| P50 | author | Georg Künze | Q57404882 |
| P2093 | author name string | Lars Thomas | |
| | David Eliezer | |
| | Daniel Huster | |
| | Holger A Scheidt | |
| | Patrick Barré | |
| P2860 | cites work | Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments | Q22253456 |
| | Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain | Q24310491 |
| | Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement | Q24569788 |
| | The cerebral proteopathies: neurodegenerative disorders of protein conformation and assembly | Q28186254 |
| | Relationship between nuclear magnetic resonance chemical shift and protein secondary structure | Q28252147 |
| | Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum | Q28262806 |
| | Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17 | Q28274687 |
| | Oxidative stress in neurodegeneration: cause or consequence? | Q28275946 |
| | Alzheimer's disease: paired helical filaments and cytomembranes | Q28301717 |
| | Structural polymorphism of 441-residue tau at single residue resolution | Q28474834 |
| | Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain | Q28910324 |
| | Residual structure in the repeat domain of tau: echoes of microtubule binding and paired helical filament formation | Q28910419 |
| | Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology | Q29617284 |
| | Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease | Q29617285 |
| | Membrane protein folding and stability: physical principles | Q29620789 |
| | How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? | Q30327310 |
| | Characterization of Alzheimer's-like paired helical filaments from the core domain of tau protein using solid-state NMR spectroscopy | Q31151419 |
| | Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease | Q31939978 |
| | Structural characterization of the core of the paired helical filament of Alzheimer disease | Q33586330 |
| | Amyloid diseases: abnormal protein aggregation in neurodegeneration | Q33723502 |
| | Amyloid ion channels: a common structural link for protein-misfolding disease | Q33906626 |
| | Area/lipid of bilayers from NMR. | Q34092451 |
| | Two-dimensional 1H/13C heteronuclear chemical shift correlation spectroscopy of lipid bilayers | Q34261251 |
| | Structure and dynamics of micelle-bound human alpha-synuclein | Q34379131 |
| | RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments | Q34737245 |
| | Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics | Q34988116 |
| | Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure | Q35171526 |
| | Progress towards a molecular-level structural understanding of amyloid fibrils | Q35753224 |
| | Profound loss of layer II entorhinal cortex neurons occurs in very mild Alzheimer's disease. | Q48963534 |
| | Alzheimer's disease: soluble oligomeric Abeta(1-40) peptide in membrane mimic environment from solution NMR and circular dichroism studies | Q49110897 |
| | Structural investigations of a human calcitonin-derived carrier peptide in a membrane environment by solid-state NMR. | Q50791428 |
| | Estimation of globular protein secondary structure from circular dichroism. | Q51259487 |
| | Analyzing protein circular dichroism spectra for accurate secondary structures. | Q52214947 |
| | A self-consistent method for the analysis of protein secondary structure from circular dichroism. | Q52400789 |
| | Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. | Q52487321 |
| | Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease. | Q53213177 |
| | Neural membrane phospholipids in Alzheimer disease. | Q53213229 |
| | Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation. | Q53285737 |
| | Ligand-dependent tau filament formation: implications for Alzheimer's disease progression. | Q53337893 |
| | C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease. | Q53343397 |
| | A thermodynamic scale for the beta-sheet forming tendencies of the amino acids. | Q53709834 |
| | Prion peptide fragment PrP[106-126] forms distinct cation channel types. | Q53904400 |
| | Influence of docosahexaenoic acid and cholesterol on lateral lipid organization in phospholipid mixtures | Q57102861 |
| | Structural properties of pore-forming oligomers of alpha-synuclein | Q57185914 |
| | Conserved and Cooperative Assembly of Membrane-Bound α-Helical States of Islet Amyloid Polypeptide† | Q57365051 |
| | Measurement of the β-sheet-forming propensities of amino acids | Q59069627 |
| | Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers | Q61844539 |
