PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
16183742-4	2005	Here we show that PIDD is a cytoplasmic protein, and that PIDD-induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP)-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD).	pidd	18-22	CASP2 and RIPK1 domain containing adaptor with death domain	Mus musculus	257-262
16183742-4	2005	Here we show that PIDD is a cytoplasmic protein, and that PIDD-induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP)-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD).	pidd	58-62	CASP2 and RIPK1 domain containing adaptor with death domain	Mus musculus	257-262
16183742-5	2005	We provide evidence that PIDD-induced cell death is associated with the early activation of caspase-2 and later activation of caspase-3 and -7.	pidd	25-29	caspase 2	Mus musculus	92-101
16183742-5	2005	We provide evidence that PIDD-induced cell death is associated with the early activation of caspase-2 and later activation of caspase-3 and -7.	pidd	25-29	caspase 3	Mus musculus	126-142
16183742-6	2005	Our results also show that caspase-2(-/-), in contrast to RAIDD(-/-), mouse embryonic fibroblasts, are only partially resistant to PIDD.	pidd	131-135	caspase 2	Mus musculus	27-36
16183742-7	2005	Our findings suggest that caspase-2 contributes to PIDD-mediated cell death, but that it is not the sole effector of this pathway.	pidd	51-55	caspase 2	Mus musculus	26-35
31533600-2	2019	p53-induced protein with a death domain (PIDD) is a well-known regulator of genotoxic stress-induced apoptosis, which is constitutively cleaved into three main fragments: PIDD-N, PIDD-C and PIDD-CC.	pidd	41-45	Wistar clone pR53P1 p53 pseudogene	Rattus norvegicus	0-3
1732306-4	1992	At baseline of the present study, the PIDD group had a mean blood glucose level of 11.8 mmol/l and a mean glycosylated hemoglobin (HBA1) level of 10.7%.	pidd	38-42	hemoglobin subunit alpha 1	Homo sapiens	131-135
31533600-10	2019	Meanwhile, the expression of PIDD was significantly increased in Brn3a (a marker of RGCs) positive cells, indicating that the localization of PIDD appeared to be confined to RGCs.	pidd	29-33	POU class 4 homeobox 1	Rattus norvegicus	65-70
31533600-10	2019	Meanwhile, the expression of PIDD was significantly increased in Brn3a (a marker of RGCs) positive cells, indicating that the localization of PIDD appeared to be confined to RGCs.	pidd	142-146	POU class 4 homeobox 1	Rattus norvegicus	65-70
31533600-11	2019	Furthermore, inhibition of PIDD prevented RGCs apoptosis by inhibiting caspase-2 and tBid activation.	pidd	27-31	caspase 2	Rattus norvegicus	71-80
31533600-12	2019	CONCLUSIONS: Taken together, PIDD may play a crucial role in RGCs apoptosis after ONC, and this process may be relevant to caspase-2 and tBid.	pidd	29-33	caspase 2	Rattus norvegicus	123-132
26621219-8	2015	In turn, DCA-induced oxidative stress resulted in caspase-2 activation and NF-kappaB/miR-21 inhibition, in a PIDD-dependent manner.	pidd	109-113	caspase 2	Rattus norvegicus	50-59
30245858-0	2018	PIDD-dependent activation of caspase-2-mediated mitochondrial injury in E1A-induced cellular sensitivity to macrophage nitric oxide-induced apoptosis.	pidd	0-4	caspase 2	Mus musculus	29-38
29309644-0	2018	PIDD mediates the association of DNA-PKcs and ATR at stalled replication forks to facilitate the ATR signaling pathway.	pidd	0-4	protein kinase, DNA-activated, catalytic subunit	Homo sapiens	33-41
29309644-0	2018	PIDD mediates the association of DNA-PKcs and ATR at stalled replication forks to facilitate the ATR signaling pathway.	pidd	0-4	ATR serine/threonine kinase	Homo sapiens	46-49
29309644-0	2018	PIDD mediates the association of DNA-PKcs and ATR at stalled replication forks to facilitate the ATR signaling pathway.	pidd	0-4	ATR serine/threonine kinase	Homo sapiens	97-100
