| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Ming-Jang Chiu, Ya-Fang Chen, Ta-Fu Chen, Shieh-Yueh Yang, Fan-Pei Gloria Yang, Tien-Wen Tseng, Jen-Jie Chieh, Jia-Chun Rare Chen, Kai-Yuan Tzen, Mau-Sun Hua, Herng-Er Horn. Plasma tau as a window to the brain-negative associations with brain volume and memory function in mild cognitive impairment and early Alzheimer's disease. Human brain mapping. vol 35. issue 7. 2015-01-22. PMID:24129926. |
however, the plasma tau levels of alzheimer's disease (ad) have not been well studied. |
2015-01-22 |
2023-08-12 |
Not clear |
| Ce Xie, Tomohiro Miyasaka, Satomi Yoshimura, Hiroyuki Hatsuta, Sawako Yoshina, Eriko Kage-Nakadai, Shohei Mitani, Shigeo Murayama, Yasuo Ihar. The homologous carboxyl-terminal domains of microtubule-associated protein 2 and TAU induce neuronal dysfunction and have differential fates in the evolution of neurofibrillary tangles. PloS one. vol 9. issue 2. 2015-01-22. PMID:24587039. |
whereas tau is widely accepted as a pathoetiological factor in human tauopathies, including alzheimer's disease (ad), it is not known whether there is a relationship between map2 and tauopathy. |
2015-01-22 |
2023-08-12 |
human |
| Thomas C Baddeley, Jennifer McCaffrey, John M D Storey, John K S Cheung, Valeria Melis, David Horsley, Charles R Harrington, Claude M Wischi. Complex disposition of methylthioninium redox forms determines efficacy in tau aggregation inhibitor therapy for Alzheimer's disease. The Journal of pharmacology and experimental therapeutics. vol 352. issue 1. 2015-01-19. PMID:25320049. |
complex disposition of methylthioninium redox forms determines efficacy in tau aggregation inhibitor therapy for alzheimer's disease. |
2015-01-19 |
2023-08-13 |
human |
| Thomas C Baddeley, Jennifer McCaffrey, John M D Storey, John K S Cheung, Valeria Melis, David Horsley, Charles R Harrington, Claude M Wischi. Complex disposition of methylthioninium redox forms determines efficacy in tau aggregation inhibitor therapy for Alzheimer's disease. The Journal of pharmacology and experimental therapeutics. vol 352. issue 1. 2015-01-19. PMID:25320049. |
methylthioninium (mt) is a tau aggregation inhibitor with therapeutic potential in alzheimer's disease (ad). |
2015-01-19 |
2023-08-13 |
human |
| Zhentao Zhang, Mingke Song, Xia Liu, Seong Su Kang, Il-Sun Kwon, Duc M Duong, Nicholas T Seyfried, William T Hu, Zhixue Liu, Jian-Zhi Wang, Liming Cheng, Yi E Sun, Shan Ping Yu, Allan I Levey, Keqiang Y. Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease. Nature medicine. vol 20. issue 11. 2015-01-19. PMID:25326800. |
cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in alzheimer's disease. |
2015-01-19 |
2023-08-13 |
mouse |
| Zhentao Zhang, Mingke Song, Xia Liu, Seong Su Kang, Il-Sun Kwon, Duc M Duong, Nicholas T Seyfried, William T Hu, Zhixue Liu, Jian-Zhi Wang, Liming Cheng, Yi E Sun, Shan Ping Yu, Allan I Levey, Keqiang Y. Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease. Nature medicine. vol 20. issue 11. 2015-01-19. PMID:25326800. |
neurofibrillary tangles (nfts), composed of truncated and hyperphosphorylated tau, are a common feature of numerous aging-related neurodegenerative diseases, including alzheimer's disease (ad). |
2015-01-19 |
2023-08-13 |
mouse |
| Alejandro Martinez-Aguila, Begoña Fonseca, Felix Hernandez, Miguel Díaz-Hernandez, Jesús Avila, Jesus Pinto. Tau triggers tear secretion by interacting with muscarinic acetylcholine receptors in New Zealand white rabbits. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24503615. |
