrane space.	tBID	16-20	phospholipase A2 group VI	Rattus norvegicus	83-90
15500442-6	2005	Although the major action may reside in the C-terminus part, tBid (cleaved Bid), un-cleaved Bid also has pro-apoptotic potential when ectopically expressed in cells or in vitro.	tBID	61-65	BH3 interacting domain death agonist	Homo sapiens	75-78
15846373-0	2005	tBid induces alterations of mitochondrial fatty acid oxidation flux by malonyl-CoA-independent inhibition of carnitine palmitoyltransferase-1.	tBID	0-4	carnitine palmitoyltransferase 1A	Homo sapiens	109-141
15846373-2	2005	We have evaluated changes in lipid metabolism on permeabilized hepatocytes treated with truncated Bid (tBid) in the presence of caspase inhibitors and exogenous cytochrome c.	tBID	103-107	BH3 interacting domain death agonist	Homo sapiens	98-101
15846373-3	2005	The measurement of beta-oxidation flux by labeled palmitate demonstrates that tBid inhibits beta-oxidation, thereby resulting in the accumulation of palmitoyl-coenzyme A (CoA) and depletion of acetyl-carnitine and acylcarnitines, which is pathognomonic for inhibition of carnitine palmitoyltransferase-1 (CPT-1).	tBID	78-82	carnitine palmitoyltransferase 1A	Homo sapiens	271-303
15846373-3	2005	The measurement of beta-oxidation flux by labeled palmitate demonstrates that tBid inhibits beta-oxidation, thereby resulting in the accumulation of palmitoyl-coenzyme A (CoA) and depletion of acetyl-carnitine and acylcarnitines, which is pathognomonic for inhibition of carnitine palmitoyltransferase-1 (CPT-1).	tBID	78-82	carnitine palmitoyltransferase 1A	Homo sapiens	305-310
15846373-4	2005	We also show that tBid decreases CPT-1 activity by a mechanism independent of both malonyl-CoA, the key inhibitory molecule of CPT-1, and Bak and/or Bax, but dependent on cardiolipin decrease.	tBID	18-22	carnitine palmitoyltransferase 1A	Homo sapiens	33-38
15846373-4	2005	We also show that tBid decreases CPT-1 activity by a mechanism independent of both malonyl-CoA, the key inhibitory molecule of CPT-1, and Bak and/or Bax, but dependent on cardiolipin decrease.	tBID	18-22	carnitine palmitoyltransferase 1A	Homo sapiens	127-132
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
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	carnitine palmitoyltransferase 1A	Homo sapiens	56-61
16167168-6	2005	Recently, we have revealed that in apoptotic cells the activated/truncated form of BID, tBID, interacts with a novel, uncharacterized protein named mitochondrial carrier homolog 2 (Mtch2).	tBID	88-92	BH3 interacting domain death agonist	Homo sapiens	83-86
16167168-6	2005	Recently, we have revealed that in apoptotic cells the activated/truncated form of BID, tBID, interacts with a novel, uncharacterized protein named mitochondrial carrier homolog 2 (Mtch2).	tBID	88-92	mitochondrial carrier 2	Homo sapiens	148-179
16167168-6	2005	Recently, we have revealed that in apoptotic cells the activated/truncated form of BID, tBID, interacts with a novel, uncharacterized protein named mitochondrial carrier homolog 2 (Mtch2).	tBID	88-92	mitochondrial carrier 2	Homo sapiens	181-186
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
15899861-0	2005	Mitochondrial carrier homolog 2 is a target of tBID in cells signaled to die by tumor necrosis factor alpha.	tBID	47-51	mitochondrial carrier 2	Mus musculus	0-31
15899861-0	2005	Mitochondrial carrier homolog 2 is a target of tBID in cells signaled to die by tumor necrosis factor alpha.	tBID	47-51	tumor necrosis factor	Mus musculus	80-107
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
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	BCL2-associated X protein	Mus musculus	161-164
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	BCL2-antagonist/killer 1	Mus musculus	168-171
15899861-3	2005	In TNF-alpha-activated FL5.12 cells, tBID becomes part of a 45-kDa cross-linkable mitochondrial complex.	tBID	37-41	tumor necrosis factor	Mus musculus	3-12
15899861-8	2005	185 kDa and that the addition of TNF-alpha to these cells leads to the recruitment of tBID and BAX to this complex.	tBID	86-90	tumor necrosis factor	Mus musculus	33-42
15899861-10	2005	These results implicate Mtch2 as a mitochondrial target of tBID and raise the possibility that the Mtch2-resident complex participates in the mitochondrial apoptotic program.	tBID	59-63	mitochondrial carrier 2	Mus musculus	24-29
15637055-1	2005	Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces programmed cell death through the caspase activation cascade and translocation of cleaved Bid (tBid) by the apical caspase-8 to mitochondria to induce oligomerization of multidomain Bax and Bak.	tBID	167-171	TNF superfamily member 10	Homo sapiens	0-55
15637055-1	2005	Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces programmed cell death through the caspase activation cascade and translocation of cleaved Bid (tBid) by the apical caspase-8 to mitochondria to induce oligomerization of multidomain Bax and Bak.	tBID	167-171	TNF superfamily member 10	Homo sapiens	57-62
15637055-1	2005	Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces programmed cell death through the caspase activation cascade and translocation of cleaved Bid (tBid) by the apical caspase-8 to mitochondria to induce oligomerization of multidomain Bax and Bak.	tBID	167-171	BH3 interacting domain death agonist	Homo sapiens	162-165
15637055-1	2005	Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces programmed cell death through the caspase activation cascade and translocation of cleaved Bid (tBid) by the apical caspase-8 to mitochondria to induce oligomerization of multidomain Bax and Bak.	tBID	167-171	caspase 8	Homo sapiens	187-196
15637055-1	2005	Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces programmed cell death through the caspase activation cascade and translocation of cleaved Bid (tBid) by the apical caspase-8 to mitochondria to induce oligomerization of multidomain Bax and Bak.	tBID	167-171	BCL2 associated X, apoptosis regulator	Homo sapiens	254-257
15637055-1	2005	Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces programmed cell death through the caspase activation cascade and translocation of cleaved Bid (tBid) by the apical caspase-8 to mitochondria to induce oligomerization of multidomain Bax and Bak.	tBID	167-171	BCL2 antagonist/killer 1	Homo sapiens	262-265
15637055-6	2005	We further established for the first time that the C-terminal domain of Mcl-1 became proapoptotic as a result of caspase-3 cleavage, and its physical interaction and cooperation with tBid, Bak, and voltage-dependent anion-selective channel 1 promoted mitochondrial apoptosis.	tBID	183-187	MCL1 apoptosis regulator, BCL2 family member	Homo sapiens	72-77
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
15690071-5	2005	S70E expression also diminished tBid-mediated cytochrome c release and blunted chemotherapy-induced activation of caspases-9 and -3 in JM1 cells.	tBID	32-36	cytochrome c, somatic	Homo sapiens	46-58
15690071-7	2005	Of those tested, vascular endothelial growth factor (VEGF) induced phosphorylation of Bcl-2 protein and blunted cytochrome c release during chemotherapy or tBid treatment of ALL cells.	tBID	156-160	vascular endothelial growth factor A	Homo sapiens	17-51
15690071-7	2005	Of those tested, vascular endothelial growth factor (VEGF) induced phosphorylation of Bcl-2 protein and blunted cytochrome c release during chemotherapy or tBid treatment of ALL cells.	tBID	156-160	vascular endothelial growth factor A	Homo sapiens	53-57
15494215-9	2005	Our results suggest that the initial release of cytochrome generates tBid that is capable of translocation into the mitochondria causing further release of cytochrome c.	tBID	69-73	cytochrome c, somatic	Homo sapiens	156-168
15351738-0	2004	Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid.	tBID	106-110	BCL2 associated X, apoptosis regulator	Rattus norvegicus	0-3
15661737-2	2005	We show here that HN also interacts with the BH3-only Bcl-2/Bax family protein, Bid, as well as a truncated form of Bid (tBid) associated with protease-mediated activation of this proapoptotic protein.	tBID	121-125	BH3 interacting domain death agonist	Homo sapiens	116-119
