Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation
about
Neurodegeneration with brain iron accumulation: update on pathogenic mechanismsNeuroferritinopathy: From ferritin structure modification to pathogenetic mechanismFerritin light-chain subunits: key elements for the electron transfer across the protein cageBrain, blood, and iron: perspectives on the roles of erythrocytes and iron in neurodegeneration.Gene co-expression networks shed light into diseases of brain iron accumulation.Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry.Behavioral characterization of mouse models of neuroferritinopathy.A novel neuroferritinopathy mouse model (FTL 498InsTC) shows progressive brain iron dysregulation, morphological signs of early neurodegeneration and motor coordination deficits.Mammalian iron metabolism and its control by iron regulatory proteinsMitochondrial ferritin is a functional iron-storage protein in cucumber (Cucumis sativus) roots.Human L-ferritin deficiency is characterized by idiopathic generalized seizures and atypical restless leg syndrome."Pumping iron"-how macrophages handle iron at the systemic, microenvironmental, and cellular levelsIron deposits in the chronically inflamed central nervous system and contributes to neurodegeneration.Identification of proteins from 4200-year-old skin and muscle tissue biopsies from ancient Egyptian mummies of the first intermediate period shows evidence of acute inflammation and severe immune response.Regulation of quinolinic acid neosynthesis in mouse, rat and human brain by iron and iron chelators in vitro.Chemistry at the protein-mineral interface in L-ferritin assists the assembly of a functional (μ3-oxo)Tris[(μ2-peroxo)] triiron(III) cluster.Self-assembly is prerequisite for catalysis of Fe(II) oxidation by catalytically active subunits of ferritin.Iron regulatory protein (IRP)-iron responsive element (IRE) signaling pathway in human neurodegenerative diseases.Iron Oxidation and Core Formation in Recombinant Heteropolymeric Human Ferritins.De novo FTL mutation: a clinical, neuroimaging, and molecular study.
P2860
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P2860
Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation
description
2010 nî lūn-bûn
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2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
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name
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@ast
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@en
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@en-gb
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@nl
type
label
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@ast
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@en
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@en-gb
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@nl
altLabel
Mutant Ferritin L-chains That ...... ce Ferritin Iron Incorporation
@en
prefLabel
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@ast
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@en
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@en-gb
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@nl
P2093
P2860
P50
P356
P1476
Mutant ferritin L-chains that ...... ce ferritin iron incorporation
@en
P2093
Angela Cattaneo
Anna Cozzi
Bernard Gallois
Béatrice Langlois d'Estaintot
Maura Poli
Paolo Santambrogio
Sara Luscieti
Thierry Granier
P2860
P304
11948-11957
P356
10.1074/JBC.M109.096404
P407
P577
2010-02-16T00:00:00Z