메뉴 건너뛰기




Volumn 39, Issue 5, 2010, Pages 1183-1191

Gluten T cell epitope targeting by TG3 and TG6; Implications for dermatitis herpetiformis and gluten ataxia

Author keywords

Autoantibodies; Dermatitis herpetiformis; Gluten; Gluten ataxia; TG3; TG6

Indexed keywords

AUTOANTIBODY; GLIADIN; GLUTAMINE; GLUTEN; PROLINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 3; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 6; UNCLASSIFIED DRUG;

EID: 78449288164     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-010-0554-y     Document Type: Article
Times cited : (73)

References (42)
  • 1
    • 0034093354 scopus 로고    scopus 로고
    • Protein crosslinking in assembly and remodelling of extracellular matrices: The role of transglutaminases
    • 1:CAS:528:DC%2BD3cXnvV2qurk%3D 10.3109/03008200009005638 10826705
    • D Aeschlimann V Thomazy 2000 Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases Connect Tissue Res 41 1 1 27 1:CAS:528:DC%2BD3cXnvV2qurk%3D 10.3109/03008200009005638 10826705
    • (2000) Connect Tissue Res , vol.41 , Issue.1 , pp. 1-27
    • Aeschlimann, D.1    Thomazy, V.2
  • 2
    • 0034695893 scopus 로고    scopus 로고
    • The intestinal T cell response to alpha-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase
    • 1:CAS:528:DC%2BD3cXhsVKqs7k%3D 10.1084/jem.191.4.603 10684852
    • H Arentz-Hansen R Korner, et al. 2000 The intestinal T cell response to alpha-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase J Exp Med 191 4 603 612 1:CAS:528:DC%2BD3cXhsVKqs7k%3D 10.1084/jem.191.4.603 10684852
    • (2000) J Exp Med , vol.191 , Issue.4 , pp. 603-612
    • Arentz-Hansen, H.1    Korner, R.2
  • 3
    • 0036724918 scopus 로고    scopus 로고
    • Celiac lesion T cells recognize epitopes that cluster in regions of gliadins rich in proline residues
    • 10.1053/gast.2002.35381 12198706
    • H Arentz-Hansen SN McAdam, et al. 2002 Celiac lesion T cells recognize epitopes that cluster in regions of gliadins rich in proline residues Gastroenterology 123 3 803 809 10.1053/gast.2002.35381 12198706
    • (2002) Gastroenterology , vol.123 , Issue.3 , pp. 803-809
    • Arentz-Hansen, H.1    McAdam, S.N.2
  • 4
    • 33644837119 scopus 로고    scopus 로고
    • Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase
    • 1:CAS:528:DC%2BD28XivVWgu7c%3D 10.1002/prot.20837 16385579
    • S Boros E Ahrman, et al. 2006 Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase Proteins 62 4 1044 1052 1:CAS:528:DC%2BD28XivVWgu7c%3D 10.1002/prot.20837 16385579
    • (2006) Proteins , vol.62 , Issue.4 , pp. 1044-1052
    • Boros, S.1    Ahrman, E.2
  • 5
    • 0028915529 scopus 로고
    • Receptor-ligand interactions measured by an improved spun column chromatography technique. A high efficiency and high throughput size separation method
    • 7537104
    • S Buus A Stryhn, et al. 1995 Receptor-ligand interactions measured by an improved spun column chromatography technique. A high efficiency and high throughput size separation method Biochim Biophys Acta 1243 3 453 460 7537104
    • (1995) Biochim Biophys Acta , vol.1243 , Issue.3 , pp. 453-460
