메뉴 건너뛰기




Volumn 342, Issue 1, 2005, Pages 1-10

Tools for the detection and quantitation of protein transglutamination

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY;

EID: 20444375830     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.10.015     Document Type: Review
Times cited : (23)

References (91)
  • 1
    • 0000719659 scopus 로고
    • An enzymically catalyzed incorporation of amines into proteins
    • N.K. Sarkar, D.D. Clarke, and H. Waelsch An enzymically catalyzed incorporation of amines into proteins Biochim. Biophys. Acta 25 1957 451 452
    • (1957) Biochim. Biophys. Acta , vol.25 , pp. 451-452
    • Sarkar, N.K.1    Clarke, D.D.2    Waelsch, H.3
  • 2
    • 2042456659 scopus 로고
    • Incorporation of histamine into liver protein in vivo
    • I. Wajda, M. Ginsburg, and H. Waelsch Incorporation of histamine into liver protein in vivo Naturwissenschaften 191 1961 1204 1205
    • (1961) Naturwissenschaften , vol.191 , pp. 1204-1205
    • Wajda, I.1    Ginsburg, M.2    Waelsch, H.3
  • 3
    • 0000096019 scopus 로고
    • Transpeptidation mechanism in blood clotting
    • L. Lorand, K. Konishi, and A. Jacobsen Transpeptidation mechanism in blood clotting Nature 194 1962 1148 1149
    • (1962) Nature , vol.194 , pp. 1148-1149
    • Lorand, L.1    Konishi, K.2    Jacobsen, A.3
  • 4
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Cross-linking enzymes with pleiotropic functions
    • L. Lorand, and R.M. Graham Transglutaminases: cross-linking enzymes with pleiotropic functions Nat. Rev. Mol. Cell. Biol. 4 2003 140 156
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 5
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • M. Griffin, R. Casadio, and C.M. Bergamini Transglutaminases: nature's biological glues Biochem. J. 368 2002 377 396
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 6
    • 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
    • P. Grenard, M.K. Bates, and D. Aeschlimann 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 2001 33066 33078
    • (2001) J. Biol. Chem. , vol.276 , pp. 33066-33078
    • Grenard, P.1    Bates, M.K.2    Aeschlimann, D.3
  • 8
    • 0022374208 scopus 로고
    • Activation of transglutaminase and production of protein-bound γ-glutamylhistamine in stimulated mouse mast cells
    • L. Fésüs, E.F. Szucs, K.E. Barrett, D.D. Metcalfe, and J.E. Folk Activation of transglutaminase and production of protein-bound γ-glutamylhistamine in stimulated mouse mast cells J. Biol. Chem. 260 1985 13771 13778
    • (1985) J. Biol. Chem. , vol.260 , pp. 13771-13778
    • Fésüs, L.1    Szucs, E.F.2    Barrett, K.E.3    Metcalfe, D.D.4    Folk, J.E.5
  • 10
    • 0033587684 scopus 로고    scopus 로고
    • A novel function for transglutaminase 1: Attachment of long-chain ω-hydroxyceramides to involucrin by ester bond formation
    • Z. Nemes, L.N. Marekov, L. Fésüs, and P.M. Steinert A novel function for transglutaminase 1: attachment of long-chain ω- hydroxyceramides to involucrin by ester bond formation Proc. Natl. Acad. Sci. USA 96 1999 8402 8407
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8402-8407
    • Nemes, Z.1    Marekov, L.N.2    Fésüs, L.3    Steinert, P.M.4
  • 11
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • C.S. Greenberg, P.J. Birckbichler, and R.H. Rice Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues FASEB J. 5 1991 3071 3077
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 12
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • L. Fesus, and M. Piacentini Transglutaminase 2: an enigmatic enzyme with diverse functions Trends Biochem. Sci. 27 2002 534 539
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 13
    • 0031905860 scopus 로고    scopus 로고