29309644-6	2018	Our results demonstrate that PIDD is required to recruit DNA-PKcs to stalled replication forks through direct binding to DNA-PKcs at the N" terminal region.	pidd	29-33	protein kinase, DNA-activated, catalytic subunit	Homo sapiens	57-65
29309644-6	2018	Our results demonstrate that PIDD is required to recruit DNA-PKcs to stalled replication forks through direct binding to DNA-PKcs at the N" terminal region.	pidd	29-33	protein kinase, DNA-activated, catalytic subunit	Homo sapiens	121-129
29309644-8	2018	Taken together, our results indicate that PIDD, but not the Ku heterodimer, mediates the DNA-PKcs activity at stalled replication forks and facilitates the ATR signaling pathway in the cellular response to replication stress.	pidd	42-46	protein kinase, DNA-activated, catalytic subunit	Homo sapiens	89-97
29309644-8	2018	Taken together, our results indicate that PIDD, but not the Ku heterodimer, mediates the DNA-PKcs activity at stalled replication forks and facilitates the ATR signaling pathway in the cellular response to replication stress.	pidd	42-46	ATR serine/threonine kinase	Homo sapiens	156-159
26621219-8	2015	In turn, DCA-induced oxidative stress resulted in caspase-2 activation and NF-kappaB/miR-21 inhibition, in a PIDD-dependent manner.	pidd	109-113	microRNA 21	Rattus norvegicus	85-91
22595758-2	2012	PIDD has been implicated in p53-mediated cell death in response to DNA damage but also in DNA repair and nuclear factor kappa-light-chain enhancer (NF-kappaB) activation upon genotoxic stress, together with RIP-1 kinase and Nemo/IKKgamma.	pidd	0-4	tumor protein p53	Homo sapiens	28-31
22595758-2	2012	PIDD has been implicated in p53-mediated cell death in response to DNA damage but also in DNA repair and nuclear factor kappa-light-chain enhancer (NF-kappaB) activation upon genotoxic stress, together with RIP-1 kinase and Nemo/IKKgamma.	pidd	0-4	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	224-228
22595758-2	2012	PIDD has been implicated in p53-mediated cell death in response to DNA damage but also in DNA repair and nuclear factor kappa-light-chain enhancer (NF-kappaB) activation upon genotoxic stress, together with RIP-1 kinase and Nemo/IKKgamma.	pidd	0-4	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	229-237
19770592-4	2009	The present study demonstrates that cisplatin induces the PIDD (p53 induced protein with a death domain) dependent activation of caspase-2.	pidd	58-62	tumor protein p53	Homo sapiens	64-67
22515271-5	2012	We show that treatment of wild-type or PIDD-null neurons with Abeta or NGF deprivation induces formation of a complex of caspase 2 and RAIDD.	pidd	39-43	caspase 2	Mus musculus	121-130
22515271-5	2012	We show that treatment of wild-type or PIDD-null neurons with Abeta or NGF deprivation induces formation of a complex of caspase 2 and RAIDD.	pidd	39-43	CASP2 and RIPK1 domain containing adaptor with death domain	Mus musculus	135-140
20966961-0	2011	Regulation of PIDD auto-proteolysis and activity by the molecular chaperone Hsp90.	pidd	14-18	heat shock protein 90 alpha family class A member 1	Homo sapiens	76-81
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	68-72	tumor protein p53	Homo sapiens	27-30
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	68-72	caspase 2	Homo sapiens	190-199
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	68-72	caspase 2	Homo sapiens	242-251
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	68-72	receptor interacting serine/threonine kinase 1	Homo sapiens	271-275
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	68-72	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	280-284
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	101-105	tumor protein p53	Homo sapiens	27-30
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	101-105	caspase 2	Homo sapiens	190-199
