An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregation (scientific article)

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P275

Creative Commons Attribution 4.0 International

copyrighted

issue

language of work or name

English

Q1860

P921

main subject

prion protein family

Q24724413

P304

page(s)

e48243

P577

publication date

2012-01-01

P1433

published in

PLOS One

Q564954

P1476

title

An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregation

P478

volume

Reverse relations

cites work (P2860)

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Q40544894	Intrabody-mediated diverting of HP1β to the cytoplasm induces co-aggregation of H3-H4 histones and lamin-B receptor
Q38639533	N-terminal truncations of human bHLH transcription factor Twist1 leads to the formation of aggresomes
Q41906667	On the intrinsic disorder status of the major players in programmed cell death pathways
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Q38186535	The aggregation of mutant p53 produces prion-like properties in cancer
Q38527233	The epigenetics of aging and neurodegeneration.
Q47279155	The yin and yang of α-synuclein-associated epigenetics in Parkinson's disease.
Q35822682	Type 2 diabetes as a protein misfolding disease.
Q27000495	Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators

P819	ADS bibcode	2012PLoSO...748243K
P356	DOI	10.1371/JOURNAL.PONE.0048243
P932	PMC publication ID	3486812
P698	PubMed publication ID	23133622
P5875	ResearchGate publication ID	232975652