15661737-3	2005	Synthetic HN peptide binds purified Bid and tBid in vitro and blocks tBid-induced release of cytochrome c and SMAC from isolated mitochondria, whereas mutant peptides that fail to bind Bid or tBid lack this activity.	tBID	69-73	cytochrome c, somatic	Homo sapiens	93-105
15661737-3	2005	Synthetic HN peptide binds purified Bid and tBid in vitro and blocks tBid-induced release of cytochrome c and SMAC from isolated mitochondria, whereas mutant peptides that fail to bind Bid or tBid lack this activity.	tBID	69-73	diablo IAP-binding mitochondrial protein	Homo sapiens	110-114
15661737-3	2005	Synthetic HN peptide binds purified Bid and tBid in vitro and blocks tBid-induced release of cytochrome c and SMAC from isolated mitochondria, whereas mutant peptides that fail to bind Bid or tBid lack this activity.	tBID	69-73	cytochrome c, somatic	Homo sapiens	93-105
15661737-3	2005	Synthetic HN peptide binds purified Bid and tBid in vitro and blocks tBid-induced release of cytochrome c and SMAC from isolated mitochondria, whereas mutant peptides that fail to bind Bid or tBid lack this activity.	tBID	69-73	diablo IAP-binding mitochondrial protein	Homo sapiens	110-114
15661737-4	2005	Moreover, HN peptide also retained protective activity on bax-/-mitochondria, indicating that HN can block tBid-induced release of apoptogenic proteins from these organelles in a Bax-independent manner.	tBID	107-111	BCL2 associated X, apoptosis regulator	Homo sapiens	58-61
15661737-4	2005	Moreover, HN peptide also retained protective activity on bax-/-mitochondria, indicating that HN can block tBid-induced release of apoptogenic proteins from these organelles in a Bax-independent manner.	tBID	107-111	BCL2 associated X, apoptosis regulator	Homo sapiens	179-182
15661737-5	2005	HN peptide inhibits tBid-induced oligomerization of Bax and Bak in mitochondrial membranes, as shown by experiments with chemical cross-linkers or gel filtration.	tBID	20-24	BCL2 associated X, apoptosis regulator	Homo sapiens	52-55
15537572-3	2005	Our results suggest that failure to observe cytochrome c release may be due to the use of different buffers because after permeabilization by caspase-8 cleaved human Bid (tBid), cytochrome c dissociation from mitochondria was highly dependent on ionic strength and required 50-80 mm KCl, NaCl, or LiCl.	tBID	171-175	caspase 8	Homo sapiens	142-151
15537572-3	2005	Our results suggest that failure to observe cytochrome c release may be due to the use of different buffers because after permeabilization by caspase-8 cleaved human Bid (tBid), cytochrome c dissociation from mitochondria was highly dependent on ionic strength and required 50-80 mm KCl, NaCl, or LiCl.	tBID	171-175	cytochrome c, somatic	Homo sapiens	178-190
15537572-7	2005	In summary, whereas tBid permeabilizes the outer membrane to cytochrome c, Smac/DIABLO, and Omi/HtrA2, the release of cytochrome c during apoptosis will be underestimated unless sufficient ionic strength is maintained to overcome the electrostatic association of cytochrome c with membranes.	tBID	20-24	cytochrome c, somatic	Homo sapiens	61-73
15537572-7	2005	In summary, whereas tBid permeabilizes the outer membrane to cytochrome c, Smac/DIABLO, and Omi/HtrA2, the release of cytochrome c during apoptosis will be underestimated unless sufficient ionic strength is maintained to overcome the electrostatic association of cytochrome c with membranes.	tBID	20-24	diablo IAP-binding mitochondrial protein	Homo sapiens	75-79
15537572-7	2005	In summary, whereas tBid permeabilizes the outer membrane to cytochrome c, Smac/DIABLO, and Omi/HtrA2, the release of cytochrome c during apoptosis will be underestimated unless sufficient ionic strength is maintained to overcome the electrostatic association of cytochrome c with membranes.	tBID	20-24	diablo IAP-binding mitochondrial protein	Homo sapiens	80-86
15537572-7	2005	In summary, whereas tBid permeabilizes the outer membrane to cytochrome c, Smac/DIABLO, and Omi/HtrA2, the release of cytochrome c during apoptosis will be underestimated unless sufficient ionic strength is maintained to overcome the electrostatic association of cytochrome c with membranes.	tBID	20-24	HtrA serine peptidase 2	Homo sapiens	96-101
15572410-6	2004	By contrast, type II signaling was facilitated by p38alpha-dependent mitochondrial presence of tBid and inhibition of Bcl-2 (Ser70) phosphorylation as well as by p38alpha/beta-dependent mitochondrial localization of Bax and inhibition of phosphorylation of Bad (Ser112/Ser155).	tBID	95-99	mitogen-activated protein kinase 14	Homo sapiens	50-58
15380478-3	2004	Also, biphasic cleavage of Bid was found in this region of the brain, with early generation of tBid-p11 within 10 min of cardiac arrest, followed by generation of tBid-p15 within 30-min reperfusion, consistent with activation of this pro-apoptotic protein.	tBID	95-99	BH3 interacting domain death agonist	Canis lupus familiaris	27-30
15380478-3	2004	Also, biphasic cleavage of Bid was found in this region of the brain, with early generation of tBid-p11 within 10 min of cardiac arrest, followed by generation of tBid-p15 within 30-min reperfusion, consistent with activation of this pro-apoptotic protein.	tBID	163-167	BH3 interacting domain death agonist	Canis lupus familiaris	27-30
15262979-6	2004	The expression of truncated Bid (tBid) and the reduction in mitochondrial transmembrane potential were blocked by caspase-2 or caspase-8, but not caspase-3, knockdown using an RNA interference technique.	tBID	33-37	BH3 interacting domain death agonist	Homo sapiens	28-31
15262979-6	2004	The expression of truncated Bid (tBid) and the reduction in mitochondrial transmembrane potential were blocked by caspase-2 or caspase-8, but not caspase-3, knockdown using an RNA interference technique.	tBID	33-37	caspase 2	Homo sapiens	114-123
15262979-6	2004	The expression of truncated Bid (tBid) and the reduction in mitochondrial transmembrane potential were blocked by caspase-2 or caspase-8, but not caspase-3, knockdown using an RNA interference technique.	tBID	33-37	caspase 8	Homo sapiens	127-136
15314281-1	2004	Bid is cleaved by caspase 8 during apoptosis and the truncated Bid (tBid) translocates to mitochondria by targeting cardiolipin.	tBID	68-72	BH3 interacting domain death agonist	Homo sapiens	63-66
15289866-10	2004	We further demonstrated that such a sensitive effect could be offset by Bcl-xL, as Bid- or tBid-induced apoptosis was completely blocked by the over-expression of Bcl-xL.	tBID	91-95	BCL2 like 1	Homo sapiens	72-78
15377860-7	2004	The translocation of tBid to the mitochondria is associated with the activation of outer mitochondrial membrane proteins Bax/Bak and the release of cytochrome C from the mitochondria.	tBID	21-25	BCL2 associated X, apoptosis regulator	Homo sapiens	121-124
15289866-10	2004	We further demonstrated that such a sensitive effect could be offset by Bcl-xL, as Bid- or tBid-induced apoptosis was completely blocked by the over-expression of Bcl-xL.	tBID	91-95	BCL2 like 1	Homo sapiens	163-169
15265702-4	2004	In MCF-7 cells, NaB increased the expression of death receptors; NaB alone or in combination with TNF-alpha, TRAIL, and anti-Fas agonist antibody increased the levels of Bid, tBid, and that of cytosolic cytochrome c.	tBID	175-179	tumor necrosis factor	Homo sapiens	98-107
15265702-4	2004	In MCF-7 cells, NaB increased the expression of death receptors; NaB alone or in combination with TNF-alpha, TRAIL, and anti-Fas agonist antibody increased the levels of Bid, tBid, and that of cytosolic cytochrome c.	tBID	175-179	TNF superfamily member 10	Homo sapiens	109-114
15148322-4	2004	Caspase 8 cleaves full-length Bid, resulting in truncated p15 tBid.	tBID	62-66	caspase 8	Homo sapiens	0-9
15148322-4	2004	Caspase 8 cleaves full-length Bid, resulting in truncated p15 tBid.	tBID	62-66	BH3 interacting domain death agonist	Homo sapiens	30-33
15148322-4	2004	Caspase 8 cleaves full-length Bid, resulting in truncated p15 tBid.	tBID	62-66	cyclin dependent kinase inhibitor 2B	Homo sapiens	58-61
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	cyclin dependent kinase inhibitor 2B	Homo sapiens	0-3
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
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 associated X, apoptosis regulator	Homo sapiens	76-79