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	101-105	caspase 2	Homo sapiens	242-251
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	101-105	receptor interacting serine/threonine kinase 1	Homo sapiens	271-275
20966961-1	2011	In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappaB activation.	pidd	101-105	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	280-284
20966961-4	2011	In this study, we screened for novel PIDD regulators and identified heat shock protein 90 (Hsp90) as a major effector in both PIDD protein maturation and activation.	pidd	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-89
20966961-4	2011	In this study, we screened for novel PIDD regulators and identified heat shock protein 90 (Hsp90) as a major effector in both PIDD protein maturation and activation.	pidd	37-41	heat shock protein 90 alpha family class A member 1	Homo sapiens	91-96
20966961-6	2011	Consequently, both PIDD-mediated NF-kappaB and caspase-2 activation are abrogated.	pidd	19-23	caspase 2	Homo sapiens	47-56
19997861-3	2010	OBJECTIVE: The objective of this study as to evaluate the efficacy, pharmacokinetics, and safety of Flebogamma 10% DIF for immunoglobulin replacement therapy in primary immunodeficiency diseases (PIDD).	pidd	196-200	tumor necrosis factor	Homo sapiens	115-118
19997861-9	2010	CONCLUSIONS: Flebogamma 10% DIF is efficacious and safe, has adequate pharmacokinetic properties, and is well-tolerated for the treatment of PIDD.	pidd	141-145	tumor necrosis factor	Homo sapiens	28-31
19770592-4	2009	The present study demonstrates that cisplatin induces the PIDD (p53 induced protein with a death domain) dependent activation of caspase-2.	pidd	58-62	caspase 2	Homo sapiens	129-138
18424335-3	2008	Many of these studies have focused on the presence and function of regulatory T (T(REG)) cells in PIDD, particularly since the discovery of murine and human syndromes associated with T(REG) deficiency.	pidd	98-102	regenerating family member 1 alpha	Homo sapiens	83-86
17437012-1	2007	The Pidd (p53-induced protein with death domain) gene was shown to be induced by the tumour suppressor p53 and to mediate p53-dependent apoptosis in mouse and human cells, through interactions with components of both the mitochondrial and the death receptor signalling pathways.	pidd	4-8	transformation related protein 53, pseudogene	Mus musculus	10-13
17437012-1	2007	The Pidd (p53-induced protein with death domain) gene was shown to be induced by the tumour suppressor p53 and to mediate p53-dependent apoptosis in mouse and human cells, through interactions with components of both the mitochondrial and the death receptor signalling pathways.	pidd	4-8	transformation related protein 53, pseudogene	Mus musculus	103-106
17437012-1	2007	The Pidd (p53-induced protein with death domain) gene was shown to be induced by the tumour suppressor p53 and to mediate p53-dependent apoptosis in mouse and human cells, through interactions with components of both the mitochondrial and the death receptor signalling pathways.	pidd	4-8	transformation related protein 53, pseudogene	Mus musculus	103-106
17637755-4	2008	Two isoforms of PIDD, PIDD (isoform 1) and LRDD (isoform 2), have already been reported and we describe here a third isoform.	pidd	16-20	p53-induced death domain protein 1	Homo sapiens	43-47
17159900-0	2007	Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway.	pidd	19-23	caspase 2	Homo sapiens	64-73
17159900-0	2007	Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway.	pidd	19-23	nuclear factor kappa B subunit 1	Homo sapiens	91-100
17159900-2	2007	PIDD (p53-induced protein with a death domain) is constitutively processed giving rise to a 48-kDa N-terminal fragment containing the leucine-rich repeats (LRRs, PIDD-N) and a 51-kDa C-terminal fragment containing the death domain (DD, PIDD-C).	pidd	0-4	tumor protein p53	Homo sapiens	6-9