Page last updated: 2024-08-22

thioflavin t and glycine

thioflavin t has been researched along with glycine in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's5 (71.43)29.6817
2010's2 (28.57)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Du, HN; Hu, HY; Hu, J; Li, HT; Luo, XY; Tang, L; Zhou, JW1
Keasling, JD; Muller, SJ; Wang, K1
Ahmed, M; Aimoto, S; Constantinescu, SN; Elliott, JI; Kienlen-Campard, P; Li, H; Liu, W; Octave, JN; Sato, T; Smith, SO1
Baud, S; Keeley, FW; Miao, M; Pomès, R; Rauscher, S1
Chang, HY; King, CY; Lee, HC; Lin, JY; Wang, HL1
Chen, YR; Chiang, CH; Kuo, PH; Liang, JR; Shen, JC; Wang, S; Wang, YT; Yuan, HS1
Chen, BP; Chen, W; Chern, Y; He, RY; Huang, JJ; Liu, GC; Sun, CS; Wang, CH; Wang, CY1

Other Studies

7 other study(ies) available for thioflavin t and glycine

ArticleYear
A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein.
    Biochemistry, 2003, Jul-29, Volume: 42, Issue:29

    Topics: Alanine; alpha-Synuclein; Amino Acid Motifs; Benzothiazoles; Circular Dichroism; Escherichia coli; Glycine; Humans; Microscopy, Atomic Force; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Peptides; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Synucleins; Thiazoles; Time Factors; Valine

2003
Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides.
    International journal of biological macromolecules, 2005, Sep-15, Volume: 36, Issue:4

    Topics: Alanine; Amino Acid Motifs; Amyloid; Benzothiazoles; Circular Dichroism; Congo Red; Gene Library; Glycine; Hydrogel, Polyethylene Glycol Dimethacrylate; Isoleucine; Leucine; Macromolecular Substances; Microscopy, Electron, Scanning; Microscopy, Electron, Transmission; Models, Molecular; Peptides; Phenylalanine; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Temperature; Thiazoles; Ultraviolet Rays; Valine; X-Ray Diffraction

2005
Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.
    Biochemistry, 2006, May-02, Volume: 45, Issue:17

    Topics: Amino Acid Sequence; Amyloid; Amyloid beta-Peptides; Animals; Benzothiazoles; Fluorescent Dyes; Glycine; Humans; Methionine; Microscopy, Electron; Molecular Sequence Data; Neurons; Nuclear Magnetic Resonance, Biomolecular; Oligopeptides; Peptide Fragments; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Spectrometry, Fluorescence; Thiazoles

2006
Proline and glycine control protein self-organization into elastomeric or amyloid fibrils.
    Structure (London, England : 1993), 2006, Volume: 14, Issue:11

    Topics: Alzheimer Disease; Amino Acid Sequence; Amyloid; Animals; Benzothiazoles; Chickens; Elastin; Entropy; Glycine; Humans; Insecta; Models, Molecular; Molecular Sequence Data; Peptides; Proline; Protein Conformation; Thiazoles; Triticum

2006
Strain-specific sequences required for yeast [PSI+] prion propagation.
    Proceedings of the National Academy of Sciences of the United States of America, 2008, Sep-09, Volume: 105, Issue:36

    Topics: Amino Acid Sequence; Benzothiazoles; Glycine; Peptide Termination Factors; Prions; Proline; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thiazoles

2008
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
The influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.
    PloS one, 2014, Volume: 9, Issue:8

    Topics: Amino Acid Sequence; Amino Acid Substitution; Amyloid; Animals; Benzothiazoles; Cell Membrane; DNA-Binding Proteins; Glycine; Mice; Molecular Sequence Data; Mutant Proteins; Mutation; Peptides; Proline; Protein Aggregates; Protein Multimerization; Protein Structure, Secondary; Spectrum Analysis, Raman; Thiazoles; Time Factors

2014