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Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2003, Volume 278, Issue 19, pp. 16462 - 16465
Journal Article
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, ISSN 1386-1425, 01/2018, Volume 189, pp. 250 - 257
The development of new acetylcholinesterase inhibitors (AChEIs) and subsequent assay of their inhibition efficiency is considered to be a key step for AD... 
MD simulation | Acetylcholinesterase activity | Cholinergic inhibitors | Thioflavin-T fluorescence quenching | Molecular docking | MECHANISM | ALZHEIMERS-DISEASE | CHOLINESTERASE-INHIBITORS | SEQUESTRATION | SPECTROSCOPY | PHARMACOLOGY | HYPOTHESIS | BINDING | Molecular dynamics | Fluorescence | Enzyme inhibitors | Anisotropy | Enzymes
Journal Article
Journal of Alzheimer's Disease, ISSN 1387-2877, 03/2019, Volume 68, Issue 2, pp. 571 - 582
Background: Biomarkers are central to current research on molecular mechanisms underlying Alzheimer’s disease (AD). Their further development is of paramount... 
Amyloidogenesis | Peptides | Protein purification | Disease detection | Variations | Fluorescence | Radioactive tracers | Patients | Blood | Proteins | Sensitivity | Molecular modelling | Aggregates | Peripheral blood | Biomarkers | Bioindicators | Separation techniques | Alzheimer's disease
Journal Article
Amyloid, ISSN 1350-6129, 07/2018, Volume 25, Issue 3, pp. 189 - 196
Thioflavin-T (ThT) is the most commonly used fluorescent dye for following amyloid formation semi-quantitatively in vitro, specifically probing the fibrillar... 
Amyloid | polymorphism | thioflavin-T | atomic force microscopy | α-synuclein | Amyloid - metabolism | Humans | Benzothiazoles - chemistry | Fluorescence | Microscopy, Atomic Force | Protein Binding | Amyloid - chemistry | Benzothiazoles - metabolism | Binding Sites | alpha-Synuclein - metabolism | alpha-Synuclein - chemistry | Index Medicus
Journal Article
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, ISSN 1350-6129, 2018, Volume 25, Issue 3, pp. 189 - 196
Thioflavin-T (ThT) is the most commonly used fluorescent dye for following amyloid formation semi-quantitatively in vitro, specifically probing the fibrillar... 
MEDICINE, RESEARCH & EXPERIMENTAL | WILD-TYPE | MUTANT | thioflavin-T | QUANTIFICATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | STATE | polymorphism | atomic force microscopy | PEPTIDE | MEDICINE, GENERAL & INTERNAL | synuclein | MODES | AMYLOID FIBRILS | BETA-SHEET | GROWTH | Amyloid | AGGREGATION
Journal Article
Bio-protocol, ISSN 2331-8325, 07/2018, Volume 8, Issue 14
Studying the aggregation of amyloid proteins like α-synuclein is a convenient and popular tool to gain kinetic insights into aggregation as well as to study... 
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 2007, Volume 360, Issue 1, pp. 135 - 138
Journal Article
Journal of Physical Chemistry B, ISSN 1520-6106, 11/2012, Volume 116, Issue 45, pp. 13389 - 13395
Journal Article
Journal of Structural Biology, ISSN 1047-8477, 03/2009, Volume 165, Issue 3, pp. 140 - 145
Journal Article
Dyes and Pigments, ISSN 0143-7208, 11/2014, Volume 110, pp. 97 - 105
Thioflavin T is a highly sensitive fluorescent marker of amyloid fibrils that has been widely used for biomedical assays. However, neither its complex... 
TICT | Thioflavin T | Amyloid fibril | Photophysical properties | Fluorescent marker | Molecular rotor | EXCITED-STATE | PROTEIN | MATERIALS SCIENCE, TEXTILES | ALZHEIMERS-DISEASE | CONGO RED | BETA-PEPTIDE | ABSORPTION-SPECTRA | ENGINEERING, CHEMICAL | DYE | IN-VITRO | CHEMISTRY, APPLIED | CHARGE-TRANSFER | BINDING | Proteins | Fluorescence | Analysis | Binding | Solvents | Dyes | Wavelengths | Aggregates | Markers | Affinity
Journal Article
Methods and Applications in Fluorescence, ISSN 2050-6120, 09/2016, Volume 4, Issue 3, pp. 034008 - 034008
Journal Article