PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. Polyamines 229-239 transglutaminase 2 Homo sapiens 161-184 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. Polyamines 246-256 transglutaminase 2 Homo sapiens 178-201 25471600-3 2015 However, polyamines can also be covalently conjugated to proteins by transglutaminase 2 (TG2). Polyamines 9-19 transglutaminase 2 Homo sapiens 69-87 1360694-0 1992 Polyamines are involved in retinoic acid-mediated induction of tissue transglutaminase in human peripheral blood monocytes. Polyamines 0-10 transglutaminase 2 Homo sapiens 63-86 1360694-8 1992 We conclude that TGc induction by RA during in vitro maturation of monocytes to macrophages may be modulated by polyamine availability. Polyamines 112-121 transglutaminase 2 Homo sapiens 17-20 33555506-1 2021 BACKGROUND: Transglutaminase 2 (TG2) mediates protein modifications by crosslinking or by incorporating polyamine in response to oxidative or DNA-damaging stress, thereby regulating apoptosis, extracellular matrix formation, and inflammation. Polyamines 104-113 transglutaminase 2 Homo sapiens 12-30 33555506-1 2021 BACKGROUND: Transglutaminase 2 (TG2) mediates protein modifications by crosslinking or by incorporating polyamine in response to oxidative or DNA-damaging stress, thereby regulating apoptosis, extracellular matrix formation, and inflammation. Polyamines 104-113 transglutaminase 2 Homo sapiens 32-35 33555506-7 2021 A transamidation reaction showed that TG2 mediated incorporation of polyamine into BAF250a. Polyamines 68-77 transglutaminase 2 Homo sapiens 38-41 30344949-1 2018 The protein crosslinking enzyme tissue transglutaminase (tTG) is an acyltransferase which catalyzes transamidation reactions between two proteins, or between a protein and a polyamine. Polyamines 174-183 transglutaminase 2 Homo sapiens 32-55 30344949-1 2018 The protein crosslinking enzyme tissue transglutaminase (tTG) is an acyltransferase which catalyzes transamidation reactions between two proteins, or between a protein and a polyamine. Polyamines 174-183 transglutaminase 2 Homo sapiens 57-60 25471600-3 2015 However, polyamines can also be covalently conjugated to proteins by transglutaminase 2 (TG2). Polyamines 9-19 transglutaminase 2 Homo sapiens 89-92 25471600-5 2015 It is anticipated that protein polyamine conjugation may affect the protein-protein interaction, protein localization, and protein function of the TG2 substrates. Polyamines 31-40 transglutaminase 2 Homo sapiens 147-150 18696180-0 2009 Protein-polyamine conjugates by transglutaminase 2 as potential markers for antineoplastic screening of natural compounds. Polyamines 8-17 transglutaminase 2 Homo sapiens 32-50 24494193-3 2014 According to the catalytic properties of TG2, protein cross-linking, polyamine conjugation, and/or deamidation are potential post-translational modifications. Polyamines 69-78 transglutaminase 2 Homo sapiens 41-44 24494193-4 2014 In this article, we have demonstrated that TG2 catalyzes either polyamine conjugation or deamidation to GlxI depending on the presence of polyamines or not. Polyamines 64-73 transglutaminase 2 Homo sapiens 43-46 24494193-4 2014 In this article, we have demonstrated that TG2 catalyzes either polyamine conjugation or deamidation to GlxI depending on the presence of polyamines or not. Polyamines 138-148 transglutaminase 2 Homo sapiens 43-46 21805137-1 2012 Transglutaminase 2 (TG2) is a multifunctional calcium-dependent enzyme which catalyzes the post-translational protein crosslinking with formation of intra- or inter-molecular epsilon(gamma-glutamyl)lysine bonds or polyamine incorporation. Polyamines 214-223 transglutaminase 2 Homo sapiens 0-18 21805137-1 2012 Transglutaminase 2 (TG2) is a multifunctional calcium-dependent enzyme which catalyzes the post-translational protein crosslinking with formation of intra- or inter-molecular epsilon(gamma-glutamyl)lysine bonds or polyamine incorporation. Polyamines 214-223 transglutaminase 2 Homo sapiens 20-23 17673261-3 2007 TG2 may catalyze the replacement reaction between Lys residues in protein and polyamines. Polyamines 78-88 transglutaminase 2 Homo sapiens 0-3 17673261-7 2007 The dissociation of [(14)C] polyamines from DC bond [(14)C] polyamines complex by TG2 could occur in the presence of non-radioactive polyamines as second amine donor, whereas in the absence, could not almost occur. Polyamines 28-38 transglutaminase 2 Homo sapiens 82-85 17673261-7 2007 The dissociation of [(14)C] polyamines from DC bond [(14)C] polyamines complex by