PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35165396-7 2022 Pharmacologically augmenting Bdnf transport by chronic lithium administration, partly via phosphorylation of Huntingtin (Htt) serine-421 and its integration into the motor machinery, restored striatal Bdnf levels and rescued PPI deficits in Disc1-LI mice. Serine 126-132 huntingtin Mus musculus 109-119 14522959-4 2003 Elevated levels of activated Ser(P)473-Akt are detected in extracts of Hdh(Q111/Q111) striatum and cultured mutant STHdh(Q111/Q111) striatal cells, compared with their wild type counterparts. Serine 29-32 huntingtin Mus musculus 71-74 35165396-7 2022 Pharmacologically augmenting Bdnf transport by chronic lithium administration, partly via phosphorylation of Huntingtin (Htt) serine-421 and its integration into the motor machinery, restored striatal Bdnf levels and rescued PPI deficits in Disc1-LI mice. Serine 126-132 huntingtin Mus musculus 121-124 32242231-8 2020 Phosphorylation defective mutation of Serine at amino acid 120 (S120) abolishes the mHTT-lowering effect of NLK, suggesting that S120 phosphorylation is an important step in the NLK-mediated lowering of mHTT. Serine 38-44 huntingtin Mus musculus 84-88 32941796-2 2021 The impact of phosphorylating serine 13/16 of mutant HTT (mHTT) on HD has been documented in cell culture and murine models. Serine 30-36 huntingtin Mus musculus 53-56 32941796-2 2021 The impact of phosphorylating serine 13/16 of mutant HTT (mHTT) on HD has been documented in cell culture and murine models. Serine 30-36 huntingtin Mus musculus 58-62 32978366-2 2020 Phosphorylation at serine-421 (pS421) of mHTT has been shown to be neuroprotective in cellular and rodent models. Serine 19-25 huntingtin Mus musculus 41-45 32242231-8 2020 Phosphorylation defective mutation of Serine at amino acid 120 (S120) abolishes the mHTT-lowering effect of NLK, suggesting that S120 phosphorylation is an important step in the NLK-mediated lowering of mHTT. Serine 38-44 huntingtin Mus musculus 203-207 25038828-4 2014 Finally, alterations in serine/arginine-rich splicing factor-6 coincide with tau missplicing, and a role of tau in HD pathogenesis is evidenced by the attenuation of motor abnormalities of mutant HTT transgenic mice in tau knockout backgrounds. Serine 24-30 huntingtin Mus musculus 196-199 25057205-5 2014 The serine/threonine kinase Akt, which regulates HTT function, rescued the spindle misorientation caused by the mHTT, by serine 421 (S421) phosphorylation, in cultured cells and in mice. Serine 4-10 huntingtin Mus musculus 49-52 31088970-4 2019 In cell culture, IKKbeta phosphorylates HTT serine (S) 13 and activates HTT degradation, a process that becomes impaired with polyQ expansion. Serine 44-50 huntingtin Mus musculus 40-43 31088970-4 2019 In cell culture, IKKbeta phosphorylates HTT serine (S) 13 and activates HTT degradation, a process that becomes impaired with polyQ expansion. Serine 52-53 huntingtin Mus musculus 40-43 27466181-2 2016 In Huntington"s disease (HD), mutant huntingtin is hypo-phosphorylated at serines 13 and 16 within N17, and increasing N17 phosphorylation has been shown to be protective in HD mouse models. Serine 74-81 huntingtin Mus musculus 37-47 27525439-0 2016 Serine 421 regulates mutant huntingtin toxicity and clearance in mice. Serine 0-6 huntingtin Mus musculus 28-38 27525439-3 2016 HTT has a highly conserved Akt phosphorylation site at serine 421, and prior work in HD models found that phosphorylation at S421 (S421-P) diminishes the toxicity of mutant HTT (mHTT) fragments in neuronal cultures. Serine 55-61 huntingtin Mus musculus 0-3 27525439-3 2016 HTT has a highly conserved Akt phosphorylation site at serine 421, and prior work in HD models found that phosphorylation at S421 (S421-P) diminishes the toxicity of mutant HTT (mHTT) fragments in neuronal cultures. Serine 55-61 huntingtin Mus musculus 173-176 24951540-6 2014 We also observed that the serine-threonine kinase IRE1 involved in endoplasmic reticulum (ER) stress responses is activated in mutant Htt-expressing cells in culture as well as in the striatum of mutant Htt transgenic (BACHD) mice. Serine 26-32 huntingtin Mus musculus 134-137 24951540-6 2014 We also observed that the serine-threonine kinase IRE1 