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	cytochrome c, somatic	Homo sapiens	105-117
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
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 associated X, apoptosis regulator	Homo sapiens	89-92
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	cytochrome c, somatic	Homo sapiens	219-231
15138279-2	2004	However, the exact mechanism by which tBID and BIM(EL) aid BAX and its close homologues in this mitochondrial protein release remains enigmatic.	tBID	38-42	BCL2 associated X, apoptosis regulator	Homo sapiens	59-62
15138279-3	2004	Here, using pure lipid vesicles, we provide evidence that tBID acts in concert with BAX to 1) form large membrane openings through both BH3-dependent and BH3-independent mechanisms, 2) cause lipid transbilayer movement concomitant with membrane permeabilization, and 3) disrupt the lipid bilayer structure of the membrane by promoting positive monolayer curvature stress.	tBID	58-62	BCL2 associated X, apoptosis regulator	Homo sapiens	84-87
15138279-5	2004	Based on these data, we propose a novel model in which tBID assists BAX not only via protein-protein but also via protein-lipid interactions to form lipidic pore-type non-bilayer structures in the outer mitochondrial membrane through which intermembrane prodeath molecules exit mitochondria during apoptosis.	tBID	55-59	BCL2 associated X, apoptosis regulator	Homo sapiens	68-71
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
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	BH3 interacting domain death agonist	Homo sapiens	38-41
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	caspase 8	Homo sapiens	56-65
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	cytochrome c, somatic	Homo sapiens	182-194
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
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	caspase 3	Homo sapiens	156-165
15377860-7	2004	The translocation of tBid to the mitochondria is associated with the activation of outer mitochondrial membrane proteins Bax/Bak and the release of cytochrome C from the mitochondria.	tBID	21-25	BCL2 antagonist/killer 1	Homo sapiens	125-128
15258470-2	2004	The constitutive balanced ratio of Bax/Bcl-XL in K562 mitochondria allowed the formation of active Bax and cytochrome c release from mitochondria in the presence of a BH3-only protein, tBid, in a cell-free system.	tBID	185-189	BCL2 associated X, apoptosis regulator	Homo sapiens	35-38
15258470-2	2004	The constitutive balanced ratio of Bax/Bcl-XL in K562 mitochondria allowed the formation of active Bax and cytochrome c release from mitochondria in the presence of a BH3-only protein, tBid, in a cell-free system.	tBID	185-189	BCL2 like 1	Homo sapiens	39-45
15258470-2	2004	The constitutive balanced ratio of Bax/Bcl-XL in K562 mitochondria allowed the formation of active Bax and cytochrome c release from mitochondria in the presence of a BH3-only protein, tBid, in a cell-free system.	tBID	185-189	BCL2 associated X, apoptosis regulator	Homo sapiens	99-102
15258470-2	2004	The constitutive balanced ratio of Bax/Bcl-XL in K562 mitochondria allowed the formation of active Bax and cytochrome c release from mitochondria in the presence of a BH3-only protein, tBid, in a cell-free system.	tBID	185-189	cytochrome c, somatic	Homo sapiens	107-119
14678945-2	2004	Activation of Bid depends on its proteolytic processing into truncated forms of tBid.	tBID	80-84	BH3 interacting domain death agonist	Rattus norvegicus	14-17
14761678-5	2004	Treatment of HepG2 cells with IH901 also induced the cleavage of cytosolic factors such as Bid and Bax and translocation of truncated Bid (tBid) to mitochondria.	tBID	139-143	BH3 interacting domain death agonist	Homo sapiens	134-137
14661970-4	2003	With both methods we find that oligomeric BaxDeltaC or full-length Bax in the presence of tBid, but not monomeric full-length Bax, strongly promotes the rate of transbilayer diffusion.	tBID	90-94	BCL2 associated X, apoptosis regulator	Homo sapiens	42-45
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
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	BH3 interacting domain death agonist	Homo sapiens	113-116
14701745-6	2004	Akt also antagonized tBID-mediated BAX activation and mitochondrial BAK oligomerization, two downstream events thought to be critical for tBID-induced apoptosis.	tBID	21-25	AKT serine/threonine kinase 1	Homo sapiens	0-3
14701745-6	2004	Akt also antagonized tBID-mediated BAX activation and mitochondrial BAK oligomerization, two downstream events thought to be critical for tBID-induced apoptosis.	tBID	21-25	BCL2 associated X, apoptosis regulator	Homo sapiens	35-38
14701745-6	2004	Akt also antagonized tBID-mediated BAX activation and mitochondrial BAK oligomerization, two downstream events thought to be critical for tBID-induced apoptosis.	tBID	138-142	AKT serine/threonine kinase 1	Homo sapiens	0-3
14701745-8	2004	Interestingly, tBID independently elicited dissociation of hexokinases from mitochondria, an effect that was antagonized by activated Akt.	tBID	15-19	AKT serine/threonine kinase 1	Homo sapiens	134-137
14701745-10	2004	These results suggest that Akt inhibits BID-mediated apoptosis downstream of BID cleavage via promotion of mitochondrial hexokinase association and antagonism of tBID-mediated BAX and BAK activation at the mitochondria.	tBID	162-166	AKT serine/threonine kinase 1	Homo sapiens	27-30
14701745-10	2004	These results suggest that Akt inhibits BID-mediated apoptosis downstream of BID cleavage via promotion of mitochondrial hexokinase association and antagonism of tBID-mediated BAX and BAK activation at the mitochondria.	tBID	162-166	BH3 interacting domain death agonist	Homo sapiens	40-43
14701745-10	2004	These results suggest that Akt inhibits BID-mediated apoptosis downstream of BID cleavage via promotion of mitochondrial hexokinase association and antagonism of tBID-mediated BAX and BAK activation at the mitochondria.	tBID	162-166	BCL2 associated X, apoptosis regulator	Homo sapiens	176-179
14661970-4	2003	With both methods we find that oligomeric BaxDeltaC or full-length Bax in the presence of tBid, but not monomeric full-length Bax, strongly promotes the rate of transbilayer diffusion.	tBID	90-94	BCL2 associated X, apoptosis regulator	Homo sapiens	67-70
14522999-8	2003	Indeed, the lipid-induced Bax conformational change is shown to be required for tBid-induced Bax oligomerization and pore formation, putting it upstream of tBid activity in this molecular pathway to Bax activation.	tBID	80-84	BCL2 associated X, apoptosis regulator	Homo sapiens	26-29
14522999-8	2003	Indeed, the lipid-induced Bax conformational change is shown to be required for tBid-induced Bax oligomerization and pore formation, putting it upstream of tBid activity in this molecular pathway to Bax activation.	tBID	80-84	BCL2 associated X, apoptosis regulator	Homo sapiens	93-96
14522999-8	2003	Indeed, the lipid-induced Bax conformational change is shown to be required for tBid-induced Bax oligomerization and pore formation, putting it upstream of tBid activity in this molecular pathway to Bax activation.	tBID	80-84	BCL2 associated X, apoptosis regulator	Homo sapiens	93-96
14522999-8	2003	Indeed, the lipid-induced Bax conformational change is shown to be required for tBid-induced Bax oligomerization and pore formation, putting it upstream of tBid activity in this molecular pathway to Bax activation.	tBID	156-160	BCL2 associated X, apoptosis regulator	Homo sapiens	26-29
14522999-8	2003	Indeed, the lipid-induced Bax conformational change is shown to be required for tBid-induced Bax oligomerization and pore formation, putting it upstream of tBid activity in this molecular pathway to Bax activation.	tBID	156-160	BCL2 associated X, apoptosis regulator	Homo sapiens	93-96
14522999-8	2003	Indeed, the lipid-induced Bax conformational change is shown to be required for tBid-induced Bax oligomerization and pore formation, putting it upstream of tBid activity in this molecular pathway to Bax activation.	tBID	156-160	BCL2 associated X, apoptosis regulator	Homo sapiens	93-96
