| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| Khalid Iqba. Tau and Alzheimer's disease: Past, present and future. Cytoskeleton (Hoboken, N.J.). 2023-12-21. PMID:38126608. |
currently, tau pathology is a major drug target for the treatment of ad and related tauopathies. |
2023-12-21 |
2023-12-23 |
human |
| Jie Yang, Naiting Shen, Jianying Shen, Ying Yang, Hong-Lian L. Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer's Disease and Other Tauopathies. Molecular neurobiology. 2023-12-19. PMID:38114762. |
complicated role of post-translational modification and protease-cleaved fragments of tau in alzheimer's disease and other tauopathies. |
2023-12-19 |
2023-12-23 |
Not clear |
| Jie Yang, Naiting Shen, Jianying Shen, Ying Yang, Hong-Lian L. Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer's Disease and Other Tauopathies. Molecular neurobiology. 2023-12-19. PMID:38114762. |
perturbations in tau's structure and function are implicated in the pathogenesis of neurodegenerative diseases collectively known as tauopathies, the most common disorder of which is alzheimer's disease (ad). |
2023-12-19 |
2023-12-23 |
Not clear |
| Jie Yang, Naiting Shen, Jianying Shen, Ying Yang, Hong-Lian L. Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer's Disease and Other Tauopathies. Molecular neurobiology. 2023-12-19. PMID:38114762. |
in tauopathies, it has been found that tau has a variety of post-translational modification (ptm) abnormalities and/or tau is cleaved into a variety of fragments by some specific proteolytic enzymes; however, the precise contributions of these abnormal modifications and fragments to disease onset and progression remain incompletely understood. |
2023-12-19 |
2023-12-23 |
Not clear |
| Jie Yang, Naiting Shen, Jianying Shen, Ying Yang, Hong-Lian L. Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer's Disease and Other Tauopathies. Molecular neurobiology. 2023-12-19. PMID:38114762. |
herein, we provide an overview about the involvement of distinctive abnormal tau ptms and different tau fragments in the pathogenesis of ad and other tauopathies and discuss the involvement of proteolytic enzymes such as caspases, calpains, and asparagine endopeptidase in mediating tau cleavage while also addressing the intercellular transmission role played by tau. |
2023-12-19 |
2023-12-23 |
Not clear |
| Yu Jung Jang, Min Gyu Choi, Byung Jae Yoo, Kyeong Jae Lee, Won Beom Jung, Seong-Gi Kim, Sun Ah Par. Interaction Between a High-Fat Diet and Tau Pathology in Mice: Implications for Alzheimer's Disease. Journal of Alzheimer's disease : JAD. 2023-12-18. PMID:38108353. |
however, its relation with tau pathology (i.e., aberrant tau protein behavior in tauopathies such as ad) has been inconclusive. |
2023-12-18 |
2023-12-21 |
mouse |
| Michel Goedert, R Anthony Crowther, Sjors H W Scheres, Maria Grazia Spillantin. Tau and neurodegeneration. Cytoskeleton (Hoboken, N.J.). 2023-12-14. PMID:38073060. |
beginning in 2017, work on human brains using high-resolution techniques has led to a structure-based classification of tauopathies, which has opened the door to a better understanding of the significance of tau filament formation. |
2023-12-14 |
2023-12-17 |
human |
| Neelam Younas, Tayyaba Saleem, Abrar Younas, Inga Zer. Nuclear face of Tau: an inside player in neurodegeneration. Acta neuropathologica communications. vol 11. issue 1. 2023-12-13. PMID:38087392. |
tau (tubulin associated unit) protein is a major hallmark of alzheimer's disease (ad) and tauopathies. |
2023-12-13 |
2023-12-17 |
human |
| Neelam Younas, Tayyaba Saleem, Abrar Younas, Inga Zer. Nuclear face of Tau: an inside player in neurodegeneration. Acta neuropathologica communications. vol 11. issue 1. 2023-12-13. PMID:38087392. |
discovery of the role of tau protein in various cellular compartments especially in the nucleus opens up a new fold of complexity in tauopathies. |
2023-12-13 |
2023-12-17 |
human |
| Jiaxing Tang, Ruiqing Sun, Jiaqian Wan, Zhengdong Xu, Yu Zou, Qingwen Zhan. Atomic insights into the inhibition of R3 domain of tau protein by epigallocatechin gallate, quercetin and gallic acid. Biophysical chemistry. vol 305. 2023-12-13. PMID:38088006. |
inhibiting tau protein aggregation has become a prospective avenue for the therapeutic development of tauopathies. |
2023-12-13 |
2023-12-17 |
Not clear |
