Page last updated: 2024-08-22

thioflavin t and 3-nitrotyrosine

thioflavin t has been researched along with 3-nitrotyrosine in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (66.67)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Duff, K; La Francois, J; Matsuoka, Y; Picciano, M1
Champy, P; Duyckaerts, C; Féger, J; Hirsch, EC; Höglinger, GU; Khondiker, ME; Lannuzel, A; Lombes, A; Medja, F; Michel, PP; Oertel, WH; Prigent, A; Ruberg, M1
Alavianmehr, MM; Ghahramani, M; Khoshaman, K; Yousefi, R1

Other Studies

3 other study(ies) available for thioflavin t and 3-nitrotyrosine

ArticleYear
Fibrillar beta-amyloid evokes oxidative damage in a transgenic mouse model of Alzheimer's disease.
    Neuroscience, 2001, Volume: 104, Issue:3

    Topics: Aging; Aldehydes; Alzheimer Disease; Amyloid beta-Peptides; Animals; Benzothiazoles; Brain; Disease Models, Animal; Immunohistochemistry; Mice; Mice, Neurologic Mutants; Mice, Transgenic; Nerve Degeneration; Neurofibrillary Tangles; Oxidative Stress; Thiazoles; Tyrosine

2001
The mitochondrial complex I inhibitor rotenone triggers a cerebral tauopathy.
    Journal of neurochemistry, 2005, Volume: 95, Issue:4

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Analysis of Variance; Animals; Antineoplastic Combined Chemotherapy Protocols; Behavior, Animal; Benzothiazoles; Body Weight; Caspase 3; Caspases; Cell Death; Cerebral Cortex; Cytarabine; Diagnostic Imaging; Dopamine and cAMP-Regulated Phosphoprotein 32; Doxorubicin; Dystonia; Electron Transport Complex III; Enzyme Activation; Glial Fibrillary Acidic Protein; Immunohistochemistry; Locomotion; Male; Microscopy, Electron, Transmission; Mitochondria; Neurons; Phosphopyruvate Hydratase; Phosphorylation; Posture; Psychomotor Performance; Rats; Rats, Inbred Lew; Rotenone; tau Proteins; Tauopathies; Thiazoles; Time Factors; Tyrosine; Tyrosine 3-Monooxygenase; Ubiquitin; Uncoupling Agents

2005
The impact of calcium ion on structure and aggregation propensity of peroxynitrite-modified lens crystallins: new insights into the pathogenesis of cataract disorders.
    Colloids and surfaces. B, Biointerfaces, 2015, Jan-01, Volume: 125

    Topics: Animals; Benzothiazoles; Calcium; Cattle; Crystallins; Hydrophobic and Hydrophilic Interactions; Lens, Crystalline; Oxidants; Peroxynitrous Acid; Protein Aggregates; Protein Carbonylation; Protein Stability; Proteolysis; Spectrometry, Fluorescence; Thiazoles; Tryptophan; Tyrosine

2015