14500711-4	2003	Noxa-induced cytochrome c release is inhibited by permeability transition pore inhibitors such as CsA or MgCl2, and Noxa induces an ultra-structural change of mitochondria yielding "swollen" mitochondria that are unlike changes induced by tBid.	tBID	239-243	phorbol-12-myristate-13-acetate-induced protein 1	Homo sapiens	0-4
14500711-4	2003	Noxa-induced cytochrome c release is inhibited by permeability transition pore inhibitors such as CsA or MgCl2, and Noxa induces an ultra-structural change of mitochondria yielding "swollen" mitochondria that are unlike changes induced by tBid.	tBID	239-243	phorbol-12-myristate-13-acetate-induced protein 1	Homo sapiens	116-120
14500711-6	2003	Moreover, Bak-oligomerization, which is an essential event for tBid-induced cytochrome c release in the extrinsic death signaling pathway, is not associated with Noxa-induced cytochrome c release.	tBID	63-67	cytochrome c, somatic	Homo sapiens	76-88
12881569-6	2003	Death signals activate "BH3-only" molecules such as tBID, BIM, or BAD, which displace VDAC2 from BAK, enabling homo-oligomerization of BAK and apoptosis.	tBID	52-56	voltage dependent anion channel 2	Homo sapiens	86-91
14550275-4	2003	Treatment of HUVEC with angiostatin at a concentration known to inhibit cell proliferation and induce apoptosis resulted in induction of p53-, Bax-, and tBid-mediated release of cytochrome c into the cytosol.	tBID	153-157	cytochrome c, somatic	Homo sapiens	178-190
14573790-6	2003	The abnormal mitochondrial metabolism and structure in PLS3(F258V)-expressing cells were associated with decreased sensitivity to UV- and tBid-induced apoptosis and diminished translocation of CL to the mitochondrial outer membrane.	tBID	138-142	phospholipid scramblase 3	Homo sapiens	55-59
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
12881569-6	2003	Death signals activate "BH3-only" molecules such as tBID, BIM, or BAD, which displace VDAC2 from BAK, enabling homo-oligomerization of BAK and apoptosis.	tBID	52-56	BCL2 antagonist/killer 1	Homo sapiens	97-100
12881569-6	2003	Death signals activate "BH3-only" molecules such as tBID, BIM, or BAD, which displace VDAC2 from BAK, enabling homo-oligomerization of BAK and apoptosis.	tBID	52-56	BCL2 antagonist/killer 1	Homo sapiens	135-138
12823542-4	2003	In contrast, while treatment with TRAIL alone significantly increased the level of tBid, the expression of Bax remained unaffected.	tBID	83-87	TNF superfamily member 10	Homo sapiens	34-39
12721291-1	2003	Caspase-8 cleaves BID to tBID, which targets mitochondria and induces oligomerization of BAX and BAK within the outer membrane, resulting in release of cytochrome c from the organelle.	tBID	25-29	caspase 8	Homo sapiens	0-9
12721291-1	2003	Caspase-8 cleaves BID to tBID, which targets mitochondria and induces oligomerization of BAX and BAK within the outer membrane, resulting in release of cytochrome c from the organelle.	tBID	25-29	BH3 interacting domain death agonist	Homo sapiens	18-21
12721291-1	2003	Caspase-8 cleaves BID to tBID, which targets mitochondria and induces oligomerization of BAX and BAK within the outer membrane, resulting in release of cytochrome c from the organelle.	tBID	25-29	BCL2 associated X, apoptosis regulator	Homo sapiens	89-92
12721291-1	2003	Caspase-8 cleaves BID to tBID, which targets mitochondria and induces oligomerization of BAX and BAK within the outer membrane, resulting in release of cytochrome c from the organelle.	tBID	25-29	BCL2 antagonist/killer 1	Homo sapiens	97-100
12721291-1	2003	Caspase-8 cleaves BID to tBID, which targets mitochondria and induces oligomerization of BAX and BAK within the outer membrane, resulting in release of cytochrome c from the organelle.	tBID	25-29	cytochrome c, somatic	Homo sapiens	152-164
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
12766488-3	2003	Proteolysis of the N-terminus (encompassing H1 and H2) of Bid yields activated "tBid" (truncated Bid), which translocates to the mitochondria and induces the efflux of cytochrome c.	tBID	80-84	H1.5 linker histone, cluster member	Homo sapiens	44-53
12766488-3	2003	Proteolysis of the N-terminus (encompassing H1 and H2) of Bid yields activated "tBid" (truncated Bid), which translocates to the mitochondria and induces the efflux of cytochrome c.	tBID	80-84	BH3 interacting domain death agonist	Homo sapiens	58-61
12766488-3	2003	Proteolysis of the N-terminus (encompassing H1 and H2) of Bid yields activated "tBid" (truncated Bid), which translocates to the mitochondria and induces the efflux of cytochrome c.	tBID	80-84	cytochrome c, somatic	Homo sapiens	168-180
12624108-6	2003	In these cells, Bid was processed into active forms of truncated Bid or tBid.	tBID	72-76	BH3 interacting domain death agonist	Homo sapiens	16-19
12846980-5	2003	Interactions between Bax and BH3 death domain proteins such as tBid result in Bax membrane integration, oligomerization, and permeabilization of the outer membrane to intermembrane proteins such as cytochrome c.	tBID	63-67	BCL2 associated X, apoptosis regulator	Homo sapiens	21-24
12846980-5	2003	Interactions between Bax and BH3 death domain proteins such as tBid result in Bax membrane integration, oligomerization, and permeabilization of the outer membrane to intermembrane proteins such as cytochrome c.	tBID	63-67	BCL2 associated X, apoptosis regulator	Homo sapiens	78-81
12846980-5	2003	Interactions between Bax and BH3 death domain proteins such as tBid result in Bax membrane integration, oligomerization, and permeabilization of the outer membrane to intermembrane proteins such as cytochrome c.	tBID	63-67	cytochrome c, somatic	Homo sapiens	198-210
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
12624108-10	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	BH3 interacting domain death agonist	Homo sapiens	84-87
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
12686415-7	2003	tBid had an opposite effect-it stimulated mitochondrial potassium uptake resulting in cytochrome c release.	tBID	0-4	cytochrome c, somatic	Homo sapiens	86-98
16120324-2	2003	While tBid permeabilizes the outer membrane and efficiently stimulates cytochrome c release, digitonin is unable to cause cytochrome c release in the absence of salt.	tBID	6-10	cytochrome c, somatic	Homo sapiens	71-83
12519725-1	2003	The proapoptotic activity of BID seems to solely depend upon its cleavage to truncated tBID.	tBID	87-91	BH3 interacting domain death agonist	Homo sapiens	29-32
12519725-5	2003	ncBID and wtBID (nc/wtBID) were much less effective than tBID in localizing to mitochondria and in inducing cytochrome c release, but only slightly less effective in inducing apoptosis.	tBID	11-15	cytochrome c, somatic	Homo sapiens	108-120
12519725-6	2003	Studies with Apaf-1- and caspase-9-deficient primary MEFs indicated that both proteins were essential for nc/wtBID and for tBID-induced apoptosis.	tBID	110-114	apoptotic peptidase activating factor 1	Homo sapiens	13-19
12519725-6	2003	Studies with Apaf-1- and caspase-9-deficient primary MEFs indicated that both proteins were essential for nc/wtBID and for tBID-induced apoptosis.	tBID	110-114	caspase 9	Homo sapiens	25-34
12180909-3	2002	At low concentrations at which caspase-8-cut Bid (tBid) alone has little effect on leakage, tBid augments the leakage caused by monomeric Bax.	tBID	92-96	BCL2 associated X, apoptosis regulator	Homo sapiens	138-141
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	caspase 8	Mus musculus	80-89
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
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	caspase 3	Mus musculus	255-264
12598529-8	2003	Caspase 8 cleaved rBid to generate two C-terminal products, p15 and p13 tBid, but produced only p15 tBid from isolated Bid.	tBID	72-76	caspase 8	Mus musculus	0-9
12598529-8	2003	Caspase 8 cleaved rBid to generate two C-terminal products, p15 and p13 tBid, but produced only p15 tBid from isolated Bid.	tBID	72-76	BH3 interacting domain death agonist	Rattus norvegicus	18-22
12598529-8	2003	Caspase 8 cleaved rBid to generate two C-terminal products, p15 and p13 tBid, but produced only p15 tBid from isolated Bid.	tBID	100-104	caspase 8	Mus musculus	0-9
12485416-0	2003	Two pathways for tBID-induced cytochrome c release from rat brain mitochondria: BAK- versus BAX-dependence.	tBID	17-21	BCL2 associated X, apoptosis regulator	Rattus norvegicus	92-95
