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Volumn 38, Issue , 2005, Pages 158-173

Tissue transglutaminase and celiac disease

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIGEN; DIAGNOSTIC AGENT; EPITOPE; GLIADIN; GUANINE NUCLEOTIDE BINDING PROTEIN; MONOCLONAL ANTIBODY; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TRANSGLUTAMINASE 2;

EID: 14544277082     PISSN: 00796263     EISSN: None     Source Type: Book Series    
DOI: 10.1159/000084239     Document Type: Review
Times cited : (4)

References (79)
  • 2
    • 0036715684 scopus 로고    scopus 로고
    • Coeliac disease: Dissecting a complex inflammatory disorder
    • Sollid LM: Coeliac disease: Dissecting a complex inflammatory disorder. Nat Rev Immunol 2002;2:647-655.
    • (2002) Nat Rev Immunol , vol.2 , pp. 647-655
    • Sollid, L.M.1
  • 6
    • 0024492512 scopus 로고
    • Evidence for a primary association of celiac disease to a particular HLA-DQ alpha/beta heterodimer
    • Sollid LM, Markussen G, Ek J, Gjerde H, Vartdal F, Thorsby E: Evidence for a primary association of celiac disease to a particular HLA-DQ alpha/beta heterodimer. J Exp Med 1989;169:345-350.
    • (1989) J Exp Med , vol.169 , pp. 345-350
    • Sollid, L.M.1    Markussen, G.2    Ek, J.3    Gjerde, H.4    Vartdal, F.5    Thorsby, E.6
  • 7
    • 0034121187 scopus 로고    scopus 로고
    • Molecular basis of celiac disease
    • Sollid LM: Molecular basis of celiac disease. Annu Rev Immunol 2000;18:53-81.
    • (2000) Annu Rev Immunol , vol.18 , pp. 53-81
    • Sollid, L.M.1
  • 10
    • 1042290533 scopus 로고    scopus 로고
    • Tissue transglutaminase-the key player in celiac disease: A review
    • Reif S, Lerner A: Tissue transglutaminase-the key player in celiac disease: a review. Autoimmun Rev 2004;3:40-45.
    • (2004) Autoimmun Rev , vol.3 , pp. 40-45
    • Reif, S.1    Lerner, A.2
  • 11
    • 0027325292 scopus 로고
    • Follow-up of patients positive in reticulin and gliadin antibody tests with normal small bowel biopsy findings
    • Collin P, Helin H, Maki M, Hallstrom O, Karvonen AL: Follow-up of patients positive in reticulin and gliadin antibody tests with normal small bowel biopsy findings. Scand J Gastroenterol 1993;28:595-598.
    • (1993) Scand J Gastroenterol , vol.28 , pp. 595-598
    • Collin, P.1    Helin, H.2    Maki, M.3    Hallstrom, O.4    Karvonen, A.L.5
  • 13
    • 0032759334 scopus 로고    scopus 로고
    • Recombinant human tissue transglutaminase ELISA for the diagnosis of gluten-sensitive enteropathy
    • Sardy M, Odenthal U, Karpati S, Paulsson M, Smyth N: Recombinant human tissue transglutaminase ELISA for the diagnosis of gluten-sensitive enteropathy. Clin Chem 1999;45:2142-2149.
    • (1999) Clin Chem , vol.45 , pp. 2142-2149
    • Sardy, M.1    Odenthal, U.2    Karpati, S.3    Paulsson, M.4    Smyth, N.5
  • 17
    • 0000576117 scopus 로고
    • Diagnostic criteria in coeliac disease
    • Meeuwisse G: Diagnostic criteria in coeliac disease. Acta Paediatr Scand 1970;59:461-463.
    • (1970) Acta Paediatr Scand , vol.59 , pp. 461-463
    • Meeuwisse, G.1
  • 18
    • 0018675777 scopus 로고
    • The diagnosis of coeliac disease. A commentary on the current practices of members of the European Society for Paediatric Gastroenterology and Nutrition (ESPGAN)
    • McNeish AS, Harms HK, Rey J, Shmerling DH, Visakorpi JK, Walker-Smith JA: The diagnosis of coeliac disease. A commentary on the current practices of members of the European Society for Paediatric Gastroenterology and Nutrition (ESPGAN). Arch Dis Child 1979;54:783-786.
