| Extra centrosomes induce PIDD1-mediated inflammation and immunosurveillance. | Extra centrosomes induce PIDD1-mediated inflammation and immunosurveillance.
Garcia-Carpio I, Braun VZ, Weiler ES, Leone M, Niñerola S, Barco A, Fava LL, Villunger A., Free PMC Article | 10/28/2023 |
| Molecular basis of neurodevelopmental disorders caused by pathogenic variants of PIDD. | Molecular basis of neurodevelopmental disorders caused by pathogenic variants of PIDD.
Ha HJ, Park HH. | 02/13/2023 |
| Pathogenic variants in PIDD1 lead to an autosomal recessive neurodevelopmental disorder with pachygyria and psychiatric features. | Pathogenic variants in PIDD1 lead to an autosomal recessive neurodevelopmental disorder with pachygyria and psychiatric features.
Zaki MS, Accogli A, Mirzaa G, Rahman F, Mohammed H, Porras-Hurtado GL, Efthymiou S, Maqbool S, Shukla A, Vincent JB, Hussain A, Mir A, Beetz C, Leubauer A, Houlden H, Gleeson JG, Maroofian R., Free PMC Article | 03/19/2022 |
| ATR signalling mediates the prosurvival function of phospho-NPM against PIDDosome mediated cell death. | ATR signalling mediates the prosurvival function of phospho-NPM against PIDDosome mediated cell death.
Hiregange D, Naick H, Rao BJ. | 08/7/2021 |
| Biallelic mutations in the death domain of PIDD1 impair caspase-2 activation and are associated with intellectual disability. | Biallelic mutations in the death domain of PIDD1 impair caspase-2 activation and are associated with intellectual disability.
Sheikh TI, Vasli N, Pastore S, Kharizi K, Harripaul R, Fattahi Z, Pande S, Naeem F, Hussain A, Mir A, Islam O, Girisha KM, Irfan M, Ayub M, Schwarzer C, Najmabadi H, Shukla A, Sladky VC, Braun VZ, Garcia-Carpio I, Villunger A, Vincent JB., Free PMC Article | 07/31/2021 |
| PIDD interaction with KEAP1 as a new mutation-independent mechanism to promote NRF2 stabilization and chemoresistance in NSCLC. | PIDD interaction with KEAP1 as a new mutation-independent mechanism to promote NRF2 stabilization and chemoresistance in NSCLC.
Ji L, Zhang R, Chen J, Xue Q, Moghal N, Tsao MS., Free PMC Article | 10/24/2020 |
| Attention-deficit/hyperactivity disorder risk alleles correlated with increased expression (and decreased methylation) of ARTN and PIDD1 and with a decreased expression (and increased methylation) of C2orf82. | Exploring genetic variation that influences brain methylation in attention-deficit/hyperactivity disorder.
Pineda-Cirera L, Shivalikanjli A, Cabana-Domínguez J, Demontis D, Rajagopal VM, Børglum AD, Faraone SV, Cormand B, Fernàndez-Castillo N., Free PMC Article | 07/18/2020 |
| Whole exome sequencing (WES) of an affected fetus, and subsequent Sanger sequencing of the second fetus, revealed a homozygous frameshift variant in CRADD, which encodes an adaptor protein that interacts with PIDD and caspase-2 to initiate apoptosis | Homozygous null variant in CRADD, encoding an adaptor protein that mediates apoptosis, is associated with lissencephaly.
Harel T, Hacohen N, Shaag A, Gomori M, Singer A, Elpeleg O, Meiner V. | 12/2/2017 |
| NPM1-dependent nucleolar PIDDosome is a key initiator of the caspase-2 activation cascade. | NPM1 directs PIDDosome-dependent caspase-2 activation in the nucleolus.
Ando K, Parsons MJ, Shah RB, Charendoff CI, Paris SL, Liu PH, Fassio SR, Rohrman BA, Thompson R, Oberst A, Sidi S, Bouchier-Hayes L., Free PMC Article | 09/16/2017 |
| PIDD expression was lower in HCC tissues and HCC cell lines, compared with the adjacent non-tumorous tissues and LO2 normal hepatocytes. PIDD could serve as an independent prognostic factor to predict the survival of HCC patients. PIDD facilitated cell cycle progression and accelerated cell proliferation in HepG2 cells, while overexpression of PIDD resulted in cell cycle arrest at G1 phase in Hep3B cells. | Low expression of PIDD is associated with cell proliferation and apoptosis in hepatocellular carcinoma.
Shi W, Huang W, Chen Y, Zhang S, Xu P, Gu X, Fan H, Xu J, Chen Y, Ni R, Lu C, Zhang X. | 02/18/2017 |
| By sequestering PIDD at the kinetochore, BubR1 acts to delay PIDDosome formation until the next cycle, defining a new mechanism by which cells evade apoptosis during mitosis. | An Inhibitor of PIDDosome Formation.
