PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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	
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	
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	
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