    • An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity
    • R. Chandrashekar, N. Tsuji, T. Morales, V. Ozols, and K. Mehta An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity Proc. Natl. Acad. Sci. USA 95 1998 531 536
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 531-536
    • Chandrashekar, R.1    Tsuji, N.2    Morales, T.3    Ozols, V.4    Mehta, K.5
  • 14
    • 0037423294 scopus 로고    scopus 로고
    • The Caenorhabditis elegans ERp60 homolog protein disulfide isomerase-3 has disulfide isomerase and transglutaminase-like cross-linking activity and is involved in the maintenance of body morphology
    • S.C. Eschenlauer, and A.P. Page The Caenorhabditis elegans ERp60 homolog protein disulfide isomerase-3 has disulfide isomerase and transglutaminase-like cross-linking activity and is involved in the maintenance of body morphology J. Biol. Chem. 278 2003 4227 4237
    • (2003) J. Biol. Chem. , vol.278 , pp. 4227-4237
    • Eschenlauer, S.C.1    Page, A.P.2
  • 15
    • 0345505270 scopus 로고    scopus 로고
    • Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity
    • B. Blaskó, A. Mádi, and L. Fésüs Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity Biochem. Biophys. Res. Commun. 303 2003 1142 1147
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 1142-1147
    • Blaskó, B.1    Mádi, A.2    Fésüs, L.3
  • 18
    • 0020974221 scopus 로고
    • Post-translational pathways for generating ε (γ-glutamyl) lysine cross-links
    • L. Lorand Post-translational pathways for generating ε (γ-glutamyl)lysine cross-links Ann. NY Acad. Sci. 421 1983 10 27
    • (1983) Ann. NY Acad. Sci. , vol.421 , pp. 10-27
    • Lorand, L.1
  • 19
    • 1342304083 scopus 로고    scopus 로고
    • Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium
    • B. Ahvazi, K.M. Boeshans, W. Idler, U. Baxa, P.M. Steinert, and F. Rastinejad Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium J. Biol. Chem. 279 2004 7180 7192
    • (2004) J. Biol. Chem. , vol.279 , pp. 7180-7192
    • Ahvazi, B.1    Boeshans, K.M.2    Idler, W.3    Baxa, U.4    Steinert, P.M.5    Rastinejad, F.6
  • 20
    • 2942705910 scopus 로고    scopus 로고
    • Crystal structure of transglutaminase 3 in complex with GMP: Structural basis for nucleotide specificity
    • B. Ahvazi, K.M. Boeshans, and P.M. Steinert Crystal structure of transglutaminase 3 in complex with GMP: structural basis for nucleotide specificity J. Biol. Chem. 2004
    • (2004) J. Biol. Chem.
    • Ahvazi, B.1    Boeshans, K.M.2    Steinert, P.M.3
  • 23
    • 0029088221 scopus 로고
    • The importance of the GTP-binding protein tissue transglutaminase in the regulation of cell cycle progression
    • S. Mian, S. el Alaoui, J. Lawry, V. Gentile, P.J. Davies, and M. Griffin The importance of the GTP-binding protein tissue transglutaminase in the regulation of cell cycle progression FEBS Lett. 370 1995 27 31
    • (1995) FEBS Lett. , vol.370 , pp. 27-31
    • Mian, S.1    El Alaoui, S.2    Lawry, J.3    Gentile, V.4    Davies, P.J.5    Griffin, M.6
  • 24
    • 0041570280 scopus 로고    scopus 로고
    • Kinetic analysis of the action of tissue transglutaminase on peptide and protein substrates
    • A. Case, and R.L. Stein Kinetic analysis of the action of tissue transglutaminase on peptide and protein substrates Biochemistry 42 2003 9466 9481
    • (2003) Biochemistry , vol.42 , pp. 9466-9481
    • Case, A.1    Stein, R.L.2
  • 25
    • 78651168687 scopus 로고
    • Structural requirements of specific substrates for guinea pig liver transglutaminase
    • J.E. Folk, and P.W. Cole Structural requirements of specific substrates for guinea pig liver transglutaminase J. Biol. Chem. 240 1965 2951 2960
    • (1965) J. Biol. Chem. , vol.240 , pp. 2951-2960
