caseins has been researched along with alpha-synuclein in 7 studies
Studies (caseins) | Trials (caseins) | Recent Studies (post-2010) (caseins) | Studies (alpha-synuclein) | Trials (alpha-synuclein) | Recent Studies (post-2010) (alpha-synuclein) |
---|---|---|---|---|---|
16,863 | 561 | 4,170 | 10,821 | 29 | 8,011 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 5 (71.43) | 29.6817 |
2010's | 2 (28.57) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cho, HI; Kim, J; Kim, TD; Ryu, HJ; Yang, CH | 1 |
Barron, LD; Blanch, EW; Goedert, M; Hecht, L; Holt, C; Jakes, R; Syme, CD | 1 |
Anderson, VE; Apetri, MM; Carey, PR; Maiti, NC; Zagorski, MG | 1 |
Cappai, R; Carver, JA; Jankova, L; Rekas, A; Thorn, DC | 1 |
Carver, JA; Ecroyd, H | 1 |
Carver, JA; Elias, AK; Ho, LH; Liu, Y; Musgrave, IF; Pukala, TL | 1 |
Avvakumova, S; Brocca, S; Colombo, M; Colzani, B; Grandori, R; Legname, G; Narkiewicz, J; Natalello, A; Prosperi, D; Rigamonti, V; Santambrogio, C; Vitali, M | 1 |
7 other study(ies) available for caseins and alpha-synuclein
Article | Year |
---|---|
Thermal behavior of proteins: heat-resistant proteins and their heat-induced secondary structural changes.
Topics: alpha-Fetoproteins; alpha-Synuclein; Amino Acid Sequence; Apolipoprotein A-I; Blood Proteins; Caseins; Circular Dichroism; Hot Temperature; Humans; Jurkat Cells; Molecular Sequence Data; Nerve Tissue Proteins; Prealbumin; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Sequence Analysis, Protein; Synucleins | 2000 |
A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins.
Topics: alpha-Synuclein; Animals; Caseins; Cattle; gamma-Synuclein; Humans; Nerve Tissue Proteins; Protein Folding; Protein Structure, Secondary; Spectrum Analysis, Raman; Synucleins; tau Proteins | 2002 |
Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein.
Topics: alpha-Synuclein; Amides; Amino Acid Sequence; Amyloid; Caseins; Circular Dichroism; Humans; Methanol; Molecular Sequence Data; Nerve Tissue Proteins; Phosvitin; Propanols; Protein Conformation; Protein Folding; Protein Structure, Secondary; Recombinant Proteins; Sodium Dodecyl Sulfate; Solutions; Spectrum Analysis, Raman; Synucleins | 2004 |
Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.
Topics: alpha-Crystallin B Chain; alpha-Synuclein; Amyloid; Animals; Benzothiazoles; beta-Crystallins; Caseins; Cattle; Chromatography, High Pressure Liquid; Humans; Kinetics; Magnetic Resonance Spectroscopy; Microscopy, Electron, Transmission; Molecular Chaperones; Protein Binding; Recombinant Proteins; Temperature; Thiazoles | 2007 |
The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation.
Topics: alpha-Crystallin B Chain; alpha-Synuclein; Amyloid; Animals; Arginine; Caseins; Cattle; Cytoprotection; Guanidine; Hot Temperature; Humans; Insulin; Lactalbumin; Mutation; Parkinson Disease | 2008 |
Hemin as a generic and potent protein misfolding inhibitor.
Topics: Alcohol Dehydrogenase; alpha-Synuclein; Amyloid; Amyloid beta-Peptides; Animals; Caseins; Catalase; gamma-Crystallins; Hemin; Humans; Oxidation-Reduction; Peptide Fragments; Protein Aggregation, Pathological; Protein Folding; Protein Structure, Secondary | 2014 |
Conformational properties of intrinsically disordered proteins bound to the surface of silica nanoparticles.
Topics: alpha-Synuclein; Animals; Caseins; Cattle; Chick Embryo; Circular Dichroism; Cyclin-Dependent Kinase Inhibitor Proteins; Electrophoresis, Polyacrylamide Gel; Humans; Intrinsically Disordered Proteins; Muramidase; Nanoparticles; Protein Binding; Protein Conformation; Protein Corona; Saccharomyces cerevisiae Proteins; Silicon Dioxide; Spectroscopy, Fourier Transform Infrared | 2018 |