PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29782321-6 2018 Importantly, although Pyk2 interacts with the established tyrosine-directed tau kinase Fyn, we identified an increased Pyk2 activity in mice which constitutively overexpress Fyn (FynCA), and a decreased activity in mice lacking Fyn (FynKO). Tyrosine 58-66 microtubule associated protein tau Homo sapiens 76-79 31689387-8 2019 Immunochemical analysis revealed that tau gene transfer significantly resulted in loss of tyrosine hydroxylase-positive dopaminergic neurons and elevated phosphorylated tau in the substantia nigra. Tyrosine 90-98 microtubule associated protein tau Homo sapiens 38-41 31234228-10 2019 The rare H1j haplotype (1.3%) was significantly associated with a lower dorsolateral putaminal tyrosine hydroxylase immunoreactivity (and therefore greater dopaminergic degeneration) compared to other microtubule-associated protein tau haplotypes (P = 0.0016). Tyrosine 95-103 microtubule associated protein tau Homo sapiens 232-235 22892311-0 2013 Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation through Src dependent PP2A (tyrosine 307) phosphorylation. Tyrosine 106-114 microtubule associated protein tau Homo sapiens 53-56 27989667-3 2017 At least 50 phosphorylation sites involving Ser, Thr and Tyr residues have been identified or proposed in hTau and a selected number of them have been implicated in hTau aggregation following latter"s proteolytic truncation. Tyrosine 57-60 microtubule associated protein tau Homo sapiens 106-110 27520374-10 2016 The phosphorylation level of tau at Tyr 18 was decreased in the si-Fyn group compared with the negative control group, but the inhibitory effect of si-Fyn on tau phosphorylation was attenuated when miR-106b expression was inhibited. Tyrosine 36-39 microtubule associated protein tau Homo sapiens 29-32 24395787-9 2014 These findings suggest a scenario in which BMAA can lead to tau pathology by inhibiting PP2A through the activation of mGluR5, the consequent release of PP2Ac from the mGluR5-PP2A complex, and its phosphorylation at Tyr(307) by Src. Tyrosine 216-219 microtubule associated protein tau Homo sapiens 60-63 23294633-0 2013 Active glycogen synthase kinase-3 and tau pathology-related tyrosine phosphorylation in pR5 human tau transgenic mice. Tyrosine 60-68 microtubule associated protein tau Homo sapiens 38-41 23294633-0 2013 Active glycogen synthase kinase-3 and tau pathology-related tyrosine phosphorylation in pR5 human tau transgenic mice. Tyrosine 60-68 microtubule associated protein tau Homo sapiens 98-101 23294633-7 2013 Our results suggest a link between increased tyrosine phosphorylation and tau aggregation. Tyrosine 45-53 microtubule associated protein tau Homo sapiens 74-77 23294633-8 2013 They also reveal for the mouse models studied, that tau- rather than an amyloid-beta peptide-induced pathology is associated with increased neuronal tyrosine phosphorylation. Tyrosine 149-157 microtubule associated protein tau Homo sapiens 52-55 28919467-1 2017 PURPOSE: Spleen tyrosine kinase (Syk) has been shown to phosphorylate tyrosine 18 of tau in vitro. Tyrosine 16-24 microtubule associated protein tau Homo sapiens 85-88 28919467-3 2017 To investigate this possibility we have studied Syk and tau phosphorylated at tyrosine 18 (pTyr18) in transgenic mice and human hippocampi. Tyrosine 78-86 microtubule associated protein tau Homo sapiens 56-59 28919467-10 2017 It possibly phosphorylates tyrosine 18 of tau and regulates other tau kinases in neurons with a fibrillary tau pathology. Tyrosine 27-35 microtubule associated protein tau Homo sapiens 42-45 26111662-6 2015 The downregulation of PTPalpha results in the abnormal tyrosine hyperphosphorylation of glycogen synthase kinase-3beta (resulting in activation) and protein phosphatase 2A (resulting in inactivation), the major tau kinase and phosphatase. Tyrosine 55-63 microtubule associated protein tau Homo sapiens 211-214 21794954-4 2012 Here, we show that phosphorylation of tau at tyrosine 18, which is a fyn phosphorylation site within PAD, prevents inhibition of anterograde FAT induced by both filamentous tau and 6D tau. Tyrosine 45-53 microtubule associated protein tau Homo sapiens 38-41 22710920-1 2013 Microtubule associated protein tau is a phosphoprotein which