PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7667312-0 1995 Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Cysteine 13-21 microtubule associated protein tau Homo sapiens 50-84 2018792-4 1991 This tau-related protein has only one blocked cysteine residue and also has a decreased tubulin binding capacity as compared with that of tau protein. Cysteine 46-54 microtubule associated protein tau Homo sapiens 5-8 34720880-11 2021 Further, recombinant 2N3R and 2N4R tau isoforms were found to be CoAlated in vitro and the site of CoAlation mapped by mass spectrometry to conserved cysteine 322, located in the microtubule binding region. Cysteine 150-158 microtubule associated protein tau Homo sapiens 35-38 34273857-4 2022 Determination of five free amino acids showed that 0.05% Cys treatment increased the Pro and Tau contents, while had no significant effect on the Cys, Glu and GABA contents. Cysteine 57-60 microtubule associated protein tau Homo sapiens 93-96 34656563-0 2021 Flipping the switch: how cysteine oxidation directs tau amyloid conformations. Cysteine 25-33 microtubule associated protein tau Homo sapiens 52-55 34720880-15 2021 Covalent modification of recombinant tau at cysteine 322 suggests that CoAlation may play an important role in protecting redox-sensitive tau cysteine from irreversible overoxidation and may modulate its acetyltransferase activity and functional interactions. Cysteine 44-52 microtubule associated protein tau Homo sapiens 37-40 34720880-15 2021 Covalent modification of recombinant tau at cysteine 322 suggests that CoAlation may play an important role in protecting redox-sensitive tau cysteine from irreversible overoxidation and may modulate its acetyltransferase activity and functional interactions. Cysteine 44-52 microtubule associated protein tau Homo sapiens 138-141 34339733-4 2021 Four-repeat tau contains two cysteines that can form an intramolecular disulfide bond, resulting in a structurally restrained compact monomer. Cysteine 29-38 microtubule associated protein tau Homo sapiens 12-15 34308969-7 2021 QUARK-based de novo modelling of the second and third microtubule-binding repeat domains, in which the two cysteine residues of 4R isoforms of Tau are located, supports the concept that this region of Tau could form transient amphipathic helices for membrane interaction. Cysteine 107-115 microtubule associated protein tau Homo sapiens 143-146 34308969-7 2021 QUARK-based de novo modelling of the second and third microtubule-binding repeat domains, in which the two cysteine residues of 4R isoforms of Tau are located, supports the concept that this region of Tau could form transient amphipathic helices for membrane interaction. Cysteine 107-115 microtubule associated protein tau Homo sapiens 201-204 35468811-0 2022 Correction to: Mical modulates Tau toxicity via cysteine oxidation in vivo. Cysteine 48-56 microtubule associated protein tau Homo sapiens 31-34 32087196-4 2020 We herein report that both wild-type PDI and its quadruple cysteine mutant only having chaperone activity, significantly inhibit pathological phosphorylation and abnormal aggregation of Tau in cells, and significantly decrease the mitochondrial damage and Tau cytotoxicity resulting from Tau aberrant aggregation, highlighting the chaperone property of PDI. Cysteine 59-67 microtubule associated protein tau Homo sapiens 256-259 35379354-0 2022 Mical modulates Tau toxicity via cysteine oxidation in vivo. Cysteine 33-41 microtubule associated protein tau Homo sapiens 16-19 35379354-6 2022 Exploration of the mechanism was pursued using a Mical inhibitor, a mutation in Mical that selectively disrupts its monooxygenase domain, Tau transgenes mutated at cysteine residues targeted by Mical and mass spectrometry analysis to quantify cysteine oxidation. Cysteine 164-172 microtubule associated protein tau Homo sapiens 138-141 33317395-0 2020 Role of cysteines in accelerating Tau filament formation. Cysteine 8-17 microtubule associated protein tau Homo sapiens 34-37 33317395-3 2020 The two cysteine residues and the two hexapeptide regions of full-length Tau play a key role in initialization and filament formation during Tau aggregation. Cysteine 8-16 microtubule associated protein tau Homo sapiens 73-76 33317395-3 2020 The two cysteine residues and the two hexapeptide regions of full-length Tau play a key role in initialization and filament formation during Tau aggregation. Cysteine 8-16 microtubule associated protein tau Homo sapiens 141-144 33317395-4 2020 The role of cysteine residues in Tau aggregation has been studied by in-vitro aggregation assay that was measured by Thioflavin S fluorescence to observe the kinetics of aggregation. Cysteine 12-20 microtubule associated protein tau Homo sapiens 33-36 33317395-6 2020 Here, we report that cysteine mutant full-length Tau can aggregate to form filaments under in-vitro conditions. Cysteine 21-29 microtubule associated protein tau Homo sapiens 49-52 33317395-9 