Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
about
The prion hypothesis in Parkinson's disease: Braak to the futureLeucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration.p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for bothSequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradationThe Guanine nucleotide exchange factor kalirin-7 is a novel synphilin-1 interacting protein and modifies synphilin-1 aggregate transport and formationPrion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular TransportRecruitment of the oncoprotein v-ErbA to aggresomes.Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotesIdentification of Cellular Proteome Modifications in Response to West Nile Virus InfectionAutophagy fights disease through cellular self-digestion14-3-3 protein targets misfolded chaperone-associated proteins to aggresomesImmunomodulators as Therapeutic Agents in Mitigating the Progression of Parkinson's DiseaseThe parkin-like human homolog of Drosophila ariadne-1 (HHARI) can induce aggresome formation in mammalian cells and is immunologically detectable in Lewy bodiesCasein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formationModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsAggresome formation and neurodegenerative diseases: therapeutic implicationsSeipinopathy: a novel endoplasmic reticulum stress-associated diseaseSirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's diseaseα-Synuclein protects against manganese neurotoxic insult during the early stages of exposure in a dopaminergic cell model of Parkinson's diseaseBiochemical assessment of precuneus and posterior cingulate gyrus in the context of brain aging and Alzheimer's diseaseRuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils.Implications of protein structure instability: from physiological to pathological secondary structure.Ubiquitination is involved in secondary growth, not initial formation of polyglutamine protein aggregates in C. elegans.Proteasome failure promotes positioning of lysosomes around the aggresome via local block of microtubule-dependent transport.Nigral proteasome inhibition in mice leads to motor and non-motor deficits and increased expression of Ser129 phosphorylated α-synucleinUbiquitin conjugating enzymes participate in polyglutamine protein aggregation.Insights into the effects of alpha-synuclein expression and proteasome inhibition on glutathione metabolism through a dynamic in silico model of Parkinson's disease: validation by cell culture data.Focal distortion of the nuclear envelope by huntingtin aggregates revealed by lamin immunostainingAggresome-forming TTRAP mediates pro-apoptotic properties of Parkinson's disease-associated DJ-1 missense mutations.Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infectionSynphilin-1 enhances α-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent mannerAggresome formation is regulated by RanBPM through an interaction with HDAC6Herpes simplex virus reorganizes the cellular DNA repair and protein quality control machinery.Synphilin-1 attenuates neuronal degeneration in the A53T alpha-synuclein transgenic mouse modelUbiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implicationsProtein quality control during erythropoiesis and hemoglobin synthesisCongenital cataract causing mutants of αA-crystallin/sHSP form aggregates and aggresomes degraded through ubiquitin-proteasome pathway.Hsp70 and its molecular role in nervous system diseasesDisentangling the relationship between lewy bodies and nigral neuronal loss in Parkinson's disease.p62/sequestosome 1 regulates aggresome formation of pathogenic ataxin-3 with expanded polyglutamine
P2860
Q22001062-054CA003-FD0D-4B2B-84E8-E947BD51A121Q24298689-100464B2-5DFA-4B47-B290-29DD42D43C6BQ24301629-94ACC9DB-6DB2-4C82-AF5E-80A812E05EF7Q24305254-515467FE-80A4-4CFA-82BA-C0E806514861Q24307589-617DF44E-B71C-4BF0-8AD1-90AA1C0E4CF1Q27307839-1D513007-D701-430E-9848-E19C5C903055Q27308854-3D847137-4053-4015-9244-7F99CF857271Q27334980-E95565C2-5804-4DD8-8470-DE1E2F4705DCQ27488891-5E1C6188-C3DE-4738-96B7-4F909842CABAQ27860902-E6BFE259-80F4-4619-8685-33114C8ED139Q27930016-1EB8A596-0419-4A50-8C6E-FD5A3D4D50F4Q28079187-C7646FD1-6310-4612-9EB2-DF94BFEB5EEAQ28117293-072E02B8-6121-4A2A-9BE9-E4EB249F9B2AQ28188133-675A2E5E-89EA-49A9-9AFD-B086F1290168Q28259424-B05F9D3A-BE3D-4C39-B5E4-BD810215258CQ28265926-B38A86E2-1521-4D99-B6D3-BF129E96DD2EQ28293837-0FC5CA11-2A8D-4B1F-BF02-CF753F090150Q28307422-F57D940C-60A1-4A90-B6A3-073670DA46E0Q28386621-8B63FEE9-2453-46F8-AB7F-FFC3FF602658Q28542628-46659571-6C7F-45B2-A447-08083E067482Q30356564-2DBBDEF5-63CD-4D66-BDA7-B5949C11D832Q30416896-ADBD5F21-0435-45A5-9CBC-85EFDF7AB9B7Q30515046-725181C5-BBAE-4493-BAC0-47A4A66CF8E5Q30576520-9865358D-E4D9-4E41-A920-D81886F51160Q30633819-C9EAF423-1896-4D9F-ACAC-0729B2AFC7BBQ33292491-C40516B8-E401-4F5D-A796-02E817EB99F3Q33365370-8EFC118A-41CF-4B39-A59E-A449135F009CQ33374464-B78415AF-7D83-4CC9-A6CF-B05E84092C22Q33385971-236CEA0A-3F1B-44FA-9842-DE4C06E001F3Q33509511-21B504A0-56D8-473A-A9F7-FA66671DD368Q33742140-221F2A90-55FB-4E58-BE26-7130EAA511B0Q33757230-F475C544-9FA8-4E5E-B4CA-772668750872Q33760836-C341A87F-05E5-46C6-88E1-2425D9A8F1E1Q33832846-E423CCCC-CE23-450E-B186-4004A952DF83Q34012297-426B21B3-5DBF-48D2-A4F0-8652A89B1DFCQ34060218-90698C4C-E363-404F-AC6C-C2C807F3AFF9Q34091248-704ADF29-0781-444F-980B-9FFAF9267EFFQ34170760-C6C23332-BD44-44C8-A289-112FE459FAEBQ34336792-4E652EC5-CEBB-4B15-BF2A-3F4518B689D3Q34358473-F01D2D22-8B0F-49EF-BEED-40D134F8F005
P2860
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
description
2004 nî lūn-bûn
@nan
2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@ast
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@en
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@nl
type
label
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@ast
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@en
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@nl
prefLabel
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@ast
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@en
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@nl
P2093
P3181
P356
P1476
Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective
@en
P2093
Eunsung Junn
M Maral Mouradian
Mikiei Tanaka
Takeshi Iwatsubo
Yong Man Kim
P304
P3181
P356
10.1074/JBC.M310994200
P407
P577
2004-02-06T00:00:00Z