PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15009681-0 2004 Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats. polyglutamine 84-97 transglutaminase 2 Homo sapiens 10-33 19998405-1 2010 Human tissue transglutaminase (TGM2) is implicated in the pathogenesis of several neurodegenerative disorders including Alzheimer"s, Parkinson"s and expanded polyglutamine (polyQ) diseases. polyglutamine 158-171 transglutaminase 2 Homo sapiens 6-29 19998405-1 2010 Human tissue transglutaminase (TGM2) is implicated in the pathogenesis of several neurodegenerative disorders including Alzheimer"s, Parkinson"s and expanded polyglutamine (polyQ) diseases. polyglutamine 158-171 transglutaminase 2 Homo sapiens 31-35 19998405-1 2010 Human tissue transglutaminase (TGM2) is implicated in the pathogenesis of several neurodegenerative disorders including Alzheimer"s, Parkinson"s and expanded polyglutamine (polyQ) diseases. polyglutamine 173-178 transglutaminase 2 Homo sapiens 6-29 19998405-1 2010 Human tissue transglutaminase (TGM2) is implicated in the pathogenesis of several neurodegenerative disorders including Alzheimer"s, Parkinson"s and expanded polyglutamine (polyQ) diseases. polyglutamine 173-178 transglutaminase 2 Homo sapiens 31-35 15009681-9 2004 In summary, TTG can increase the solubility of expanded polyQ proteins by catalyzing intermolecular cross-links. polyglutamine 56-61 transglutaminase 2 Homo sapiens 12-15 10037459-3 1999 Recent studies have shown that expanded polyglutamine (Qn) repeats are excellent glutaminyl-donor substrates of tissue transglutaminase, and that the substrate activity increases with increasing size of the polyglutamine domain. polyglutamine 40-53 transglutaminase 2 Homo sapiens 112-135 11285271-3 2001 Because in vitro expanded polyglutamine repeats are glutaminyl-donor substrates of tissue transglutaminase (tTG), it has been hypothesized that tTG may contribute to the formation of these aggregates in HD. polyglutamine 26-39 transglutaminase 2 Homo sapiens 83-106 11285271-3 2001 Because in vitro expanded polyglutamine repeats are glutaminyl-donor substrates of tissue transglutaminase (tTG), it has been hypothesized that tTG may contribute to the formation of these aggregates in HD. polyglutamine 26-39 transglutaminase 2 Homo sapiens 108-111 11285271-3 2001 Because in vitro expanded polyglutamine repeats are glutaminyl-donor substrates of tissue transglutaminase (tTG), it has been hypothesized that tTG may contribute to the formation of these aggregates in HD. polyglutamine 26-39 transglutaminase 2 Homo sapiens 144-147 11738471-6 2002 In vitro, polyglutamine constructs and huntingtin are substrates of tTG. polyglutamine 10-23 transglutaminase 2 Homo sapiens 68-71 11738472-0 2002 Cross linking of polyglutamine domains catalyzed by tissue transglutaminase is greatly favored with pathological-length repeats: does transglutaminase activity play a role in (CAG)(n)/Q(n)-expansion diseases? polyglutamine 17-30 transglutaminase 2 Homo sapiens 52-75 11742130-1 2002 Polyglutamine domains are excellent substrates for tissue transglutaminase resulting in the formation of cross-links with polypeptides containing lysyl residues. polyglutamine 0-13 transglutaminase 2 Homo sapiens 51-74 11742130-2 2002 This finding suggests that tissue transglutaminase may play a role in the pathology of neurodegenerative diseases associated with polyglutamine expansion. polyglutamine 130-143 transglutaminase 2 Homo sapiens 27-50 11442349-4 2001 Because in vitro expanded polyglutamine repeats are excellent glutaminyl-donor substrates of tissue transglutaminase (tTG), it has been hypothesized that tTG may contribute to the formation of these aggregates in HD. polyglutamine 26-39 transglutaminase 2 Homo sapiens 93-116 11442349-4 2001 Because in vitro expanded polyglutamine repeats are excellent glutaminyl-donor substrates of tissue transglutaminase (tTG), it has been hypothesized that tTG may contribute to the formation of these aggregates in HD. polyglutamine 26-39 transglutaminase 2 Homo sapiens 118-121 11442349-4 2001 Because in vitro expanded polyglutamine repeats are excellent glutaminyl-donor substrates of tissue transglutaminase (tTG), it has been hypothesized that tTG may contribute to the formation of these aggregates in HD. polyglutamine 26-39 transglutaminase 2 Homo sapiens 154-157 10037459-3 1999 Recent studies have shown that expanded polyglutamine (Qn) repeats are excellent glutaminyl-donor substrates of tissue transglutaminase, and that the substrate activity increases with increasing size of the polyglutamine domain. polyglutamine 207-220 transglutaminase 2 Homo sapiens 112-135 9575137-1 1998 Tissue transglutaminase is a calcium-dependent transamidating enzyme that has been postulated to play a role in the pathology of expanded CAG repeat disorders with polyglutamine expansions expressed within the affected proteins. polyglutamine 164-177 transglutaminase 2 Homo sapiens 0-23 9587422-0 1998 Tissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favored with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases. polyglutamine 110-123 transglutaminase 2 Homo sapiens 0-23 9587422-1 1998 To investigate possible biochemical mechanisms underlying the "toxic gain of function" associated with polyglutamine expansions, the ability of guinea pig liver tissue transglutaminase to catalyze covalent attachments of various polyamines to polyglutamine peptides was examined. polyglutamine 103-116 transglutaminase 2 Homo sapiens 161-184 9587422-4 1998 In the presence of tissue transglutaminase, purified glyceraldehyde-3-phosphate dehydrogenase (a key glycolytic enzyme that binds tightly to the polyglutamine domains of both huntingtin and dentatorubral-pallidoluysian atrophy proteins) is covalently attached to polyglutamine peptides in vitro, resulting in the formation of high-M(r) aggregates. polyglutamine 145-158 transglutaminase 2 Homo sapiens 19-42 9587422-6 1998 Possibly, expansion of polyglutamine domains (thus far known to occur in the gene products associated with at least seven neurodegenerative diseases) leads to increased/aberrant tissue transglutaminase-catalyzed cross-linking reactions with both polyamines and susceptible proteins, such as glyceraldehyde-3-phosphate dehydrogenase. polyglutamine 23-36 transglutaminase 2 Homo sapiens 178-201 9356496-7 1997 The results suggest that tissue transglutaminase-catalyzed covalent linkages involving the larger poly-Q domains may disrupt cerebral energy metabolism in CAG/Qn expansion diseases. polyglutamine 98-104 transglutaminase 2 Homo sapiens 25-48