serine has been researched along with humanin in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 1 (25.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Aiso, S; Chiba, T; Hashimoto, Y; Ishizaka, M; Kanekura, K; Kawasumi, M; Kita, Y; Nawa, M; Niikura, T; Nishimoto, I; Tajima, H; Terashita, K; Yamada, M; Yamagishi, Y | 1 |
Arakawa, T; Kita, Y; Niikura, T; Tajima, H | 1 |
Benaki, D; Evangelou, A; Livaniou, E; Mikros, E; Pelecanou, M; Vlassi, M; Zikos, C | 1 |
Alsanousi, N; Fujiwara, T; Furuita, K; Kojima, C; Lee, YH; So, M; Sugiki, T | 1 |
4 other study(ies) available for serine and humanin
Article | Year |
---|---|
Two serine residues distinctly regulate the rescue function of Humanin, an inhibiting factor of Alzheimer's disease-related neurotoxicity: functional potentiation by isomerization and dimerization.
Topics: Alzheimer Disease; Amino Acid Substitution; Amyloid beta-Peptides; Amyloid beta-Protein Precursor; Animals; Cell Death; Cells, Cultured; Dimerization; Dose-Response Relationship, Drug; Drug Synergism; Hybrid Cells; Intracellular Signaling Peptides and Proteins; Isomerism; Mice; Neurons; Neuroprotective Agents; Phosphorylation; Proteins; Rats; Recombinant Fusion Proteins; Serine; Structure-Activity Relationship; Transfection | 2003 |
The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism.
Topics: Alzheimer Disease; Circular Dichroism; Glycine; Humans; Hydrophobic and Hydrophilic Interactions; Intracellular Signaling Peptides and Proteins; Mutation; Protein Structure, Secondary; Serine; Solubility; Temperature; Ultraviolet Rays | 2006 |
Solution structure of Ser14Gly-humanin, a potent rescue factor against neuronal cell death in Alzheimer's disease.
Topics: Alzheimer Disease; Amino Acid Sequence; Apoptosis; Base Sequence; Circular Dichroism; Glycine; Humans; Intracellular Signaling Peptides and Proteins; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Neurons; Neuroprotective Agents; Protein Structure, Secondary; Serine | 2006 |
Solution NMR structure and inhibitory effect against amyloid-β fibrillation of Humanin containing a d-isomerized serine residue.
Topics: Amyloid beta-Peptides; Circular Dichroism; Humans; Intracellular Signaling Peptides and Proteins; Isomerism; Microscopy, Electron, Transmission; Nuclear Magnetic Resonance, Biomolecular; Serine | 2016 |