Compounds > thioflavin t
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thioflavin t and Amyotrophic Lateral Sclerosis

thioflavin t has been researched along with Amyotrophic Lateral Sclerosis in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (14.29)29.6817
2010's5 (71.43)24.3611
2020's1 (14.29)2.80

Authors

AuthorsStudies
Baumer, KM; Koone, JC; Shaw, BF1
Bennett, RE; Commins, C; Dujardin, S; Eftekharzadeh, B; Fan, Z; Hernandez-Vega, A; Hyman, AA; Hyman, BT; Kamath, T; Laskowski, PR; MacKenzie, D; Mandelkow, E; Molliex, AM; Muller, D; Roe, AD; Taylor, JP; Tepper, K; Vanderburg, C; Wegmann, S; Zoltowska, KM1
Cristóvão, JS; Gomes, CM; Henriques, BJ1
Chia, R; Collinge, J; Fisher, EM; Jackson, GS; Jones, S; Tattum, MH1
Botelho, HM; Cardoso, I; Fritz, G; Gomes, CM; Leal, SS; Morozova-Roche, LA; Yanamandra, K1
Chen, YR; Chiang, CH; Kuo, PH; Liang, JR; Shen, JC; Wang, S; Wang, YT; Yuan, HS1
Cashman, NR; Chakrabartty, A; Crow, JP; Cunningham, P; Dahan, S; Furtos-Matei, A; Kondejewski, LH; Qi, XF; Rakhit, R1

Other Studies

7 other study(ies) available for thioflavin t and Amyotrophic Lateral Sclerosis

ArticleYear
Kinetic Variability in Seeded Formation of ALS-Linked SOD1 Fibrils Across Multiple Generations.
    ACS chemical neuroscience, 2020, 02-05, Volume: 11, Issue:3

    Topics: Amyloid; Amyotrophic Lateral Sclerosis; Benzothiazoles; Family Characteristics; Mutation; Saccharomyces cerevisiae; Superoxide Dismutase; Superoxide Dismutase-1

2020
Tau protein liquid-liquid phase separation can initiate tau aggregation.
    The EMBO journal, 2018, 04-03, Volume: 37, Issue:7

    Topics: Aged, 80 and over; Alzheimer Disease; Amino Acid Sequence; Amyotrophic Lateral Sclerosis; Animals; Benzothiazoles; Biophysical Phenomena; Brain; Cloning, Molecular; DNA-Binding Proteins; Escherichia coli; Female; HEK293 Cells; Heterogeneous Nuclear Ribonucleoprotein A1; Humans; Liquid-Liquid Extraction; Mice; Mice, Transgenic; Molecular Weight; Neuroblastoma; Neurodegenerative Diseases; Neurofibrillary Tangles; Neurons; Phosphorylation; Protein Aggregation, Pathological; Recombinant Proteins; Sequence Analysis, Protein; Sf9 Cells; tau Proteins

2018
Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation.
    Methods in molecular biology (Clifton, N.J.), 2019, Volume: 1873

    Topics: Amyloidogenic Proteins; Amyotrophic Lateral Sclerosis; Anilino Naphthalenesulfonates; Benzothiazoles; Circular Dichroism; Dynamic Light Scattering; Fluorescent Dyes; Gene Expression; Humans; Models, Molecular; Protein Aggregation, Pathological; Protein Conformation; Protein Folding; Recombinant Proteins; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Superoxide Dismutase-1

2019
Superoxide dismutase 1 and tgSOD1 mouse spinal cord seed fibrils, suggesting a propagative cell death mechanism in amyotrophic lateral sclerosis.
    PloS one, 2010, May-13, Volume: 5, Issue:5

    Topics: Amyloid; Amyotrophic Lateral Sclerosis; Animals; Benzothiazoles; Cell Death; Humans; Kinetics; Mice; Mice, Transgenic; Microscopy, Electron; Protein Stability; Spinal Cord; Subcellular Fractions; Superoxide Dismutase; Superoxide Dismutase-1; Thiazoles; Time Factors

2010
S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation.
    The Journal of biological chemistry, 2012, Dec-07, Volume: 287, Issue:50

    Topics: Amyloid; Amyotrophic Lateral Sclerosis; Benzothiazoles; Calcium; Cell Cycle Proteins; Cell Line, Tumor; Humans; Kinetics; Protein Structure, Quaternary; Protein Structure, Secondary; S100 Calcium Binding Protein A6; S100 Proteins; Spectroscopy, Fourier Transform Infrared; Superoxide Dismutase; Superoxide Dismutase-1; Thiazoles

2012
The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.
    The Journal of biological chemistry, 2013, Mar-29, Volume: 288, Issue:13

    Topics: Amino Acid Motifs; Amyloidogenic Proteins; Amyotrophic Lateral Sclerosis; Benzothiazoles; Chromatography; Circular Dichroism; Dimerization; DNA-Binding Proteins; DNA, Complementary; Frontotemporal Lobar Degeneration; Glutathione Transferase; Glycine; Humans; Neurodegenerative Diseases; Peptides; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Scattering, Radiation; Thiazoles; X-Rays

2013
Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis.
    The Journal of biological chemistry, 2002, Dec-06, Volume: 277, Issue:49

    Topics: Amino Acids; Amyotrophic Lateral Sclerosis; Benzothiazoles; Binding Sites; Chromatography, Liquid; Circular Dichroism; Erythrocytes; Humans; Hydrogen-Ion Concentration; Light; Microscopy, Atomic Force; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Neurons; Oxygen; Protein Binding; Protein Folding; Scattering, Radiation; Superoxide Dismutase; Thiazoles; Zinc

2002