threonine has been researched along with Amyloid Deposits in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (40.00) | 29.6817 |
| 2010's | 2 (40.00) | 24.3611 |
| 2020's | 1 (20.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bjerke, M; Bridel, C; De Deyn, PP; Engelborghs, S; Nagels, G; Niemantsverdriet, E; Rozemuller, A; Sieben, A; Somers, C; Struyfs, H; Teunissen, CE; Van Broeckhoven, C; Vermeiren, Y | 1 |
| Chen, SG; Gao, J; Huntley, ML; Perry, G; Siedlak, SL; Termsarasab, P; Wang, L; Wang, X; Yan, T | 1 |
| De Deyn, PP; Engelborghs, S; Koopman, K; Le Bastard, N; Martin, JJ; Nagels, G | 1 |
| Hornbeck, L; Judge, M; Padmanabhan, J; Potter, H | 1 |
| Ishihara, T; Kitamoto, T; Nakashima, H; Ogino, K; Shimabuku, A; Shin, RW; Taki, T | 1 |
5 other study(ies) available for threonine and Amyloid Deposits
| Article | Year |
|---|---|
Associating Alzheimer's disease pathology with its cerebrospinal fluid biomarkers.
Topics: Aged; Alzheimer Disease; Amyloid beta-Peptides; Apolipoprotein E4; Biomarkers; Disease Progression; Female; Humans; Male; Peptide Fragments; Plaque, Amyloid; tau Proteins; Threonine | 2022 |
Rab10 Phosphorylation is a Prominent Pathological Feature in Alzheimer's Disease.
Topics: Aged; Aged, 80 and over; Alzheimer Disease; Brain; Female; Humans; Male; Middle Aged; Neurofibrillary Tangles; Phosphorylation; Plaque, Amyloid; rab GTP-Binding Proteins; Threonine | 2018 |
Improved discrimination of autopsy-confirmed Alzheimer's disease (AD) from non-AD dementias using CSF P-tau(181P).
Topics: Aged; Aged, 80 and over; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Autopsy; Biomarkers; Brain; Catalytic Domain; Dementia; Diagnosis, Differential; Female; Humans; Male; Neurofibrillary Tangles; Peptide Fragments; Phosphorylation; Plaque, Amyloid; Predictive Value of Tests; Sensitivity and Specificity; tau Proteins; Threonine | 2009 |
Mitosis-specific phosphorylation of amyloid precursor protein at threonine 668 leads to its altered processing and association with centrosomes.
Topics: Alzheimer Disease; Amyloid beta-Protein Precursor; Animals; Blotting, Western; Brain; Cell Cycle Proteins; Centrosome; Disease Models, Animal; Humans; Immunohistochemistry; Immunoprecipitation; Mice; Mice, Inbred C57BL; Mice, Transgenic; Mitosis; Phosphorylation; Plaque, Amyloid; Protein Processing, Post-Translational; RNA, Small Interfering; Threonine; Transfection | 2011 |
Amyloid precursor protein cytoplasmic domain with phospho-Thr668 accumulates in Alzheimer's disease and its transgenic models: a role to mediate interaction of Abeta and tau.
Topics: Alzheimer Disease; Amyloid beta-Peptides; Amyloid beta-Protein Precursor; Animals; Blotting, Western; Cytoplasm; Enzyme-Linked Immunosorbent Assay; Humans; Immunohistochemistry; Mice; Mice, Inbred C57BL; Mice, Transgenic; Neurofibrillary Tangles; Phosphorylation; Plaque, Amyloid; tau Proteins; Threonine | 2007 |