PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22956985-0	2012	Deletion of the huntingtin proline-rich region does not significantly affect normal huntingtin function in mice.	Proline	27-34	huntingtin	Mus musculus	16-26	
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	16-26	
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	28-31	
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	63-73	
34459410-1	2021	BACKGROUND: The Huntingtin (HTT) N-terminal domains encoded by Huntingtin"s (HTT) exon 1 consist of an N17 domain, the polyglutamine (polyQ) stretch and a proline-rich region (PRR).	Proline	155-162	huntingtin	Mus musculus	77-80	
28211815-0	2017	Generation and Characterization of Knock-in Mouse Models Expressing Versions of Huntingtin with Either an N17 or a Combined PolyQ and Proline-Rich Region Deletion.	Proline	134-141	huntingtin	Mus musculus	80-90	
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	Proline	167-174	huntingtin	Mus musculus	53-63	
28211815-1	2017	BACKGROUND: The polyglutamine (polyQ) stretch of the Huntingtin protein (HTT) in mammals is flanked by a highly conserved 17 amino acid N-terminal domain (N17), and a proline-rich region (PRR).	Proline	167-174	huntingtin	Mus musculus	73-76	
31282030-6	2019	While differences in the human and mouse exon 1 HTT proteins (e.g., proline rich sequences) could also contribute to the phenotypic differences, our data indicate that the incomplete splicing of HTT and approaches to lower the levels of the exon 1 HTT transcript should be pursued as therapeutic targets.	Proline	68-75	huntingtin	Mus musculus	48-51	
22892315-2	2012	Although studies in vitro have suggested that the mutant htt can act in a potentially dominant negative fashion by sequestering wild-type htt into insoluble protein aggregates, the role of the length of the normal htt polyQ stretch, and the adjacent proline-rich region (PRR) in modulating HD mouse model pathogenesis is currently unknown.	Proline	250-257	huntingtin	Mus musculus	57-60	
19864571-4	2009	We previously showed that V(L)12.3, an intrabody recognizing the N terminus of Htt, and Happ1, an intrabody recognizing the proline-rich domain of Htt, both reduce mHtt-induced toxicity and aggregation in cell culture and brain slice models of HD.	Proline	124-131	huntingtin	Mus musculus	147-150	
17975550-8	2008	We suggest, that the C-terminal domain of exon 1 Huntingtin, namely the proline rich domain, is responsible for mediating a neuroprotective effect against excitotoxicity.	Proline	72-79	huntingtin	Mus musculus	49-59	
16405500-10	2006	Moreover, interaction of both mutant and wild-type huntingtin exon 1 fragments with brain lipids caused bilayer perturbation, mediated through a proline-rich region adjacent to the polyglutamines.	Proline	145-152	huntingtin	Mus musculus	51-61	
17373643-8	2007	Furthermore, the 2B4 epitope resides within the proline-rich region of Huntingtin, which is critical for polyQ aggregation and toxicity.	Proline	48-55	huntingtin	Mus musculus	71-81	
15371500-5	2004	Activation of IKK is likely mediated by direct interaction with mutant Htt, because the expanded polyglutamine stretch and adjacent proline-rich motifs in mutant Htt interact with IKKgamma, a regulatory subunit of IKK.	Proline	132-139	huntingtin	Mus musculus	71-74	
15371500-5	2004	Activation of IKK is likely mediated by direct interaction with mutant Htt, because the expanded polyglutamine stretch and adjacent proline-rich motifs in mutant Htt interact with IKKgamma, a regulatory subunit of IKK.	Proline	132-139	huntingtin	Mus musculus	162-165