PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35169703-4 2022 The polyQ mutation at the N-terminus of the huntingtin protein alters its natural interactions with neural phospholipids in vitro, suggesting that the specific lipid composition of brain regions could influence their vulnerability to interference by mutant huntingtin; however, this has not yet been demonstrated in vivo. Phospholipids 107-120 huntingtin Homo sapiens 44-54 16085648-0 2005 Huntingtin associates with acidic phospholipids at the plasma membrane. Phospholipids 34-47 huntingtin Homo sapiens 0-10 16085648-6 2005 Our data support a new model in which huntingtin directly binds membranes through electrostatic interactions with acidic phospholipids. Phospholipids 121-134 huntingtin Homo sapiens 38-48 35631226-3 2022 HTT interacts with phospholipids in vitro; however, its interactions are changed when the protein is mutated in HD. Phospholipids 19-32 huntingtin Homo sapiens 0-3 35439000-4 2022 Here, the impact of unsaturation in phospholipid tails on htt-lipid interaction and htt aggregation was determined. Phospholipids 36-48 huntingtin Homo sapiens 58-61 35439000-4 2022 Here, the impact of unsaturation in phospholipid tails on htt-lipid interaction and htt aggregation was determined. Phospholipids 36-48 huntingtin Homo sapiens 84-87 35169703-4 2022 The polyQ mutation at the N-terminus of the huntingtin protein alters its natural interactions with neural phospholipids in vitro, suggesting that the specific lipid composition of brain regions could influence their vulnerability to interference by mutant huntingtin; however, this has not yet been demonstrated in vivo. Phospholipids 107-120 huntingtin Homo sapiens 257-267 30594931-1 2019 BACKGROUND: Previous studies suggest that Huntingtin, the protein mutated in Huntington"s disease (HD), is required for actin based changes in cell morphology, and undergoes stimulus induced targeting to plasma membranes where it interacts with phospholipids involved in cell signaling. Phospholipids 245-258 huntingtin Homo sapiens 42-52 29335600-4 2018 Yet, little is known about how mutant huntingtin may affect phospholipids membrane fluidity. Phospholipids 60-73 huntingtin Homo sapiens 38-48 24415136-0 2014 Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations. Phospholipids 70-82 huntingtin Homo sapiens 24-34 24415136-2 2014 As with other amyloid proteins, misfolding of huntingtin is related to Huntington"s disease through pathways that can involve interactions with phospholipid membranes. Phospholipids 144-156 huntingtin Homo sapiens 46-56 26958885-11 2016 Our characterization of Huntingtin"s amino-terminus provides insights into the structural origin of its ability to oligomerize and interact with phospholipid bilayers, processes closely linked to the biological functions of this protein. Phospholipids 145-157 huntingtin Homo sapiens 24-34 25762330-0 2015 Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulations. Phospholipids 49-61 huntingtin Homo sapiens 12-22 25062673-0 2013 Huntingtin interactions with membrane phospholipids: strategic targets for therapeutic intervention? Phospholipids 38-51 huntingtin Homo sapiens 0-10 25062673-4 2013 Recent investigations prove that Htt associates with membranes by direct interactions with phospholipids in membranes. Phospholipids 91-104 huntingtin Homo sapiens 33-36 25062673-6 2013 Htt has a particular affinity for a specific class of phospholipids called phosphatidylinositol phosphates; individual species of these phospholipids propagate signals promoting cell survival and regulating changes in morphology. Phospholipids 54-67 huntingtin Homo sapiens 0-3 25062673-6 2013 Htt has a particular affinity for a specific class of phospholipids called phosphatidylinositol phosphates; individual species of these phospholipids propagate signals promoting cell survival and regulating changes in morphology. Phospholipids 136-149 huntingtin Homo sapiens 0-3 25062673-7 2013 Mutant Htt fragments can disrupt synthetic phospholipid bilayers and full-length mutant Htt shows increased binding to numerous phospholipids, supporting the idea that mutant Htt can introduce pathology at the level of phospholipid interactions. Phospholipids 43-55 huntingtin Homo sapiens 7-10 25062673-7 2013 Mutant Htt fragments can disrupt synthetic phospholipid bilayers and full-length mutant Htt shows increased binding to numerous phospholipids, supporting the idea that mutant Htt can introduce pathology at the level of phospholipid interactions. Phospholipids 128-141 huntingtin Homo sapiens 88-91 25062673-7 2013 Mutant Htt fragments can disrupt synthetic phospholipid bilayers and full-length mutant Htt shows increased binding to numerous phospholipids, supporting the idea that mutant Htt can introduce pathology at the level of phospholipid interactions. Phospholipids 128-141 huntingtin Homo sapiens 88-91 25062673-9 2013 Understanding the relationship of Htt with membrane phospholipids, and the impact of mutant Htt on membrane-related functions and lipid metabolism, may help identify new modes of therapeutic intervention for Huntington"s disease. Phospholipids 52-65 huntingtin Homo sapiens 34-37 19566678-3 2009 Previously we reported that exogenously expressed huntingtin bound pure phospholipids using protein-lipid overlays. Phospholipids 72-85 huntingtin Homo sapiens 50-60