2020 On the other hand, the cysteine mutant delayed the initial Tau aggregation. Cysteine 23-31 microtubule associated protein tau Homo sapiens 59-62 33317395-10 2020 This indicates the importance of cysteine residues in accelerating initial Tau nucleation for its aggregation. Cysteine 33-41 microtubule associated protein tau Homo sapiens 75-78 33317395-11 2020 The filament morphology of wild-type and cysteine mutant Tau has been characterized using transmission electron microscopy and high-resolution transmission electron microscopy. Cysteine 41-49 microtubule associated protein tau Homo sapiens 57-60 32087196-4 2020 We herein report that both wild-type PDI and its quadruple cysteine mutant only having chaperone activity, significantly inhibit pathological phosphorylation and abnormal aggregation of Tau in cells, and significantly decrease the mitochondrial damage and Tau cytotoxicity resulting from Tau aberrant aggregation, highlighting the chaperone property of PDI. Cysteine 59-67 microtubule associated protein tau Homo sapiens 186-189 29714059-0 2018 Blocking the Thiol at Cysteine-322 Destabilizes Tau Protein and Prevents Its Oligomer Formation. Cysteine 22-30 microtubule associated protein tau Homo sapiens 48-51 32087196-4 2020 We herein report that both wild-type PDI and its quadruple cysteine mutant only having chaperone activity, significantly inhibit pathological phosphorylation and abnormal aggregation of Tau in cells, and significantly decrease the mitochondrial damage and Tau cytotoxicity resulting from Tau aberrant aggregation, highlighting the chaperone property of PDI. Cysteine 59-67 microtubule associated protein tau Homo sapiens 256-259 30315761-5 2019 This study demonstrates that labeling a single-cysteine form of the pro-aggregant tau four-repeat region (K18) with either Alexa Fluor 488-C5-maleimide or N-ethylmaleimide in reducing conditions stabilizes oligomers by impeding their further aggregation. Cysteine 47-55 microtubule associated protein tau Homo sapiens 82-85 30218010-4 2018 Using maleimide-functionalized labels grafted on the two natural cysteine residues of Tau, we found in both cases that Tau remains highly flexible in these regions confirming the fuzziness of Tau:MTs complexes. Cysteine 65-73 microtubule associated protein tau Homo sapiens 86-89 30218010-4 2018 Using maleimide-functionalized labels grafted on the two natural cysteine residues of Tau, we found in both cases that Tau remains highly flexible in these regions confirming the fuzziness of Tau:MTs complexes. Cysteine 65-73 microtubule associated protein tau Homo sapiens 119-122 30218010-4 2018 Using maleimide-functionalized labels grafted on the two natural cysteine residues of Tau, we found in both cases that Tau remains highly flexible in these regions confirming the fuzziness of Tau:MTs complexes. Cysteine 65-73 microtubule associated protein tau Homo sapiens 119-122 30853336-1 2019 BACKGROUND: Aggregation of tau into paired helical filament (PHF) is a hallmark of Alzheimer"s disease (AD), and Cys-mediated disulfide bond formation plays a vital role in tau fibrillation. Cysteine 113-116 microtubule associated protein tau Homo sapiens 27-30 30853336-1 2019 BACKGROUND: Aggregation of tau into paired helical filament (PHF) is a hallmark of Alzheimer"s disease (AD), and Cys-mediated disulfide bond formation plays a vital role in tau fibrillation. Cysteine 113-116 microtubule associated protein tau Homo sapiens 173-176 30853336-2 2019 While intermolecular disulfide bond between Cys residues in microtubule-binding repeat (MTBR) region facilitates tau aggregation, intramolecular disulfide bond attenuates the same, though the molecular basis for such phenomenon remains obscure. Cysteine 44-47 microtubule associated protein tau Homo sapiens 113-116 29714059-3 2018 Here we uncover a critical role of the free thiol at Cys-322 in determining tau stability. Cysteine 53-56 microtubule associated protein tau Homo sapiens 76-79 29714059-5 2018 Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322. Cysteine 147-150 microtubule associated protein tau Homo sapiens 29-32 29714059-5 2018 Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322. Cysteine 147-150 microtubule associated protein tau Homo sapiens 88-91 29714059-5 2018 Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322. Cysteine 147-150 microtubule associated protein tau Homo sapiens 88-91 29714059-5 2018 Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322. Cysteine 162-165 microtubule associated protein tau Homo sapiens 29-32 29714059-5 2018 Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322. Cysteine 162-165 microtubule associated protein tau Homo sapiens 88-91 29714059-5 2018 Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322. Cysteine 162-165 microtubule associated protein tau Homo sapiens 88-91 26671725-0 2015 Toxic tau oligomer formation blocked by capping of cysteine residues with 1,2-dihydroxybenzene groups. Cysteine 51-59 microtubule