SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
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Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.Divergent signaling via SUMO modification: potential for CFTR modulation.The mitochondrial-derived peptide humanin activates the ERK1/2, AKT, and STAT3 signaling pathways and has age-dependent signaling differences in the hippocampus.The Roles of SUMO in Metabolic Regulation.Post-translational Modifications and Protein Quality Control in Motor Neuron and Polyglutamine Diseases.Sumoylation: Implications for Neurodegenerative Diseases.Causative Genes in Amyotrophic Lateral Sclerosis and Protein Degradation Pathways: a Link to Neurodegeneration.SENP1 and SENP2 regulate SUMOylation of amyloid precursor protein.Minimotifs dysfunction is pervasive in neurodegenerative disorders
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P2860
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
@ast
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
@en
type
label
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
@ast
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
@en
prefLabel
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
@ast
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
@en
P2860
P1433
P1476
SUMO3 modification accelerates the aggregation of ALS-linked SOD1 mutants.
@en
P2093
Takako Niikura
Yoshiko Kita
P2860
P304
P356
10.1371/JOURNAL.PONE.0101080
P407
P50
P577
2014-06-27T00:00:00Z