| scholarly article | Q13442814 |
| P50 | author | Henrike Heise | Q1247601 |
| Tuomas Knowles | Q56481348 | ||
| Martin Muschol | Q88145933 | ||
| Dieter Willbold | Q28320581 | ||
| Philipp Neudecker | Q30169549 | ||
| Lothar Gremer | Q30169555 | ||
| Georg Meisl | Q41524506 | ||
| Wolfgang Hoyer | Q42544571 | ||
| P2093 | author name string | Tatiana Miti | |
| Ghanim Ullah | |||
| Jeremy Barton | |||
| Clara S R Grüning | |||
| Daniel Schölzel | |||
| Carlos Perez | |||
| Filip Hasecke | |||
| Garrett Matthews | |||
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| Human lysozyme gene mutations cause hereditary systemic amyloidosis | Q34362632 | ||
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| Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrils | Q34416296 | ||
| Protein aggregation: folding aggregates, inclusion bodies and amyloid | Q34460420 | ||
| The molecular basis of distinct aggregation pathways of islet amyloid polypeptide | Q34675944 | ||
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| Amyloid beta-protein assembly and Alzheimer disease | Q34849544 | ||
| Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy | Q34964783 | ||
| pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers | Q35590322 | ||
| The systemic amyloidoses | Q35607024 | ||
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| Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation | Q35859557 | ||
| Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation | Q36303237 | ||
| Polymorphism in the intermediates and products of amyloid assembly | Q36717593 | ||
| α-Synuclein oligomers and clinical implications for Parkinson disease | Q36718306 | ||
| Functional amyloid--from bacteria to humans. | Q36782474 | ||
| Folding versus aggregation: polypeptide conformations on competing pathways | Q36858313 | ||
| Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein | Q36950121 | ||
| Structural fingerprints and their evolution during oligomeric vs. oligomer-free amyloid fibril growth | Q37028081 | ||
| Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion | Q37263559 | ||
| Structure-neurotoxicity relationships of amyloid beta-protein oligomers | Q37329557 | ||
| On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants | Q37731494 | ||
| The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes | Q37979641 | ||
| The amyloid state of proteins in human diseases | Q37994283 | ||
| Molecular mechanisms of amyloid oligomers toxicity | Q38005284 | ||
| Systemic amyloidoses | Q38085664 | ||
| Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors | Q38749471 | ||
| Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients. | Q38957210 | ||
| Preparation and Characterization of Neurotoxic Tau Oligomers | Q39636310 | ||
| The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation | Q39665703 | ||
| The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity | Q39681329 | ||
| Macromolecular crowding converts the human recombinant PrPC to the soluble neurotoxic beta-oligomers | Q39713564 | ||
| Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide | Q40116497 | ||
| Molecular mechanisms of protein aggregation from global fitting of kinetic models. | Q40133096 | ||
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| Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments | Q41055389 | ||
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| Neuropathological diagnosis of Alzheimer's disease: a perspective from longitudinal clinicopathological studies | Q41612685 | ||
| The neuropathological diagnosis of Alzheimer's disease: clinical-pathological studies | Q41612695 | ||
| The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions | Q41696172 | ||
| Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variants | Q41808931 | ||
| FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. | Q41819553 | ||
| Amyloid-β forms fibrils by nucleated conformational conversion of oligomers | Q42058603 | ||
| The off-rate of monomers dissociating from amyloid-β protofibrils | Q42085979 | ||
| Stable, metastable, and kinetically trapped amyloid aggregate phases | Q42099746 | ||
| Fibril fragmentation enhances amyloid cytotoxicity | Q42201660 | ||
| Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution | Q42237530 | ||
| A Disulfide-Linked Amyloid-β Peptide Dimer Forms a Protofibril-like Oligomer through a Distinct Pathway from Amyloid Fibril Formation | Q42953845 | ||
| The Aggregation Paths and Products of Aβ42 Dimers Are Distinct from Those of the Aβ42 Monomer | Q43020455 | ||
| Scaling behaviour and rate-determining steps in filamentous self-assembly | Q44939383 | ||
| Off-pathway aggregation can inhibit fibrillation at high protein concentrations | Q44976343 | ||
| Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases | Q45072759 | ||
| Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation. | Q45104269 | ||
| Antiparallel beta-sheet: a signature structure of the oligomeric amyloid beta-peptide | Q45738154 | ||
| Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH. | Q46088526 | ||
| Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct | Q46148419 | ||
| A pH-Induced Switch in Human Glucagon-like Peptide-1 Aggregation Kinetics | Q46442647 | ||
| P275 | copyright license | Creative Commons Attribution-NonCommercial 3.0 Unported | Q18810331 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 27 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | general chemistry | Q909510 |
| self-assembly | Q910150 | ||
| P304 | page(s) | 5937-5948 | |
| P577 | publication date | 2018-06-13 | |
| P1433 | published in | Chemical Science | Q2962267 |
| P1476 | title | Origin of metastable oligomers and their effects on amyloid fibril self-assembly | |
| P478 | volume | 9 |
| Q64099425 | Atomic force microscopy for single molecule characterisation of protein aggregation |
| Q89941986 | Halogenation of the N-Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid-β Sequence 7-12 |
| Q92724345 | Interference with Amyloid-β Nucleation by Transient Ligand Interaction |
| Q90384233 | Kinetic Transition in Amyloid Assembly as a Screening Assay for Oligomer-Selective Dyes |
| Q99710980 | Network Hamiltonian models reveal pathways to amyloid fibril formation |
| Q89551362 | Protofibrils of Amyloid-β are Important Targets of a Disease-Modifying Approach for Alzheimer's Disease |
| Q90189862 | Structure and Aggregation Mechanisms in Amyloids |
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