ArticlePloS one2012
An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Post-Translational Modifications (PTMs) of mutp53 and Epigenetic Changes Induced by mutp53.Biology · 2024Review
- The Common Denominators of Parkinson's Disease Pathogenesis and Methamphetamine Abuse.Current neuropharmacology · 2024Review
- Challenges in Brugada Syndrome Stratification: InvestigatingInternational journal of molecular sciences · 2023Article
- Amyloid-like p53 as prognostic biomarker in serous ovarian cancer-a study of the OVCAD consortium.Oncogene · 2023Article
- Energy Crisis Links to Autophagy and Ferroptosis in Alzheimer's Disease: Current Evidence and Future Avenues.Current neuropharmacology · 2023Article
- p53 amyloid aggregation in cancer: function, mechanism, and therapy.Experimental hematology & oncology · 2022Review
- Regulation of Social Stress and Neural Degeneration by Activity-Regulated Genes and Epigenetic Mechanisms in Dopaminergic Neurons.Molecular neurobiology · 2020Review
- p53 reactivation with induction of massive apoptosis-1 (PRIMA-1) inhibits amyloid aggregation of mutant p53 in cancer cells.The Journal of biological chemistry · 2019Article
- Inhibition of Cyclooxygenase-2 (COX-2) Initiates Autophagy and Potentiates MPTP-Induced Autophagic Cell Death of Human Neuroblastoma Cells, SH-SY5Y: an Inside in the Pathology of Parkinson's Disease.Molecular neurobiology · 2018Article
- N-terminal truncations of human bHLH transcription factor Twist1 leads to the formation of aggresomes.Molecular and cellular biochemistry · 2018Article
- CBP/p300 Bromodomains Regulate Amyloid-like Protein Aggregation upon Aberrant Lysine Acetylation.Cell chemical biology · 2017Article
- The epigenetics of aging and neurodegeneration.Progress in neurobiology · 2015Review
- Type 2 diabetes as a protein misfolding disease.Trends in molecular medicine · 2015Review
- Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.Experimental & molecular medicine · 2015Review
- Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators.Frontiers in molecular biosciences · 2014Review
- Epigenetic landscape of Parkinson's disease: emerging role in disease mechanisms and therapeutic modalities.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2013Review
- Expanding the prion concept to cancer biology: dominant-negative effect of aggregates of mutant p53 tumour suppressor.Bioscience reports · 2013Review
- Dissecting the pathways that destabilize mutant p53: the proteasome or autophagy?Cell cycle (Georgetown, Tex.) · 2013Article
- On the intrinsic disorder status of the major players in programmed cell death pathways.F1000Research · 2013Article
- Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging.International journal of cell biology · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Several human diseases including neurodegenerative disorders and cancer are associated with abnormal accumulation and aggregation of misfolded proteins. Proteins with high tendency to aggregate include the p53 gene product, TAU and alpha synuclein. The potential toxicity of aberrantly folded proteins is limited via their transport into intracellular sub-compartments, the aggresomes, where misfolded proteins are stored or cleared via autophagy. We have identified a region of the acetyltransferase p300 that is highly disordered and displays similarities with prion-like domains. We show that this region is encoded as an alternative spliced variant independently of the acetyltransferase domain, and provides an interaction interface for various misfolded proteins, promoting their aggregation. p300 enhances aggregation of TAU and of p53 and is a component of cellular aggregates in both tissue culture cells and in alpha-synuclein positive Lewy bodies of patients affected by Parkinson disease. Down-regulation of p300 impairs aggresome formation and enhances cytotoxicity induced by misfolded protein stress. These data unravel a novel activity of p300, offer new insights into the function of disordered domains and implicate p300 in pathological aggregation that occurs in neurodegeneration and cancer.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.