    • Buus, S.1    Stryhn, A.2
  • 6
    • 0028822335 scopus 로고
    • Biochemical, structural, and transglutaminase substrate properties of human loricrin, the major epidermal cornified cell envelope protein
    • 1:CAS:528:DyaK2MXpt1eis7c%3D 10.1074/jbc.270.44.26382 7592852
    • E Candi G Melino, et al. 1995 Biochemical, structural, and transglutaminase substrate properties of human loricrin, the major epidermal cornified cell envelope protein J Biol Chem 270 44 26382 26390 1:CAS:528:DyaK2MXpt1eis7c%3D 10.1074/jbc.270.44.26382 7592852
    • (1995) J Biol Chem , vol.270 , Issue.44 , pp. 26382-26390
    • Candi, E.1    Melino, G.2
  • 7
    • 0023849698 scopus 로고
    • In vitro (organ culture) studies of the toxicity of specific A-gliadin peptides in celiac disease
    • 3335296
    • G de Ritis S Auricchio, et al. 1988 In vitro (organ culture) studies of the toxicity of specific A-gliadin peptides in celiac disease Gastroenterology 94 1 41 49 3335296
    • (1988) Gastroenterology , vol.94 , Issue.1 , pp. 41-49
    • De Ritis, G.1    Auricchio, S.2
  • 8
    • 0030838044 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as the autoantigen of celiac disease
    • 1:CAS:528:DyaK2sXkt1Kqtrc%3D 10.1038/nm0797-797 9212111
    • W Dieterich T Ehnis, et al. 1997 Identification of tissue transglutaminase as the autoantigen of celiac disease Nat Med 3 7 797 801 1:CAS:528:DyaK2sXkt1Kqtrc%3D 10.1038/nm0797-797 9212111
    • (1997) Nat Med , vol.3 , Issue.7 , pp. 797-801
    • Dieterich, W.1    Ehnis, T.2
  • 9
    • 0031760420 scopus 로고    scopus 로고
    • Autoantibodies to tissue transglutaminase as predictors of celiac disease
    • 1:CAS:528:DyaK1cXotVWmurs%3D 10.1016/S0016-5085(98)70007-1 9834256
    • W Dieterich E Laag, et al. 1998 Autoantibodies to tissue transglutaminase as predictors of celiac disease Gastroenterology 115 6 1317 1321 1:CAS:528:DyaK1cXotVWmurs%3D 10.1016/S0016-5085(98)70007-1 9834256
    • (1998) Gastroenterology , vol.115 , Issue.6 , pp. 1317-1321
    • Dieterich, W.1    Laag, E.2
  • 10
    • 33645129719 scopus 로고    scopus 로고
    • Cross linking to tissue transglutaminase and collagen favours gliadin toxicity in coeliac disease
    • 1:CAS:528:DC%2BD28XjslWls74%3D 10.1136/gut.2005.069385 16188922
    • W Dieterich B Esslinger, et al. 2006 Cross linking to tissue transglutaminase and collagen favours gliadin toxicity in coeliac disease Gut 55 4 478 484 1:CAS:528:DC%2BD28XjslWls74%3D 10.1136/gut.2005.069385 16188922
    • (2006) Gut , vol.55 , Issue.4 , pp. 478-484
    • Dieterich, W.1    Esslinger, B.2
  • 11
    • 65249091991 scopus 로고    scopus 로고
    • A quantitative analysis of transglutaminase 2-mediated deamidation of gluten peptides: Implications for the T-cell response in celiac disease
    • 1:CAS:528:DC%2BD1MXit1eksrs%3D 10.1021/pr800960n 19239248
    • S Dorum SW Qiao, et al. 2009 A quantitative analysis of transglutaminase 2-mediated deamidation of gluten peptides: implications for the T-cell response in celiac disease J Proteome Res 8 4 1748 1755 1:CAS:528:DC%2BD1MXit1eksrs%3D 10.1021/pr800960n 19239248
    • (2009) J Proteome Res , vol.8 , Issue.4 , pp. 1748-1755