associated protein tau Homo sapiens 6-9 27890528-7 2017 The results from isothermal titration calorimetry show that Zn2+ binds to full-length human Tau by interacting with Cys-291 and Cys-322, forming a 1:1 Zn2+-Tau complex. Cysteine 116-119 microtubule associated protein tau Homo sapiens 92-95 27890528-7 2017 The results from isothermal titration calorimetry show that Zn2+ binds to full-length human Tau by interacting with Cys-291 and Cys-322, forming a 1:1 Zn2+-Tau complex. Cysteine 116-119 microtubule associated protein tau Homo sapiens 156-159 27890528-7 2017 The results from isothermal titration calorimetry show that Zn2+ binds to full-length human Tau by interacting with Cys-291 and Cys-322, forming a 1:1 Zn2+-Tau complex. Cysteine 128-131 microtubule associated protein tau Homo sapiens 92-95 27890528-7 2017 The results from isothermal titration calorimetry show that Zn2+ binds to full-length human Tau by interacting with Cys-291 and Cys-322, forming a 1:1 Zn2+-Tau complex. Cysteine 128-131 microtubule associated protein tau Homo sapiens 156-159 27601475-10 2016 NO-linked chemical modification on cysteine residues of tau could block tau aggregation, and therefore, increasing 8-nitro-cGMP levels in the brain could become a potential therapeutic strategy for Alzheimer"s disease. Cysteine 35-43 microtubule associated protein tau Homo sapiens 56-59 27601475-10 2016 NO-linked chemical modification on cysteine residues of tau could block tau aggregation, and therefore, increasing 8-nitro-cGMP levels in the brain could become a potential therapeutic strategy for Alzheimer"s disease. Cysteine 35-43 microtubule associated protein tau Homo sapiens 72-75 27601475-2 2016 Tau contains one or two cysteine residues in three or four repeats of the microtubule binding region following alternative splicing of exon 10, and formation of intermolecular cysteine disulfide bonds accelerates tau aggregation. Cysteine 24-32 microtubule associated protein tau Homo sapiens 0-3 27601475-2 2016 Tau contains one or two cysteine residues in three or four repeats of the microtubule binding region following alternative splicing of exon 10, and formation of intermolecular cysteine disulfide bonds accelerates tau aggregation. Cysteine 24-32 microtubule associated protein tau Homo sapiens 213-216 26671725-4 2015 Specifically, we demonstrate that 1,2-dihydroxybenzene-containing compounds bind to and cap cysteine residues of tau and prevent its aggregation by hindering interactions between tau molecules. Cysteine 92-100 microtubule associated protein tau Homo sapiens 113-116 26671725-4 2015 Specifically, we demonstrate that 1,2-dihydroxybenzene-containing compounds bind to and cap cysteine residues of tau and prevent its aggregation by hindering interactions between tau molecules. Cysteine 92-100 microtubule associated protein tau Homo sapiens 179-182 26671725-6 2015 Thus, compounds that target the cysteine residues of tau may prove useful in halting the progression of Alzheimer"s disease and other tauopathies. Cysteine 32-40 microtubule associated protein tau Homo sapiens 53-56 23443659-0 2013 Aminothienopyridazines and methylene blue affect Tau fibrillization via cysteine oxidation. Cysteine 72-80 microtubule associated protein tau Homo sapiens 49-52 25066125-3 2014 Elimination of zinc binding through amino acid substitution of Cys residues has a minimal effect on phosphorylation levels yet essentially eliminates Tau toxicity. Cysteine 63-66 microtubule associated protein tau Homo sapiens 150-153 25066125-5 2014 Importantly, restoration of zinc-binding ability to Tau(*) by introduction of a zinc-binding residue (His) into the original Cys positions restores zinc-responsive toxicities in proportion to zinc-binding affinities. Cysteine 125-128 microtubule associated protein tau Homo sapiens 52-55 23443659-7 2013 Active ATPZs were found to promote the oxidation of the two cysteine residues within 4-R Tau by a redox cycling mechanism, resulting in the formation of a disulfide-containing compact monomer that was refractory to fibrillization. Cysteine 60-68 microtubule associated protein tau Homo sapiens 89-92 23443659-10 2013 Interestingly, methylene blue, an inhibitor of Tau fibrillization under evaluation in Alzheimer disease clinical trials, caused a similar oxidation of cysteines in Tau and other molecules. Cysteine 151-160 microtubule associated protein tau Homo sapiens 164-167 19826005-0 2009 Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322. Cysteine 80-83 microtubule associated protein tau Homo sapiens 60-63 19826005-0 2009 Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322. Cysteine 92-95 microtubule associated protein tau Homo sapiens 60-63 19826005-9 2009 The results from isothermal titration calorimetry show that one Zn(2+) binds to one Tau molecule via tetrahedral coordination to Cys-291 and Cys-322 as well as two histidines, with moderate, micromolar affinity. Cysteine 129-132 microtubule associated protein tau