Pages that link to "Q82655827"
Jump to navigation
Jump to search
The following pages link to High-resolution atomic force microscopy of soluble Abeta42 oligomers (Q82655827):
Displaying 50 items.
- Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils (Q24631702) (← links)
- Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeutics (Q26822002) (← links)
- Wireless-electrodeless quartz-crystal-microbalance biosensors for studying interactions among biomolecules: a review (Q27027667) (← links)
- Crystal Structure of the Amyloid-β p3 Fragment Provides a Model for Oligomer Formation in Alzheimer's Disease (Q27666598) (← links)
- Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation (Q28534489) (← links)
- Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange (Q30437131) (← links)
- Toxic fibrillar oligomers of amyloid-β have cross-β structure (Q30514124) (← links)
- Preparation of fluorescently-labeled amyloid-beta peptide assemblies: the effect of fluorophore conjugation on structure and function (Q33682529) (← links)
- Intrinsic Linear Heterogeneity of Amyloid β Protein Fibrils Revealed by Higher Resolution Mass-per-length Determinations (Q33715947) (← links)
- Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders (Q33716773) (← links)
- Calcium ions promote formation of amyloid β-peptide (1-40) oligomers causally implicated in neuronal toxicity of Alzheimer's disease (Q33862507) (← links)
- An improved method for generating consistent soluble amyloid-beta oligomer preparations for in vitro neurotoxicity studies (Q33988301) (← links)
- Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR (Q34228566) (← links)
- Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process (Q34332006) (← links)
- Surface effects mediate self-assembly of amyloid-β peptides (Q34419863) (← links)
- Alzheimer's Disease Drug Candidates Stabilize A-β Protein Native Structure by Interacting with the Hydrophobic Core (Q34568137) (← links)
- How ionic strength affects the conformational behavior of human and rat beta amyloids--a computational study (Q34743876) (← links)
- Insight into Amyloid Structure Using Chemical Probes (Q34990429) (← links)
- Self-Assembly of Aβ40, Aβ42 and Aβ43 Peptides in Aqueous Mixtures of Fluorinated Alcohols (Q35755711) (← links)
- Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy (Q36374381) (← links)
- Safety and tolerability of BAN2401--a clinical study in Alzheimer's disease with a protofibril selective Aβ antibody (Q36769531) (← links)
- Fine mapping of the amyloid β-protein binding site on myelin basic protein (Q36806584) (← links)
- Amyloid β-Protein Assembly and Alzheimer's Disease: Dodecamers of Aβ42, but Not of Aβ40, Seed Fibril Formation (Q36848561) (← links)
- Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: implications for cell toxicity (Q36957373) (← links)
- Natural compounds may open new routes to treatment of amyloid diseases (Q36983212) (← links)
- Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42. (Q36996040) (← links)
- Beta amyloid oligomers and fibrils stimulate differential activation of primary microglia (Q37077638) (← links)
- Computational simulations of the early steps of protein aggregation (Q37079408) (← links)
- Hacking the code of amyloid formation: the amyloid stretch hypothesis (Q37079411) (← links)
- Preparing Synthetic Aβ in Different Aggregation States (Q37119634) (← links)
- Pre-amyloid oligomers budding:a metastatic mechanism of proteotoxicity (Q37360313) (← links)
- Oligomeric amyloid β induces IL-1β processing via production of ROS: implication in Alzheimer's disease (Q37424131) (← links)
- Structures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretase (Q37469347) (← links)
- Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils (Q39439924) (← links)
- Site-specific blockade of RAGE-Vd prevents amyloid-beta oligomer neurotoxicity (Q39982408) (← links)
- Mechanism of an ATP-independent protein disaggregase: I. structure of a membrane protein aggregate reveals a mechanism of recognition by its chaperone (Q40600352) (← links)
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions. (Q41702344) (← links)
- Aggregation pathways of the amyloid β(1-42) peptide depend on its colloidal stability and ordered β-sheet stacking (Q41763155) (← links)
- Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM (Q41943054) (← links)
- Characterization of the nucleation barriers for protein aggregation and amyloid formation (Q41950121) (← links)
- Capping of aβ42 oligomers by small molecule inhibitors (Q41954365) (← links)
- Few Ramachandran Angle Changes Provide Interaction Strength Increase in Aβ42 versus Aβ40 Amyloid Fibrils (Q42033500) (← links)
- Inhibitory Effect of Curcumin-Cu(II) and Curcumin-Zn(II) Complexes on Amyloid-Beta Peptide Fibrillation. (Q42071511) (← links)
- A chemical screening approach reveals that indole fluorescence is quenched by pre-fibrillar but not fibrillar amyloid-beta (Q43066105) (← links)
- Precise, fast and flexible determination of protein interactions by affinity capillary electrophoresis. Part 2: cations (Q43754169) (← links)
- Transformation of amyloid β(1-40) oligomers into fibrils is characterized by a major change in secondary structure (Q44808414) (← links)
- A Strategy for Designing a Peptide Probe for Detection of β‐Amyloid Oligomers (Q45398214) (← links)
- Unfolding of CPR3 Gets Initiated at the Active Site and Proceeds via Two Intermediates (Q51113683) (← links)
- Studies of the growth, evolution, and self‐aggregation of β‐amyloid fibrils using tapping‐mode atomic force microscopy (Q53320104) (← links)
- Synthesis and effects of flavonoid structure variation on amyloid-β aggregation (Q58896414) (← links)