12485416-1	2003	The mechanisms of truncated BID (tBID)-induced Cyt c release from non-synaptosomal brain mitochondria were examined.	tBID	33-37	BH3 interacting domain death agonist	Rattus norvegicus	28-31
12485416-6	2003	tBID plus monomeric BAX produced twice as much Cyt c release as did tBID or oligomeric BAX alone.	tBID	68-72	BCL2 associated X, apoptosis regulator	Rattus norvegicus	20-23
12485416-9	2003	Recombinant Bcl-xL inhibited Cyt c release induced by tBID alone or in combination with monomeric BAX.	tBID	54-58	Bcl2-like 1	Rattus norvegicus	12-18
12485416-11	2003	Thus, tBID can induce mPT-independent Cyt c release from brain mitochondria by interacting with exogenous BAX and/or with endogenous BAK that may involve VDAC.	tBID	6-10	BCL2 associated X, apoptosis regulator	Rattus norvegicus	106-109
12393866-5	2002	The cleavage product of Bid degradation (truncated Bid, tBid) was not detectable in the mitochondria.	tBID	56-60	BH3 interacting domain death agonist	Homo sapiens	24-27
12393866-9	2002	TNF induced a depletion of full-length Bid from the mitochondria and the cytosol but induced an accumulation of mitochondrial tBid.	tBID	126-130	tumor necrosis factor	Homo sapiens	0-3
12393866-14	2002	With TNF Bax translocation occurs as Bid is depleted and can be dissociated from the accumulation of tBid.	tBID	101-105	tumor necrosis factor	Homo sapiens	5-8
12393866-14	2002	With TNF Bax translocation occurs as Bid is depleted and can be dissociated from the accumulation of tBid.	tBID	101-105	BCL2 associated X, apoptosis regulator	Homo sapiens	9-12
12193163-0	2002	Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein.	tBID	56-60	BCL2 associated X, apoptosis regulator	Homo sapiens	0-3
12193163-2	2002	Bax oligomerization can also be induced by incubating isolated mitochondria containing endogenous Bax with recombinant tBid (caspase-8-cleaved Bid) in vitro.	tBID	119-123	BCL2 associated X, apoptosis regulator	Homo sapiens	0-3
12193163-2	2002	Bax oligomerization can also be induced by incubating isolated mitochondria containing endogenous Bax with recombinant tBid (caspase-8-cleaved Bid) in vitro.	tBID	119-123	BCL2 associated X, apoptosis regulator	Homo sapiens	98-101
12193163-6	2002	However, in the presence of tBid, the protein formed large complexes in mitochondrial membranes and induced the release of cytochrome c.	tBID	28-32	cytochrome c, somatic	Homo sapiens	123-135
12193163-7	2002	tBid also induced Bax oligomerization in isolated mitochondrial outer membranes, but not in other membranes, such as plasma membranes or microsomes.	tBID	0-4	BCL2 associated X, apoptosis regulator	Homo sapiens	18-21
12193163-8	2002	Moreover, tBid-induced Bax oligomerization was inhibited when mitochondria were pretreated with protease K. The presence of the voltage-dependent anion channel was not required either for Bax oligomerization or for Bax-induced cytochrome c release.	tBID	10-14	BCL2 associated X, apoptosis regulator	Homo sapiens	23-26
12193163-8	2002	Moreover, tBid-induced Bax oligomerization was inhibited when mitochondria were pretreated with protease K. The presence of the voltage-dependent anion channel was not required either for Bax oligomerization or for Bax-induced cytochrome c release.	tBID	10-14	cytochrome c, somatic	Homo sapiens	227-239
12404119-8	2002	Although tBid-dependent release of Cytochrome c, AIF, adenylate kinase, Smac/DIABLO and Omi/HtrA2 could be demonstrated, none of the caspases were detectable both in the supernatant and the mitochondrial fraction after treatment.	tBID	9-13	diablo, IAP-binding mitochondrial protein	Mus musculus	72-76
12404119-8	2002	Although tBid-dependent release of Cytochrome c, AIF, adenylate kinase, Smac/DIABLO and Omi/HtrA2 could be demonstrated, none of the caspases were detectable both in the supernatant and the mitochondrial fraction after treatment.	tBID	9-13	diablo, IAP-binding mitochondrial protein	Mus musculus	77-83
12404119-8	2002	Although tBid-dependent release of Cytochrome c, AIF, adenylate kinase, Smac/DIABLO and Omi/HtrA2 could be demonstrated, none of the caspases were detectable both in the supernatant and the mitochondrial fraction after treatment.	tBID	9-13	HtrA serine peptidase 2	Mus musculus	92-97
12207176-2	2002	Bid action has been proposed to involve the mitochondrial re-location of its truncated form, tBid, to facilitate the release of apoptogenic proteins like cytochrome c.	tBID	93-97	BH3 interacting domain death agonist	Homo sapiens	0-3
12207176-2	2002	Bid action has been proposed to involve the mitochondrial re-location of its truncated form, tBid, to facilitate the release of apoptogenic proteins like cytochrome c.	tBID	93-97	cytochrome c, somatic	Homo sapiens	154-166
12207176-4	2002	To advance our knowledge, this review evaluates the basic steps of Bid activation--caspase cleavage, dissociation of tBid, and lipid-mediated mitochondrial relocation--and their structure-function aspects.	tBID	117-121	BH3 interacting domain death agonist	Homo sapiens	67-70
12154014-3	2002	The active truncated form of BID (tBID) triggers the mitochondrial activation of caspase-9 by inducing the activation of BAK or BAX.	tBID	34-38	BH3 interacting domain death agonist	Homo sapiens	29-32
12082098-4	2002	The promotion of leakage by tBid is also inhibited by several substances that promote positive membrane curvature, including lysophosphatidylcholine, tritrpticin, a potent antimicrobial peptide, and cyclosporin A, a known inhibitor of cytochrome c release from mitochondria.	tBID	28-32	cytochrome c, somatic	Homo sapiens	235-247
12082098-8	2002	Bcl-X(L) inhibits leakage and lipid mixing induced by tBid.	tBID	54-58	BCL2 like 1	Homo sapiens	0-8
12082098-12	2002	Our results suggest that the anti-apoptotic activity of Bcl-X(L) is not a consequence of its interaction with membranes, but rather with other proteins, such as tBid.	tBID	161-165	BCL2 like 1	Homo sapiens	56-64
12154014-3	2002	The active truncated form of BID (tBID) triggers the mitochondrial activation of caspase-9 by inducing the activation of BAK or BAX.	tBID	34-38	caspase 9	Homo sapiens	81-90
12154014-3	2002	The active truncated form of BID (tBID) triggers the mitochondrial activation of caspase-9 by inducing the activation of BAK or BAX.	tBID	34-38	BCL2 associated X, apoptosis regulator	Homo sapiens	128-131
12154014-7	2002	We find that CK2 inhibits Apo2L/TRAIL-induced caspase-8-mediated cleavage of BID, thereby reducing the formation of tBID.	tBID	116-120	TNF superfamily member 10	Homo sapiens	26-31
12154014-7	2002	We find that CK2 inhibits Apo2L/TRAIL-induced caspase-8-mediated cleavage of BID, thereby reducing the formation of tBID.	tBID	116-120	TNF superfamily member 10	Homo sapiens	32-37
12154014-7	2002	We find that CK2 inhibits Apo2L/TRAIL-induced caspase-8-mediated cleavage of BID, thereby reducing the formation of tBID.	tBID	116-120	caspase 8	Homo sapiens	46-55
12154014-7	2002	We find that CK2 inhibits Apo2L/TRAIL-induced caspase-8-mediated cleavage of BID, thereby reducing the formation of tBID.	tBID	116-120	BH3 interacting domain death agonist	Homo sapiens	77-80
12154014-8	2002	In addition, CK2 promotes nuclear factor kappa B (NF-kappa B)-mediated expression of Bcl-x(L), which sequesters tBID and curtails its ability to activate BAX.	tBID	112-116	nuclear factor kappa B subunit 1	Homo sapiens	26-48
12154014-8	2002	In addition, CK2 promotes nuclear factor kappa B (NF-kappa B)-mediated expression of Bcl-x(L), which sequesters tBID and curtails its ability to activate BAX.	tBID	112-116	nuclear factor kappa B subunit 1	Homo sapiens	50-60
12154014-8	2002	In addition, CK2 promotes nuclear factor kappa B (NF-kappa B)-mediated expression of Bcl-x(L), which sequesters tBID and curtails its ability to activate BAX.	tBID	112-116	BCL2 like 1	Homo sapiens	85-93
12154014-10	2002	Conversely, reduction of the Bcl-x(L)/tBID ratio by inhibition of CK2 renders such cancer cells sensitive to Apo2L/TRAIL-induced activation of caspase-9 and apoptosis.	tBID	38-42	TNF superfamily member 10	Homo sapiens	109-114
12154014-10	2002	Conversely, reduction of the Bcl-x(L)/tBID ratio by inhibition of CK2 renders such cancer cells sensitive to Apo2L/TRAIL-induced activation of caspase-9 and apoptosis.	tBID	38-42	TNF superfamily member 10	Homo sapiens	115-120
