PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22178474-1	2012	The 17-amino-acid N-terminal segment (htt(NT)) that leads into the polyglutamine (polyQ) segment in the Huntington"s disease protein huntingtin (htt) dramatically increases aggregation rates and changes the aggregation mechanism, compared to a simple polyQ peptide of similar length.	17-amino-acid	4-17	huntingtin	Homo sapiens	38-41	
22978784-0	2012	All-atom stability and oligomerization simulations of polyglutamine nanotubes with and without the 17-amino-acid N-terminal fragment of the Huntingtin protein.	17-amino-acid	99-112	huntingtin	Homo sapiens	140-150	
22978784-4	2012	Its aggregation is modulated by the number of glutamine residues as well as by the surrounding amino acid sequences such as the 17-amino-acid N-terminal fragment of Huntingtin which increases the aggregation rate.	17-amino-acid	128-141	huntingtin	Homo sapiens	165-175	
24415136-3	2014	Experimental results suggest that the N-terminal 17-amino-acid sequence (htt(NT)) positioned just before the Q(N) region is important for the binding of huntingtin to membranes.	17-amino-acid	49-62	huntingtin	Homo sapiens	153-163	
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	76-79	
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	96-106	
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	108-111	
22178478-2	2012	Recently, we demonstrated a critical role for the 17-amino-acid N-terminus (htt(NT) segment) of huntingtin (htt) in the oligomer-mediated amyloid assembly of htt N-terminal fragments.	17-amino-acid	50-63	huntingtin	Homo sapiens	108-111	
22178474-1	2012	The 17-amino-acid N-terminal segment (htt(NT)) that leads into the polyglutamine (polyQ) segment in the Huntington"s disease protein huntingtin (htt) dramatically increases aggregation rates and changes the aggregation mechanism, compared to a simple polyQ peptide of similar length.	17-amino-acid	4-17	huntingtin	Homo sapiens	133-143	
22178474-1	2012	The 17-amino-acid N-terminal segment (htt(NT)) that leads into the polyglutamine (polyQ) segment in the Huntington"s disease protein huntingtin (htt) dramatically increases aggregation rates and changes the aggregation mechanism, compared to a simple polyQ peptide of similar length.	17-amino-acid	4-17	huntingtin	Homo sapiens	145-148	
19270701-2	2009	We show here that the 17-amino-acid flanking sequence (HTT(NT)) N-terminal to the polyQ in the toxic huntingtin exon 1 fragment imparts onto this peptide a complex alternative aggregation mechanism.	17-amino-acid	22-35	huntingtin	Homo sapiens	101-111