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Keywords: tau
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Biochem Soc Trans (2019) 47 (3): 827–838.
Published: 13 May 2019
..., and tau have been associated with familial and sporadic forms of the disease. aSyn is the major component of Lewy bodies and Lewy neurites, which are pathognomonic protein inclusions in PD. Hyperphosphorylated tau protein accumulates in neurofibrillary tangles in the brains of Alzheimer's disease patients...
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Biochem Soc Trans (2012) 40 (5): 1058–1062.
Published: 19 September 2012
... orchestrated by LRRK2 and deregulated under pathological conditions. 1 email [email protected] 7 3 2012 © The Authors Journal compilation © 2012 Biochemical Society 2012 autophosphorylation GTPase leucine-rich repeat kinase 2 (LRRK2) moesin Parkinson's disease tau...
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Biochem Soc Trans (2012) 40 (5): 1080–1085.
Published: 19 September 2012
... and leading to PD pathology autophagy cytoskeleton dopamine leucine-rich repeat kinase 2 (LRRK2) Parkinson's disease tau Both the normal and pathological functions of LRRK2 remain to be established. It will be particularly informative to determine more specifically the functional...
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Biochem Soc Trans (2012) 40 (4): 641–643.
Published: 20 July 2012
...Efthimios M.C. Skoulakis; Amritpal Mudher It is an exciting time for tau researchers as it is now generally accepted that abnormal tau species are required to mediate the toxic effects of amyloid β-peptide oligomers in Alzheimer's disease. Tau may play multiple roles in neurophysiology...
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Biochem Soc Trans (2012) 40 (4): 721–727.
Published: 20 July 2012
... and fibrils of the Aβ (amyloid β-peptide) and tau protein accumulate in specific brain regions. This is associated with the progressive destruction of synaptic circuits controlling memory and higher mental function. The primary signalling mechanisms that (i) become defective in AD to alter the normal...
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Biochem Soc Trans (2012) 40 (4): 667–671.
Published: 20 July 2012
...Sarah M. Ward; Diana S. Himmelstein; Jody K. Lancia; Lester I. Binder AD (Alzheimer's disease) is a progressive neurodegenerative disorder characterized by the extracellular accumulation of amyloid β-peptide and the intracellular accumulation of tau. Although there is much evidence linking tau...
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Biochem Soc Trans (2012) 40 (4): 644–652.
Published: 20 July 2012
...Yipeng Wang; Eckhard Mandelkow Tau aggregates are present in several neurodegenerative diseases and correlate with the severity of memory deficit in AD (Alzheimer's disease). However, the triggers of tau aggregation and tau-induced neurodegeneration are still elusive. The impairment of protein...
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Biochem Soc Trans (2012) 40 (4): 672–676.
Published: 20 July 2012
...Anne Rovelet-Lecrux; Dominique Campion Mutations of the MAPT (microtubule-associated protein tau) gene are associated with FTLD (frontotemporal lobar degeneration) with tau pathology. These mutations result in a decreased ability of tau to bind MTs (microtubules), an increased production of tau...
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Biochem Soc Trans (2012) 40 (4): 677–680.
Published: 20 July 2012
...Michael Niblock; Jean-Marc Gallo Six tau isoforms differing in their affinity for microtubules are produced by alternative splicing from the MAPT (microtubule-associated protein tau) gene in adult human brain. Several MAPT mutations causing the familial tauopathy, FTDP-17 (frontotemporal dementia...
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Biochem Soc Trans (2012) 40 (4): 693–697.
Published: 20 July 2012
...Catherine M. Cowan; Shmma Quraishe; Amritpal Mudher Insoluble aggregates of the microtubule-associated protein tau characterize a number of neurodegenerative diseases collectively termed tauopathies. These aggregates comprise abnormally hyperphosphorylated and misfolded tau proteins. Research...
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Biochem Soc Trans (2012) 40 (4): 656–660.
Published: 20 July 2012
...Jeanna M. Wheeler; Chris R. Guthrie; Brian C. Kraemer Tauopathies are neurodegenerative diseases, including AD (Alzheimer's disease) and FTLD-T (tau-positive frontotemporal lobar degeneration), with shared pathology presenting as accumulation of detergent-insoluble hyperphosphorylated tau deposits...
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Biochem Soc Trans (2012) 40 (4): 687–692.
