PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32575755-5 2020 To advance our understanding of the impact of ubiquitination on tau protein aggregation and function, we applied disulfide-coupling chemistry to modify tau protein at position 353 with Lys48- or Lys63-linked di-ubiquitin, two representative polyubiquitin chains that differ in topology and structure. Disulfides 113-122 microtubule associated protein tau Homo sapiens 152-155 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. Disulfides 126-135 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. Disulfides 126-135 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. Disulfides 21-30 microtubule associated protein tau Homo sapiens 113-116 30853336-3 2019 Thus intramolecular disulfide-bonded tau monomer might be an excellent model to understand the unique features of aggregation-resistant tau conformer. Disulfides 20-29 microtubule associated protein tau Homo sapiens 37-40 30853336-3 2019 Thus intramolecular disulfide-bonded tau monomer might be an excellent model to understand the unique features of aggregation-resistant tau conformer. Disulfides 20-29 microtubule associated protein tau Homo sapiens 136-139 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. Disulfides 116-125 microtubule associated protein tau Homo sapiens 29-32 30218010-0 2018 Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges. Disulfides 51-60 microtubule associated protein tau Homo sapiens 4-7 30218010-5 2018 More interestingly, using labels linked by a disulfide bridge, we evidenced for the first time thiol disulfide exchanges between alphabeta-tubulin or MTs and Tau. Disulfides 45-54 microtubule associated protein tau Homo sapiens 158-161 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. Disulfides 116-125 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. Disulfides 116-125 microtubule associated protein tau Homo sapiens 88-91 15341514-0 2004 Molecular aging of tau: disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo. Disulfides 24-33 microtubule associated protein tau Homo sapiens 19-22 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. Disulfides 155-164 microtubule associated protein tau Homo sapiens 89-92 23443659-8 2013 Moreover, the ATPZs facilitated intermolecular disulfide formation between 3-R Tau monomers, leading to dimers that were capable of fibrillization. Disulfides 47-56 microtubule associated protein tau Homo sapiens 79-82 22249117-6 2012 Moreover, further NO treatment induced the formation of SDS-stable insoluble tau mega-aggregates that were composed of dephosphorylated full-length tau molecules and other proteins, and were stabilized through disulfide bonds. Disulfides 210-219 microtubule associated protein tau Homo sapiens 77-80 16104002-3 2005 This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly. Disulfides 314-323 microtubule associated protein tau Homo sapiens 132-135 16104002-3 2005 This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly. Disulfides 314-323 microtubule associated protein tau Homo sapiens 261-264 16104002-3 2005 This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly. Disulfides 314-323 microtubule associated protein tau Homo sapiens 261-264 16104002-3 2005 This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly. Disulfides 314-323 microtubule associated protein tau Homo sapiens 261-264 34339733-10 2021 Surprisingly, fibrils composed of compact tau disaggregate upon reduction, highlighting the importance of the intramolecular disulfide bond for fibril stability. Disulfides 125-134 microtubule associated protein tau Homo sapiens 42-45 8985176-4 1996 The RNA-induced assembly of PHFs is dependent on the formation of intermolecular disulfide bridges involving Cys322 in the third repeat of tau, and it includes the dimerization of tau as an early intermediate. Disulfides 81-90 microtubule associated protein tau Homo sapiens 139-142 34339733-4 2021 Four-repeat tau contains two cysteines that can form an intramolecular disulfide bond, resulting in a structurally restrained compact monomer. Disulfides 71-80 microtubule associated protein tau Homo sapiens 12-15 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. Disulfides 129-138 microtubule associated protein tau Homo sapiens 102-105 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. Disulfides 129-138 microtubule associated protein tau Homo sapiens 227-230 9665729-4 1998 Disulfide-linked dimers of tau constructs representing the repeat domain assemble into PHFs most efficiently, but other tau isoforms or constructs form bona fide PHFs as well. Disulfides 0-9 microtubule associated protein tau Homo sapiens 27-30 34656563-2 2021 In a recent issue, Weismiller et al showed that intramolecular disulfide links between cys291 and cys322 for a specific tau isoform containing 4 microtubule-binding repeats direct the formation of a structurally distinct amyloid polymorph. Disulfides 63-72 microtubule associated protein tau Homo sapiens 120-123 2833758-8 1988 If similar material is boiled in 2% NaDodSO4 in the absence of a sulfhydryl reducing agent, the tau immunoreactivity is removed less efficiently, suggesting that tau epitopes are bound to the ubiquitin reactive material in a manner partially dependent on covalent disulfide bridges. Disulfides 264-273 microtubule associated protein tau Homo sapiens 162-165