11934844-7	2002	Production of tBID then sustains mitochondrial injury and perpetuates caspase-9 activation.	tBID	14-18	caspase 9	Rattus norvegicus	70-79
11929871-9	2002	However, Bfl-1 remains tightly and selectively bound to tBid and blocks collaboration between tBid and Bax or Bak in the plane of the mitochondrial membrane, thereby preventing mitochondrial apoptotic activation.	tBID	56-60	BCL2 related protein A1	Homo sapiens	9-14
11929871-9	2002	However, Bfl-1 remains tightly and selectively bound to tBid and blocks collaboration between tBid and Bax or Bak in the plane of the mitochondrial membrane, thereby preventing mitochondrial apoptotic activation.	tBID	94-98	BCL2 related protein A1	Homo sapiens	9-14
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
11805084-2	2002	tBID translocates to the mitochondria to induce the oligomerization of BAX or BAK, resulting in the release of cytochrome c (Cyt c).	tBID	0-4	BCL2-associated X protein	Mus musculus	71-74
11805084-2	2002	tBID translocates to the mitochondria to induce the oligomerization of BAX or BAK, resulting in the release of cytochrome c (Cyt c).	tBID	0-4	BCL2-antagonist/killer 1	Mus musculus	78-81
11805084-3	2002	Here we demonstrate that in tumor necrosis factor alpha-activated FL5.12 cells, tBID becomes part of a 45-kDa cross-linkable mitochondrial complex that does not include BAX or BAK.	tBID	80-84	tumor necrosis factor	Mus musculus	28-55
11805084-6	2002	To test the functional consequence of tBID oligomerization, we expressed a chimeric FKBP-tBID molecule.	tBID	38-42	FK506 binding protein 1a	Mus musculus	84-88
11805084-6	2002	To test the functional consequence of tBID oligomerization, we expressed a chimeric FKBP-tBID molecule.	tBID	89-93	FK506 binding protein 1a	Mus musculus	84-88
11782443-5	2002	Release of Smac/DIABLO from mitochondria through the TRAIL-caspase-8-tBid-Bax cascade is required to remove the inhibitory effect of XIAP and allow apoptosis to proceed.	tBID	69-73	diablo IAP-binding mitochondrial protein	Homo sapiens	11-15
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
11859412-3	2002	Several mitochondrial proteins were identified to be released in a tBid-dependent way, among which cytochrome c, DIABLO/Smac, adenylate kinase 2, acyl-CoA-binding protein, endonuclease G, polypyrimidine tract-binding protein, a type-I RNA helicase, a WD-40 repeat-containing protein and the serine protease Omi.	tBID	67-71	diablo, IAP-binding mitochondrial protein	Mus musculus	113-119
11859412-3	2002	Several mitochondrial proteins were identified to be released in a tBid-dependent way, among which cytochrome c, DIABLO/Smac, adenylate kinase 2, acyl-CoA-binding protein, endonuclease G, polypyrimidine tract-binding protein, a type-I RNA helicase, a WD-40 repeat-containing protein and the serine protease Omi.	tBID	67-71	diablo, IAP-binding mitochondrial protein	Mus musculus	120-124
11859412-3	2002	Several mitochondrial proteins were identified to be released in a tBid-dependent way, among which cytochrome c, DIABLO/Smac, adenylate kinase 2, acyl-CoA-binding protein, endonuclease G, polypyrimidine tract-binding protein, a type-I RNA helicase, a WD-40 repeat-containing protein and the serine protease Omi.	tBID	67-71	adenylate kinase 2	Mus musculus	126-144
11859412-3	2002	Several mitochondrial proteins were identified to be released in a tBid-dependent way, among which cytochrome c, DIABLO/Smac, adenylate kinase 2, acyl-CoA-binding protein, endonuclease G, polypyrimidine tract-binding protein, a type-I RNA helicase, a WD-40 repeat-containing protein and the serine protease Omi.	tBID	67-71	HtrA serine peptidase 2	Mus musculus	291-310
11741882-0	2002	Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization.	tBID	18-22	cytochrome c, somatic	Homo sapiens	31-43
11741882-0	2002	Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization.	tBID	18-22	diablo IAP-binding mitochondrial protein	Homo sapiens	48-52
11741882-0	2002	Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization.	tBID	18-22	diablo IAP-binding mitochondrial protein	Homo sapiens	53-59
11741882-3	2002	Using green fluorescent protein fusion proteins and immunostaining in individual permeabilized HepG2 cells, first we demonstrated that truncated Bid (15.5-kDa C-terminal fragment, tBid) evoked a rapid and essentially complete release of cytochrome c and Smac/DIABLO from every mitochondrion.	tBID	180-184	BH3 interacting domain death agonist	Homo sapiens	145-148
11741882-3	2002	Using green fluorescent protein fusion proteins and immunostaining in individual permeabilized HepG2 cells, first we demonstrated that truncated Bid (15.5-kDa C-terminal fragment, tBid) evoked a rapid and essentially complete release of cytochrome c and Smac/DIABLO from every mitochondrion.	tBID	180-184	cytochrome c, somatic	Homo sapiens	237-249
11741882-3	2002	Using green fluorescent protein fusion proteins and immunostaining in individual permeabilized HepG2 cells, first we demonstrated that truncated Bid (15.5-kDa C-terminal fragment, tBid) evoked a rapid and essentially complete release of cytochrome c and Smac/DIABLO from every mitochondrion.	tBID	180-184	diablo IAP-binding mitochondrial protein	Homo sapiens	254-258
11741882-3	2002	Using green fluorescent protein fusion proteins and immunostaining in individual permeabilized HepG2 cells, first we demonstrated that truncated Bid (15.5-kDa C-terminal fragment, tBid) evoked a rapid and essentially complete release of cytochrome c and Smac/DIABLO from every mitochondrion.	tBID	180-184	diablo IAP-binding mitochondrial protein	Homo sapiens	259-265
11741882-4	2002	To establish at a resolution of seconds the kinetics of tBid-induced cytochrome c and Smac/DIABLO release and depolarization, we monitored the mitochondrial membrane potential (DeltaPsi(m)) fluorimetrically in permeabilized cells and applied a rapid filtration method to obtain cytosolic fractions for Western blotting.	tBID	56-60	cytochrome c, somatic	Homo sapiens	69-81
11741882-4	2002	To establish at a resolution of seconds the kinetics of tBid-induced cytochrome c and Smac/DIABLO release and depolarization, we monitored the mitochondrial membrane potential (DeltaPsi(m)) fluorimetrically in permeabilized cells and applied a rapid filtration method to obtain cytosolic fractions for Western blotting.	tBID	56-60	diablo IAP-binding mitochondrial protein	Homo sapiens	86-90
11741882-4	2002	To establish at a resolution of seconds the kinetics of tBid-induced cytochrome c and Smac/DIABLO release and depolarization, we monitored the mitochondrial membrane potential (DeltaPsi(m)) fluorimetrically in permeabilized cells and applied a rapid filtration method to obtain cytosolic fractions for Western blotting.	tBID	56-60	diablo IAP-binding mitochondrial protein	Homo sapiens	91-97
11741882-5	2002	We found that subnanomolar doses of tBid were sufficient to evoke cytochrome c release and mitochondrial depolarization, whereas full-length Bid was 100-fold less effective.	tBID	36-40	cytochrome c, somatic	Homo sapiens	66-78
11741882-6	2002	Bcl-x(L) prevented tBid-induced cytochrome c release and depolarization.	tBID	19-23	BCL2 like 1	Homo sapiens	0-8
11741882-6	2002	Bcl-x(L) prevented tBid-induced cytochrome c release and depolarization.	tBID	19-23	cytochrome c, somatic	Homo sapiens	32-44
11741882-7	2002	In response to 2.5 nm tBid, cytochrome c release started after a 10 s delay, displayed rapid progression, and was complete at 50-70 s. Release of Smac/DIABLO was synchronized with cytochrome c release, whereas the loss of DeltaPsi(m) lagged slightly behind cytochrome c release.	tBID	22-26	cytochrome c, somatic	Homo sapiens	28-40
11741882-7	2002	In response to 2.5 nm tBid, cytochrome c release started after a 10 s delay, displayed rapid progression, and was complete at 50-70 s. Release of Smac/DIABLO was synchronized with cytochrome c release, whereas the loss of DeltaPsi(m) lagged slightly behind cytochrome c release.	tBID	22-26	diablo IAP-binding mitochondrial protein	Homo sapiens	146-150
11741882-7	2002	In response to 2.5 nm tBid, cytochrome c release started after a 10 s delay, displayed rapid progression, and was complete at 50-70 s. Release of Smac/DIABLO was synchronized with cytochrome c release, whereas the loss of DeltaPsi(m) lagged slightly behind cytochrome c release.	tBID	22-26	diablo IAP-binding mitochondrial protein	Homo sapiens	151-157