potentially has 80 serine/threonine and 5 tyrosine phosphorylation sites. Tyrosine 103-111 microtubule associated protein tau Homo sapiens 0-34 21794954-4 2012 Here, we show that phosphorylation of tau at tyrosine 18, which is a fyn phosphorylation site within PAD, prevents inhibition of anterograde FAT induced by both filamentous tau and 6D tau. Tyrosine 45-53 microtubule associated protein tau Homo sapiens 173-176 21794954-5 2012 Moreover, Fyn-mediated phosphorylation of tyrosine 18 is reduced in disease-associated forms of tau (e.g., tau filaments). Tyrosine 42-50 microtubule associated protein tau Homo sapiens 96-99 21794954-5 2012 Moreover, Fyn-mediated phosphorylation of tyrosine 18 is reduced in disease-associated forms of tau (e.g., tau filaments). Tyrosine 42-50 microtubule associated protein tau Homo sapiens 107-110 21514440-0 2011 Tyrosine nitration within the proline-rich region of Tau in Alzheimer"s disease. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 53-56 21514440-2 2011 Previously, we showed in vitro that within the tau protein the N-terminal tyrosine residues (Y18 and Y29) are more susceptible to nitrative modifications than other tyrosine sites (Y197 and Y394). Tyrosine 74-82 microtubule associated protein tau Homo sapiens 47-50 21514440-2 2011 Previously, we showed in vitro that within the tau protein the N-terminal tyrosine residues (Y18 and Y29) are more susceptible to nitrative modifications than other tyrosine sites (Y197 and Y394). Tyrosine 165-173 microtubule associated protein tau Homo sapiens 47-50 20609109-0 2010 Tyrosine phosphorylation of tau accompanies disease progression in transgenic mouse models of tauopathy. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 28-31 21799250-5 2011 Fyn also induces tyrosine phosphorylation of tau. Tyrosine 17-25 microtubule associated protein tau Homo sapiens 45-48 20609109-11 2010 CONCLUSIONS: Our results provide evidence for the association of tyrosine-phosphorylated tau with mechanisms of neuropathogenesis and indicate that SFK activation and cell cycle activation are also involved in JNPL3. Tyrosine 65-73 microtubule associated protein tau Homo sapiens 89-92 19897570-5 2010 The present results indicate that a compound that interacts specifically with the Tyr residue or an antibody recognizing the region containing the Tyr residue becomes a candidate for inhibiting tau fibrillation. Tyrosine 82-85 microtubule associated protein tau Homo sapiens 194-197 20599975-4 2010 Levels of p-GSK-3beta phosphorylated at Tyr 216, which hyperphosphorylates Tau to produce toxic pathological forms of p-Tau, were higher in striata of both PD and PDD compared to controls, but were unaltered in IFG. Tyrosine 40-43 microtubule associated protein tau Homo sapiens 75-78 20599975-4 2010 Levels of p-GSK-3beta phosphorylated at Tyr 216, which hyperphosphorylates Tau to produce toxic pathological forms of p-Tau, were higher in striata of both PD and PDD compared to controls, but were unaltered in IFG. Tyrosine 40-43 microtubule associated protein tau Homo sapiens 120-123 19897570-5 2010 The present results indicate that a compound that interacts specifically with the Tyr residue or an antibody recognizing the region containing the Tyr residue becomes a candidate for inhibiting tau fibrillation. Tyrosine 147-150 microtubule associated protein tau Homo sapiens 194-197 16452634-4 2006 Using neuronal cells expressing the LPA(1) receptor, we show that LPA(1) mediates tyrosine phosphorylation and activation of GSK-3 with subsequent phosphorylation of the microtubule-associated protein tau via the G(i)-linked PIP(2) hydrolysis-Ca(2+) mobilization pathway. Tyrosine 82-90 microtubule associated protein tau Homo sapiens 170-204 20110609-4 2010 By contrast, full-length tau is secreted by a separate mechanism that is correlated with phosphorylation of tau at tyrosine 18 and dendritic degeneration, is exacerbated by tauopathy mutations, and blocked by mutations that inhibit tau:tau interactions. Tyrosine 115-123 microtubule associated protein tau Homo sapiens 25-28 20110609-4 2010 By contrast, full-length tau is secreted by a separate mechanism that is correlated with phosphorylation of tau at tyrosine 18 and dendritic degeneration, is exacerbated by tauopathy mutations, and blocked by mutations