Published: 20 July 2012
...Tara M. Caffrey; Richard Wade-Martins The microtubule-associated protein tau ( MAPT or tau) is of great interest in the field of neurodegeneration as there is a well-established genetic link between the MAPT gene locus and tauopathies, a diverse group of neurodegenerative dementias and movement...
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Biochem Soc Trans (2010) 38 (4): 1012–1015.
Published: 26 July 2010
...Amy M. Pooler; Diane P. Hanger Tau is an abundant microtubule-associated protein which regulates the stability of the cytoskeleton. Tau binds microtubules directly through microtubule-binding domains in its C-terminus. However, tau is not only located in the cytosol of cells, but also associated...
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Biochem Soc Trans (2010) 38 (4): 993–995.
Published: 26 July 2010
...Frank M. LaFerla Aβ (amyloid β-peptide) and tau are the main proteins that misfold and accumulate in amyloid plaques and NFTs (neurofibrillary tangles) of Alzheimer's disease and other neurological disorders. Historically, because plaques and NFTs accumulate in diverse cellular compartments, i.e...
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Biochem Soc Trans (2010) 38 (4): 1016–1020.
Published: 26 July 2010
...Diane P. Hanger; Selina Wray Deposition of highly phosphorylated tau in the brain is the most significant neuropathological and biochemical characteristic of the group of neurodegenerative disorders termed the tauopathies. The discovery of tau fragments in these diseases suggests that tau cleavage...
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Biochem Soc Trans (2010) 38 (4): 977–980.
Published: 26 July 2010
...Jesús Avila; Elena Gómez de Barreda; Tobias Engel; Jose J. Lucas; Félix Hernández The MAP (microtubule-associated protein) tau binds to tubulin, the main component of MTs (microtubules), which results in the stabilization of MT polymers. Tau binds to the C-terminal of tubulin, like other MAPs...
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Biochem Soc Trans (2010) 38 (4): 955–961.
Published: 26 July 2010
...Yipeng Wang; Sarika Garg; Eva-Maria Mandelkow; Eckhard Mandelkow Tau aggregation is a hallmark of several neurodegenerative diseases, including AD (Alzheimer's disease), although the mechanism underlying tau aggregation remains unclear. Recent studies show that the proteolysis of tau plays...
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Biochem Soc Trans (2010) 38 (4): 981–987.
Published: 26 July 2010
...Katerina Papanikolopoulou; Stylianos Kosmidis; Sofia Grammenoudi; Efthimios M.C. Skoulakis The heterogeneous pathology of tauopathies and the differential susceptibility of different neuronal types to WT (wild-type) and mutant tau suggest that phosphorylation at particular sites rather than...
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Biochem Soc Trans (2010) 38 (4): 953–954.
Published: 26 July 2010
...Efthimios M.C. Skoulakis; Amritpal Mudher Tauopathies are a clinically diverse group of neurodegenerative dementias involving perturbations of the level or phosphorylation state of the microtubule-binding axonal protein tau. Despite intense effort in recent years, the precise role of tau...
Articles
Biochem Soc Trans (2010) 38 (4): 973–976.
Published: 26 July 2010
...Jeanna M. Wheeler; Chris R. Guthrie; Brian C. Kraemer We previously developed a transgenic Caenorhabditis elegans model of human tauopathy disorders by expressing human tau in nematode worm neurons to explore genetic pathways contributing to tau-induced neurodegeneration. This animal model...
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Biochem Soc Trans (2010) 38 (4): 996–1000.
Published: 26 July 2010
...] are still imperfectly understood. Many transgenic mice overexpressing wild-type or mutant tau proteins have been generated to investigate the physiopathology of tauopathies. Most of the mice overexpressing wild-type tau do not develop NFTs, but can develop a severe axonopathy, whereas overexpression...
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Biochem Soc Trans (2010) 38 (2): 545–551.
Published: 22 March 2010
...Ayodeji A. Asuni; V. Hugh Perry; Vincent O'Connor Hyperphosphorylation of the microtubule-associated protein tau is a significant determinant in AD (Alzheimer's disease), where it is associated with disrupted axonal transport and probably causes synaptic dysfunction. Although less well studied...
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Biochem Soc Trans (2005) 33 (4): 591–594.
Published: 01 August 2005
... the molecular mechanisms leading to dementia. The chief neuropathological changes during Alzheimer's disease, namely neurofibrillary tangles and amyloid plaques, have helped us to determine which molecules to focus upon in the animal models, specifically Aβ (amyloid β) and tau. This paper presents my...