Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
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C-terminal region of MAP7 domain containing protein 3 (MAP7D3) promotes microtubule polymerization by binding at the C-terminal tail of tubulinRegulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegenerationMAP2 and tau bind longitudinally along the outer ridges of microtubule protofilamentsHuman fetal tau protein isoform: possibilities for Alzheimer's disease treatmentAβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function.Direct force measurements reveal that protein Tau confers short-range attractions and isoform-dependent steric stabilization to microtubules.Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formationTau StructuresThe Dark Matter of BiologyThe emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's diseaseThe effect of a DeltaK280 mutation on the unfolded state of a microtubule-binding repeat in TauStructural polymorphism of 441-residue tau at single residue resolutionA decade and a half of protein intrinsic disorder: biology still waits for physicsGlobPlot: Exploring protein sequences for globularity and disorderNatively unfolded proteins: a point where biology waits for physicsThe unfoldomics decade: an update on intrinsically disordered proteins.Understanding protein non-folding.Toward a consensus in protein structure nomenclature.The amino terminus of tau inhibits kinesin-dependent axonal transport: implications for filament toxicity.Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport.Amyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cellsDifferentiating Alzheimer disease-associated aggregates with small molecules.Protein disorder in the human diseasome: unfoldomics of human genetic diseases.Unfoldomics of human diseases: linking protein intrinsic disorder with diseasesA nucleated assembly mechanism of Alzheimer paired helical filaments.What's in a name? Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered.Evidence for two distinct binding sites for tau on microtubulesOxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filamentsX-ray diffraction from intact tau aggregates in human brain tissueThe solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.Bioinformatic analysis of pathogenic missense mutations of activin receptor like kinase 1 ectodomainStructural Insight into Tau Protein's Paradox of Intrinsically Disordered Behavior, Self-Acetylation Activity, and AggregationQuantitative analysis of tau-microtubule interaction using FRET.From Alzheimer to Huntington: why is a structural understanding so difficult?Intrinsic disorder in scaffold proteins: getting more from lessProtein disulfide isomerase interacts with tau protein and inhibits its fibrillization.Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease.Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.Regulation and aggregation of intrinsically disordered peptidesTau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure.
P2860
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P2860
Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
description
1994 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1994
@ast
im September 1994 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
wetenschappelijk artikel (gepubliceerd op 1994/09/30)
@nl
наукова стаття, опублікована у вересні 1994
@uk
مقالة علمية (نشرت في 30-9-1994)
@ar
name
Structural studies of tau prot ...... no evidence for beta-structure
@ast
Structural studies of tau prot ...... no evidence for beta-structure
@en
type
label
Structural studies of tau prot ...... no evidence for beta-structure
@ast
Structural studies of tau prot ...... no evidence for beta-structure
@en
prefLabel
Structural studies of tau prot ...... no evidence for beta-structure
@ast
Structural studies of tau prot ...... no evidence for beta-structure
@en
P2093
P921
P3181
P1476
Structural studies of tau prot ...... no evidence for beta-structure
@en
P2093
E. Mandelkow
E. Schönbrunn-Hanebeck
O. Schweers
P304
24290–24297
P3181
P407
P577
1994-09-30T00:00:00Z