    • Folk, J.E.1    Cole, P.W.2
  • 27
    • 0027516486 scopus 로고
    • Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes
    • D. Aeschlimann, A. Wetterwald, H. Fleisch, and M. Paulsson Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes J. Cell Biol. 120 1993 1461 1470
    • (1993) J. Cell Biol. , vol.120 , pp. 1461-1470
    • Aeschlimann, D.1    Wetterwald, A.2    Fleisch, H.3    Paulsson, M.4
  • 28
    • 1842332757 scopus 로고    scopus 로고
    • Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis
    • Z. Nemes Jr., R. Ádany, M. Balázs, P. Boross, and L. Fésüs Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis J. Biol. Chem. 272 1997 20577 20583
    • (1997) J. Biol. Chem. , vol.272 , pp. 20577-20583
    • Nemes Jr., Z.1    Ádany, R.2    Balázs, M.3    Boross, P.4    Fésüs, L.5
  • 31
    • 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
    • S. Orru, I. Caputo, A. D'Amato, M. Ruoppolo, and C. Esposito 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. 278 2003 31766 31773
    • (2003) J. Biol. Chem. , vol.278 , pp. 31766-31773
    • Orru, S.1    Caputo, I.2    D'Amato, A.3    Ruoppolo, M.4    Esposito, C.5
  • 32
    • 0035988899 scopus 로고    scopus 로고
    • Gliadin is a good substrate of several transglutaminases: Possible implication in the pathogenesis of coeliac disease
    • H. Skovbjerg, O. Noren, D. Anthonsen, J. Moller, and H. Sjoström Gliadin is a good substrate of several transglutaminases: possible implication in the pathogenesis of coeliac disease Scand. J. Gastroenterol. 37 2002 812 817
    • (2002) Scand. J. Gastroenterol. , vol.37 , pp. 812-817
    • Skovbjerg, H.1    Noren, O.2    Anthonsen, D.3    Moller, J.4    Sjoström, H.5
  • 33
    • 0026660488 scopus 로고
    • A microtiter plate transglutaminase assay utilizing 5-(biotinamido) pentylamine as substrate
    • T.F. Slaughter, K.E. Achyuthan, T.S. Lai, and C.S. Greenberg A microtiter plate transglutaminase assay utilizing 5-(biotinamido)pentylamine as substrate Anal. Biochem. 205 1992 166 171
    • (1992) Anal. Biochem. , vol.205 , pp. 166-171
    • Slaughter, T.F.1    Achyuthan, K.E.2    Lai, T.S.3    Greenberg, C.S.4
  • 34
    • 0036235139 scopus 로고    scopus 로고
    • Immunohistological analysis of transglutaminase factor XIIIA expression in mouse embryonic growth plate
    • M.V. Nurminskaya, and T.F. Linsenmayer Immunohistological analysis of transglutaminase factor XIIIA expression in mouse embryonic growth plate J. Orthop. Res. 20 2002 575 578
    • (2002) J. Orthop. Res. , vol.20 , pp. 575-578
    • Nurminskaya, M.V.1    Linsenmayer, T.F.2
  • 36
    • 0036783252 scopus 로고    scopus 로고
    • Detection of in situ activation of transglutaminase during apoptosis: Correlation with the cell cycle phase by multiparameter flow and laser scanning cytometry
    • J. Grabarek, B. Ardelt, J. Kunicki, and Z. Darzynkiewicz Detection of in situ activation of transglutaminase during apoptosis: correlation with the cell cycle phase by multiparameter flow and laser scanning cytometry Cytometry 49 2002 83 89
    • (2002) Cytometry , vol.49 , pp. 83-89
    • Grabarek, J.1    Ardelt, B.2    Kunicki, J.3    Darzynkiewicz, Z.4
  • 39
    • 0025823541 scopus 로고
    • Cross-linking of laminin-nidogen complexes by tissue transglutaminase. a novel mechanism for basement membrane stabilization
    • D. Aeschlimann, and M. Paulsson Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization J. Biol. Chem. 266 1991 15308 15317
    • (1991) J. Biol. Chem. , vol.266 , pp. 15308-15317
    • Aeschlimann, D.1    Paulsson, M.2
  • 40
    • 0030863635 scopus 로고    scopus 로고
    • Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis
    • S. Oliverio, A. Amendola, F. Di Sano, M.G. Farrace, L. Fésüs, Z. Nemes, L. Piredda, A. Spinedi, and M. Piacentini Tissue transglutaminase- dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis Mol. Cell. Biol. 17 1997 6040 6048
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6040-6048
    • Oliverio, S.1    Amendola, A.2    Di Sano, F.3    Farrace, M.G.4    Fésüs, L.5    Nemes, Z.6    Piredda, L.7    Spinedi, A.8    Piacentini, M.9
  • 42
    • 0035150905 scopus 로고    scopus 로고
    • A simple assay and histochemical localization of transglutaminase activity using a derivative of green fluorescent protein as substrate
    • Y. Furutani, A. Kato, M. Notoya, M.A. Ghoneim, and S. Hirose A simple assay and histochemical localization of transglutaminase activity using a derivative of green fluorescent protein as substrate J. Histochem. Cytochem. 49 2001 247 258
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 247-258
    • Furutani, Y.1    Kato, A.2    Notoya, M.3    Ghoneim, M.A.4    Hirose, S.5
  • 43
    • 0027166195 scopus 로고
    • Regulation of transglutaminase activity by GTP in digitonin permeabilized Yoshida tumor cells
    • C.M. Bergamini, M. Signorini, L. Caselli, and P. Melandri Regulation of transglutaminase activity by GTP in digitonin permeabilized Yoshida tumor cells Biochem. Mol. Biol. Int. 30 1993 727 732
    • (1993) Biochem. Mol. Biol. Int. , vol.30 , pp. 727-732
    • Bergamini, C.M.1    Signorini, M.2    Caselli, L.3    Melandri, P.4
  • 44
    • 2342424238 scopus 로고    scopus 로고
    • Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides
    • B. Fleckenstein, S.W. Qiao, M.R. Larsen, G. Jung, P. Roepstorff, and L.M. Sollid Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides J. Biol. Chem. 279 2004 17607 17616
    • (2004) J. Biol. Chem. , vol.279 , pp. 17607-17616
    • Fleckenstein, B.1    Qiao, S.W.2    Larsen, M.R.3    Jung, G.4    Roepstorff, P.5    Sollid, L.M.6
  • 45
    • 0033574631 scopus 로고    scopus 로고
    • Involucrin cross-linking by transglutaminase 1. Binding to membranes directs residue specificity
    • Z. Nemes, L.N. Marekov, and P.M. Steinert Involucrin cross-linking by transglutaminase 1. Binding to membranes directs residue specificity J. Biol. Chem. 274 1999 11013 11021
    • (1999) J. Biol. Chem. , vol.274 , pp. 11013-11021
    • Nemes, Z.1    Marekov, L.N.2    Steinert, P.M.3
  • 46
    • 0029967884 scopus 로고    scopus 로고
    • The transglutaminase 1 enzyme is variably acylated by myristate and palmitate during differentiation in epidermal keratinocytes
    • P.M. Steinert, S.Y. Kim, S.I. Chung, and L.N. Marekov The transglutaminase 1 enzyme is variably acylated by myristate and palmitate during differentiation in epidermal keratinocytes J. Biol. Chem. 271 1996 26242 26250
    • (1996) J. Biol. Chem. , vol.271 , pp. 26242-26250
    • Steinert, P.M.1    Kim, S.Y.2    Chung, S.I.3    Marekov, L.N.4
  • 47
    • 1242272870 scopus 로고    scopus 로고
    • Expression of cytosolic and membrane associated tissue transglutaminase in rat hepatic stellate cells and its upregulation during transdifferentiation to myofibroblasts in culture
    • C. Schnabel, I. Sawitza, C.G. Tag, B. Lahme, A.M. Gressner, and K. Breitkopf Expression of cytosolic and membrane associated tissue transglutaminase in rat hepatic stellate cells and its upregulation during transdifferentiation to myofibroblasts in culture Hepatol. Res. 28 2004 140 145
    • (2004) Hepatol. Res. , vol.28 , pp. 140-145
    • Schnabel, C.1    Sawitza, I.2    Tag, C.G.3    Lahme, B.4    Gressner, A.M.5    Breitkopf, K.6
  • 48
    • 0028946284 scopus 로고
    • Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: Identification of osteonectin as a major glutaminyl substrate