| Michael P Vigers, Samuel Lobo, Saeed Najafi, Austin Dubose, Karen Tsay, Pritam Ganguly, Andrew P Longhini, Yingying Jin, Steven K Buratto, Kenneth S Kosik, M Scott Shell, Joan-Emma Shea, Songi Ha. Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangement. bioRxiv : the preprint server for biology. 2023-12-11. PMID:38077065. |
tau forms toxic fibrillar aggregates in a family of neurodegenerative diseases known as tauopathies. |
2023-12-11 |
2023-12-17 |
Not clear |
| Michael P Vigers, Samuel Lobo, Saeed Najafi, Austin Dubose, Karen Tsay, Pritam Ganguly, Andrew P Longhini, Yingying Jin, Steven K Buratto, Kenneth S Kosik, M Scott Shell, Joan-Emma Shea, Songi Ha. Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangement. bioRxiv : the preprint server for biology. 2023-12-11. PMID:38077065. |
this study debuts a strategy of identifying a critical segment of tau that forms a folding motif that is characteristic of a family of tauopathies and isolating it as a standalone peptide that form seeding-competent fibrils. |
2023-12-11 |
2023-12-17 |
Not clear |
| Michael S LaCroix, Efrosini Artikis, Brian D Hitt, Joshua D Beaver, Sandi-Jo Estill-Terpack, Kelly Gleason, Carol A Tamminga, Bret M Evers, Charles L White, Byron Caughey, Marc I Diamon. Tau seeding without tauopathy. The Journal of biological chemistry. 2023-12-10. PMID:38072056. |
neurodegenerative tauopathies such as alzheimer's disease (ad) are caused by brain accumulation of tau assemblies. |
2023-12-10 |
2023-12-17 |
mouse |
| Shannon Zhuang, Pijush Chakraborty, Markus Zweckstette. Regulation of tau by peptidyl-prolyl isomerases. Current opinion in structural biology. vol 84. 2023-12-07. PMID:38061261. |
abnormal hyperphosphorylation and aggregation of tau characterize a group of diseases called tauopathies. |
2023-12-07 |
2023-12-17 |
Not clear |
| Shannon Zhuang, Pijush Chakraborty, Markus Zweckstette. Regulation of tau by peptidyl-prolyl isomerases. Current opinion in structural biology. vol 84. 2023-12-07. PMID:38061261. |
therefore, the ability of ppiases to structurally modify and regulate tau should be further investigated due to its potential therapeutic implications for alzheimer's disease and other tauopathies. |
2023-12-07 |
2023-12-17 |
Not clear |
| Kerry T Sun, Tark Patel, Sang-Gyun Kang, Allan Yarahmady, Mahalashmi Srinivasan, Olivier Julien, Jónathan Heras, Sue-Ann Mo. Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation. ACS chemical neuroscience. 2023-12-06. PMID:38054595. |
the accumulation of tau fibrils is associated with neurodegenerative diseases, which are collectively termed tauopathies. |
2023-12-06 |
2023-12-10 |
Not clear |
| Kerry T Sun, Tark Patel, Sang-Gyun Kang, Allan Yarahmady, Mahalashmi Srinivasan, Olivier Julien, Jónathan Heras, Sue-Ann Mo. Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation. ACS chemical neuroscience. 2023-12-06. PMID:38054595. |
cryo-em studies have shown that the packed fibril core of tau adopts distinct structures in different tauopathies, such as alzheimer's disease, corticobasal degeneration, and progressive supranuclear palsy. |
2023-12-06 |
2023-12-10 |
Not clear |
| Kerry T Sun, Tark Patel, Sang-Gyun Kang, Allan Yarahmady, Mahalashmi Srinivasan, Olivier Julien, Jónathan Heras, Sue-Ann Mo. Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation. ACS chemical neuroscience. 2023-12-06. PMID:38054595. |
a subset of tauopathies are linked to missense mutations in the tau protein, but it is not clear whether these mutations impact the structure of tau fibrils. |
2023-12-06 |
2023-12-10 |
Not clear |
| Bryan Alava, Gabriela Hery, Silvana Sidhom, Stefan Prokop, Karyn Esser, Jose Abisambr. Targeted brain-specific tauopathy compromises peripheral skeletal muscle integrity and function. bioRxiv : the preprint server for biology. 2023-11-28. PMID:38014109. |
tauopathies are neurodegenerative disorders in which the pathological intracellular aggregation of the protein tau causes cognitive deficits. |
2023-11-28 |
2023-11-29 |
mouse |
| Evan Pretti, M Scott Shel. Mapping the configurational landscape and aggregation phase behavior of the tau protein fragment PHF6. Proceedings of the National Academy of Sciences of the United States of America. vol 120. issue 48. 2023-11-24. PMID:37983502. |
the phf6 (val-gln-ile-val-tyr-lys) motif, found in all isoforms of the microtubule-associated protein tau, forms an integral part of ordered cores of amyloid fibrils formed in tauopathies and is thought to play a fundamental role in tau aggregation. |
2023-11-24 |
2023-11-28 |
Not clear |