that inhibit tau:tau interactions. Tyrosine 115-123 microtubule associated protein tau Homo sapiens 108-111 20110609-4 2010 By contrast, full-length tau is secreted by a separate mechanism that is correlated with phosphorylation of tau at tyrosine 18 and dendritic degeneration, is exacerbated by tauopathy mutations, and blocked by mutations that inhibit tau:tau interactions. Tyrosine 115-123 microtubule associated protein tau Homo sapiens 108-111 20110609-4 2010 By contrast, full-length tau is secreted by a separate mechanism that is correlated with phosphorylation of tau at tyrosine 18 and dendritic degeneration, is exacerbated by tauopathy mutations, and blocked by mutations that inhibit tau:tau interactions. Tyrosine 115-123 microtubule associated protein tau Homo sapiens 108-111 20110615-0 2010 Tau phosphorylated at tyrosine 394 is found in Alzheimer"s disease tangles and can be a product of the Abl-related kinase, Arg. Tyrosine 22-30 microtubule associated protein tau Homo sapiens 0-3 20110615-4 2010 Recent reports state that tau can be phosphorylated at tyrosine residues by kinases including Fyn, Syk, and c-abl (Abl). Tyrosine 55-63 microtubule associated protein tau Homo sapiens 26-29 20110615-5 2010 Proteomic analyses show that tau phosphorylated at tyrosine 394 (Y394) exists within PHF samples taken from Alzheimer"s disease brains. Tyrosine 51-59 microtubule associated protein tau Homo sapiens 29-32 18562203-2 2008 While different post-translational modifications have been identified that accelerate tau aggregation, nitration at tyrosine residues prevents or slows tau filament formation in vitro. Tyrosine 116-124 microtubule associated protein tau Homo sapiens 152-155 18562203-5 2008 A clone, termed Tau-nY18, reacts specifically with tau proteins nitrated at Tyr 18 and fails to cross-react with other nitrated tyrosine residues spanning the length of the molecule or with other proteins known to be nitrated in neurodegenerative diseases. Tyrosine 76-79 microtubule associated protein tau Homo sapiens 16-19 18562203-5 2008 A clone, termed Tau-nY18, reacts specifically with tau proteins nitrated at Tyr 18 and fails to cross-react with other nitrated tyrosine residues spanning the length of the molecule or with other proteins known to be nitrated in neurodegenerative diseases. Tyrosine 76-79 microtubule associated protein tau Homo sapiens 51-54 18562203-5 2008 A clone, termed Tau-nY18, reacts specifically with tau proteins nitrated at Tyr 18 and fails to cross-react with other nitrated tyrosine residues spanning the length of the molecule or with other proteins known to be nitrated in neurodegenerative diseases. Tyrosine 128-136 microtubule associated protein tau Homo sapiens 16-19 19542604-0 2009 The microtubule-associated protein tau is also phosphorylated on tyrosine. Tyrosine 65-73 microtubule associated protein tau Homo sapiens 4-38 16533051-7 2006 These studies set the stage for future high-resolution structural characterization of these intermediates and the basis by which Tyr(310) may direct pathologic versus normal tau function. Tyrosine 129-132 microtubule associated protein tau Homo sapiens 174-177 16014719-0 2005 Tyrosine 394 is phosphorylated in Alzheimer"s paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 70-73 15913839-0 2005 Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Tyrosine 16-24 microtubule associated protein tau Homo sapiens 12-15 15913839-0 2005 Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Tyrosine 16-24 microtubule associated protein tau Homo sapiens 74-77 15913839-2 2005 It has been shown that aggregated tau is phosphorylated at serine, threonine, and tyrosine residues. Tyrosine 82-90 microtubule associated protein tau Homo sapiens 34-37 15913839-3 2005 However, the occurrence of tyrosine phosphorylation on tau proteins at different states of tau aggregation has not been shown. Tyrosine 27-35 microtubule associated protein tau Homo sapiens 55-58 15913839-3 2005 However, the occurrence of tyrosine phosphorylation on tau proteins at different states of tau aggregation has not been shown. Tyrosine 27-35 microtubule associated protein tau Homo sapiens 91-94 15913839-6 2005 Mass spectrometry analyses of immunopurified brain tau proteins from JNPL3 and Alzheimer"s disease affected individual