    • Dorum, S.1    Qiao, S.W.2
  • 12
    • 0035109676 scopus 로고    scopus 로고
    • Current approaches to diagnosis and treatment of celiac disease: An evolving spectrum
    • 1:STN:280:DC%2BD3M7lvV2msA%3D%3D 10.1053/gast.2001.22123 11179241
    • A Fasano C Catassi 2001 Current approaches to diagnosis and treatment of celiac disease: an evolving spectrum Gastroenterology 120 3 636 651 1:STN:280:DC%2BD3M7lvV2msA%3D%3D 10.1053/gast.2001.22123 11179241
    • (2001) Gastroenterology , vol.120 , Issue.3 , pp. 636-651
    • Fasano, A.1    Catassi, C.2
  • 13
    • 0037072829 scopus 로고    scopus 로고
    • Gliadin T cell epitope selection by tissue transglutaminase in celiac disease. Role of enzyme specificity and pH influence on the transamidation versus deamidation process
    • 1:CAS:528:DC%2BD38Xnt1Sqtr4%3D 10.1074/jbc.M204521200 12093810
    • B Fleckenstein O Molberg, et al. 2002 Gliadin T cell epitope selection by tissue transglutaminase in celiac disease. Role of enzyme specificity and pH influence on the transamidation versus deamidation process J Biol Chem 277 37 34109 34116 1:CAS:528:DC%2BD38Xnt1Sqtr4%3D 10.1074/jbc.M204521200 12093810
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 34109-34116
    • Fleckenstein, B.1    Molberg, O.2
  • 14
    • 2342424238 scopus 로고    scopus 로고
    • Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides
    • 1:CAS:528:DC%2BD2cXjt1GntLY%3D 10.1074/jbc.M310198200 14747475
    • B Fleckenstein SW Qiao, et al. 2004 Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides J Biol Chem 279 17 17607 17616 1:CAS:528:DC%2BD2cXjt1GntLY%3D 10.1074/jbc.M310198200 14747475
    • (2004) J Biol Chem , vol.279 , Issue.17 , pp. 17607-17616
    • Fleckenstein, B.1    Qiao, S.W.2
  • 15
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation
    • 1:CAS:528:DyaL3sXhsFKrsLo%3D 6133417
    • JE Folk 1983 Mechanism and basis for specificity of transglutaminase- catalyzed epsilon-(gamma-glutamyl) lysine bond formation Adv Enzymol Relat Areas Mol Biol 54 1 56 1:CAS:528:DyaL3sXhsFKrsLo%3D 6133417
    • (1983) Adv Enzymol Relat Areas Mol Biol , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 16
    • 0029068264 scopus 로고
    • Dermatitis herpetiformis
    • 1:STN:280:DyaK28%2FitlOntQ%3D%3D 10.1016/0950-3528(95)90036-5 7549032
    • L Fry 1995 Dermatitis herpetiformis Baillieres Clin Gastroenterol 9 2 371 393 1:STN:280:DyaK28%2FitlOntQ%3D%3D 10.1016/0950-3528(95)90036-5 7549032
    • (1995) Baillieres Clin Gastroenterol , vol.9 , Issue.2 , pp. 371-393
    • Fry, L.1
  • 17
    • 77956127888 scopus 로고
    • The preparation of I-131-labelled human growth hormone of high specific radioactivity
    • 1:CAS:528:DyaF2cXjt1Cqtw%3D%3D 14097352
    • FC Greenwood WM Hunter, et al. 1963 The preparation of I-131-labelled human growth hormone of high specific radioactivity Biochem J 89 114 123 1:CAS:528:DyaF2cXjt1Cqtw%3D%3D 14097352
    • (1963) Biochem J , vol.89 , pp. 114-123
    • Greenwood, F.C.1    Hunter, W.M.2
  • 18
    • 0035980007 scopus 로고    scopus 로고
    • Evolution of transglutaminase genes: Identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z
