PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26106822-0 2015 Detection of huntingtin exon 1 phosphorylation by Phos-Tag SDS-PAGE: Predominant phosphorylation on threonine 3 and regulation by IKKbeta. Sodium Dodecyl Sulfate 59-62 huntingtin Homo sapiens 13-23 12888569-2 2003 Previously, we have shown that mutant htt fragments with polyglutamine (polyQ) tracts in the pathological range (>37 glutamines) form SDS-resistant aggregates with a fibrillar morphology, whereas wild-type htt fragments with normal polyQ domains do not aggregate. Sodium Dodecyl Sulfate 134-137 huntingtin Homo sapiens 38-41 12888569-4 2003 We found that mutant htt promotes the aggregation of wild-type htt, causing the formation of SDS-resistant co-aggregates with a fibrillar morphology. Sodium Dodecyl Sulfate 93-96 huntingtin Homo sapiens 21-24 12888569-4 2003 We found that mutant htt promotes the aggregation of wild-type htt, causing the formation of SDS-resistant co-aggregates with a fibrillar morphology. Sodium Dodecyl Sulfate 93-96 huntingtin Homo sapiens 63-66 11359930-4 2001 Inhibition of proteasome activity resulted in a twofold increase in the amount of ubiquitinated, SDS-resistant aggregates, indicating that inclusion bodies accumulate when the capacity of the ubiquitin-proteasome system to degrade aggregation-prone huntingtin protein is exhausted. Sodium Dodecyl Sulfate 97-100 huntingtin Homo sapiens 249-259 11285271-6 2001 In the cells expressing the mutant truncated huntingtin construct, numerous SDS-resistant aggregates were present in the cytoplasm and nucleus. Sodium Dodecyl Sulfate 76-79 huntingtin Homo sapiens 45-55 26106822-5 2015 Using a modified SDS-PAGE protocol (Phos-Tag) followed by Western blotting with specific anti-HUNTINGTIN antibodies, we efficiently resolved huntingtin fragments expressed in cellular contexts based on the presence of phosphorylated residues, we defined threonine 3 as the major site of huntingtin N17 phosphorylation and, finally, we identified IKK-beta as a kinase capable of phosphorylating threonine 3 in N-terminal hungtingtin fragments. Sodium Dodecyl Sulfate 17-20 huntingtin Homo sapiens 141-151 22375012-7 2012 A soluble mutant htt fragment of about 180 kDa was detected with anti-htt antibody Ab1 (htt-(1-17)) and increased when lysates were treated with denaturants (SDS, 8 M urea, DTT, or trypsin) before BNP. Sodium Dodecyl Sulfate 158-161 huntingtin Homo sapiens 17-20 25446099-6 2015 Deletion of HTT-N17 leads to formation of tinier, SDS-soluble nuclear aggregates formed by N-terminal mutant HTT. Sodium Dodecyl Sulfate 50-53 huntingtin Homo sapiens 12-19 25446099-6 2015 Deletion of HTT-N17 leads to formation of tinier, SDS-soluble nuclear aggregates formed by N-terminal mutant HTT. Sodium Dodecyl Sulfate 50-53 huntingtin Homo sapiens 12-15 20140226-7 2010 Deletion of these actin-binding regions renders the polyglutamine-expanded forms of ARN127 and Htt exon 1 less aggregation-prone, and increases the SDS-solubility of aggregates that do form. Sodium Dodecyl Sulfate 148-151 huntingtin Homo sapiens 95-98 18065495-6 2008 Furthermore, we observed SDS-soluble wild-type htt (wthtt)-wthtt, wthtt-muhtt and muhtt-muhtt interactions, which were enhanced by the presence of Pak1. Sodium Dodecyl Sulfate 25-28 huntingtin Homo sapiens 47-50 17213954-6 2007 Htt fragments were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and detected with anti-Htt antibodies. Sodium Dodecyl Sulfate 32-53 huntingtin Homo sapiens 0-3 17213954-6 2007 Htt fragments were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and detected with anti-Htt antibodies. Sodium Dodecyl Sulfate 90-93 huntingtin Homo sapiens 0-3