TG2 could occur in the presence of non-radioactive polyamines as second amine donor, whereas in the absence, could not almost occur. Polyamines 60-70 transglutaminase 2 Homo sapiens 82-85 17673261-7 2007 The dissociation of [(14)C] polyamines from DC bond [(14)C] polyamines complex by TG2 could occur in the presence of non-radioactive polyamines as second amine donor, whereas in the absence, could not almost occur. Polyamines 60-70 transglutaminase 2 Homo sapiens 82-85 17673261-9 2007 These results demonstrate that TG2 catalyzes the replacement reaction between added [(14)C] polyamine and DC bond [(14)C] polyamine. Polyamines 92-101 transglutaminase 2 Homo sapiens 31-34 16876317-1 2006 Tissue transglutaminase (TG2) can induce post-translational modification of proteins, resulting in protein cross-linking or incorporation of polyamines into substrates, and can also function as a signal transducing G protein. Polyamines 141-151 transglutaminase 2 Homo sapiens 0-23 16146723-1 2006 Tissue transglutaminase (TG2, EC 2.3.2.13) is a ubiquitous enzyme that catalyzes Ca2+-dependent post-translational modification of proteins by inserting highly stable (epsilon-[gamma-glutamyl] lysine) isopeptide bonds or by conjugating polyamines at selected peptide-bound glutamine residues. Polyamines 236-246 transglutaminase 2 Homo sapiens 0-23 15362860-3 2004 tTG is known to serve as an adhesion coreceptor for beta1/beta3 integrins and as an enzyme that catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Polyamines 159-169 transglutaminase 2 Homo sapiens 0-3 15135339-1 2004 Ubiquitous tissue transglutaminase (tTG) is one member of the large transglutaminase (TG) family, which catalyze posttranslational modification of proteins by establishing epsilon(gamma-glutamyl)lysine cross-linking and/or covalent incorporation of polyamines. Polyamines 249-259 transglutaminase 2 Homo sapiens 11-34 15069073-1 2004 Tissue transglutaminase (TG2) is a ubiquitous enzyme that cross-links glutamine residues with lysine residues, resulting in protein polymerization, cross-linking of dissimilar proteins, and incorporation of diamines and polyamines into proteins. Polyamines 220-230 transglutaminase 2 Homo sapiens 0-23 15135339-1 2004 Ubiquitous tissue transglutaminase (tTG) is one member of the large transglutaminase (TG) family, which catalyze posttranslational modification of proteins by establishing epsilon(gamma-glutamyl)lysine cross-linking and/or covalent incorporation of polyamines. Polyamines 249-259 transglutaminase 2 Homo sapiens 36-39 12527383-0 2003 Differential incorporation of biotinylated polyamines by transglutaminase 2. Polyamines 43-53 transglutaminase 2 Homo sapiens 57-75 14517264-0 2003 Transglutaminase 2 inhibits Rb binding of human papillomavirus E7 by incorporating polyamine. Polyamines 83-92 transglutaminase 2 Homo sapiens 0-18 14517264-1 2003 Transglutaminase 2 (TGase 2) is one of a family of enzymes that catalyze protein modification through the incorporation of polyamines into substrates or the formation of protein crosslinks. Polyamines 123-133 transglutaminase 2 Homo sapiens 0-18 14517264-1 2003 Transglutaminase 2 (TGase 2) is one of a family of enzymes that catalyze protein modification through the incorporation of polyamines into substrates or the formation of protein crosslinks. Polyamines 123-133 transglutaminase 2 Homo sapiens 20-27 14517264-5 2003 TGase 2 incorporates polyamines into a conserved glutamine residue in the zinc-binding domain of HPV18 E7 protein. Polyamines 21-31 transglutaminase 2 Homo sapiens 0-7 12527383-1 2003 Polyamine incorporation or cross-linking of proteins, post-translational modifications mediated by transglutaminase 2 (TGase 2), have been implicated in a variety of physiological functions including cell adhesion, extracellular matrix formation and apoptosis. Polyamines 0-9 transglutaminase 2 Homo sapiens 99-117 12527383-1 2003 Polyamine incorporation or cross-linking of proteins, post-translational modifications mediated by transglutaminase 2 (TGase 2), have been implicated in a variety of physiological functions including cell adhesion, extracellular matrix formation and apoptosis. Polyamines 0-9 transglutaminase 2 Homo sapiens 119-126 11738471-13 2002 Given the fact that the levels of polyamines in cells is in the millimolar range and the crosslinking and polyaminating reactions catalyzed by tTG are competing reactions, intracellularly polyamination is likely to be the predominant reaction. Polyamines 34-44 transglutaminase 2 Homo sapiens 143-146