uncovered novel tau tyrosine-phosphorylated sites. Tyrosine 139-147 microtubule associated protein tau Homo sapiens 51-54 15913839-6 2005 Mass spectrometry analyses of immunopurified brain tau proteins from JNPL3 and Alzheimer"s disease affected individual uncovered novel tau tyrosine-phosphorylated sites. Tyrosine 139-147 microtubule associated protein tau Homo sapiens 135-138 15913839-7 2005 Further studies demonstrated that the abundance of tyrosine-phosphorylated tau increases in an age-dependent manner in JNPL3 mice. Tyrosine 51-59 microtubule associated protein tau Homo sapiens 75-78 15913839-8 2005 Tyrosine-phosphorylated tau was detected in both soluble and sarkosyl-insoluble preparations derived from brain and spinal cord, and localized in neurons containing aggregated tau. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 24-27 15913839-8 2005 Tyrosine-phosphorylated tau was detected in both soluble and sarkosyl-insoluble preparations derived from brain and spinal cord, and localized in neurons containing aggregated tau. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 176-179 15913839-9 2005 The phosphorylation of tyrosine residues in tau appeared to occur along with that of serine and threonine residues and was not detectable in non-transgenic littermates and transgenic mice expressing 0N4R wild-type human tau. Tyrosine 23-31 microtubule associated protein tau Homo sapiens 44-47 15913839-9 2005 The phosphorylation of tyrosine residues in tau appeared to occur along with that of serine and threonine residues and was not detectable in non-transgenic littermates and transgenic mice expressing 0N4R wild-type human tau. Tyrosine 23-31 microtubule associated protein tau Homo sapiens 220-223 16014719-4 2005 Using mass spectrometry, we positively identified phosphorylated Tyr-394 in PHF-tau from an Alzheimer brain and in human fetal brain tau. Tyrosine 65-68 microtubule associated protein tau Homo sapiens 76-83 16014719-4 2005 Using mass spectrometry, we positively identified phosphorylated Tyr-394 in PHF-tau from an Alzheimer brain and in human fetal brain tau. Tyrosine 65-68 microtubule associated protein tau Homo sapiens 80-83 16014719-5 2005 When wild-type human tau was transfected into fibroblasts or neuroblastoma cells, treatment with pervanadate caused tau to become phosphorylated on tyrosine by endogenous kinases. Tyrosine 148-156 microtubule associated protein tau Homo sapiens 21-24 16014719-5 2005 When wild-type human tau was transfected into fibroblasts or neuroblastoma cells, treatment with pervanadate caused tau to become phosphorylated on tyrosine by endogenous kinases. Tyrosine 148-156 microtubule associated protein tau Homo sapiens 116-119 16014719-6 2005 By replacing each of the five tyrosines in tau with phenylalanine, we identified Tyr-394 as the major site of tyrosine phosphorylation in tau. Tyrosine 30-39 microtubule associated protein tau Homo sapiens 43-46 16014719-6 2005 By replacing each of the five tyrosines in tau with phenylalanine, we identified Tyr-394 as the major site of tyrosine phosphorylation in tau. Tyrosine 30-39 microtubule associated protein tau Homo sapiens 138-141 16014719-6 2005 By replacing each of the five tyrosines in tau with phenylalanine, we identified Tyr-394 as the major site of tyrosine phosphorylation in tau. Tyrosine 81-84 microtubule associated protein tau Homo sapiens 43-46 16014719-6 2005 By replacing each of the five tyrosines in tau with phenylalanine, we identified Tyr-394 as the major site of tyrosine phosphorylation in tau. Tyrosine 81-84 microtubule associated protein tau Homo sapiens 138-141 16014719-6 2005 By replacing each of the five tyrosines in tau with phenylalanine, we identified Tyr-394 as the major site of tyrosine phosphorylation in tau. Tyrosine 30-38 microtubule associated protein tau Homo sapiens 43-46 16014719-6 2005 By replacing each of the five tyrosines in tau with phenylalanine, we identified Tyr-394 as the major site of tyrosine phosphorylation in tau. Tyrosine 30-38 microtubule associated protein tau Homo sapiens 138-141 16014719-7 2005 Tyrosine phosphorylation of tau was inhibited by PP2 (4-amino-5-(4-chlorophenyl-7-(t-butyl)pyrazolo[3,4-d]pyrimidine), which is known to inhibit Src-family kinases and c-Abl. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 28-31 16014719-8 2005 Cotransfection of tau and kinases showed that Tyr-18 was the major site for Fyn phosphorylation, but Tyr-394 was the main residue for Abl. Tyrosine 46-49 microtubule associated protein tau Homo sapiens 18-21 16014719-8 2005 Cotransfection of tau and kinases showed that Tyr-18 was the major site for Fyn phosphorylation, but Tyr-394 was the main residue for Abl. Tyrosine 101-104 microtubule associated protein tau Homo sapiens 18-21 16014719-11 2005 These results show that phosphorylation of tau on Tyr-394 is a physiological event that is potentially part of a signal relay and suggest that Abl could have a pathogenic role in Alzheimer"s disease. Tyrosine 50-53 microtubule associated protein tau Homo sapiens 43-46 16014719-0 2005 Tyrosine 394 is phosphorylated in Alzheimer"s paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 87-90 15615649-3 2005 The subsequent finding that tau is tyrosine phosphorylated has led to the observation that tau in neurofibrillary tangles is tyrosine phosphorylated. Tyrosine 35-43 microtubule associated protein tau Homo sapiens 28-31 15683253-7 2005 Tyrosine (Tyr) residues are critical for ONOO(-)-mediated oligomerization, as tau proteins lacking all Tyr residues fail to generate oligomers upon ONOO- treatment. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 78-81 15683253-7 2005 Tyrosine (Tyr) residues are critical for ONOO(-)-mediated oligomerization, as tau proteins lacking all Tyr residues fail to generate oligomers upon ONOO- treatment. Tyrosine 0-3 microtubule associated protein tau Homo sapiens 78-81 15683253-7 2005 Tyrosine (Tyr) residues are critical for ONOO(-)-mediated oligomerization, as tau proteins lacking all Tyr residues fail to generate oligomers upon ONOO- treatment. Tyrosine 10-13 microtubule associated protein tau Homo sapiens 78-81 15615649-3 2005 The subsequent finding that tau is tyrosine phosphorylated has led to the observation that tau in neurofibrillary tangles is tyrosine phosphorylated. Tyrosine 35-43 microtubule associated protein tau Homo sapiens 91-94 15615649-3 2005 The subsequent finding that tau is tyrosine phosphorylated has led to the observation that tau in neurofibrillary tangles is tyrosine phosphorylated. Tyrosine 125-133 microtubule associated protein tau Homo sapiens 28-31 15615649-3 2005 The subsequent finding that tau is tyrosine phosphorylated has led to the observation that tau in neurofibrillary tangles is tyrosine phosphorylated. Tyrosine 125-133 microtubule associated protein tau Homo sapiens 91-94 14999081-2 2004 The discovery that tau could be phosphorylated on tyrosine and evidence that Abeta signal transduction involved tyrosine phosphorylation led us to question whether tyrosine phosphorylation of tau occurred during the neurodegenerative process. Tyrosine 50-58 microtubule associated protein tau Homo sapiens 19-22 14999081-6 2004 Moreover, immunocytochemical studies indicated that tyrosine phosphorylated tau was present in the neurofibrillary tangles in AD brain. Tyrosine 52-60 microtubule associated protein tau Homo sapiens 76-79 14999081-7 2004 However, the staining pattern excluded neuropil threads and dystrophic neurites indicating that tyrosine phosphorylated tau was distributed in AD brain in a manner dissimilar from other abnormally phosphorylated tau. Tyrosine 96-104 microtubule associated protein tau Homo sapiens 120-123 14660656-5 2004 In aged, dehydrated tau 2-19 gel, proline carbonyls lose their bonds to water and tyrosine becomes deprotonated, as demonstrated by UVRR spectroscopy. Tyrosine 82-90 microtubule associated protein tau Homo sapiens 20-23 7537044-0 1994 Tyrosine- versus serine-phosphorylation leads to conformational changes in a synthetic tau peptide. Tyrosine 0-8 microtubule associated protein tau Homo sapiens 87-90 7537044-3 1994 Here we describe the effect of serine- versus tyrosine-phosphorylation on the conformation of a synthetic tau peptide. Tyrosine 46-54 microtubule associated protein tau Homo sapiens 106-109 8388744-6 1993 Proline-directed kinases, whose activity is regulated by phosphorylation on tyrosine, may be responsible for abnormal tau phosphorylation. Tyrosine 76-84 microtubule associated protein tau Homo sapiens 118-121 34569575-2 2021 The peptides include the