PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33096080-0 2020 Structural Model of the Proline-rich Domain of Huntingtin exon-1 fibrils. Proline 24-31 huntingtin Homo sapiens 47-57 30808748-1 2019 The N-terminal region of the huntingtin protein, encoded by exon-1, comprises an amphiphilic domain (httNT), a polyglutamine (Q n ) tract, and a proline-rich sequence. Proline 145-152 huntingtin Homo sapiens 29-39 32266815-3 2020 Here, we apply site-specific isotopic labeling to obtain high-resolution NMR data on the cis/trans equilibrium of prolines within the poly-P repeats of huntingtin exon 1, the causative agent of Huntington"s disease. Proline 114-122 huntingtin Homo sapiens 152-162 32402249-1 2020 The causative agent of Huntington"s disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment (N17) and a proline-rich region (PRR), which promote and inhibit the aggregation propensity of the protein, respectively, by poorly understood mechanisms. Proline 170-177 huntingtin Homo sapiens 96-106 29358329-5 2018 We confirm that profilin achieves its cellular effects through direct binding to the C-terminal proline-rich region of Htt-NTFs. Proline 96-103 huntingtin Homo sapiens 119-122 30538129-4 2019 Huntingtin enters the nucleus via an importin beta1- and 2-dependent proline-tyrosine nuclear localization signal (PY-NLS), which has a unique intervening sequence in huntingtin. Proline 69-76 huntingtin Homo sapiens 0-10 30538129-4 2019 Huntingtin enters the nucleus via an importin beta1- and 2-dependent proline-tyrosine nuclear localization signal (PY-NLS), which has a unique intervening sequence in huntingtin. Proline 69-76 huntingtin Homo sapiens 167-177 29754822-4 2018 We found that huntingtin exon1 proteins can form reversible liquid-like assemblies, a process driven by huntingtin"s polyQ tract and proline-rich region. Proline 133-140 huntingtin Homo sapiens 14-24 30252478-0 2018 Dynamics of the Proline-Rich C-Terminus of Huntingtin Exon-1 Fibrils. Proline 16-23 huntingtin Homo sapiens 43-53 17373643-0 2007 Mapping of the epitope of monoclonal antibody 2B4 to the proline-rich region of human Huntingtin, a region critical for aggregation and toxicity. Proline 57-64 huntingtin Homo sapiens 86-96 22178478-8 2012 In the other class, nucleation is actively suppressed by a proline-rich polyQ segment covalently attached to htt(NT). Proline 59-66 huntingtin Homo sapiens 109-112 21566141-3 2011 Besides the pathogenic polyQ expansion, Htt also contains a proline-rich region (PRR) located exactly in the C terminus to the polyQ tract. Proline 60-67 huntingtin Homo sapiens 40-43 19710014-3 2009 The first exon of Htt encodes 17 amino acids followed by a poly(Q) repeat of variable length and culminating with a proline-rich domain of 50 amino acids. Proline 116-123 huntingtin Homo sapiens 18-21 18768695-0 2008 Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity. Proline 24-31 huntingtin Homo sapiens 55-65 18768695-3 2008 However, other parts of the protein, including the 17 N-terminal amino acids and two proline (polyP) repeat domains, regulate the toxicity of mutant Htt. Proline 85-92 huntingtin Homo sapiens 149-152 27458341-4 2016 These altered kinetics arise from the shift of a proline-induced translational pause site away from Htt"s localization sequence due to the expansion of the CAG-repeat segment between the poly-proline and localization sequences. Proline 49-56 huntingtin Homo sapiens 100-103 27595037-2 2016 We show that expression of a mutant human huntingtin exon-1-GFP fusion construct results in nonspecific gene dysregulation that is significantly reduced by 50% due to coexpression of INT41, an intrabody specific for the proline-rich region of the huntingtin protein. Proline 220-227 huntingtin Homo sapiens 42-52 27595037-2 2016 We show that expression of a mutant human huntingtin exon-1-GFP fusion construct results in nonspecific gene dysregulation that is significantly reduced by 50% due to coexpression of INT41, an intrabody specific for the proline-rich region of the huntingtin protein. Proline 220-227 huntingtin Homo sapiens 247-257 24412394-0 2014 Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin. Proline 91-98 huntingtin Homo sapiens 114-124 24412394-5 2014 This autoinhibitory structure regulates interaction between the WW domain of HYPB and the proline-rich region (PRR) of Htt, as evidenced by NMR and immunofluorescence techniques. Proline 90-97 huntingtin Homo sapiens 119-122 23012356-0 2012 Identification of a karyopherin beta1/beta2 proline-tyrosine nuclear localization signal in huntingtin protein. Proline 44-51 huntingtin Homo sapiens 92-102 23012356-3 2012 Here, using a live cell assay and affinity chromatography, we show that huntingtin has a karyopherin beta2-dependent proline-tyrosine (PY)-NLS in the amino terminus of the protein. Proline 117-124 huntingtin Homo sapiens 72-82 21332223-4 2011 Trimethylamine N-oxide (TMAO) and proline redirect amyloid fibrillogenesis of the pathological huntingtin exon 1 to nonamyloidogenic amorphous assemblies via two dissimilar molecular mechanisms. Proline 34-41 huntingtin Homo sapiens 95-105 18094623-6 2008 We show that the proline-rich region is essential for the Bag3-mediated stimulation of mutated huntingtin clearance. Proline 17-24 huntingtin Homo sapiens 95-105 14715959-6 2004 Removal of a series of prolines adjacent to the polyglutamine region in htt blocked formation of the shell of the htt body and redistribution of dynamin, HIP1, SH3GL3, and proteasome to it. Proline 23-31 huntingtin Homo sapiens 72-75 17161366-0 2006 Structural insights into the specific binding of huntingtin proline-rich region with the SH3 and WW domains. Proline 60-67 huntingtin Homo sapiens 49-59 17161366-2 2006 We report the specific interactions of Htt proline-rich region (PRR) with the SH3GL3-SH3 domain and HYPA-WW1-2 domain pair by NMR. Proline 43-50 huntingtin Homo sapiens 39-42 14715959-6 2004 Removal of a series of prolines adjacent to the polyglutamine region in htt blocked formation of the shell of the htt body and redistribution of dynamin, HIP1, SH3GL3, and proteasome to it. Proline 23-31 huntingtin Homo sapiens 114-117 12486229-0 2002 Glutamine/proline-rich PQE-1 proteins protect Caenorhabditis elegans neurons from huntingtin polyglutamine neurotoxicity. Proline 10-17 huntingtin Homo sapiens 82-92 9079622-1 1997 Based on the presence of multiple proline-rich motifs in the huntingtin sequence, we tested its possible association with epidermal growth factor (EGF) receptor signaling complexes through SH3 domain-containing modules. Proline 34-41 huntingtin Homo sapiens 61-71 9700202-6 1998 This interaction is mediated by huntingtin"s proline-rich region and is enhanced by lengthening the adjacent glutamine tract. Proline 45-52 huntingtin Homo sapiens 32-42 34445734-4 2021 The huntingtin models consist of a wild-type structure, one mutant with 45 glutamine residues and the second mutant with nine additional key-point mutations from glutamine residues into proline residues (9P(EM) model). Proline 186-193 huntingtin Homo sapiens 4-14