Page last updated: 2024-08-22

thioflavin t and Protein Folding Diseases

thioflavin t has been researched along with Protein Folding Diseases in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's7 (100.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Al-Hilaly, YK; Serpell, LC; Vadukul, DM1
Amani, S; Naeem, A2
Griffin, MD; Howlett, GJ; Mao, Y; Mok, YF; Roberts, BR; Ryan, TM; Zlatic, CO1
Benesch, J; Buell, AK; De Genst, E; Dobson, CM; Knowles, TP; Müller, T; Zhang, Y1
Baldus, M; Giriens, V; Hickman, DT; Karastaneva, H; López-Deber, MP; Madani, R; Muhs, A; Nagel-Steger, L; Nand, D; Ndao, DM; Nicolau, C; Pfeifer, A; Pihlgren, M; Riesner, D; Silva, AB; St-Pierre, A; Willbold, D1
Goto, Y; Kitayama, H; Lee, YH; Lin, Y; Naiki, H; Ogi, H; Sakurai, K; So, M; Yagi, H; Yoshimura, Y1

Other Studies

7 other study(ies) available for thioflavin t and Protein Folding Diseases

ArticleYear
Methods for Structural Analysis of Amyloid Fibrils in Misfolding Diseases.
    Methods in molecular biology (Clifton, N.J.), 2019, Volume: 1873

    Topics: Amyloid; Amyloid beta-Peptides; Amyloidogenic Proteins; Benzothiazoles; Circular Dichroism; Immunohistochemistry; Microscopy, Electron, Transmission; Models, Molecular; Peptide Fragments; Protein Binding; Protein Conformation; Protein Multimerization; Proteostasis Deficiencies; Quantitative Structure-Activity Relationship; X-Ray Diffraction

2019
Detection and analysis of amorphous aggregates and fibrils of cytochrome c in the presence of phenolic acids.
    International journal of biological macromolecules, 2013, Volume: 58

    Topics: Animals; Antioxidants; Benzothiazoles; Coumaric Acids; Cytochromes c; Fluorescent Dyes; Gallic Acid; Horses; Microscopy, Fluorescence; Multiprotein Complexes; Protein Multimerization; Protein Stability; Protein Structure, Quaternary; Protein Structure, Secondary; Proteostasis Deficiencies; Single-Cell Analysis; Thiazoles; Tryptophan

2013
Deciphering aggregates, prefibrillar oligomers and protofibrils of cytochrome c.
    Amino acids, 2014, Volume: 46, Issue:8

    Topics: Anilino Naphthalenesulfonates; Benzothiazoles; Circular Dichroism; Cytochromes c; DNA Damage; Humans; Microscopy, Electron, Scanning; Neurodegenerative Diseases; Polyethylene Glycols; Protein Aggregates; Protein Conformation; Protein Folding; Proteostasis Deficiencies; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Surface-Active Agents; Thiazoles; Trifluoroethanol

2014
Fluphenazine·HCl and Epigallocatechin Gallate Modulate the Rate of Formation and Structural Properties of Apolipoprotein C-II Amyloid Fibrils.
    Biochemistry, 2015, Jun-23, Volume: 54, Issue:24

    Topics: Amyloid; Antipsychotic Agents; Apolipoprotein C-II; Benzothiazoles; Binding, Competitive; Catechin; Drug Discovery; Drugs, Investigational; Fluphenazine; Humans; Kinetics; Microscopy, Electron, Transmission; Neuroprotective Agents; Particle Size; Protein Aggregates; Protein Conformation; Proteostasis Deficiencies; Recombinant Proteins; Small Molecule Libraries; Thiazoles; Ultracentrifugation

2015
Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.
    Chembiochem : a European journal of chemical biology, 2016, 10-17, Volume: 17, Issue:20

    Topics: Amyloid; Benzothiazoles; Binding Sites; Diffusion; Humans; Kinetics; Ligands; Microfluidic Analytical Techniques; Nanoparticles; Particle Size; Protein Aggregates; Proteostasis Deficiencies; Thiazoles

2016
Sequence-independent control of peptide conformation in liposomal vaccines for targeting protein misfolding diseases.
    The Journal of biological chemistry, 2011, Apr-22, Volume: 286, Issue:16

    Topics: Alzheimer Disease; Animals; Benzothiazoles; Circular Dichroism; Female; Humans; Immunoglobulin G; Liposomes; Magnetic Resonance Spectroscopy; Mice; Mice, Inbred C57BL; Peptides; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Proteostasis Deficiencies; Thiazoles; Vaccines

2011
Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation.
    Proceedings of the National Academy of Sciences of the United States of America, 2012, Sep-04, Volume: 109, Issue:36

    Topics: Amyloid; Anilino Naphthalenesulfonates; Benzothiazoles; beta 2-Microglobulin; Escherichia coli; Fluorescence; Humans; Hydrogen-Ion Concentration; Kinetics; Microscopy, Electron; Protein Conformation; Protein Folding; Proteostasis Deficiencies; Sodium Chloride; Thiazoles; Ultrasonics

2012