    • (1979) Arch Dis Child , vol.54 , pp. 783-786
    • McNeish, A.S.1    Harms, H.K.2    Rey, J.3    Shmerling, D.H.4    Visakorpi, J.K.5    Walker-Smith, J.A.6
  • 19
    • 0017680149 scopus 로고
    • The ε-(γ-glutamyl)lysine crosslink and the catalytic role of transglutaminases
    • Folk JE, Finlayson JS: The ε-(γ-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv Protein Chem 1977;31:1-133.
    • (1977) Adv Protein Chem , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 20
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • Achyuthan KE, Greenberg CS: Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. J Biol Chem 1987;262:1901-1906.
    • (1987) J Biol Chem , vol.262 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 22
    • 2642536093 scopus 로고    scopus 로고
    • Tissue transglutaminase has intrinsic kinase activity: Identification of transglutaminase 2 as an insulin-like growth factor binding protein-3 kinase
    • Mishra S, Murphy LJ: Tissue transglutaminase has intrinsic kinase activity: Identification of transglutaminase 2 as an insulin-like growth factor binding protein-3 kinase. J Biol Chem 2004;279:23863-23868.
    • (2004) J Biol Chem , vol.279 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 23
    • 0034093354 scopus 로고    scopus 로고
    • Protein crosslinking in assembly and remodelling of extracellular matrices: The role of transglutaminases
    • Aeschlimann D, Thomazy V: Protein crosslinking in assembly and remodelling of extracellular matrices: The role of transglutaminases. Connect Tissue Res 2000;41:1-27.
    • (2000) Connect Tissue Res , vol.41 , pp. 1-27
    • Aeschlimann, D.1    Thomazy, V.2
  • 24
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin M, Casadio R, Bergamini CM: Transglutaminases: Nature's biological glues. Biochem J 2002;368:377-396.
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 25
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L, Graham RM: Transglutaminases: Crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 2003;4:140-156.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 26
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • Lesort M, Attanavanich K, Zhang J, Johnson GV: Distinct nuclear localization and activity of tissue transglutaminase. J Biol Chem 1998;273:11991-11994.
    • (1998) J Biol Chem , vol.273 , pp. 11991-11994
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.4
  • 27
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov SS, Krylov D, Fleischman LF, Belkin AM: Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J Cell Biol 2000;148:825-838.
    • (2000) J Cell Biol , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 28
    • 0037053359 scopus 로고    scopus 로고
    • Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts
    • Balklava Z, Verderio E, Collighan R, Gross S, Adams J, Griffin M: Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts. J Biol Chem 2002;277:16567-16575.
    • (2002) J Biol Chem , vol.277 , pp. 16567-16575
    • Balklava, Z.1    Verderio, E.2    Collighan, R.3    Gross, S.4    Adams, J.5    Griffin, M.6
  • 32
    • 0028907482 scopus 로고
    • Isolation and characterization of the human tissue transglutaminase gene promoter
    • Lu S, Saydak M, Gentile V, Stein JP, Davies PJA: Isolation and characterization of the human tissue transglutaminase gene promoter. J Biol Chem 1995;270:9748-9756.
    • (1995) J Biol Chem , vol.270 , pp. 9748-9756
    • Lu, S.1    Saydak, M.2    Gentile, V.3    Stein, J.P.4    Davies, P.J.A.5
  • 33
    • 0030051022 scopus 로고    scopus 로고
    • Identification and characterization of a versatile retinoid response element (retinoid acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter
    • Nagy L, Saydak M, Shipley N, Lu S, Basilion JP, Yan ZH, Syka P, Chandraratna RAS, Stein JP, Heyman RA, Davies PJA: Identification and characterization of a versatile retinoid response element (retinoid acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter. J Biol Chem 1996;271:4355-4365.
    • (1996) J Biol Chem , vol.271 , pp. 4355-4365
    • Nagy, L.1    Saydak, M.2    Shipley, N.3    Lu, S.4    Basilion, J.P.5    Yan, Z.H.6    Syka, P.7    Chandraratna, R.A.S.8    Stein, J.P.9    Heyman, R.A.10    Davies, P.J.A.11
  • 34
    • 0032557461 scopus 로고    scopus 로고
    • Identification of a transforming growth factor-β1/bone morphogenetic protein 4 (TGFβ1/BMP4) response element within the mouse tissue transglutaminase gene promoter
    • Ritter SJ, Davies PJA: Identification of a transforming growth factor-β1/bone morphogenetic protein 4 (TGFβ1/BMP4) response element within the mouse tissue transglutaminase gene promoter. J Biol Chem 1998;273:12798-12806.
