Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation.
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MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune responseA novel role of CPEB3 in regulating EGFR gene transcription via association with Stat5b in neuronsSumoylation in Synaptic Function and DysfunctionPotential roles for prions and protein-only inheritance in cancerPrion-like polymerization as a signaling mechanismDesigning tools for assumption-proof brain mappingA growing family: the expanding universe of the bacterial cytoskeletonAsparagine repeats in Plasmodium falciparum proteins: good for nothing?Insoluble cellular prion protein and its association with prion and Alzheimer diseasesNext generation organelles: structure and role of germ granules in the germlineContribution of Orb2A stability in regulated amyloid-like oligomerization of Drosophila Orb2Rebels with a cause: molecular features and physiological consequences of yeast prionsEngineering enhanced protein disaggregases for neurodegenerative diseaseAmyloid-associated activity contributes to the severity and toxicity of a prion phenotypeSUMOylation Is an Inhibitory Constraint that Regulates the Prion-like Aggregation and Activity of CPEB3Neuralized1 activates CPEB3: a function for nonproteolytic ubiquitin in synaptic plasticity and memory storageNew Phosphospecific Antibody Reveals Isoform-Specific Phosphorylation of CPEB3 ProteinAre aberrant phase transitions a driver of cellular aging?Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial feversTransient CPEB dimerization and translational controlHeritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Misassembly of full-length Disrupted-in-Schizophrenia 1 protein is linked to altered dopamine homeostasis and behavioral deficits.Strengthening relationships: amyloids create adhesion nanodomains in yeasts.Prions, amyloids, and RNA: Pieces of a puzzle.Biology and genetics of prions causing neurodegenerationThe Surprising Role of Amyloid Fibrils in HIV InfectionShort- and long-term memory are modulated by multiple isoforms of the fragile X mental retardation proteinCharacterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEBDrosophila Orb2 targets genes involved in neuronal growth, synapse formation, and protein turnover.Luminidependens (LD) is an Arabidopsis protein with prion behavior.Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.PrionHome: a database of prions and other sequences relevant to prion phenomena.A role for neuronal piRNAs in the epigenetic control of memory-related synaptic plasticityThe tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.AU-rich element-binding protein negatively regulates CCAAT enhancer-binding protein mRNA stability during long-term synaptic plasticity in Aplysia.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humansGenomics and proteomics in solving brain complexity.Specificity factors in cytoplasmic polyadenylationMolecular constraints on synaptic tagging and maintenance of long-term potentiation: a predictive model.Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation.
P2860
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P2860
Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年学术文章
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2010年学术文章
@zh-cn
2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
@yue
name
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@ast
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@en
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@nl
type
label
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@ast
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@en
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@nl
prefLabel
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@ast
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@en
Aplysia CPEB can form prion-li ...... ute to long-term facilitation.
@nl
P2093
P1433
P1476
Aplysia CPEB can form prion-li ...... bute to long-term facilitation
@en
P2093
Eric R Kandel
Erica White-Grindley
Yun-Beom Choi
P304
P356
10.1016/J.CELL.2010.01.008
P407
P577
2010-02-01T00:00:00Z