Homo sapiens 84-87 19826005-9 2009 The results from isothermal titration calorimetry show that one Zn(2+) binds to one Tau molecule via tetrahedral coordination to Cys-291 and Cys-322 as well as two histidines, with moderate, micromolar affinity. Cysteine 141-144 microtubule associated protein tau Homo sapiens 84-87 19826005-10 2009 Our data demonstrate that low micromolar zinc accelerates the fibrillization of human Tau protein via bridging Cys-291 and Cys-322 in physiological reducing conditions, providing clues to understanding the relationship between zinc dyshomeostasis and the etiology of neurodegenerative diseases. Cysteine 111-114 microtubule associated protein tau Homo sapiens 86-89 19826005-10 2009 Our data demonstrate that low micromolar zinc accelerates the fibrillization of human Tau protein via bridging Cys-291 and Cys-322 in physiological reducing conditions, providing clues to understanding the relationship between zinc dyshomeostasis and the etiology of neurodegenerative diseases. Cysteine 123-126 microtubule associated protein tau Homo sapiens 86-89 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 71-74 microtubule associated protein tau Homo sapiens 102-105 11437366-0 2001 Role of cysteine-291 and cysteine-322 in the polymerization of human tau into Alzheimer-like filaments. Cysteine 8-16 microtubule associated protein tau Homo sapiens 69-72 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 71-74 microtubule associated protein tau Homo sapiens 227-230 11437366-0 2001 Role of cysteine-291 and cysteine-322 in the polymerization of human tau into Alzheimer-like filaments. Cysteine 25-33 microtubule associated protein tau Homo sapiens 69-72 11437366-2 2001 Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments. Cysteine 97-100 microtubule associated protein tau Homo sapiens 76-79 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 83-86 microtubule associated protein tau Homo sapiens 102-105 11437366-2 2001 Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments. Cysteine 97-100 microtubule associated protein tau Homo sapiens 76-79 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 83-86 microtubule associated protein tau Homo sapiens 227-230 11437366-2 2001 Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments. Cysteine 97-100 microtubule associated protein tau Homo sapiens 76-79 11437366-2 2001 Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments. Cysteine 140-143 microtubule associated protein tau Homo sapiens 38-41 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 83-86 microtubule associated protein tau Homo sapiens 102-105 11437366-2 2001 Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments. Cysteine 140-143 microtubule associated protein tau Homo sapiens 76-79 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 83-86 microtubule associated protein tau Homo sapiens 227-230 11437366-2 2001 Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments. Cysteine 140-143 microtubule associated protein tau Homo sapiens 76-79 11437366-2 2001 Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments. Cysteine 140-143 microtubule associated protein tau Homo sapiens 76-79 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 83-86 microtubule associated protein tau Homo sapiens 102-105 11437366-3 2001 We report heparin-dependent in vitro polymerization of human recombinant tau (1-383 isoform), containing both Cys-291 and Cys-322, into paired helical filaments as characterized by electron microscopy. Cysteine 110-113 microtubule associated protein tau Homo sapiens 73-76 11437366-8 2001 Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization. Cysteine 83-86 microtubule associated protein tau Homo sapiens 227-230 11437366-3 2001 We report heparin-dependent in vitro polymerization of human recombinant tau (1-383 isoform), containing both Cys-291 and Cys-322, into paired helical filaments as characterized by electron microscopy. Cysteine 122-125 microtubule associated protein tau Homo sapiens 73-76 11087369-5 2000 Using sulfhydryl protective agents and site-directed mutagenesis, we found that cysteine-dependent oxidation of the tau molecule is not required for its polymerization and may even be inhibitory. Cysteine 80-88 microtubule associated protein tau Homo sapiens 116-119 9273897-3 1997 tau contains two cysteine residues in repeat units 2 and 3, but only the R3-R3 homodimer is present in PHF-tau. Cysteine 17-25 microtubule associated protein tau Homo sapiens 0-3 9273897-4 1997 A serine residue two amino acids downstream of the R3 cysteine is a major phosphate acceptor site for protein kinase C. In the work repeated here, we used synthetic peptides corresponding to R2, R3 and phosphorylated R3 to determine the binding of the tau repeat peptides to a peptide fragment corresponding to the C-terminal domain of beta-tubulin and to study the kinetics of homo- and heterodimer formation. Cysteine 54-62 microtubule associated protein tau Homo sapiens 252-255