    • (1998) J Biol Chem , vol.273 , pp. 12798-12806
    • Ritter, S.J.1    Davies, P.J.A.2
  • 37
    • 0034743940 scopus 로고    scopus 로고
    • Increases in renal ε-(γ-glutamyl)-lysine crosslinks result from compartment-specific changes in tissue transglutaminase in early experimental diabetic nephropathy: Pathologic implications
    • Skill NJ, Griffin M, El Nahas AM, Sanai T, Haylor JL, Fisher M, Jamie MF, Mould NN, Johnson TS: Increases in renal ε-(γ-glutamyl)-lysine crosslinks result from compartment-specific changes in tissue transglutaminase in early experimental diabetic nephropathy: Pathologic implications. Lab Invest 2001;81:705-716.
    • (2001) Lab Invest , vol.81 , pp. 705-716
    • Skill, N.J.1    Griffin, M.2    El Nahas, A.M.3    Sanai, T.4    Haylor, J.L.5    Fisher, M.6    Jamie, M.F.7    Mould, N.N.8    Johnson, T.S.9
  • 38
    • 0043124302 scopus 로고    scopus 로고
    • Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source
    • Gross SR, Balklava Z, Griffin M: Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source. J Invest Dermatol 2003;121:412-423.
    • (2003) J Invest Dermatol , vol.121 , pp. 412-423
    • Gross, S.R.1    Balklava, Z.2    Griffin, M.3
  • 39
    • 0029815574 scopus 로고    scopus 로고
    • Peptide binding characteristics of the coeliac disease-associated DQ (α1 *0501, β1 *0201) molecule
    • Van de Wal Y, Kooy YMC, Drijfhout JW, Amons R, Koning F: Peptide binding characteristics of the coeliac disease-associated DQ (α1 *0501, β1 *0201) molecule. Immunogenetics 1996;44:246-253.
    • (1996) Immunogenetics , vol.44 , pp. 246-253
    • Van De Wal, Y.1    Kooy, Y.M.C.2    Drijfhout, J.W.3    Amons, R.4    Koning, F.5
  • 41
    • 0021969767 scopus 로고
    • Human jejunal transglutaminase: Demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coelaic disease
    • Brace SE, Bjarnason I, Peters TJ: Human jejunal transglutaminase: Demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coelaic disease. Clin Sci 1985;68:573-579.
    • (1985) Clin Sci , vol.68 , pp. 573-579
    • Brace, S.E.1    Bjarnason, I.2    Peters, T.J.3
  • 43
    • 1642447710 scopus 로고    scopus 로고
    • Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease
    • USA
    • Kim C-Y, Quarsten H, Bergseng E, Khosla C, Sollid LM: Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. Proc Natl Acad Sci USA 2004;101:4175-4179.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 4175-4179
    • Kim, C.-Y.1    Quarsten, H.2    Bergseng, E.3    Khosla, C.4    Sollid, L.M.5
  • 44
    • 0035019083 scopus 로고    scopus 로고
    • T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase
    • Molberg O, McAdam S, Lundin KEA, Kristiansen C, Arentz-Hansen H, Kett K, Sollid LM: T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase. Eur J Immunol 2001;31:1317-1323.
    • (2001) Eur J Immunol , vol.31 , pp. 1317-1323
    • Molberg, O.1    McAdam, S.2    Lundin, K.E.A.3    Kristiansen, C.4    Arentz-Hansen, H.5    Kett, K.6    Sollid, L.M.7
  • 45
    • 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
    • Fleckenstein B, Molberg O, Qiao SW, Schmid DG, von der Mulbe F, Elgstoen K, Jung G, Sollid LM: 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 2002;277:34106-34116.
    • (2002) J Biol Chem , vol.277 , pp. 34106-34116
    • Fleckenstein, B.1    Molberg, O.2    Qiao, S.W.3    Schmid, D.G.4    Von Der Mulbe, F.5    Elgstoen, K.6    Jung, G.7    Sollid, L.M.8
  • 46
    • 0032577588 scopus 로고    scopus 로고
    • The rho-deamidating cytotoxic necrotizing factor 1 from escherichia coli possesses transglutaminase activity: Cysteine 866 and histidine 881 are essential for enzyme activity
    • Schmidt G, Selzer J, Lerm M, Aktories K: The rho-deamidating cytotoxic necrotizing factor 1 from escherichia coli possesses transglutaminase activity: Cysteine 866 and histidine 881 are essential for enzyme activity. J Biol Chem 1998;273:13669-13674.