    • 1:CAS:528:DC%2BD3MXmvFCmuro%3D 10.1074/jbc.M102553200 11390390
    • P Grenard MK Bates, et al. 2001 Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z J Biol Chem 276 35 33066 33078 1:CAS:528: DC%2BD3MXmvFCmuro%3D 10.1074/jbc.M102553200 11390390
    • (2001) J Biol Chem , vol.276 , Issue.35 , pp. 33066-33078
    • Grenard, P.1    Bates, M.K.2
  • 19
    • 0032517527 scopus 로고    scopus 로고
    • Clinical, radiological, neurophysiological, and neuropathological characteristics of gluten ataxia
    • 1:STN:280:DyaK1M%2FlslagtQ%3D%3D 10.1016/S0140-6736(98)05342-2 9843103
    • M Hadjivassiliou RA Grunewald, et al. 1998 Clinical, radiological, neurophysiological, and neuropathological characteristics of gluten ataxia Lancet 352 9140 1582 1585 1:STN:280:DyaK1M%2FlslagtQ%3D%3D 10.1016/S0140- 6736(98)05342-2 9843103
    • (1998) Lancet , vol.352 , Issue.9140 , pp. 1582-1585
    • Hadjivassiliou, M.1    Grunewald, R.A.2
  • 20
    • 33646177232 scopus 로고    scopus 로고
    • Autoantibody targeting of brain and intestinal transglutaminase in gluten ataxia
    • 1:CAS:528:DC%2BD28Xnt1CksQ%3D%3D 10.1212/01.wnl.0000196480.55601.3a 16476935
    • M Hadjivassiliou M Maki, et al. 2006 Autoantibody targeting of brain and intestinal transglutaminase in gluten ataxia Neurology 66 3 373 377 1:CAS:528:DC%2BD28Xnt1CksQ%3D%3D 10.1212/01.wnl.0000196480.55601.3a 16476935
    • (2006) Neurology , vol.66 , Issue.3 , pp. 373-377
    • Hadjivassiliou, M.1    Maki, M.2
  • 21
    • 54849410089 scopus 로고    scopus 로고
    • Autoantibodies in gluten ataxia recognize a novel neuronal transglutaminase
    • 1:CAS:528:DC%2BD1cXht1yisr3P 10.1002/ana.21450 18825674
    • M Hadjivassiliou P Aeschlimann, et al. 2008 Autoantibodies in gluten ataxia recognize a novel neuronal transglutaminase Ann Neurol 64 3 332 343 1:CAS:528:DC%2BD1cXht1yisr3P 10.1002/ana.21450 18825674
    • (2008) Ann Neurol , vol.64 , Issue.3 , pp. 332-343
    • Hadjivassiliou, M.1    Aeschlimann, P.2
  • 22
    • 76449102440 scopus 로고    scopus 로고
    • Gluten sensitivity: From gut to brain
    • 1:CAS:528:DC%2BC3cXjs12lurc%3D 10.1016/S1474-4422(09)70290-X 20170845
    • M Hadjivassiliou DS Sanders, et al. 2010 Gluten sensitivity: from gut to brain Lancet Neurol 9 3 318 330 1:CAS:528:DC%2BC3cXjs12lurc%3D 10.1016/S1474-4422(09)70290-X 20170845
    • (2010) Lancet Neurol , vol.9 , Issue.3 , pp. 318-330
    • Hadjivassiliou, M.1    Sanders, D.S.2
  • 23
    • 0035013377 scopus 로고    scopus 로고
    • Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse tissues and cell lines
    • 1:CAS:528:DC%2BD3MXivFartbk%3D 10.1016/S1357-2725(01)00033-4 11331204
    • K Hitomi Y Horio, et al. 2001 Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse tissues and cell lines Int J Biochem Cell Biol 33 5 491 498 1:CAS:528:DC%2BD3MXivFartbk%3D 10.1016/S1357-2725(01)00033-4 11331204
    • (2001) Int J Biochem Cell Biol , vol.33 , Issue.5 , pp. 491-498
    • Hitomi, K.1    Horio, Y.2
  • 24
    • 0034747325 scopus 로고    scopus 로고
    • N(epsilon)-(gamma-L-glutamyl)-L-lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington's disease
