Pages that link to "Q37513839"

The following pages link to Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy (Q37513839):

Displaying 49 items.

• A Guide to Structured Illumination TIRF Microscopy at High Speed with Multiple Colors (Q28828306) (← links)
• Ultrafast propagation of β-amyloid fibrils in oligomeric cloud (Q30597091) (← links)
• Filming protein fibrillogenesis in real time. (Q30609136) (← links)
• Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates (Q30610715) (← links)
• Highly potent soluble amyloid-β seeds in human Alzheimer brain but not cerebrospinal fluid (Q30842997) (← links)
• Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation. (Q33795294) (← links)
• Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry (Q33916228) (← links)
• Probing exchange pathways in one-dimensional aggregates with super-resolution microscopy (Q34418271) (← links)
• In Situ Visualization of Block Copolymer Self-Assembly in Organic Media by Super-Resolution Fluorescence Microscopy. (Q35811775) (← links)
• Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells (Q35996987) (← links)
• De novo design of a biologically active amyloid. (Q36193149) (← links)
• Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons (Q36802355) (← links)
• Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease. (Q37049183) (← links)
• The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation (Q38240692) (← links)
• Diffraction-unlimited imaging: from pretty pictures to hard numbers (Q38365738) (← links)
• Advanced imaging of tau pathology in Alzheimer Disease: New perspectives from super resolution microscopy and label-free nanoscopy. (Q38870940) (← links)
• Super-resolution imaging of alpha-synuclein polymorphisms and their potential role in neurodegeneration. (Q39127625) (← links)
• Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology. (Q39322110) (← links)
• Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation (Q39545174) (← links)
• Polarized super-resolution structural imaging inside amyloid fibrils using Thioflavine T. (Q42172090) (← links)
• From single-molecule spectroscopy to super-resolution imaging of the neuron: a review (Q42291690) (← links)
• Fluorescence Self-Quenching from Reporter Dyes Informs on the Structural Properties of Amyloid Clusters Formed in Vitro and in Cells (Q42318208) (← links)
• β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces. (Q42374822) (← links)
• Pre-aggregation kinetics and intermediates of α-synuclein monitored by the ESIPT probe 7MFE. (Q46236939) (← links)
• Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification (Q46242764) (← links)
• Vertebrate food products as a potential source of prion-like α-synuclein. (Q46252338) (← links)
• Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states (Q47449222) (← links)
• Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla (Q47722422) (← links)
• The attachment of α-synuclein to a fiber: A coarse-grain approach. (Q48044175) (← links)
• C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction (Q49829897) (← links)
• Fluorescence nanoscopy in cell biology (Q50216769) (← links)
• Detection of oligomers and fibrils of α-synuclein by AIEgen with strong fluorescence. (Q53244268) (← links)
• Physiological carboxy-truncation of α-synuclein potentiates the prion-like formation of pathological inclusions (Q57458019) (← links)
• A new era for understanding amyloid structures and disease (Q57787227) (← links)
• High-speed atomic force microscopy reveals structural dynamics of α-synuclein monomers and dimers (Q57829038) (← links)
• Different Structural Conformers of Monomeric α-Synuclein Identified after Lyophilizing and Freezing (Q57948233) (← links)
• C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH (Q57986252) (← links)
• Defining the Dynamic Conformational Networks of Cross-β Peptide Assembly (Q58074760) (← links)
• Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the Nanoscale (Q58090111) (← links)
• Live-cell super-resolution microscopy reveals a primary role for diffusion in polyglutamine-driven aggresome assembly (Q58607360) (← links)
• α-Synuclein-Confocal Nanoscanning (ASYN-CONA), a Bead-Based Assay for Detecting Early-Stage α-Synuclein Aggregation (Q64283401) (← links)
• AFM-STED correlative nanoscopy reveals a dark side in fluorescence microscopy imaging. (Q64989313) (← links)
• Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein. (Q64992649) (← links)
• An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils (Q83229847) (← links)
• Structural progression of amyloid-β Arctic mutant aggregation in cells revealed by multiparametric imaging (Q90028502) (← links)
• Study of alpha-synuclein fibrillation: state of the art and expectations (Q90175415) (← links)
• An Easy Path for Correlative Electron and Super-Resolution Light Microscopy (Q90999632) (← links)
• Thermophoretic trap for single amyloid fibril and protein aggregation studies (Q93000952) (← links)
• Nanostructures Formed by Custom-Made Peptides Based on Amyloid Peptide Sequences and Their Inhibition by 2-Hydroxynaphthoquinone (Q98771537) (← links)