    • (1998) J Biol Chem , vol.273 , pp. 13669-13674
    • Schmidt, G.1    Selzer, J.2    Lerm, M.3    Aktories, K.4
  • 47
    • 0037462498 scopus 로고    scopus 로고
    • Gluten peptides and celiac disease
    • Koning F, Vader W: Gluten peptides and celiac disease. Science 2003;299:513-515.
    • (2003) Science , vol.299 , pp. 513-515
    • Koning, F.1    Vader, W.2
  • 51
    • 0034066695 scopus 로고    scopus 로고
    • In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope
    • Anderson RP, Degano P, Godkin AJ, Jewell DP, Hill AVS: In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope. Nat Med 2000;6:337-342.
    • (2000) Nat Med , vol.6 , pp. 337-342
    • Anderson, R.P.1    Degano, P.2    Godkin, A.J.3    Jewell, D.P.4    Hill, A.V.S.5
  • 57
    • 0032528813 scopus 로고    scopus 로고
    • Cutting edge: Selective deamidation but tissue transglutaminase strongly enhances gliadin-specific T cell reactivity
    • Van der Wal Y, Kooy Y, van Veelen P, Pena S, Mearin L, Papadopulos G, Koning F: Cutting edge: Selective deamidation but tissue transglutaminase strongly enhances gliadin-specific T cell reactivity. J Immunol 1998;161:1585-1588.
    • (1998) J Immunol , vol.161 , pp. 1585-1588
    • Van Der Wal, Y.1    Kooy, Y.2    Van Veelen, P.3    Pena, S.4    Mearin, L.5    Papadopulos, G.6    Koning, F.7
  • 59
    • 0031438699 scopus 로고    scopus 로고
    • Autoantibodies in celiac disease: Tissue transglutaminase-guilt by association?
    • Sollid LM, Molberg O, McAdam S, Lundin KE: Autoantibodies in celiac disease: Tissue transglutaminase-guilt by association? Gut 1997;41:851-852.
    • (1997) Gut , vol.41 , pp. 851-852
    • Sollid, L.M.1    Molberg, O.2    McAdam, S.3    Lundin, K.E.4
  • 60
    • 0031749237 scopus 로고    scopus 로고
    • Exposing gliadin as a tasty food for lymphocytes
    • Schuppan D, Dieterich W, Riecken EO: Exposing gliadin as a tasty food for lymphocytes. Nat Med 1998;3:666-667.
    • (1998) Nat Med , vol.3 , pp. 666-667
    • Schuppan, D.1    Dieterich, W.2    Riecken, E.O.3
  • 62
    • 0041355325 scopus 로고    scopus 로고
    • Proteomics identification of acyl-acceptor and acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line. Implications for celiac disease
    • Orrù S, Caputo I, D'Amato A, Ruoppolo M, Esposito C: Proteomics identification of acyl-acceptor and acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line. Implications for celiac disease. J Biol Chem 2003;278:31766-31773.
    • (2003) J Biol Chem , vol.278 , pp. 31766-31773
    • Orrù, S.1    Caputo, I.2    D'Amato, A.3    Ruoppolo, M.4    Esposito, C.5
  • 64
    • 0029078178 scopus 로고
    • The humoral immune system in celiac disease
    • Maki M: The humoral immune system in celiac disease. Baillieres Clin Gastroenterol 1995;9:231-249.
    • (1995) Baillieres Clin Gastroenterol , vol.9 , pp. 231-249
    • Maki, M.1
  • 66
    • 0035215592 scopus 로고    scopus 로고
    • Increased levels of IgA antibodies against desmin in children with coeliac disease
    • Teesalu K, Uibo O, Kalkkinen N, Janmey P, Uibo R: Increased levels of IgA antibodies against desmin in children with coeliac disease. Int Arch Allergy Immunol 2001;126:157-166.