11741882-7	2002	In response to 2.5 nm tBid, cytochrome c release started after a 10 s delay, displayed rapid progression, and was complete at 50-70 s. Release of Smac/DIABLO was synchronized with cytochrome c release, whereas the loss of DeltaPsi(m) lagged slightly behind cytochrome c release.	tBID	22-26	cytochrome c, somatic	Homo sapiens	180-192
11741882-7	2002	In response to 2.5 nm tBid, cytochrome c release started after a 10 s delay, displayed rapid progression, and was complete at 50-70 s. Release of Smac/DIABLO was synchronized with cytochrome c release, whereas the loss of DeltaPsi(m) lagged slightly behind cytochrome c release.	tBID	22-26	cytochrome c, somatic	Homo sapiens	180-192
11741882-8	2002	Furthermore, tBid-induced cytochrome c release was insensitive to changes in substrate composition, but tBid-induced depolarization did not occur in the presence of extramitochondrial ATP supply.	tBID	13-17	cytochrome c, somatic	Homo sapiens	26-38
11741882-9	2002	Thus, tBid-induced permeabilization of the outer membrane permits rapid release of cytochrome c and Smac/DIABLO from all domains of the intermembrane space.	tBID	6-10	cytochrome c, somatic	Homo sapiens	83-95
11741882-9	2002	Thus, tBid-induced permeabilization of the outer membrane permits rapid release of cytochrome c and Smac/DIABLO from all domains of the intermembrane space.	tBID	6-10	diablo IAP-binding mitochondrial protein	Homo sapiens	100-104
11741882-9	2002	Thus, tBid-induced permeabilization of the outer membrane permits rapid release of cytochrome c and Smac/DIABLO from all domains of the intermembrane space.	tBID	6-10	diablo IAP-binding mitochondrial protein	Homo sapiens	105-111
11741882-10	2002	The tBid-induced loss of DeltaPsi(m) occurs after cytochrome c release and reflects impairment of oxidative metabolism.	tBID	4-8	cytochrome c, somatic	Homo sapiens	50-62
11803371-2	2002	Proteome analysis of supernatant of isolated mitochondria exposed to recombinant tBid, a proapoptotic Bcl-2 member, revealed the presence of the serine protease Omi, also called HtrA2.	tBID	81-85	B cell leukemia/lymphoma 2	Mus musculus	102-107
11803371-2	2002	Proteome analysis of supernatant of isolated mitochondria exposed to recombinant tBid, a proapoptotic Bcl-2 member, revealed the presence of the serine protease Omi, also called HtrA2.	tBID	81-85	HtrA serine peptidase 2	Mus musculus	145-164
11803371-2	2002	Proteome analysis of supernatant of isolated mitochondria exposed to recombinant tBid, a proapoptotic Bcl-2 member, revealed the presence of the serine protease Omi, also called HtrA2.	tBID	81-85	HtrA serine peptidase 2	Mus musculus	178-183
11782314-4	2002	We have found that the "BH3-only" molecule tBID induces a striking remodeling of mitochondrial structure with mobilization of the cytochrome c stores (approximately 85%) in cristae.	tBID	43-47	cytochrome c, somatic	Homo sapiens	130-142
11782443-5	2002	Release of Smac/DIABLO from mitochondria through the TRAIL-caspase-8-tBid-Bax cascade is required to remove the inhibitory effect of XIAP and allow apoptosis to proceed.	tBID	69-73	diablo IAP-binding mitochondrial protein	Homo sapiens	16-22
11782443-5	2002	Release of Smac/DIABLO from mitochondria through the TRAIL-caspase-8-tBid-Bax cascade is required to remove the inhibitory effect of XIAP and allow apoptosis to proceed.	tBID	69-73	TNF superfamily member 10	Homo sapiens	53-58
11782443-5	2002	Release of Smac/DIABLO from mitochondria through the TRAIL-caspase-8-tBid-Bax cascade is required to remove the inhibitory effect of XIAP and allow apoptosis to proceed.	tBID	69-73	caspase 8	Homo sapiens	59-68
11782443-5	2002	Release of Smac/DIABLO from mitochondria through the TRAIL-caspase-8-tBid-Bax cascade is required to remove the inhibitory effect of XIAP and allow apoptosis to proceed.	tBID	69-73	BCL2 associated X, apoptosis regulator	Homo sapiens	74-77
11782443-5	2002	Release of Smac/DIABLO from mitochondria through the TRAIL-caspase-8-tBid-Bax cascade is required to remove the inhibitory effect of XIAP and allow apoptosis to proceed.	tBID	69-73	X-linked inhibitor of apoptosis	Homo sapiens	133-137
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
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
11279213-9	2001	Disruption of the catalytic core of YopP abolished the rapid generation of tBid, thereby hampering induction of apoptosis by Y. enterocolitica.	tBID	75-79	yopP	Yersinia enterocolitica	36-40
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
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 antagonist/killer 1	Homo sapiens	165-168
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 associated X, apoptosis regulator	Homo sapiens	172-175
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	cytochrome c, somatic	Homo sapiens	205-217
11326099-3	2001	We find that cells lacking both Bax and Bak, but not cells lacking only one of these components, are completely resistant to tBID-induced cytochrome c release and apoptosis.	tBID	125-129	BCL2 associated X, apoptosis regulator	Homo sapiens	32-35
11326099-3	2001	We find that cells lacking both Bax and Bak, but not cells lacking only one of these components, are completely resistant to tBID-induced cytochrome c release and apoptosis.	tBID	125-129	BCL2 antagonist/killer 1	Homo sapiens	40-43
11326099-3	2001	We find that cells lacking both Bax and Bak, but not cells lacking only one of these components, are completely resistant to tBID-induced cytochrome c release and apoptosis.	tBID	125-129	cytochrome c, somatic	Homo sapiens	138-150
11585909-2	2001	Bid action has been proposed to involve the relocation of its truncated form, tBid, to mitochondria to facilitate the release of apoptogenic cytochrome c.	tBID	78-82	BH3 interacting domain death agonist	Homo sapiens	0-3
11585909-2	2001	Bid action has been proposed to involve the relocation of its truncated form, tBid, to mitochondria to facilitate the release of apoptogenic cytochrome c.	tBID	78-82	cytochrome c, somatic	Homo sapiens	141-153
11585909-6	2001	Secondly, native and recombinant Bid, as well as tBid, displayed lipid transfer activity under the same conditions and at the same nanomolar concentrations leading to mitochondrial relocation and release of cytochrome c.	tBID	49-53	cytochrome c, somatic	Homo sapiens	207-219
11716782-2	2001	Once associated with mitochondria, truncated Bid (tBid) causes the potent release of cytochrome c, endonuclease G, and smac.	tBID	50-54	BH3 interacting domain death agonist	Homo sapiens	45-48
11716782-2	2001	Once associated with mitochondria, truncated Bid (tBid) causes the potent release of cytochrome c, endonuclease G, and smac.	tBID	50-54	cytochrome c, somatic	Homo sapiens	85-97
11716782-2	2001	Once associated with mitochondria, truncated Bid (tBid) causes the potent release of cytochrome c, endonuclease G, and smac.	tBID	50-54	endonuclease G	Homo sapiens	99-113
11716782-5	2001	Additionally, tBidG94E lowers the cytochrome c releasing activity of tBid without affecting its targeting to mitochondria.	tBID	14-18	cytochrome c, somatic	Homo sapiens	34-46
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
11752628-3	2000	The pro-apoptotic protein BID is unique in that its proteolytic cleavage product, tBID, is posttranslationally myristoylated.	tBID	82-86	BH3 interacting domain death agonist	Homo sapiens	26-29
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	cyclin dependent kinase inhibitor 2B	Mus musculus	4-7
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	133-137	BCL2-associated X protein	Mus musculus	197-200
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	133-137	BCL2-associated X protein	Mus musculus	197-200
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
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	BCL2-antagonist/killer 1	Mus musculus	56-59
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	BCL2-associated X protein	Mus musculus	63-66
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	BCL2-antagonist/killer 1	Mus musculus	219-222