in recent years, in vitro experiments have shown that the spread of alzheimer's disease is caused by a non-conventional activation of muscarinic receptors by dephosphorylated extracellular tau protein. |
2015-01-16 |
2023-08-12 |
Not clear |
| Jesús Avila, Diana Simón, Miguel Díaz-Hernández, Jesús Pintor, Félix Hernánde. Sources of extracellular tau and its signaling. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24531154. |
indeed, phosphorylated tau protein is the main component of tau aggregates, such as the neurofibrillary tangles present in the brain of alzheimer's disease patients. |
2015-01-16 |
2023-08-12 |
Not clear |
| Jesús Avila, Diana Simón, Miguel Díaz-Hernández, Jesús Pintor, Félix Hernánde. Sources of extracellular tau and its signaling. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24531154. |
however, extracellular tau could also damage neurons and since neuronal death is widespread in alzheimer's disease, mainly among cholinergic neurons, these cells may represent a possible source of extracellular tau. |
2015-01-16 |
2023-08-12 |
Not clear |
| C L Sayas, Jesús Ávil. Crosstalk between axonal classical microtubule-associated proteins and end binding proteins during axon extension: possible implications in neurodegeneration. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24531158. |
furthermore, we discuss the potential implications of the dysregulation of the interplay between tau and ebs in neurodegenerative disorders such as alzheimer's disease. |
2015-01-16 |
2023-08-12 |
Not clear |
| Diane P Hanger, Dawn H W Lau, Emma C Phillips, Marie K Bondulich, Tong Guo, Benjamin W Woodward, Amy M Pooler, Wendy Nobl. Intracellular and extracellular roles for tau in neurodegenerative disease. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24595196. |
this function of tau is influenced by tau phosphorylation state, which is significantly increased in alzheimer's disease and related tauopathies. |
2015-01-16 |
2023-08-12 |
Not clear |
| Diana L Castillo-Carranza, Julia E Gerson, Urmi Sengupta, Marcos J Guerrero-Muñoz, Cristian A Lasagna-Reeves, Rakez Kaye. Specific targeting of tau oligomers in Htau mice prevents cognitive impairment and tau toxicity following injection with brain-derived tau oligomeric seeds. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24603946. |
the most common neurodegenerative disease, alzheimer's disease, is a tauopathy, characterized by the presence of aggregated tau, namely in the form of neurofibrillary tangles. |
2015-01-16 |
2023-08-12 |
mouse |
| Diana L Castillo-Carranza, Julia E Gerson, Urmi Sengupta, Marcos J Guerrero-Muñoz, Cristian A Lasagna-Reeves, Rakez Kaye. Specific targeting of tau oligomers in Htau mice prevents cognitive impairment and tau toxicity following injection with brain-derived tau oligomeric seeds. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24603946. |
historically, neurofibrillary tangles have been considered the main tau species of interest in alzheimer's disease; however, we and others have shown that tau oligomers may be the most toxic form and the species responsible for the spread of pathology. |
2015-01-16 |
2023-08-12 |
mouse |
| Sudad Saman, Norman C Y Lee, Itoro Inoyo, Jun Jin, Zhihan Li, Thomas Doyle, Ann C McKee, Garth F Hal. Proteins recruited to exosomes by tau overexpression implicate novel cellular mechanisms linking tau secretion with Alzheimer's disease. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24718102. |
proteins recruited to exosomes by tau overexpression implicate novel cellular mechanisms linking tau secretion with alzheimer's disease. |