    • (2001) Int Arch Allergy Immunol , vol.126 , pp. 157-166
    • Teesalu, K.1    Uibo, O.2    Kalkkinen, N.3    Janmey, P.4    Uibo, R.5
  • 68
    • 1842332757 scopus 로고    scopus 로고
    • Identification of cytoplasmic actin as an abunant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis
    • Nemes Z, Adany R, Balas M, Boross P, Fesus L: Identification of cytoplasmic actin as an abunant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis. J Biol Chem 1996;272:20577-20583.
    • (1996) J Biol Chem , vol.272 , pp. 20577-20583
    • Nemes, Z.1    Adany, R.2    Balas, M.3    Boross, P.4    Fesus, L.5
  • 69
    • 0034805874 scopus 로고    scopus 로고
    • Identification of protein substrates for transglutaminase in Caenorhabditis elegans
    • Madi A, Kele Z, Janaky T, Punyiczki M, Fesus L: Identification of protein substrates for transglutaminase in Caenorhabditis elegans. Biochem Biophys Res Commun 2001;283:964-968.
    • (2001) Biochem Biophys Res Commun , vol.283 , pp. 964-968
    • Madi, A.1    Kele, Z.2    Janaky, T.3    Punyiczki, M.4    Fesus, L.5
  • 70
    • 0033578417 scopus 로고    scopus 로고
    • Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II
    • Feng JF, Readon M, Yadav SP, Im MJ: Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II. Biochemistry 1999;38:10743-10749.
    • (1999) Biochemistry , vol.38 , pp. 10743-10749
    • Feng, J.F.1    Readon, M.2    Yadav, S.P.3    Im, M.J.4
  • 73
    • 1442299238 scopus 로고    scopus 로고
    • The role of the immune response against tissue transglutaminase in the pathogenesis of coeliac disease
    • Freitag T, Schulze-Koops H, Niedobitek G, Melino G, Schuppan D: The role of the immune response against tissue transglutaminase in the pathogenesis of coeliac disease. Autoimmun Rev 2004;3:13-20.
    • (2004) Autoimmun Rev , vol.3 , pp. 13-20
    • Freitag, T.1    Schulze-Koops, H.2    Niedobitek, G.3    Melino, G.4    Schuppan, D.5
  • 75
    • 0242329754 scopus 로고    scopus 로고
    • Autoantibodies of patients with coeliac disease are insufficient to block tissue transglutaminase activity
    • Dieterich W, Trapp D, Esslinger B, Leidenberger M, Piper J, Hahn E, Schuppan D: Autoantibodies of patients with coeliac disease are insufficient to block tissue transglutaminase activity. Gut 2003;52:1562-1566.
    • (2003) Gut , vol.52 , pp. 1562-1566
    • Dieterich, W.1    Trapp, D.2    Esslinger, B.3    Leidenberger, M.4    Piper, J.5    Hahn, E.6    Schuppan, D.7
  • 76
    • 0033011434 scopus 로고    scopus 로고
    • Serum Immunoglobulin A from patients with celiac disease inhibits human T84 intestinal crypt epithelial cell differentiation
    • Halttunen T, Mäki M: Serum Immunoglobulin A from patients with celiac disease inhibits human T84 intestinal crypt epithelial cell differentiation. Gastroenterology 1999;116:566-572.
    • (1999) Gastroenterology , vol.116 , pp. 566-572
    • Halttunen, T.1    Mäki, M.2
  • 78
    • 33644632497 scopus 로고    scopus 로고
    • Antibodies against Type 2 transglutaminase modulate actin rearrangements and cell cycle in several cell line
    • Caputo I, Barone MV, Troncone R, Auricchio S, Esposito C: Antibodies against Type 2 transglutaminase modulate actin rearrangements and cell cycle in several cell line. J Pediatr Gastroenterol Nutr 2004;39 (suppl 3):S775.
    • (2004) J Pediatr Gastroenterol Nutr , vol.39 , Issue.3 SUPPL.
    • Caputo, I.1    Barone, M.V.2    Troncone, R.3    Auricchio, S.4    Esposito, C.5
  • 79
    • 0037352689 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of gluten peptide analogs as selective inhibitors of human tissue transglutaminase
    • Hausch F, Halttunen T, Maki M, Khosla C: Design, synthesis, and evaluation of gluten peptide analogs as selective inhibitors of human tissue transglutaminase. Chem Biol 2003;10:225-231.
    • (2003) Chem Biol , vol.10 , pp. 225-231
    • Hausch, F.1    Halttunen, T.2    Maki, M.3    Khosla, C.4


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