scholarly article | Q13442814 |
P50 | author | Zachary M March | Q57033787 |
David W Colby | Q58210652 | ||
Anne Skaja Robinson | Q59565753 | ||
P2093 | author name string | Olga A Morozova | |
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A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis | Q33720044 | ||
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Transmission of tau pathology induced by synthetic preformed tau filaments | Q34675848 | ||
Polymerization of hyperphosphorylated tau into filaments eliminates its inhibitory activity | Q34695519 | ||
Seeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles | Q34869120 | ||
Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein | Q35604223 | ||
Phosphorylation of tau antagonizes apoptosis by stabilizing beta-catenin, a mechanism involved in Alzheimer's neurodegeneration | Q35652167 | ||
Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. | Q35852028 | ||
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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 unit | Q37435073 | ||
Design and construction of diverse mammalian prion strains | Q37453512 | ||
Propagation of tau misfolding from the outside to the inside of a cell. | Q39873721 | ||
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A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities | Q41879896 | ||
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Three- and four-repeat tau regulate the dynamic instability of two distinct microtubule subpopulations in qualitatively different manners. Implications for neurodegeneration | Q43702910 | ||
Conformational variations in an infectious protein determine prion strain differences | Q44187524 | ||
Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments | Q44244212 | ||
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 dispersion | Q44959545 | ||
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 diversity | Q46433690 | ||
Purification of paired helical filament tau and normal tau from human brain tissue | Q48100643 | ||
The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis | Q48539775 | ||
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 sulfation | Q48553846 | ||
Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms | Q48571996 | ||
Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans | Q48891767 | ||
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 spectroscopy | Q57187328 | ||
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work | Q57897029 | ||
Sequential changes of tau-site-specific phosphorylation during development of paired helical filaments | Q71603714 | ||
SCREENING FOR AMYLOID WITH THE THIOFLAVIN-T FLUORESCENT METHOD | Q78440796 | ||
P4510 | describes a project that uses | ImageJ | Q1659584 |
P433 | issue | 40 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Alzheimer's disease | Q11081 |
P304 | page(s) | 6960-6967 | |
P577 | publication date | 2013-09-27 | |
P1433 | published in | Biochemistry | Q764876 |
P1476 | title | Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein | |
P478 | volume | 52 |
Q47715943 | Amyloidogenesis of Tau protein |
Q90341753 | Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils |
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Q61799266 | Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer's and Pick's diseases |
Q50258556 | Identification of the Tau phosphorylation pattern that drives its aggregation |
Q92264705 | In vitro 0N4R tau fibrils contain a monomorphic β-sheet core enclosed by dynamically heterogeneous fuzzy coat segments |
Q55715541 | Inert and seed-competent tau monomers suggest structural origins of aggregation. |
Q28084859 | Legal but lethal: functional protein aggregation at the verge of toxicity |
Q26747418 | NMR Meets Tau: Insights into Its Function and Pathology |
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Q31024674 | Propagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies |
Q38214594 | Protein phosphorylation in neurodegeneration: friend or foe? |
Q34383788 | Proteopathic tau seeding predicts tauopathy in vivo. |
Q33559303 | Roles of tau protein in health and disease |
Q90664222 | Seeding selectivity and ultrasensitive detection of tau aggregate conformers of Alzheimer disease |
Q36408405 | Sensitive Detection of Proteopathic Seeding Activity with FRET Flow Cytometry |
Q50261748 | Simplified method to obtain enhanced expression of tau protein from E. coli and one-step purification by direct boiling |
Q92070007 | Strains of Pathological Protein Aggregates in Neurodegenerative Diseases |
Q90182376 | Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples |
Q33600755 | Synthetic extreme environments: overlooked sources of potential biotechnologically relevant microorganisms |
Q35985428 | Tau 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 |
Q22252512 | Tau-aggregation inhibitor therapy for Alzheimer's disease |
Q90227644 | The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer's Disease (AD) |
Q48128847 | Ultrasensitive and selective detection of 3-repeat tau seeding activity in Pick disease brain and cerebrospinal fluid |
Q37415258 | Unique pathological tau conformers from Alzheimer's brains transmit tau pathology in nontransgenic mice |
Q52686361 | α-Synuclein Oligomers Induce a Unique Toxic Tau Strain. |
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