Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein

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Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/BI400866W
P932PMC publication ID4142060
P698PubMed publication ID24033133
P5875ResearchGate publication ID256607684

P50authorZachary M MarchQ57033787
David W ColbyQ58210652
Anne Skaja RobinsonQ59565753
P2093author name stringOlga A Morozova
P2860cites workRepeat motifs of tau bind to the insides of microtubules in the absence of taxolQ24540276
Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filamentsQ24599152
Transmission and spreading of tauopathy in transgenic mouse brainQ24651334
Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's diseaseQ28242505
New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometryQ28290064
Distinct α-synuclein strains differentially promote tau inclusions in neuronsQ28293967
Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domainQ28910324
Tau suppression in a neurodegenerative mouse model improves memory functionQ29615831
Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathologyQ29617284
Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrilsQ29617476
Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.Q30420123
Alpha-helix structure in Alzheimer's disease aggregates of tau-protein.Q30734348
Prion diseases and their biochemical mechanismsQ33584925
A nucleated assembly mechanism of Alzheimer paired helical filamentsQ33608410
Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.Q33666468
Identification of oligomers at early stages of tau aggregation in Alzheimer's diseaseQ33713341
A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresisQ33720044
Characterization of tau fibrillization in vitroQ33742830
Transmission of tau pathology induced by synthetic preformed tau filamentsQ34675848
Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activityQ34695519
Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tanglesQ34869120
Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau proteinQ35604223
Phosphorylation of tau antagonizes apoptosis by stabilizing beta-catenin, a mechanism involved in Alzheimer's neurodegenerationQ35652167
Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].Q35852028
Mutation in the tau gene in familial multiple system tauopathy with presenile dementiaQ36507684
Polymorphism in the intermediates and products of amyloid assemblyQ36717593
Brain homogenates from human tauopathies induce tau inclusions in mouse brainQ36915421
Neurofibrillary tangle-like tau pathology induced by synthetic tau fibrils in primary neurons over-expressing mutant tau.Q36918222
Straight and paired helical filaments in Alzheimer disease have a common structural unitQ37435073
Design and construction of diverse mammalian prion strainsQ37453512
Propagation of tau misfolding from the outside to the inside of a cell.Q39873721
Transmission electron microscopy of amyloid fibrilsQ41615473
A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilitiesQ41879896
Conformational diversity of wild-type Tau fibrils specified by templated conformation changeQ42114209
Three- and four-repeat tau regulate the dynamic instability of two distinct microtubule subpopulations in qualitatively different manners. Implications for neurodegenerationQ43702910
Conformational variations in an infectious protein determine prion strain differencesQ44187524
Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filamentsQ44244212
β-Sheet core of tau paired helical filaments revealed by solid-state NMR.Q44431945
Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersionQ44959545
Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation.Q46031118
Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversityQ46433690
Purification of paired helical filament tau and normal tau from human brain tissueQ48100643
The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysisQ48539775
Alzheimer-like changes in microtubule-associated protein Tau induced by sulfated glycosaminoglycans. Inhibition of microtubule binding, stimulation of phosphorylation, and filament assembly depend on the degree of sulfationQ48553846
Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoformsQ48571996
Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycansQ48891767
Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules.Q52200995
A68: a major subunit of paired helical filaments and derivatized forms of normal Tau.Q53296439
Ligand-dependent tau filament formation: implications for Alzheimer's disease progression.Q53337893
Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopyQ57187328
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this workQ57897029
Sequential changes of tau-site-specific phosphorylation during development of paired helical filamentsQ71603714
SCREENING FOR AMYLOID WITH THE THIOFLAVIN-T FLUORESCENT METHODQ78440796
P4510describes a project that usesImageJQ1659584
P433issue40
P407language of work or nameEnglishQ1860
P921main subjectAlzheimer's diseaseQ11081
P304page(s)6960-6967
P577publication date2013-09-27
P1433published inBiochemistryQ764876
P1476titleConformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein
P478volume52

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cites work (P2860)
Q47715943Amyloidogenesis of Tau protein
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Q61799266Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer's and Pick's diseases
Q50258556Identification of the Tau phosphorylation pattern that drives its aggregation
Q92264705In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments
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Q28084859Legal but lethal: functional protein aggregation at the verge of toxicity
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Q38214594Protein phosphorylation in neurodegeneration: friend or foe?
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Q33559303Roles of tau protein in health and disease
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Q36408405Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry
Q50261748Simplified method to obtain enhanced expression of tau protein from E. coli and one-step purification by direct boiling
Q92070007Strains of Pathological Protein Aggregates in Neurodegenerative Diseases
Q90182376Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples
Q33600755Synthetic extreme environments: overlooked sources of potential biotechnologically relevant microorganisms
Q35985428Tau pathology spread in PS19 tau transgenic mice following locus coeruleus (LC) injections of synthetic tau fibrils is determined by the LC's afferent and efferent connections
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Q90227644The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer's Disease (AD)
Q48128847Ultrasensitive and selective detection of 3-repeat tau seeding activity in Pick disease brain and cerebrospinal fluid
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Q52686361α-Synuclein Oligomers Induce a Unique Toxic Tau Strain.

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