PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12899634-1 2003 Tissue transglutaminase (TGase) catalyzes transfer of gamma-acyl moieties of Gln residues in peptides or protein substrates to either water or amine nucleophiles through an acyl-enzyme intermediate formed from initial acyl-transfer to an active site Cys residue. Amines 143-148 transglutaminase 2 Homo sapiens 0-23 15009681-7 2004 Inhibition of TTG cross-linking by primary amine substrates including putrescine and biotinylated pentylamine antagonized TTG"s ability to form soluble complexes. Amines 43-48 transglutaminase 2 Homo sapiens 14-17 15009681-7 2004 Inhibition of TTG cross-linking by primary amine substrates including putrescine and biotinylated pentylamine antagonized TTG"s ability to form soluble complexes. Amines 43-48 transglutaminase 2 Homo sapiens 122-125 15009681-11 2004 Furthermore, the effectiveness of a primary amine substrate at inhibiting formation of insoluble inclusions may be related to their ability to inhibit intermolecular cross-linking by TTG. Amines 44-49 transglutaminase 2 Homo sapiens 183-186 12862427-4 2003 These beta-sheet fibrillar nanostructures were then covalently coupled to pendant amine-containing biomolecules via tissue transglutaminase. Amines 82-87 transglutaminase 2 Homo sapiens 116-139 12907337-10 2003 The presence in the celiac mucosa of proteins able to act as amine-donor substrates suggests that tissue transglutaminase-mediated post-translational modification of proteins cross-linked with gliadin peptides may represent a pathogenic mechanism of CD. Amines 61-66 transglutaminase 2 Homo sapiens 98-121 12533191-7 2003 Using labelled primary amines as an indicator of tTG activity within these "wounded cells", we demonstrate that tTG modifies a wide range of proteins that are present in both the perinuclear and intranuclear spaces. Amines 23-29 transglutaminase 2 Homo sapiens 112-115 7829248-2 1995 TGase2 catalyzes an acyl-transfer reaction between peptide-bound glutamine residues and primary amines, including the epsilon-amino group of lysine residues. Amines 96-102 transglutaminase 2 Homo sapiens 0-6 11061429-1 2000 The "tissue" transglutaminase is a multifunctional enzyme that in its cross-linking configuration catalyzes Ca2+ -dependent reactions resulting in post-translational modification of proteins by establishing epsilon(gamma-glutamyl) lysine cross-links and/or covalent incorporation of biogenic amines (di- and poly-amines and histamine) into proteins. Amines 292-298 transglutaminase 2 Homo sapiens 4-29 8611158-2 1996 An ELSA (enzyme-linked sorbent assay) plate assay was developed for intracellular tTGase activity, using the incorporation of a biotinylated primary amine, 5-{[(N-biotinoylamino)hexanoyl]amino}pentylamine(biotin-x-cadaveri ne; BTC), into endogenous protein substrates of tTGase. Amines 149-154 transglutaminase 2 Homo sapiens 82-88 23797785-7 2013 We investigated TGM-2 crosslinking of several biogenic amines (serotonin, histamine, dopamine and noradrenaline) to fibrinogen. Amines 55-61 transglutaminase 2 Homo sapiens 16-21 1680857-4 1991 We studied whether tissue transglutaminase and/or activated Factor XIII (plasma derived or recombinant FXIIIa) incorporate primary amines into Lp(a). Amines 131-137 transglutaminase 2 Homo sapiens 19-42 28357481-2 2017 The antigenic protein tissue transglutaminase was chemically modified, introducing disulfide groups through different moieties of the molecule (amine, carboxylic, and hydroxyl groups), self-assembled on gold surfaces, and used for the detection of IgA and IgG autoantibodies. Amines 144-149 transglutaminase 2 Homo sapiens 22-45 28357481-3 2017 The modified proteins were evaluated using enzyme-linked immunosorbent assay and surface plasmon resonance, which showed that only introduction of the disulfide groups through amine moieties in the tissue transglutaminase preserved its antigenic properties. Amines 176-181 transglutaminase 2 Homo sapiens 198-221 26487698-5 2016 In the present study we provide evidence that S100A4 is an interacting partner and also a specific amine donor of TG2. Amines 99-104 transglutaminase 2 Homo sapiens 114-117 1349282-0 1992 The carboxy-terminal lysine of alpha B-crystallin is an amine-donor substrate for tissue transglutaminase. Amines 56-61 transglutaminase 2 Homo sapiens 82-105 2887447-0 1987 Beta B1 crystallin is an amine-donor substrate for tissue transglutaminase. Amines 25-30 transglutaminase 2 Homo sapiens 51-74 32045569-0 2020 Solution-phase synthesis of the fluorogenic TGase 2 acyl donor Z-Glu(HMC)-Gly-OH and its use for inhibitor and amine substrate characterisation. Amines 111-116 transglutaminase 2 Homo sapiens 44-51 29362136-1 2018 Tissue transglutaminase (tTG) is capable of binding and hydrolyzing GTP, as well as catalyzing an enzymatic transamidation reaction that crosslinks primary amines to glutamine residues. Amines 156-162 transglutaminase 2 Homo sapiens 0-23 29362136-1 2018 Tissue transglutaminase (tTG) is capable of binding and hydrolyzing GTP, as well as catalyzing an enzymatic transamidation reaction that crosslinks primary amines to glutamine residues. Amines 156-162 transglutaminase 2 Homo sapiens 25-28 27040940-5 2016 Quantitative TG2 kinase activity was determined by selective