congo red has been researched along with Neurodegenerative Diseases in 11 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 9 (81.82) | 29.6817 |
2010's | 2 (18.18) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bertoncini, CW; Christodoulou, J; Cremades, N; Dobson, CM; Lendel, C; Schenk, D; Toth, G; Vendruscolo, M; Waudby, CA | 1 |
Adachi, N; Hide, I; Ogawa, K; Onji, T; Saito, N; Sakai, N; Seki, T; Takahashi, H; Tanaka, S; Yamamoto, K | 1 |
Amani, S; Naeem, A | 1 |
Mahlke, C; Sánchez, I; Yuan, J | 1 |
Crowe, A; Crystal, AS; Giasson, BI; Kung, MP; Lee, VM; Trojanowski, JQ; Zhuang, ZP | 1 |
Hori, S; Kakizuka, A | 1 |
Barrio, JR; Bresjanac, M; Kepe, V; Petric, A; Popovic, M; Smid, LM; Vidmar, G; Vovko, TD | 1 |
Anisimov, SV; Frid, P; Popovic, N | 1 |
Akagi, T; Hashikawa, T; Morishima, I; Nukina, N; Tanaka, M | 1 |
Akagi, T; Hashikawa, T; Kikuchi, N; Matsuda, K; Murayama, M; Murayama, O; Nakao, S; Park, JM; Sato, S; Sun, X; Takashima, A; Tanemura, K; Yamaguchi, H; Yoshiike, Y | 1 |
Akagi, T; Hashikawa, T; Ichikawa, M; Murayama, M; Takashima, A; Tanemura, K; Tominaga, T; Yamaguchi, H | 1 |
2 review(s) available for congo red and Neurodegenerative Diseases
Article | Year |
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[Therapeutic targets in polyglutamine diseases].
Topics: Adenosine Triphosphatases; Animals; Antineoplastic Agents; Benzoquinones; Cell Cycle Proteins; Congo Red; Drug Delivery Systems; Drug Design; Endoplasmic Reticulum; Histone Deacetylase Inhibitors; Humans; Hydroxamic Acids; Lactams, Macrocyclic; Neurodegenerative Diseases; Peptides; Protein Processing, Post-Translational; Quinones; RNA Interference; Valosin Containing Protein; Vorinostat | 2004 |
Congo red and protein aggregation in neurodegenerative diseases.
Topics: Amyloid beta-Peptides; Animals; Coloring Agents; Congo Red; Humans; Inclusion Bodies; Neurodegenerative Diseases; Neuroprotective Agents; Plaque, Amyloid; Protein Folding; Staining and Labeling | 2007 |
9 other study(ies) available for congo red and Neurodegenerative Diseases
Article | Year |
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On the mechanism of nonspecific inhibitors of protein aggregation: dissecting the interactions of alpha-synuclein with Congo red and lacmoid.
Topics: alpha-Synuclein; Congo Red; Humans; Microscopy, Atomic Force; Molecular Sequence Data; Molecular Structure; Neurodegenerative Diseases; Parkinson Disease; Protein Conformation; Protein Folding; Signal Transduction; Small Molecule Libraries; Spectrophotometry, Ultraviolet | 2009 |
Congo red, an amyloid-inhibiting compound, alleviates various types of cellular dysfunction triggered by mutant protein kinase cγ that causes spinocerebellar ataxia type 14 (SCA14) by inhibiting oligomerization and aggregation.
Topics: Amyloid; Animals; Apoptosis; Cells, Cultured; Cerebellum; Coloring Agents; Congo Red; Dendrites; Dose-Response Relationship, Drug; Embryo, Mammalian; Humans; Mice; Mice, Inbred ICR; Mutant Proteins; Mutation, Missense; Neuroblastoma; Neurodegenerative Diseases; Protein Kinase C; Purkinje Cells; Spinocerebellar Ataxias; Spinocerebellar Degenerations | 2010 |
Deciphering structural intermediates and genotoxic fibrillar aggregates of albumins: a molecular mechanism underlying for degenerative diseases.
Topics: Acetonitriles; Albumins; Benzothiazoles; Circular Dichroism; Congo Red; Humans; Lymphocytes; Microscopy, Electron, Scanning; Neurodegenerative Diseases; Ovalbumin; Protein Structure, Secondary; Sodium Chloride; Spectroscopy, Fourier Transform Infrared; Thiazoles; X-Ray Diffraction | 2013 |
Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders.
Topics: Adenosine Triphosphate; Animals; Caspases; Cell Death; Congo Red; Disease Models, Animal; Enzyme Activation; HeLa Cells; Humans; Huntington Disease; Mice; Mice, Transgenic; Neurodegenerative Diseases; Peptides; Protein Binding; Protein Structure, Quaternary; Recombinant Fusion Proteins; Survival Rate; Trinucleotide Repeat Expansion; Weight Loss | 2003 |
A comparison of amyloid fibrillogenesis using the novel fluorescent compound K114.
Topics: alpha-Synuclein; Amyloid; Congo Red; Fluorescent Dyes; Humans; Nerve Tissue Proteins; Neurodegenerative Diseases; Sensitivity and Specificity; Spectrometry, Fluorescence; Staining and Labeling; Styrenes; Synucleins; tau Proteins | 2003 |
The 2,6-disubstituted naphthalene derivative FDDNP labeling reliably predicts Congo red birefringence of protein deposits in brain sections of selected human neurodegenerative diseases.
Topics: Birefringence; Congo Red; Fluorescent Dyes; Fluorine Radioisotopes; Humans; Molecular Probe Techniques; Naphthalenes; Nerve Tissue Proteins; Neurodegenerative Diseases; Neurofibrillary Tangles; Nitriles; Plaque, Amyloid; Predictive Value of Tests; Radionuclide Imaging; Reproducibility of Results; Sensitivity and Specificity | 2006 |
Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases.
Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Circular Dichroism; Congo Red; Dose-Response Relationship, Drug; Escherichia coli; Glutamine; Immunoblotting; Magnetic Resonance Spectroscopy; Microscopy, Electron; Models, Molecular; Molecular Sequence Data; Mutation; Myoglobin; Neurodegenerative Diseases; Peptides; Plasmids; Protein Conformation; Protein Folding; Protein Structure, Secondary; Sequence Homology, Amino Acid; Spectrophotometry, Infrared; Time Factors; Trinucleotide Repeat Expansion; Ultraviolet Rays; Whales | 2001 |
Formation of filamentous tau aggregations in transgenic mice expressing V337M human tau.
Topics: Animals; Benzothiazoles; Brain; Cerebral Cortex; Coloring Agents; Congo Red; Disease Models, Animal; Female; Gene Expression Regulation; Hippocampus; Humans; Immunohistochemistry; Male; Mice; Mice, Neurologic Mutants; Mice, Transgenic; Microscopy, Electron; Mutation, Missense; Neurodegenerative Diseases; Neurofibrillary Tangles; Neurons; Protein Structure, Secondary; tau Proteins; Thiazoles; Transfection; Ubiquitin | 2001 |
Neurodegeneration with tau accumulation in a transgenic mouse expressing V337M human tau.
Topics: Amino Acid Substitution; Animals; Behavior, Animal; Brain; Cell Count; Coloring Agents; Congo Red; Hippocampus; Humans; In Vitro Techniques; Mice; Mice, Transgenic; Mutation; Neurodegenerative Diseases; Neurons; Phosphorylation; RNA, Messenger; Sodium Dodecyl Sulfate; Solubility; tau Proteins | 2002 |