PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31358058-7 2019 Our recent study indicates that Casp2-catalyzed tau cleavage at aspartate 314 (tau 2N4R isoform numbering system) mediates synaptotoxicity, cognitive deficits and neurodegeneration in cellular and mouse models of frontotemporal dementia; further, levels of Deltatau314, the soluble, N-terminal cleavage product, are elevated in individuals with mild cognitive impairment and Alzheimer"s disease, compared with cognitively normal individuals. Aspartic Acid 64-73 microtubule associated protein tau Homo sapiens 48-51 31358058-7 2019 Our recent study indicates that Casp2-catalyzed tau cleavage at aspartate 314 (tau 2N4R isoform numbering system) mediates synaptotoxicity, cognitive deficits and neurodegeneration in cellular and mouse models of frontotemporal dementia; further, levels of Deltatau314, the soluble, N-terminal cleavage product, are elevated in individuals with mild cognitive impairment and Alzheimer"s disease, compared with cognitively normal individuals. Aspartic Acid 64-73 microtubule associated protein tau Homo sapiens 79-82 24226268-2 2013 Here, we report immunohistochemical staining of the Tau-C3 antibody, which recognizes Asp(421)-truncated tau, in a group of AD cases with different extents of cognitive impairment. Aspartic Acid 86-89 microtubule associated protein tau Homo sapiens 52-55 24226268-5 2013 On the other hand, despite in vitro evidence that caspase-3 cleaves monomeric tau at Asp(421), to date, this truncation has not been demonstrated to be executed by this protease in polymeric tau entities. Aspartic Acid 85-88 microtubule associated protein tau Homo sapiens 78-81 29908160-0 2018 Pseudo-phosphorylation at AT8 epitopes regulates the tau truncation at aspartate 421. Aspartic Acid 71-80 microtubule associated protein tau Homo sapiens 53-56 24226268-2 2013 Here, we report immunohistochemical staining of the Tau-C3 antibody, which recognizes Asp(421)-truncated tau, in a group of AD cases with different extents of cognitive impairment. Aspartic Acid 86-89 microtubule associated protein tau Homo sapiens 105-108 24226268-3 2013 In the hippocampus, we found distinct nonfibrillary aggregates of Asp(421)-truncated tau. Aspartic Acid 66-69 microtubule associated protein tau Homo sapiens 85-88 21919991-0 2012 Ubiquitin is associated with early truncation of tau protein at aspartic acid(421) during the maturation of neurofibrillary tangles in Alzheimer"s disease. Aspartic Acid 64-77 microtubule associated protein tau Homo sapiens 49-52 21919991-1 2012 Pathological processing of tau protein during the formation and maturation of neurofibrillary tangles (NFTs) includes abnormal phosphorylation, conformational changes and truncation of the C-terminus at aspartic-acid(421) (apoptotic product) and glutamic-acid(391) residues. Aspartic Acid 203-216 microtubule associated protein tau Homo sapiens 27-30 22396417-5 2012 Overexpression of wild-type Tau or mutated forms in which these sites had been changed to either unphosphorylatable alanines or phosphomimetic aspartates inhibited mitochondrial movement in the neurite processes of PC12 cells as well as the axons of mouse brain cortical neurons. Aspartic Acid 143-153 microtubule associated protein tau Homo sapiens 28-31 18198423-11 2007 In addition; truncation at Asp-421 of the C-terminus of tau protein, as detected by Tau-C3, is also an early molecular event in tau protein aggregation prior to PHF formation in AD. Aspartic Acid 27-30 microtubule associated protein tau Homo sapiens 56-59 18198423-11 2007 In addition; truncation at Asp-421 of the C-terminus of tau protein, as detected by Tau-C3, is also an early molecular event in tau protein aggregation prior to PHF formation in AD. Aspartic Acid 27-30 microtubule associated protein tau Homo sapiens 128-131 15748781-5 2005 Immunohistochemical studies indicate that cleavage at aspartic acid(421) occurs after formation of the Alz50 epitope but prior to formation of the Tau-66 epitope and truncation at glutamic acid(391) (formation of the MN423 epitope). Aspartic Acid 54-67 microtubule associated protein tau Homo sapiens 147-150 16606369-1 2006 The tangles of Alzheimer"s disease (AD) are comprised of the tau protein displaying numerous alterations, including phosphorylation at serine 422 (S422) and truncation at aspartic acid 421 (D421). Aspartic Acid 171-184 microtubule associated protein tau Homo sapiens 61-64 12846581-2 2003 Previous work has indicated that the C-terminal region of tau inhibits polymerization in vitro, and a growing body of evidence implicates caspase cleavage of tau at Asp 421 in the C-terminus as an important inducer of tau polymerization in Alzheimer"s disease. Aspartic Acid 165-168 microtubule associated protein tau Homo sapiens 158-161 12846581-2 2003 Previous work has indicated that the C-terminal region of tau inhibits polymerization in vitro, and a growing body of evidence implicates caspase cleavage of tau at Asp 421 in the C-terminus as an important inducer of tau polymerization in Alzheimer"s disease. Aspartic Acid 165-168 microtubule associated protein tau Homo sapiens 158-161 34818016-4 2022 Examination of a large set of human brain samples revealed a striking relationship between Alzheimer"s disease (AD) status and isomerization of aspartic acid in a peptide from tau. Aspartic Acid 144-157 microtubule associated protein tau Homo sapiens 176-179 32123248-3 2020 Our recent study suggests that caspase-2 (Casp2)-catalyzed tau cleavage at aspartate 314 mediates synaptic dysfunction and memory impairment in mouse and cellular models of neurodegenerative disorders. Aspartic Acid 75-84 microtubule associated protein tau Homo sapiens 59-62 12888622-3 2003 Here, we report that tau is proteolyzed by multiple caspases at a highly conserved aspartate residue (Asp421) in its C terminus in vitro and in neurons treated with amyloid-beta (Abeta) (1-42) peptide. Aspartic Acid 83-92 microtubule associated protein tau Homo sapiens 21-24