    • 1:CAS:528:DC%2BD3MXptFOhtrk%3D 10.1046/j.1471-4159.2001.00673.x 11739625
    • TM Jeitner MB Bogdanov, et al. 2001 N(epsilon)-(gamma-L-glutamyl)-L- lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington's disease J Neurochem 79 5 1109 1112 1:CAS:528:DC%2BD3MXptFOhtrk%3D 10.1046/j.1471-4159.2001.00673.x 11739625
    • (2001) J Neurochem , vol.79 , Issue.5 , pp. 1109-1112
    • Jeitner, T.M.1    Bogdanov, M.B.2
  • 25
    • 33751071631 scopus 로고    scopus 로고
    • Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2
    • 1:CAS:528:DC%2BD28XhtFygsrbE 10.1110/ps.051818406 17075129
    • Z Keresztessy E Csosz, et al. 2006 Phage display selection of efficient glutamine-donor substrate peptides for transglutaminase 2 Protein Sci 15 11 2466 2480 1:CAS:528:DC%2BD28XhtFygsrbE 10.1110/ps.051818406 17075129
    • (2006) Protein Sci , vol.15 , Issue.11 , pp. 2466-2480
    • Keresztessy, Z.1    Csosz, E.2
  • 26
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • 1:CAS:528:DC%2BD3sXnsFaqtg%3D%3D 10.1038/nrm1014 12563291
    • L Lorand RM Graham 2003 Transglutaminases: crosslinking enzymes with pleiotropic functions Nat Rev Mol Cell Biol 4 2 140 156 1:CAS:528: DC%2BD3sXnsFaqtg%3D%3D 10.1038/nrm1014 12563291
    • (2003) Nat Rev Mol Cell Biol , vol.4 , Issue.2 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 27
    • 0031779478 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
    • 1:CAS:528:DyaK1cXjsFymurs%3D 10.1038/nm0698-713 9623982
    • O Molberg SN McAdam, et al. 1998 Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease Nat Med 4 6 713 717 1:CAS:528:DyaK1cXjsFymurs%3D 10.1038/nm0698-713 9623982
    • (1998) Nat Med , vol.4 , Issue.6 , pp. 713-717
    • Molberg, O.1    McAdam, S.N.2
  • 28
    • 0034743767 scopus 로고    scopus 로고
    • N(epsilon)(gamma-glutamyl)lysine in cerebrospinal fluid marks Alzheimer type and vascular dementia
    • 1:CAS:528:DC%2BD3MXjvFSjs7g%3D 10.1016/S0197-4580(01)00224-X 11378245
    • Z Nemes L Fesus, et al. 2001 N(epsilon)(gamma-glutamyl)lysine in cerebrospinal fluid marks Alzheimer type and vascular dementia Neurobiol Aging 22 3 403 406 1:CAS:528:DC%2BD3MXjvFSjs7g%3D 10.1016/S0197-4580(01)00224-X 11378245
    • (2001) Neurobiol Aging , vol.22 , Issue.3 , pp. 403-406
    • Nemes, Z.1    Fesus, L.2
  • 29
    • 0037039447 scopus 로고    scopus 로고
    • High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: Implications for celiac sprue
    • 1:CAS:528:DC%2BD3MXovV2gt7g%3D 10.1021/bi011715x 11772038
    • JL Piper GM Gray, et al. 2002 High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: implications for celiac sprue Biochemistry 41 1 386 393 1:CAS:528:DC%2BD3MXovV2gt7g%3D 10.1021/bi011715x 11772038
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 386-393
    • Piper, J.L.1    Gray, G.M.2
  • 30
    • 21244462254 scopus 로고    scopus 로고
    • Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: Importance of proline spacing and glutamine deamidation
    • 1:CAS:528:DC%2BD2MXltlyntbc%3D 15972656
    • SW Qiao E Bergseng, et al. 2005 Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: importance of proline spacing and glutamine deamidation J Immunol 175 1 254 261 1:CAS:528:DC%2BD2MXltlyntbc%3D 15972656