| | Pore formation by the cytotoxic islet amyloid peptide amylin | Q70915133 |
| | Studies on phosphatidylcholine vesicles. Formation and physical characteristics | Q72369607 |
| | Tau dephosphorylation at tau-1 site correlates with its association to cell membrane | Q73471049 |
| | Folding of the repeat domain of tau upon binding to lipid surfaces | Q80109857 |
| | Structure determination of membrane proteins by NMR spectroscopy | Q80435122 |
| | Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease. | Q35764771 |
| | Post-translational modifications of tau protein in Alzheimer's disease | Q35934376 |
| | Pathways of tau fibrillization. | Q35992129 |
| | Amyloid peptide channels | Q36035620 |
| | Recent atomic models of amyloid fibril structure | Q36431049 |
| | Mutation in the tau gene in familial multiple system tauopathy with presenile dementia | Q36507684 |
| | Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane | Q36579443 |
| | Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? | Q36595270 |
| | A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients | Q36732974 |
| | Structural principles of tau and the paired helical filaments of Alzheimer's disease | Q36817219 |
| | Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases. | Q36836607 |
| | The interaction of beta-amyloid protein fragment (12-28) with lipid environments. | Q36850362 |
| | Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure | Q36964038 |
| | How is protein aggregation in amyloidogenic diseases modulated by biological membranes? | Q37009881 |
| | Tau aggregation and toxicity in tauopathic neurodegenerative diseases | Q37238281 |
| | The two-fold aspect of the interplay of amyloidogenic proteins with lipid membranes. | Q37341219 |
| | The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes | Q37470642 |
| | Amyloidogenic protein-membrane interactions: mechanistic insight from model systems | Q37771927 |
| | Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding | Q39143073 |
| | Smoothed orientational order profile of lipid bilayers by 2H-nuclear magnetic resonance | Q39622780 |
| | Preparation and Characterization of Neurotoxic Tau Oligomers | Q39636310 |
| | Poly-L-glutamine forms cation channels: relevance to the pathogenesis of the polyglutamine diseases | Q40164617 |
| | Chemical shifts as a tool for structure determination | Q40576242 |
| | Dynamics of amyloid β fibrils revealed by solid-state NMR. | Q40649097 |
| | A new hypothesis for the mechanism of amyloid toxicity, based on the calcium channel activity of amyloid beta protein (A beta P) in phospholipid bilayer membranes | Q40779597 |
| | Membrane phospholipid alterations in Alzheimer's disease: deficiency of ethanolamine plasmalogens | Q41454656 |
| | Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide | Q42146193 |
| | Tau is a candidate gene for chromosome 17 frontotemporal dementia | Q42456776 |
| | Membrane-bound alpha-synuclein forms an extended helix: long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles | Q43198829 |
| | Reductive alkylation of amino groups in proteins | Q43840768 |
| | Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro | Q44429258 |
| | Structural and dynamical changes of the bindin B18 peptide upon binding to lipid membranes. A solid-state NMR study | Q44503686 |
| | Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions | Q46458473 |
| | Production of large unilamellar vesicles by a rapid extrusion procedure: characterization of size distribution, trapped volume and ability to maintain a membrane potential | Q47228596 |
| | Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution | Q47838808 |
| | Microtubule-associated protein tau. A component of Alzheimer paired helical filaments | Q48344680 |
| | Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease | Q48448000 |
| | Sequence of neurofibrillary changes in aging and Alzheimer's disease: A confocal study with phospho-tau antibody, AD2. | Q48492282 |
| | The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis | Q48539775 |
| | Neurodegenerative disease: amyloid pores from pathogenic mutations | Q48544171 |
| | Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans | Q48891767 |
| P433 | issue | 9 | |
| P304 | page(s) | 2302-2313 | |
| P577 | publication date | 2012-04-06 | |
| P1433 | published in | Biochimica et Biophysica Acta | Q864239 |
| P1476 | title | Binding of the three-repeat domain of tau to phospholipid membranes induces an aggregated-like state of the protein | |
| P478 | volume | 1818 | |