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.
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Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genesPathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersThe TDP-43 N-terminal domain structure at high resolutionDifferential roles of the ubiquitin proteasome system and autophagy in the clearance of soluble and aggregated TDP-43 speciesSingle cell imaging and quantification of TDP-43 and α-synuclein intercellular propagation.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.Subcellular localization and RNAs determine FUS architecture in different cellular compartments.TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.Staging TDP-43 pathology in Alzheimer's disease.Protein aggregation in amyotrophic lateral sclerosis.Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates.Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins.Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils.Molecular neuropathology of frontotemporal dementia: insights into disease mechanisms from postmortem studies.Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis.Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptides.Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis.An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds.Yeast models for amyloid disease.Delineating the membrane-disrupting and seeding properties of the TDP-43 amyloidogenic core.Casein kinase II phosphorylation of cyclin F at serine 621 regulates the Lys48-ubiquitylation E3 ligase activity of the SCF(cyclin F) complex.Flortaucipir tau PET imaging in semantic variant primary progressive aphasia.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 ProteinTHEME 10IN VITROEXPERIMENTAL MODELSAmyloid assembly and disassembly
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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.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Inclusions in frontotemporal l ...... ), have properties of amyloid.
@en
type
label
Inclusions in frontotemporal l ...... ), have properties of amyloid.
@en
prefLabel
Inclusions in frontotemporal l ...... ), have properties of amyloid.
@en
P2093
P2860
P1476
Inclusions in frontotemporal l ...... S), have properties of amyloid
@en
P2093
Changiz Geula
Eileen H Bigio
Esther N Bit-Ivan
Marsel Mesulam
Melanie Peterson
Nailah Siddique
Rakhee Ganti
Teepu Siddique
P2860
P2888
P304
P356
10.1007/S00401-013-1089-6
P577
2013-02-03T00:00:00Z