    • (2005) J Immunol , vol.175 , Issue.1 , pp. 254-261
    • Qiao, S.W.1    Bergseng, E.2
  • 31
    • 0037128650 scopus 로고    scopus 로고
    • Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis
    • 1:CAS:528:DC%2BD38Xitl2gt7c%3D 10.1084/jem.20011299 11901200
    • M Sardy S Karpati, et al. 2002 Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis J Exp Med 195 6 747 757 1:CAS:528:DC%2BD38Xitl2gt7c%3D 10.1084/jem.20011299 11901200
    • (2002) J Exp Med , vol.195 , Issue.6 , pp. 747-757
    • Sardy, M.1    Karpati, S.2
  • 32
    • 0037183929 scopus 로고    scopus 로고
    • Structural basis for gluten intolerance in celiac sprue
    • 1:CAS:528:DC%2BD38XntlWlt70%3D 10.1126/science.1074129 12351792
    • L Shan O Molberg, et al. 2002 Structural basis for gluten intolerance in celiac sprue Science 297 5590 2275 2279 1:CAS:528:DC%2BD38XntlWlt70%3D 10.1126/science.1074129 12351792
    • (2002) Science , vol.297 , Issue.5590 , pp. 2275-2279
    • Shan, L.1    Molberg, O.2
  • 33
    • 26844558196 scopus 로고    scopus 로고
    • Identification and analysis of multivalent proteolytically resistant peptides from gluten: Implications for celiac sprue
    • 1:CAS:528:DC%2BD2MXotVSksrw%3D 10.1021/pr050173t 16212427
    • L Shan SW Qiao, et al. 2005 Identification and analysis of multivalent proteolytically resistant peptides from gluten: implications for celiac sprue J Proteome Res 4 5 1732 1741 1:CAS:528:DC%2BD2MXotVSksrw%3D 10.1021/pr050173t 16212427
    • (2005) J Proteome Res , vol.4 , Issue.5 , pp. 1732-1741
    • Shan, L.1    Qiao, S.W.2
  • 34
    • 0036715684 scopus 로고    scopus 로고
    • Coeliac disease: Dissecting a complex inflammatory disorder
    • 1:CAS:528:DC%2BD38Xmslantro%3D 10.1038/nri885 12209133
    • LM Sollid 2002 Coeliac disease: dissecting a complex inflammatory disorder Nat Rev Immunol 2 9 647 655 1:CAS:528:DC%2BD38Xmslantro%3D 10.1038/nri885 12209133
    • (2002) Nat Rev Immunol , vol.2 , Issue.9 , pp. 647-655
    • Sollid, L.M.1
  • 35
    • 0031438699 scopus 로고    scopus 로고
    • Autoantibodies in coeliac disease: Tissue transglutaminase-guilt by association?
    • 1:CAS:528:DyaK1cXks1aktQ%3D%3D 10.1136/gut.41.6.851 9462222
    • LM Sollid O Molberg, et al. 1997 Autoantibodies in coeliac disease: tissue transglutaminase-guilt by association? Gut 41 6 851 852 1:CAS:528:DyaK1cXks1aktQ%3D%3D 10.1136/gut.41.6.851 9462222
    • (1997) Gut , vol.41 , Issue.6 , pp. 851-852
    • Sollid, L.M.1    Molberg, O.2
  • 36
    • 54049147249 scopus 로고    scopus 로고
    • The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions
    • 1:CAS:528:DC%2BD1cXht12kurrP 18793760
    • J Stamnaes B Fleckenstein, et al. 2008 The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions Biochim Biophys Acta 1784 11 1804 1811 1:CAS:528:DC%2BD1cXht12kurrP 18793760
    • (2008) Biochim Biophys Acta , vol.1784 , Issue.11 , pp. 1804-1811
    • Stamnaes, J.1    Fleckenstein, B.2
  • 37
    • 33745846379 scopus 로고    scopus 로고
    • Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: Identification of peptide substrates for TGASE 2 and Factor XIIIA
    • 1:CAS:528:DC%2BD28XmtFyksLc%3D 10.1074/jbc.M513538200 16636049
    • Y Sugimura M Hosono, et al. 2006 Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: identification of peptide substrates for TGASE 2 and Factor XIIIA J Biol Chem 281 26 17699 17706 1:CAS:528:DC%2BD28XmtFyksLc%3D 10.1074/jbc.M513538200 16636049
    • (2006) J Biol Chem , vol.281 , Issue.26 , pp. 17699-17706
    • Sugimura, Y.1    Hosono, M.2
  • 38
    • 0031762794 scopus 로고    scopus 로고
    • Tissue transglutaminase autoantibody enzyme-linked immunosorbent assay in detecting celiac disease
    • 1:CAS:528:DyaK1cXotVWmurg%3D 10.1016/S0016-5085(98)70008-3 9834257
    • S Sulkanen T Halttunen, et al. 1998 Tissue transglutaminase autoantibody enzyme-linked immunosorbent assay in detecting celiac disease Gastroenterology 115 6 1322 1328 1:CAS:528:DyaK1cXotVWmurg%3D 10.1016/S0016-5085(98)70008-3 9834257
    • (1998) Gastroenterology , vol.115 , Issue.6 , pp. 1322-1328
    • Sulkanen, S.1    Halttunen, T.2
  • 39
    • 0038271789 scopus 로고    scopus 로고
    • Transglutaminase 2-/- mice reveal a phagocytosis-associated crosstalk between macrophages and apoptotic cells
    • 1:CAS:528:DC%2BD3sXlt1WqsLc%3D 10.1073/pnas.0832466100 12810961
    • Z Szondy Z Sarang, et al. 2003 Transglutaminase 2-/- mice reveal a phagocytosis-associated crosstalk between macrophages and apoptotic cells Proc Natl Acad Sci USA 100 13 7812 7817 1:CAS:528:DC%2BD3sXlt1WqsLc%3D 10.1073/pnas.0832466100 12810961
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.13 , pp. 7812-7817
    • Szondy, Z.1    Sarang, Z.2
  • 40
    • 0023940746 scopus 로고
    • The biology and enzymology of eukaryotic protein acylation
    • 1:CAS:528:DyaL1cXlsVClt7o%3D 10.1146/annurev.bi.57.070188.000441 3052287
    • DA Towler JI Gordon, et al. 1988 The biology and enzymology of eukaryotic protein acylation Annu Rev Biochem 57 69 99 1:CAS:528:DyaL1cXlsVClt7o%3D 10.1146/annurev.bi.57.070188.000441 3052287
    • (1988) Annu Rev Biochem , vol.57 , pp. 69-99
    • Towler, D.A.1    Gordon, J.I.2
  • 41
    • 0037018095 scopus 로고    scopus 로고
    • Specificity of tissue transglutaminase explains cereal toxicity in celiac disease
    • 1:CAS:528:DC%2BD38XitV2nu7g%3D 10.1084/jem.20012028 11877487
    • LW Vader A de Ru, et al. 2002 Specificity of tissue transglutaminase explains cereal toxicity in celiac disease J Exp Med 195 5 643 649 1:CAS:528:DC%2BD38XitV2nu7g%3D 10.1084/jem.20012028 11877487
    • (2002) J Exp Med , vol.195 , Issue.5 , pp. 643-649
    • Vader, L.W.1    De Ru, A.2
  • 42
    • 0036082955 scopus 로고    scopus 로고
    • The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides
    • 1:CAS:528:DC%2BD38Xlt12gsrY%3D 10.1053/gast.2002.33606 12055577
    • W Vader Y Kooy, et al. 2002 The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides Gastroenterology 122 7 1729 1737 1:CAS:528:DC%2BD38Xlt12gsrY%3D 10.1053/gast.2002.33606 12055577
    • (2002) Gastroenterology , vol.122 , Issue.7 , pp. 1729-1737
    • Vader, W.1    Kooy, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.