Thompson R, Shah RB, Liu PH, Gupta YK, Ando K, Aggarwal AK, Sidi S., Free PMC Article | 08/22/2015 |
| The ATM phosphorylation of the PIDD DD enables a binary switch through which cells elect to survive or die upon DNA injury. | PIDD death-domain phosphorylation by ATM controls prodeath versus prosurvival PIDDosome signaling.
Ando K, Kernan JL, Liu PH, Sanda T, Logette E, Tschopp J, Look AT, Wang J, Bouchier-Hayes L, Sidi S., Free PMC Article | 01/26/2013 |
| PIDD performs key functions upon UV irradiation, including TLS, NHEJ, NF-kappaB activation and cell death. | PIDD orchestrates translesion DNA synthesis in response to UV irradiation.
Logette E, Schuepbach-Mallepell S, Eckert MJ, Leo XH, Jaccard B, Manzl C, Tardivel A, Villunger A, Quadroni M, Gaide O, Tschopp J., Free PMC Article | 08/27/2011 |
| Hsp90 has a major role in controlling PIDD functional activity. | Regulation of PIDD auto-proteolysis and activity by the molecular chaperone Hsp90.
Tinel A, Eckert MJ, Logette E, Lippens S, Janssens S, Jaccard B, Quadroni M, Tschopp J., Free PMC Article | 06/4/2011 |
| a new splicing variant of PIDD named PIDD4 is reported. | PIDD4, a novel PIDD isoform without the LRR domain, can independently induce cell apoptosis in cytoplasm.
Huang L, Han D, Yang X, Qin B, Ji G, Yu L. | 06/4/2011 |
| point mutations on RAIDD (R147E) and on PIDD (Y814A) exert a dominant negative effect on the formation of the PIDDosome, and that this effect cannot be applied after the PIDDosome has been formed | Identification and analysis of dominant negative mutants of RAIDD and PIDD.
Jang TH, Bae JY, Park OK, Kim JH, Cho KH, Jeon JH, Park HH. | 07/26/2010 |
| Total caspase-2 is upregulated during tumour progression in renal cell carcinomas. | PIDDosome expression and the role of caspase-2 activation for chemotherapy-induced apoptosis in RCCs.
Heikaus S, Pejin I, Gabbert HE, Ramp U, Mahotka C., Free PMC Article | 06/14/2010 |
| p53-mediated apoptosis occurs by a PIDD- and caspase 2-dependent mechanism, and p53's full transcriptional regulatory functions may be required only for events that are downstream of cytochrome c release | A role for caspase 2 and PIDD in the process of p53-mediated apoptosis.
Baptiste-Okoh N, Barsotti AM, Prives C., Free PMC Article | 01/21/2010 |
| PIDD isoforms are capable of activating nuclear factor-kappaB in response to genotoxic stress, but only isoform 1 interacts with RIP-associated ICH-1/CED-3 homologous protein with a death domain and activates caspase-2. | p53-induced protein with a death domain (PIDD) isoforms differentially activate nuclear factor-kappaB and caspase-2 in response to genotoxic stress.
Cuenin S, Tinel A, Janssens S, Tschopp J. | 01/21/2010 |
| No correlation between Pidd expression and the p53 mutation status of oral squamous cell carcinoma, suggesting that Pidd expression may be regulated by p53-independent mechanisms. | The expression of p53-induced protein with death domain (Pidd) and apoptosis in oral squamous cell carcinoma.
Bradley G, Tremblay S, Irish J, MacMillan C, Baker G, Gullane P, Benchimol S., Free PMC Article | 01/21/2010 |
| PIDD plays a critical role in DNA-damage-induced NF-kappaB activation, controlling the balance between life and death upon DNA damage. | PIDD mediates NF-kappaB activation in response to DNA damage.
Janssens S, Tinel A, Lippens S, Tschopp J. | 01/21/2010 |
| The functional consequences of the identified PIDD/nucleolin interaction remain to be elucidated, but may be related to a recently discovered new role for PIDD in the activation of NF-kappaB upon genotoxic stress. | Upon intracellular processing, the C-terminal death domain-containing fragment of the p53-inducible PIDD/LRDD protein translocates to the nucleoli and interacts with nucleolin.
Pick R, Badura S, Bösser S, Zörnig M. | 01/21/2010 |
| activation of caspase-2 occurs in a complex that contains PIDD, whose expression is induced by p53, and RAIDD; increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli | The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress.
Tinel A, Tschopp J. | 01/21/2010 |
| PIDD autoproteolysis marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway | Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway.
Tinel A, Janssens S, Lippens S, Cuenin S, Logette E, Jaccard B, Quadroni M, Tschopp J., Free PMC Article | 01/21/2010 |
| PIDD death domain (DD) and RAIDD DD assemble into an oligomeric complex. Within the PIDDosome, the interaction between PIDD and RAIDD is mediated by a homotypic interaction between their death domains. | Crystallization and preliminary X-ray crystallographic studies of the oligomeric death-domain complex between PIDD and RAIDD.
Park HH, Wu H., Free PMC Article | 01/21/2010 |