native fragment tau(9-16) (Ac-EVMEDHAG-NH2), and the Gln/Lys and Tyr/Ala mutated peptides (Ac-KGGYTMHK-NH2 and Ac-KGGATMHK-NH2) of tau(26-33). Tyrosine 90-93 microtubule associated protein tau Homo sapiens 156-159 32341125-3 2020 Very little is known about how phosphorylation of tyrosine residues influences the structure, aggregation, and microtubule- and lipid-binding properties of Tau. Tyrosine 50-58 microtubule associated protein tau Homo sapiens 156-159 32341125-0 2020 Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau. Tyrosine 34-42 microtubule associated protein tau Homo sapiens 134-137 32341125-4 2020 Here, we sought to determine the relative contributions of phosphorylation of one or several of the five tyrosine residues in Tau (Tyr-18, -29, -197, -310, and -394) to the regulation of its biophysical, aggregation, and functional properties. Tyrosine 105-113 microtubule associated protein tau Homo sapiens 126-129 32341125-4 2020 Here, we sought to determine the relative contributions of phosphorylation of one or several of the five tyrosine residues in Tau (Tyr-18, -29, -197, -310, and -394) to the regulation of its biophysical, aggregation, and functional properties. Tyrosine 131-134 microtubule associated protein tau Homo sapiens 126-129 32341125-5 2020 We used a combination of site-specific mutagenesis and in vitro phosphorylation by c-Abl kinase to generate Tau species phosphorylated at all five tyrosine residues, all tyrosine residues except Tyr-310 or Tyr-394 (pTau-Y310F and pTau-Y394F, respectively) and Tau phosphorylated only at Tyr-310 or Tyr-394 (4F/pTyr-310 or 4F/pTyr-394). Tyrosine 147-155 microtubule associated protein tau Homo sapiens 108-111 32341125-5 2020 We used a combination of site-specific mutagenesis and in vitro phosphorylation by c-Abl kinase to generate Tau species phosphorylated at all five tyrosine residues, all tyrosine residues except Tyr-310 or Tyr-394 (pTau-Y310F and pTau-Y394F, respectively) and Tau phosphorylated only at Tyr-310 or Tyr-394 (4F/pTyr-310 or 4F/pTyr-394). Tyrosine 170-178 microtubule associated protein tau Homo sapiens 108-111 32341125-5 2020 We used a combination of site-specific mutagenesis and in vitro phosphorylation by c-Abl kinase to generate Tau species phosphorylated at all five tyrosine residues, all tyrosine residues except Tyr-310 or Tyr-394 (pTau-Y310F and pTau-Y394F, respectively) and Tau phosphorylated only at Tyr-310 or Tyr-394 (4F/pTyr-310 or 4F/pTyr-394). Tyrosine 195-198 microtubule associated protein tau Homo sapiens 108-111 32341125-5 2020 We used a combination of site-specific mutagenesis and in vitro phosphorylation by c-Abl kinase to generate Tau species phosphorylated at all five tyrosine residues, all tyrosine residues except Tyr-310 or Tyr-394 (pTau-Y310F and pTau-Y394F, respectively) and Tau phosphorylated only at Tyr-310 or Tyr-394 (4F/pTyr-310 or 4F/pTyr-394). Tyrosine 206-209 microtubule associated protein tau Homo sapiens 108-111 32341125-5 2020 We used a combination of site-specific mutagenesis and in vitro phosphorylation by c-Abl kinase to generate Tau species phosphorylated at all five tyrosine residues, all tyrosine residues except Tyr-310 or Tyr-394 (pTau-Y310F and pTau-Y394F, respectively) and Tau phosphorylated only at Tyr-310 or Tyr-394 (4F/pTyr-310 or 4F/pTyr-394). Tyrosine 206-209 microtubule associated protein tau Homo sapiens 108-111 32341125-5 2020 We used a combination of site-specific mutagenesis and in vitro phosphorylation by c-Abl kinase to generate Tau species phosphorylated at all five tyrosine residues, all tyrosine residues except Tyr-310 or Tyr-394 (pTau-Y310F and pTau-Y394F, respectively) and Tau phosphorylated only at Tyr-310 or Tyr-394 (4F/pTyr-310 or 4F/pTyr-394). Tyrosine 206-209 microtubule associated protein tau Homo sapiens 108-111 32341125-8 2020 Our findings underscore Tyr-310 phosphorylation has a unique role in the regulation of Tau aggregation, microtubule, and lipid interactions. Tyrosine 24-27 microtubule associated protein tau Homo sapiens 87-90 32341125-9 2020 These results also highlight the importance of conducting further studies to elucidate the role of Tyr-310 in the regulation of Tau"s normal functions and pathogenic properties. Tyrosine 99-102 microtubule associated protein tau Homo sapiens 128-131