detection of substrate protein phosphorylation on the surface of well-type amine arrays. Amines 136-141 transglutaminase 2 Homo sapiens 13-16 26250429-6 2016 The W278F mutation resulted in six times elevated amine incorporating transamidase activity demonstrating the regulatory significance of W278 and W332 in TG2 and that mutations can change opposed activities located at the same active site. Amines 50-55 transglutaminase 2 Homo sapiens 154-157 19655169-9 2010 RESULTS: We found that the primary amine of GlcN plays a key role in TGase 2 inhibition. Amines 35-40 transglutaminase 2 Homo sapiens 69-76 21910960-1 2011 Tissue transglutaminase (tTG) is a calcium-dependent enzyme that catalyzes crosslinking of peptidic glutamine residues with primary amines via isopeptide bonds and hydrolysis of ATP or GTP. Amines 132-138 transglutaminase 2 Homo sapiens 0-23 21910960-1 2011 Tissue transglutaminase (tTG) is a calcium-dependent enzyme that catalyzes crosslinking of peptidic glutamine residues with primary amines via isopeptide bonds and hydrolysis of ATP or GTP. Amines 132-138 transglutaminase 2 Homo sapiens 25-28 21440023-5 2011 Upon Ca(2+) ionophore (A23187) induced activation of cellular tTG (measured by incorporation of the tTG-specific amine substrate 5-(biotinamido)pentylamine (BAP) into cellular proteins) in neuroblastoma SH-SY5Y cells, only Z006 (0.3-30 muM) retained the capacity to completely inhibit tTG activity. Amines 113-118 transglutaminase 2 Homo sapiens 62-65 21440023-5 2011 Upon Ca(2+) ionophore (A23187) induced activation of cellular tTG (measured by incorporation of the tTG-specific amine substrate 5-(biotinamido)pentylamine (BAP) into cellular proteins) in neuroblastoma SH-SY5Y cells, only Z006 (0.3-30 muM) retained the capacity to completely inhibit tTG activity. Amines 113-118 transglutaminase 2 Homo sapiens 100-103 21440023-5 2011 Upon Ca(2+) ionophore (A23187) induced activation of cellular tTG (measured by incorporation of the tTG-specific amine substrate 5-(biotinamido)pentylamine (BAP) into cellular proteins) in neuroblastoma SH-SY5Y cells, only Z006 (0.3-30 muM) retained the capacity to completely inhibit tTG activity. Amines 113-118 transglutaminase 2 Homo sapiens 100-103 20112034-1 2010 Tissue transglutaminase (TG2) is a multifunctional member of the transglutaminase (TGase) family (E.C.2.3.2.13), which catalyzes in a calcium-dependent reaction the formation of covalent bonds between the gamma-carboxamide groups of peptide-bound glutamine residues and various primary amines. Amines 286-292 transglutaminase 2 Homo sapiens 0-23 22160262-1 2013 Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. Amines 157-163 transglutaminase 2 Homo sapiens 0-18 22160262-1 2013 Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. Amines 157-163 transglutaminase 2 Homo sapiens 20-23 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. Amines 32-37 transglutaminase 2 Homo sapiens 82-85 18420267-3 2008 A novel sequence spanning residues 2800-2807 of human fibrillin-1 (EDGFFKI) was first identified as an amine donor substrate for tTGase, using a previously characterized APQQEA derived from human osteonectin as an amine acceptor probe. Amines 103-108 transglutaminase 2 Homo sapiens 129-135 18420267-3 2008 A novel sequence spanning residues 2800-2807 of human fibrillin-1 (EDGFFKI) was first identified as an amine donor substrate for tTGase, using a previously characterized APQQEA derived from human osteonectin as an amine acceptor probe. Amines 214-219 transglutaminase 2 Homo sapiens 129-135 17086478-1 2007 Tissue transglutaminase catalyzes irreversible post-translational modification of specific protein substrates by either crosslinkage or incorporation of primary amines into glutamine residues, through glutamyl-amide isopeptide bonds. Amines 161-167 transglutaminase 2 Homo sapiens 0-23 18505736-1 2008 We have studied the interaction of the enzyme tissue transglutaminase (tTG), catalyzing cross-link formation between protein-bound glutamine residues and primary amines, with Parkinson"s disease-associated alpha-synuclein protein variants at physiologically relevant concentrations. Amines 162-168 transglutaminase 2 Homo sapiens 46-69 18505736-1 2008 We have studied the interaction of the enzyme tissue transglutaminase (tTG), catalyzing cross-link formation between protein-bound glutamine residues and primary amines, with Parkinson"s disease-associated alpha-synuclein protein variants at physiologically relevant concentrations. Amines 162-168 transglutaminase 2 Homo sapiens 71-74 17075129-2 2006 As a novel means of specificity analysis, we adapted the phage display technique to select glutamine-donor substrates from a random heptapeptide library via binding to recombinant TG2 and elution with a synthetic amine-donor substrate. Amines 95-100 transglutaminase 2 Homo sapiens 180-183 16385579-2 2006 We here used hexapeptide probes to determine the amine donor (K) and acceptor (Q) sites for tTG in Hsp20. Amines 49-54 transglutaminase 2 Homo sapiens 92-95 16636049-3 2006 Screening was performed by selecting phage clones expressing peptides that incorporated biotin-labeled primary amine by the catalytic reactions of TGase 2 and activated Factor XIII (Factor XIIIa). Amines 111-116 transglutaminase 2 Homo sapiens 147-154