11175253-1	2000	The BH3 domain of tBID is not required for targeting but remains on the mitochondrial surface where it is required to trigger BAK to release cytochrome c. tBID functions not as a pore-forming protein but as a membrane targeted and concentrated death ligand.	tBID	18-22	BCL2-antagonist/killer 1	Mus musculus	126-129
11175253-1	2000	The BH3 domain of tBID is not required for targeting but remains on the mitochondrial surface where it is required to trigger BAK to release cytochrome c. tBID functions not as a pore-forming protein but as a membrane targeted and concentrated death ligand.	tBID	155-159	BCL2-antagonist/killer 1	Mus musculus	126-129
11175253-2	2000	tBID induces oligomerization of BAK, and both Bid and Bak knockout mice indicate the importance of this event in the release of cytochrome c. In parallel, the full pro-apoptotic member BAX, which is highly homologous to BAK, rapidly forms pores in liposomes that release intravesicular FITC-cytochrome c approximately 20A.	tBID	0-4	BCL2-antagonist/killer 1	Mus musculus	32-35
11175253-2	2000	tBID induces oligomerization of BAK, and both Bid and Bak knockout mice indicate the importance of this event in the release of cytochrome c. In parallel, the full pro-apoptotic member BAX, which is highly homologous to BAK, rapidly forms pores in liposomes that release intravesicular FITC-cytochrome c approximately 20A.	tBID	0-4	BCL2-associated X protein	Mus musculus	185-188
11175253-2	2000	tBID induces oligomerization of BAK, and both Bid and Bak knockout mice indicate the importance of this event in the release of cytochrome c. In parallel, the full pro-apoptotic member BAX, which is highly homologous to BAK, rapidly forms pores in liposomes that release intravesicular FITC-cytochrome c approximately 20A.	tBID	0-4	BCL2-antagonist/killer 1	Mus musculus	220-223
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	35-39	caspase 8	Mus musculus	24-33
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	35-39	BCL2-associated X protein	Mus musculus	62-65
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	35-39	BCL2-associated X protein	Mus musculus	197-200
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	35-39	BCL2-associated X protein	Mus musculus	197-200
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	133-137	caspase 8	Mus musculus	24-33
11139284-3	2000	The cleavage product of caspase-8, tBID, induced insertion of BAX into mitochondria in vivo, and reconstitution in vitro showed that tBID, either directly or indirectly, relieved inhibition of the BAX transmembrane signal-anchor by the NH2-terminal domain, resulting in integration of BAX into mitochondrial membrane.	tBID	133-137	BCL2-associated X protein	Mus musculus	62-65
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
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	caspase 8	Mus musculus	140-148
10982793-3	2000	In the current study, we investigated the mechanism by which tBid regulated cytochrome c release in terms of its relationship to mitochondrial permeability transition and Bax, another Bcl-2 family protein.	tBID	61-65	BCL2-associated X protein	Mus musculus	171-174
10982793-3	2000	In the current study, we investigated the mechanism by which tBid regulated cytochrome c release in terms of its relationship to mitochondrial permeability transition and Bax, another Bcl-2 family protein.	tBID	61-65	B cell leukemia/lymphoma 2	Mus musculus	184-189
10950869-0	2000	tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c.	tBID	0-4	cytochrome c, somatic	Homo sapiens	68-80
10950869-1	2000	TNFR1/Fas engagement results in the cleavage of cytosolic BID to truncated tBID, which translocates to mitochondria.	tBID	75-79	TNF receptor superfamily member 1A	Homo sapiens	0-5
10950869-1	2000	TNFR1/Fas engagement results in the cleavage of cytosolic BID to truncated tBID, which translocates to mitochondria.	tBID	75-79	BH3 interacting domain death agonist	Homo sapiens	58-61
10950869-4	2000	Instead, we demonstrate that tBID functions as a membrane-targeted death ligand in which an intact BH3 domain is required for cytochrome c release, but not for targeting.	tBID	29-33	cytochrome c, somatic	Homo sapiens	126-138
10950869-5	2000	Bak-deficient mitochondria and blocking antibodies reveal tBID binds to its mitochondrial partner BAK to release cytochrome c, a process independent of permeability transition.	tBID	58-62	cytochrome c, somatic	Homo sapiens	113-125
10950869-6	2000	Activated tBID results in an allosteric activation of BAK, inducing its intramembranous oligomerization into a proposed pore for cytochrome c efflux, integrating the pathway from death receptors to cell demise.	tBID	10-14	cytochrome c, somatic	Homo sapiens	129-141
10801801-4	2000	The COOH-terminal cleavage fragment of Bid (tBid) becomes localized to mitochondrial membranes and triggers the release of cytochrome c.	tBID	44-48	cytochrome c, somatic	Homo sapiens	123-135
10801801-12	2000	Overexpression of stabilized tBid proteins significantly enhanced cytochrome c release and subsequent apoptosis induction approximately 2-fold compared with wild type tBid.	tBID	29-33	cytochrome c, somatic	Homo sapiens	66-78
10949027-3	2000	Rather, TNF-alpha induced a tBid-dependent conformational change in Bax that allowed an interaction between E1B 19K and conformationally altered Bax, which caused inhibition of cytochrome c release and caspase-9 activation.	tBID	28-32	tumor necrosis factor	Homo sapiens	8-17
11025668-4	2000	Bid normally exists in an inactive state in the cytosol, but after cleavage by caspase 8, the carboxy-terminal portion (tBid) moves from cytosol to mitochondria, where it induces release of cytochrome c.	tBID	120-124	BH3 interacting domain death agonist	Homo sapiens	0-3
11025668-4	2000	Bid normally exists in an inactive state in the cytosol, but after cleavage by caspase 8, the carboxy-terminal portion (tBid) moves from cytosol to mitochondria, where it induces release of cytochrome c.	tBID	120-124	cytochrome c, somatic	Homo sapiens	190-202
10801801-4	2000	The COOH-terminal cleavage fragment of Bid (tBid) becomes localized to mitochondrial membranes and triggers the release of cytochrome c.	tBID	44-48	BH3 interacting domain death agonist	Homo sapiens	39-42
10949027-3	2000	Rather, TNF-alpha induced a tBid-dependent conformational change in Bax that allowed an interaction between E1B 19K and conformationally altered Bax, which caused inhibition of cytochrome c release and caspase-9 activation.	tBID	28-32	BCL2 associated X, apoptosis regulator	Homo sapiens	68-71
10949027-3	2000	Rather, TNF-alpha induced a tBid-dependent conformational change in Bax that allowed an interaction between E1B 19K and conformationally altered Bax, which caused inhibition of cytochrome c release and caspase-9 activation.	tBID	28-32	small nucleolar RNA, H/ACA box 73A	Homo sapiens	108-111
10949027-3	2000	Rather, TNF-alpha induced a tBid-dependent conformational change in Bax that allowed an interaction between E1B 19K and conformationally altered Bax, which caused inhibition of cytochrome c release and caspase-9 activation.	tBID	28-32	BCL2 associated X, apoptosis regulator	Homo sapiens	145-148
10949027-3	2000	Rather, TNF-alpha induced a tBid-dependent conformational change in Bax that allowed an interaction between E1B 19K and conformationally altered Bax, which caused inhibition of cytochrome c release and caspase-9 activation.	tBID	28-32	cytochrome c, somatic	Homo sapiens	177-189
10949027-3	2000	Rather, TNF-alpha induced a tBid-dependent conformational change in Bax that allowed an interaction between E1B 19K and conformationally altered Bax, which caused inhibition of cytochrome c release and caspase-9 activation.	tBID	28-32	caspase 9	Homo sapiens	202-211
9727492-2	1998	While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria.	tBID	62-66	BH3 interacting domain death agonist	Homo sapiens	57-60
9727492-3	1998	tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion.	tBID	0-4	cytochrome c, somatic	Homo sapiens	83-95
9727492-3	1998	tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion.	tBID	0-4	caspase 8	Homo sapiens	111-118
9727492-3	1998	tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion.	tBID	0-4	caspase 8	Homo sapiens	230-237
9727492-4	1998	Coexpression of BclxL inhibits all the apoptotic changes induced by tBID.	tBID	68-72	BCL2 like 1	Homo sapiens	16-21