PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23725463-2	2014	We investigated polyglutamine (CAG) and a polyglycine (GGC) tract in Italian men with defective spermatogenesis.	polyglycine	42-53	gamma-glutamylcyclotransferase	Homo sapiens	55-58	
15044606-1	2004	The androgen receptor (AR) has two polymorphic sites in exon 1, characterized by different numbers of CAG and GGC repeats resulting in variable lengths of polyglutamine and polyglycine stretches.	polyglycine	173-184	gamma-glutamylcyclotransferase	Homo sapiens	110-113	
15987717-4	2005	The aim of this study was to evaluate eRF3/GSPT1 gene as a potential genetic susceptibility associated locus for gastric cancer, analysing a stable GGC expansion in exon 1 encoding a polyglycine tract in the N-terminal domain of the protein.	polyglycine	183-194	gamma-glutamylcyclotransferase	Homo sapiens	148-151	
22101789-3	2012	The eRF3a/GSPT1 exon 1 contains a trinucleotide GGC repeat coding for a polyglycine expansion in the N-terminal of the protein.	polyglycine	72-83	gamma-glutamylcyclotransferase	Homo sapiens	48-51	
19963113-2	2009	GSPT1 contains a GGC(n) polymorphism in exon 1, encoding a polyglycine expansion in the N-terminal of the protein.	polyglycine	59-70	gamma-glutamylcyclotransferase	Homo sapiens	17-20	
15757859-2	2005	The androgen receptor has two polymorphic sites in exon 1, with different numbers of CAG and GGC repeats, resulting in variable lengths of polyglutamine and polyglycine stretches.	polyglycine	157-168	gamma-glutamylcyclotransferase	Homo sapiens	93-96	
14743468-1	2004	BACKGROUND: The amino-terminal transcriptional activation domain of the androgen receptor (AR) gene contains two polymorphic trinucleotide repeat segments that encode polyglutamine (CAG)n and polyglycine (GGC)n tracts.	polyglycine	192-203	gamma-glutamylcyclotransferase	Homo sapiens	205-208	
34694469-0	2021	Upstream open reading frame with NOTCH2NLC GGC expansion generates polyglycine aggregates and disrupts nucleocytoplasmic transport: implications for polyglycine diseases.	polyglycine	67-78	gamma-glutamylcyclotransferase	Homo sapiens	43-46	
14652007-1	2003	Human androgen receptor (AR) gene contains two polymorphic trinucleotide repeats of CAG and GGC, which code for polyglutamine and polyglycine tracts in the N-terminal domain in which the receptor activity resides.	polyglycine	130-141	gamma-glutamylcyclotransferase	Homo sapiens	92-95	
10502720-1	1999	Several reports have suggested that one or both of the trinucleotide repeat polymorphisms in the human androgen receptor (hAR) gene, (CAG)n coding for polyglutamine and (GGC)n coding for polyglycine, may be associated with prostate cancer risk; but no study has investigated their association with disease progression.	polyglycine	187-198	gamma-glutamylcyclotransferase	Homo sapiens	170-173	
34694469-0	2021	Upstream open reading frame with NOTCH2NLC GGC expansion generates polyglycine aggregates and disrupts nucleocytoplasmic transport: implications for polyglycine diseases.	polyglycine	149-160	gamma-glutamylcyclotransferase	Homo sapiens	43-46	
33693509-7	2021	Immunofluorescence on OPDM muscle samples and expressing mutant NOTCH2NLC with (GGC)69 repeat expansions in HEK293 cells indicated that mutant NOTCH2NLC-polyGlycine protein might be a major component of intranuclear inclusions, and contribute to toxicity in cultured cells.	polyglycine	153-164	gamma-glutamylcyclotransferase	Homo sapiens	80-83	
34081916-2	2021	(2021) show that a polyglycine-expanded protein, uN2CpolyG, is translated from an expansion of GGC repeats in the 5" UTR of the NOTCH2NLC (Notch homolog 2 N-terminal-like C) gene, defining a new pathological mechanism for neuronal intranuclear inclusion diseases (NIID).	polyglycine	19-30	gamma-glutamylcyclotransferase	Homo sapiens	95-98	
33887199-0	2021	Translation of GGC repeat expansions into a toxic polyglycine protein in NIID defines a novel class of human genetic disorders: the polyG diseases.	polyglycine	50-61	gamma-glutamylcyclotransferase	Homo sapiens	15-18	
33887199-6	2021	These results suggest that translation of expanded GGC repeats into a novel and pathogenic polyglycine-containing protein underlies the presence of intranuclear inclusions and neurodegeneration in NIID.	polyglycine	91-102	gamma-glutamylcyclotransferase	Homo sapiens	51-54