involved in endoplasmic reticulum (ER) stress responses is activated in mutant Htt-expressing cells in culture as well as in the striatum of mutant Htt transgenic (BACHD) mice. Serine 26-32 huntingtin Mus musculus 203-206 22999956-0 2012 Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties. Serine 0-6 huntingtin Mus musculus 34-44 24301680-5 2014 The beneficial effect of FTY720 administration was associated with a significant strengthening of neuronal activity and connectivity and, with reduction of mutant huntingtin aggregates, and it was also paralleled by increased phosphorylation of mutant huntingtin at serine 13/16 residues that are predicted to attenuate protein toxicity. Serine 266-272 huntingtin Mus musculus 252-262 23678106-2 2013 Here, we demonstrate that wild-type huntingtin, the protein mutated in HD, modulates anxiety/depression-related behaviors according to its phosphorylation at serines 1181 and 1201. Serine 158-165 huntingtin Mus musculus 36-46 23409115-6 2013 Its binding to Htt is regulated by the rho-associated kinase (ROCK), which phosphorylates profilin at Ser-137. Serine 102-105 huntingtin Mus musculus 15-18 22999956-8 2012 First, these negatively charged Ser replacements impair the assembly of the alpha-helical oligomers that play a critical role in htt amyloid nucleation, thus providing an explanation for reduced amyloid formation rates. Serine 32-35 huntingtin Mus musculus 129-132 22623107-7 2012 In addition, prevention of phosphorylation at the two serine sites altered mHtt toxicity and accumulation. Serine 54-60 huntingtin Mus musculus 75-79 21623356-1 2011 Two serine residues within the first 17 amino acid residues of huntingtin (N17) are crucial for modulation of mutant huntingtin toxicity in cell and mouse genetic models of Huntington"s disease. Serine 4-10 huntingtin Mus musculus 63-73 21623356-1 2011 Two serine residues within the first 17 amino acid residues of huntingtin (N17) are crucial for modulation of mutant huntingtin toxicity in cell and mouse genetic models of Huntington"s disease. Serine 4-10 huntingtin Mus musculus 117-127 17352936-8 2007 Selective phosphorylation of mutant htt on serine 421 may also contribute, as phosphorylation of mutant htt reduces its toxicity and is decreased in the striatum compared to other regions of the brain. Serine 43-49 huntingtin Mus musculus 36-39 21245084-4 2011 Here, we report that serine 16 (S16) in htt is important for the generation of small N-terminal fragments that are able to accumulate in the nucleus and form aggregates. Serine 21-27 huntingtin Mus musculus 40-43 20064390-1 2009 The N-terminal 17 amino acids of huntingtin (NT17) can be phosphorylated on serines 13 and 16; however, the significance of these modifications in Huntington"s disease pathogenesis remains unknown. Serine 76-83 huntingtin Mus musculus 33-43 20064390-2 2009 In this study, we developed BAC transgenic mice expressing full-length mutant huntingtin (fl-mhtt) with serines 13 and 16 mutated to either aspartate (phosphomimetic or SD) or alanine (phosphoresistant or SA). Serine 104-111 huntingtin Mus musculus 78-88 20064390-5 2009 Moreover, modification of these serines in expanded repeat huntingtin peptides modulates aggregation and amyloid fibril formation in vitro. Serine 32-39 huntingtin Mus musculus 59-69 17352936-8 2007 Selective phosphorylation of mutant htt on serine 421 may also contribute, as phosphorylation of mutant htt reduces its toxicity and is decreased in the striatum compared to other regions of the brain. Serine 43-49 huntingtin Mus musculus 104-107 15843398-0 2005 Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo. Serine 30-36 huntingtin Mus musculus 0-10 15843398-3 2005 Huntingtin is phosphorylated on serine-421 (S421) by the pro-survival signaling protein kinase Akt (PKB) and this has been previously shown to be protective against the toxicity of polyglutamine-expanded htt in cell culture. Serine 32-38 huntingtin Mus musculus 0-10 15843398-3 2005 Huntingtin is phosphorylated on serine-421 (S421) by the pro-survival signaling protein kinase Akt (PKB) and this has been previously shown to be protective against the toxicity of polyglutamine-expanded htt in cell culture. Serine 32-38 huntingtin Mus musculus 204-207