Siah-1 facilitates ubiquitination and degradation of synphilin-1
about
The Guanine nucleotide exchange factor kalirin-7 is a novel synphilin-1 interacting protein and modifies synphilin-1 aggregate transport and formationA novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the brains of Alzheimer's patients and targets ATP6V0C for degradationNUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1Structure-Based Design of Covalent Siah InhibitorsSynphilin-1 binds ATP and regulates intracellular energy statusDopaminergic neurons generated from monkey embryonic stem cells function in a Parkinson primate model.siah-1 Protein is necessary for high glucose-induced glyceraldehyde-3-phosphate dehydrogenase nuclear accumulation and cell death in Muller cellsThe ubiquitin ligase Siah2 and the hypoxia response.Oxidatively modified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease: many pathways to neurodegenerationLys-63-linked ubiquitination by E3 ubiquitin ligase Nedd4-1 facilitates endosomal sequestration of internalized α-synuclein.Proteasome inhibition promotes Parkin-Ubc13 interaction and lysine 63-linked ubiquitinationHerpes simplex virus immediate-early protein ICP0 is targeted by SIAH-1 for proteasomal degradation.Splicing variants of porcine synphilin-1The aggravating role of the ubiquitin-proteasome system in neurodegeneration.A novel obesity model: synphilin-1-induced hyperphagia and obesity in mice.The Protein Complex of Neurodegeneration-related Phosphoinositide Phosphatase Sac3 and ArPIKfyve Binds the Lewy Body-associated Synphilin-1, Preventing Its Aggregation.The role of ubiquitin-protein ligases in neurodegenerative disease.Synphilin-1 alters metabolic homeostasis in a novel Drosophila obesity modelSiah-1b is a direct transcriptional target of p53: identification of the functional p53 responsive element in the siah-1b promoterSynphilin-1A inhibits seven in absentia homolog (SIAH) and modulates alpha-synuclein monoubiquitylation and inclusion formation.Site-specific differences in proteasome-dependent degradation of monoubiquitinated α-synuclein.Molecular pathology of Lewy body diseases.Mediation of Af4 protein function in the cerebellum by Siah proteinsUbiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease.Molecular chaperones as rational drug targets for Parkinson's disease therapeutics.Novel siRNA delivery strategy: a new "strand" in CNS translational medicine?Regulators and effectors of Siah ubiquitin ligases.Synphilin-1 attenuates mutant LRRK2-induced neurodegeneration in Parkinson's disease models.E3 Ubiquitin Ligase Siah-1 is Down-regulated and Fails to Target Natural HBx Truncates for Degradation in Hepatocellular Carcinoma.Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: implications for proteasomal function and Lewy body formation.Specific induction of neuronal cells from bone marrow stromal cells and application for autologous transplantation.A Caenorhabditis elegans Parkin mutant with altered solubility couples alpha-synuclein aggregation to proteotoxic stress.The E3 ubiquitin ligase Siah-1 suppresses avian reovirus infection by targeting p10 for degradation.TRAF6 promotes atypical ubiquitination of mutant DJ-1 and alpha-synuclein and is localized to Lewy bodies in sporadic Parkinson's disease brains.SIAH1; SIAH2 bind SNCAIPSIAH1; SIAH2 ubiquitinate SNCAIPSynphilin-1 inhibits alpha-synuclein degradation by the proteasome.The PINK1, synphilin-1 and SIAH-1 complex constitutes a novel mitophagy pathway.Unconventional secretion of misfolded proteins promotes adaptation to proteasome dysfunction in mammalian cells.Synphilin-1A is a phosphoprotein phosphatase 1-interacting protein and affects PPP1 sorting to subcellular compartments.
P2860
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P2860
Siah-1 facilitates ubiquitination and degradation of synphilin-1
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@ast
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@en
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@en-gb
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@nl
type
label
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@ast
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@en
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@en-gb
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@nl
prefLabel
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@ast
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@en
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@en-gb
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@nl
P2093
P921
P356
P1476
Siah-1 facilitates ubiquitination and degradation of synphilin-1
@en
P2093
Akira Kikuchi
Eizo Iseki
Hiroshi Yamashita
Masayasu Matsumoto
Shosei Kishida
Takeshi Nakamura
Tetsuya Takahashi
Yoshito Nagano
P304
P356
10.1074/JBC.M306347200
P407
P577
2003-12-19T00:00:00Z