Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB).
about
Is tau ready for admission to the prion club?Potential roles for prions and protein-only inheritance in cancerContribution of Orb2A stability in regulated amyloid-like oligomerization of Drosophila Orb2Engineering enhanced protein disaggregases for neurodegenerative diseaseTransient CPEB dimerization and translational controlPrions, amyloids, and RNA: Pieces of a puzzle.Characterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEBLuminidependens (LD) is an Arabidopsis protein with prion behavior.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Orientation of aromatic residues in amyloid cores: structural insights into prion fiber diversityDiscovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.Amyloid-like assembly of the low complexity domain of yeast Nab3.Prions in yeast.Modifiers of solid RNP granules control normal RNP dynamics and mRNA activity in early developmentDrosophila CPEB Orb2A mediates memory independent of Its RNA-binding domainAmyloidogenic Oligomerization Transforms Drosophila Orb2 from a Translation Repressor to an Activator.Cell-to-cell propagation of infectious cytosolic protein aggregatesEnergy landscapes of a mechanical prion and their implications for the molecular mechanism of long-term memoryTranslation repressors, an RNA helicase, and developmental cues control RNP phase transitions during early development.Physiological and environmental control of yeast prions.Human prion diseases: molecular, cellular and population biology.The Role of Functional Prion-Like Proteins in the Persistence of Memory.Long-term memory consolidation: The role of RNA-binding proteins with prion-like domains.A Putative Biochemical Engram of Long-Term Memory.The Rho Termination Factor of Clostridium botulinum Contains a Prion-Like Domain with a Highly Amyloidogenic Core.PrionScan: an online database of predicted prion domains in complete proteomes.Transmissible proteins: expanding the prion heresy.Active conversion to the prion state as a molecular switch for cellular adaptation to environmental stress.Proteomic characterization of the abdominal ganglion of Aplysia californica-a protein resource for neuroscience.Trans-acting translational regulatory RNA binding proteins.Discovering Putative Prion-Like Proteins in : A Computational and Experimental AnalysisDual roles for ATP in the regulation of phase separated protein aggregates in oocyte nucleoli
P2860
Q24630925-45EE0840-EC13-494D-97FE-8801F55F3593Q26825056-3603F745-60DA-443C-906E-D3551A454D55Q27315988-DD4B32E9-AAFC-4E2A-AFB3-8366276EA7B8Q28083809-579B65AB-23AF-4C57-8B53-E4BD9C1098FFQ30419697-A3A4D809-7D1B-493C-96C4-09A492939948Q33363261-B59D4B3A-04D7-4F02-A6E2-45B82535DF12Q33919840-FA1FD41D-491D-4D6D-9210-1A7CF7016DF6Q34046710-7F20A09E-6194-4B60-9560-F629CDD58AB6Q34263380-81598E14-6717-4AEF-A87D-54A13913592FQ34661497-134ABAA6-8FCC-4BB7-89DD-5BECB0B079AEQ34714516-986A6DE5-EB9B-4EC3-8272-C4D6896ACB0FQ36147649-B019DB1A-36FC-4355-AFE5-C77537CB753FQ36154362-9D9AACF3-A485-4DB5-A726-82A8ED450B13Q36266144-73B39B55-8504-4D0D-8778-F55AF5B17A03Q36345678-B8A65F4D-B900-4C13-B482-68B9DE5F161CQ36361150-1BE6E772-1402-4FDE-8168-E1CE0A6A8EBEQ36762492-5844DF3E-324B-49AE-82B9-1BD29DCA2071Q37173197-2F11CFDB-6248-436C-A68F-30A34FE93204Q37407831-6B11F510-648E-46B1-8879-618B1B4E449BQ37633376-E1E4472F-A440-4700-A800-CF26E7C9CDF1Q38075119-6BB3211A-6AD1-49BC-BDC6-D3C3996D4D43Q38796068-697496A3-7861-48D3-AD35-69919F2700D8Q38977612-4B4FADBE-032E-4689-BFE7-B0DF3DE780C4Q39211232-2E8CFCD7-AFC4-4611-BFC2-3CC1E161119CQ41773166-6041650D-6EE5-42A5-A616-1C32D678DADCQ41951068-A57908B4-65B1-459D-8D66-4F0AEAEFD710Q42080116-73975316-36EC-4708-9415-DF0BD4404706Q44436665-5EC0DD03-4F04-4F01-9F25-FC5440E4BC98Q47624783-14CA4573-0799-44B9-B948-CF7596CD7354Q50006995-4331B021-988C-4A79-A363-DB66661A17B2Q56346105-681982DD-5870-44D9-9D4C-75FDDBC997B4Q56534985-4AA7B1AD-644A-40BF-B471-3E79530CBE76
P2860
Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB).
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Protein-only mechanism induces ...... lement binding protein (CPEB).
@ast
Protein-only mechanism induces ...... lement binding protein (CPEB).
@en
Protein-only mechanism induces ...... lation element binding protein
@nl
type
label
Protein-only mechanism induces ...... lement binding protein (CPEB).
@ast
Protein-only mechanism induces ...... lement binding protein (CPEB).
@en
Protein-only mechanism induces ...... lation element binding protein
@nl
prefLabel
Protein-only mechanism induces ...... lement binding protein (CPEB).
@ast
Protein-only mechanism induces ...... lement binding protein (CPEB).
@en
Protein-only mechanism induces ...... lation element binding protein
@nl
P2860
P356
P1476
Protein-only mechanism induces ...... lement binding protein (CPEB).
@en
P2093
Sven U Heinrich
P2860
P304
P356
10.1073/PNAS.1019368108
P407
P577
2011-01-26T00:00:00Z