TDP-43 skeins show properties of amyloid in a subset of ALS cases.
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The TDP-43 N-terminal domain structure at high resolutionSpreading of pathology in neurodegenerative diseases: a focus on human studiesDifferential roles of the ubiquitin proteasome system and autophagy in the clearance of soluble and aggregated TDP-43 speciesPrions, amyloids, and RNA: Pieces of a puzzle.Single cell imaging and quantification of TDP-43 and α-synuclein intercellular propagation.Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.The influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution.Frontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine.In vivo characterization of chronic traumatic encephalopathy using [F-18]FDDNP PET brain imaging.ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function.TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Protein aggregation in amyotrophic lateral sclerosis.Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates.TDP-43 in amyotrophic lateral sclerosis - is it a prion disease?Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins.Molecular neuropathology of frontotemporal dementia: insights into disease mechanisms from postmortem studies.Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo.Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid.Label-Free LC-MS/MS Proteomic Analysis of Cerebrospinal Fluid Identifies Protein/Pathway Alterations and Candidate Biomarkers for Amyotrophic Lateral SclerosisAn Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds.Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111.Flortaucipir tau PET imaging in semantic variant primary progressive aphasia.Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.Pathomechanisms of TDP-43 in neurodegeneration.Imaging Protein Misfolding in the Brain Using β-Sheet LigandsThe RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the ProteinAmyloid assembly and disassembly
P2860
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P2860
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
@ast
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
@en
type
label
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
@ast
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
@en
prefLabel
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
@ast
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
@en
P2093
P2860
P1476
TDP-43 skeins show properties of amyloid in a subset of ALS cases.
@en
P2093
Anna Stieber
Felix Geser
John L Robinson
Linda K Kwong
Virginia M-Y Lee
Vivianna M Van Deerlin
P2860
P2888
P304
P356
10.1007/S00401-012-1055-8
P577
2012-11-03T00:00:00Z