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