2015-01-16 |
2023-08-13 |
human |
| Sudad Saman, Norman C Y Lee, Itoro Inoyo, Jun Jin, Zhihan Li, Thomas Doyle, Ann C McKee, Garth F Hal. Proteins recruited to exosomes by tau overexpression implicate novel cellular mechanisms linking tau secretion with Alzheimer's disease. Journal of Alzheimer's disease : JAD. vol 40 Suppl 1. 2015-01-16. PMID:24718102. |
tau misprocessing to form aggregates and other toxic species has emerged as a major feature in our developing understanding of the etiology and pathogenesis of alzheimer's disease (ad). |
2015-01-16 |
2023-08-13 |
human |
| Markus Storbeck, Kristina Hupperich, John Antonydas Gaspar, Kesavan Meganathan, Lilian Martínez Carrera, Radu Wirth, Agapios Sachinidis, Brunhilde Wirt. Neuronal-specific deficiency of the splicing factor Tra2b causes apoptosis in neurogenic areas of the developing mouse brain. PloS one. vol 9. issue 2. 2015-01-10. PMID:24586484. |
tra2b has been shown to be involved in splicing processes of nasp (nuclear autoantigenic sperm protein), mapt (microtubule associated protein tau) and smn (survival motor neuron), and is therefore implicated in spermatogenesis and neurological diseases like alzheimer's disease, dementia, parkinson's disease and spinal muscular atrophy. |
2015-01-10 |
2023-08-12 |
mouse |
| Sarah M Ward, Diana S Himmelstein, Yan Ren, Yifan Fu, Xiao-Wen Yu, Kaleigh Roberts, Lester I Binder, Naruhiko Sahar. TOC1: a valuable tool in assessing disease progression in the rTg4510 mouse model of tauopathy. Neurobiology of disease. vol 67. 2015-01-06. PMID:24631720. |
with the help of other novel antibodies, the use of this antibody will aid in providing a better understanding of tau toxicity within alzheimer's disease and other tauopathies. |
2015-01-06 |
2023-08-12 |
mouse |
| Gayathri Ramachandran, Erix A Milán-Garcés, Jayant B Udgaonkar, Mrinalini Purani. Resonance Raman spectroscopic measurements delineate the structural changes that occur during tau fibril formation. Biochemistry. vol 53. issue 41. 2014-12-31. PMID:25284680. |
the aggregation of the microtubule-associated protein, tau, into amyloid fibrils is a hallmark of neurodegenerative diseases such as the tauopathies and alzheimer's disease. |
2014-12-31 |
2023-08-13 |
Not clear |
| Yafeng Xue, Paul T Wan, Per Hillertz, Fritz Schweikart, Yanlong Zhao, Lisa Wissler, Niek Dekke. X-ray structural analysis of tau-tubulin kinase 1 and its interactions with small molecular inhibitors. ChemMedChem. vol 8. issue 11. 2014-12-29. PMID:24039150. |
hyperphosphorylation of tau protein is the primary cause of tau pathology and neuronal death associated with alzheimer's disease. |
2014-12-29 |
2023-08-12 |
Not clear |
| Mari Takalo, Annakaisa Haapasalo, Henna Martiskainen, Kaisa M A Kurkinen, Henna Koivisto, Pasi Miettinen, Vinoth K M Khandelwal, Susanna Kemppainen, Dorota Kaminska, Petra Mäkinen, Ville Leinonen, Jussi Pihlajamäki, Hilkka Soininen, Markku Laakso, Heikki Tanila, Mikko Hiltune. High-fat diet increases tau expression in the brain of T2DM and AD mice independently of peripheral metabolic status. The Journal of nutritional biochemistry. vol 25. issue 6. 2014-12-23. PMID:24746833. |
to investigate the effects of both genetic and high-fat-induced diabetic phenotype on the expression and exon 10 splicing of tau, we used the alzheimer's disease mouse model (apde9) cross-bred with the type 2 diabetes mouse model over-expressing insulin-like growth factor 2 in the pancreas. |
2014-12-23 |
2023-08-13 |
mouse |