Subunit structure of paired helical filaments in Alzheimer's disease
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Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazinesTau Protein Hyperphosphorylation and Aggregation in Alzheimer's Disease and Other Tauopathies, and Possible Neuroprotective StrategiesMicrotubule bundling by tau proteins in vivo: analysis of functional domainsCytoskeletal pathologies of Alzheimer diseaseNucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constantsCognitive deterioration and associated pathology induced by chronic low-level aluminum ingestion in a translational rat model provides an explanation of Alzheimer's disease, tests for susceptibility and avenues for treatment.Utilizing the peptidyl-prolyl cis-trans isomerase pin1 as a probe of its phosphorylated target proteins. Examples of binding to nuclear proteins in a human kidney cell line and to tau in Alzheimer's diseased brain.Atomic force microscopy contact, tapping, and jumping modes for imaging biological samples in liquids.Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels.Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability.Structure of core domain of fibril-forming PHF/Tau fragments.RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments.Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure.The repeat region of microtubule-associated protein tau forms part of the core of the paired helical filament of Alzheimer's disease.Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein.Ultrastructural instability of paired helical filaments from corticobasal degeneration as examined by scanning transmission electron microscopy.Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. An immunohistochemical study.Sequestration of tau by granulovacuolar degeneration in Alzheimer's disease.Structural analysis of Pick's disease-derived and in vitro-assembled tau filaments14-3-3ζ Mediates Tau Aggregation in Human Neuroblastoma M17 Cells.The ubiquitin-proteasome system and the autophagic-lysosomal system in Alzheimer disease.Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitroTwisted ribbon structure of paired helical filaments revealed by atomic force microscopy.Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated KinaseStraight and paired helical filaments in Alzheimer disease have a common structural unitExpression and purification of tau protein and its frontotemporal dementia variants using a cleavable histidine tagEfficacy and safety of tau-aggregation inhibitor therapy in patients with mild or moderate Alzheimer's disease: a randomised, controlled, double-blind, parallel-arm, phase 3 trial.Measurement of distinct immunochemical presentations of tau protein in Alzheimer disease.Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review.Characterization by atomic force microscopy of Alzheimer paired helical filaments under physiological conditions.Dorothy Russell Memorial Lecture. The molecular pathology of Alzheimer's disease: are we any closer to understanding the neurodegenerative process?Differential assembly of human tau isoforms in the presence of arachidonic acid.Image reconstruction of the Alzheimer paired helical filament.Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA.Intracellular neurofibrillary tangle-like aggregations. A constantly present amyloid alteration in the aging choroid plexus.Tau in Alzheimer's disease and Down's syndrome is insoluble and abnormally phosphorylated.Fibers of tau fragments, but not full length tau, exhibit a cross beta-structure: implications for the formation of paired helical filaments.Alzheimer's paired helical filaments share epitopes with neurofilament side armsAlzheimer neurofibrillary tangles contain phosphorylated and hidden neurofilament epitopes.
P2860
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P2860
Subunit structure of paired helical filaments in Alzheimer's disease
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
1985年论文
@zh
1985年论文
@zh-cn
name
Subunit structure of paired helical filaments in Alzheimer's disease
@en
type
label
Subunit structure of paired helical filaments in Alzheimer's disease
@en
prefLabel
Subunit structure of paired helical filaments in Alzheimer's disease
@en
P2093
P2860
P356
P1476
Subunit structure of paired helical filaments in Alzheimer's disease
@en
P2093
P2860
P304
P356
10.1083/JCB.100.6.1905
P407
P577
1985-06-01T00:00:00Z