    • D. Aeschlimann, O. Kaupp, and M. Paulsson Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: identification of osteonectin as a major glutaminyl substrate J. Cell Biol. 129 1995 881 892
    • (1995) J. Cell Biol. , vol.129 , pp. 881-892
    • Aeschlimann, D.1    Kaupp, O.2    Paulsson, M.3
  • 49
    • 0034743940 scopus 로고    scopus 로고
    • Increases in renal ε-(γ-glutamyl)-lysine cross-links result from compartment-specific changes in tissue transglutaminase in early experimental diabetic nephropathy: Pathologic implications
    • N.J. Skill, M. Griffin, A.M. El Nahas, T. Sanai, J.L. Haylor, M. Fisher, M.F. Jamie, N.N. Mould, and T.S. Johnson Increases in renal ε-(γ- glutamyl)-lysine cross-links result from compartment-specific changes in tissue transglutaminase in early experimental diabetic nephropathy: pathologic implications Lab. Invest. 81 2001 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
  • 51
    • 4644336256 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the formation of alpha-synuclein cross-links in Parkinson's disease
    • G. Andringa, K.Y. Lam, M. Chegary, X. Wang, T.N. Chase, and M.C. Bennett Tissue transglutaminase catalyzes the formation of alpha-synuclein cross-links in Parkinson's disease FASEB J. 18 2004 932 934
    • (2004) FASEB J. , vol.18 , pp. 932-934
    • Andringa, G.1    Lam, K.Y.2    Chegary, M.3    Wang, X.4    Chase, T.N.5    Bennett, M.C.6
  • 52
    • 0036135523 scopus 로고    scopus 로고
    • Protein cross-linking, tissue transglutaminase, alternative splicing and neurodegeneration
    • B.A. Citron, Z. Suo, K. SantaCruz, P.J. Davies, F. Qin, and B.W. Festoff Protein cross-linking, tissue transglutaminase, alternative splicing and neurodegeneration Neurochem. Int. 40 2002 69 78
    • (2002) Neurochem. Int. , vol.40 , pp. 69-78
    • Citron, B.A.1    Suo, Z.2    Santacruz, K.3    Davies, P.J.4    Qin, F.5    Festoff, B.W.6
  • 54
    • 0037452813 scopus 로고    scopus 로고
    • Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies
    • E. Junn, R.D. Ronchetti, M.M. Quezado, S.Y. Kim, and M.M. Mouradian Tissue transglutaminase-induced aggregation of alpha-synuclein: implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies Proc. Natl. Acad. Sci. USA 100 2003 2047 2052
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2047-2052
    • Junn, E.1    Ronchetti, R.D.2    Quezado, M.M.3    Kim, S.Y.4    Mouradian, M.M.5
  • 56
    • 0036134831 scopus 로고    scopus 로고
    • Transglutaminase bonds in neurofibrillary tangles and paired helical filament tau early in Alzheimer's disease
    • S.M. Singer, G.M. Zainelli, M.A. Norlund, J.M. Lee, and N.A. Muma Transglutaminase bonds in neurofibrillary tangles and paired helical filament tau early in Alzheimer's disease Neurochem. Int. 40 2002 17 30
    • (2002) Neurochem. Int. , vol.40 , pp. 17-30
    • Singer, S.M.1    Zainelli, G.M.2    Norlund, M.A.3    Lee, J.M.4    Muma, N.A.5
  • 58
    • 0025811049 scopus 로고
    • ε (γ-glutamyl) lysine in benign and malignant human breast lesions: An immunohistochemical study
    • ε (γ-glutamyl) lysine in benign and malignant human breast lesions: an immunohistochemical study Int. J. Cancer 48 1991 215 220
    • (1991) Int. J. Cancer , vol.48 , pp. 215-220
    • Roch, A.M.1    Noel, P.2    El Alaoui, S.3    Charlot, C.4    Quash, G.5
  • 59
    • 1542375349 scopus 로고    scopus 로고
    • Immunoblot analysis reveals that isopeptide antibodies do not specifically recognize the ε-(γ-glutamyl)lysine bonds formed by transglutaminase activity
    • G.V. Johnson, and R. LeShoure Jr. Immunoblot analysis reveals that isopeptide antibodies do not specifically recognize the ε-(γ- glutamyl)lysine bonds formed by transglutaminase activity J. Neurosci. Methods 134 2004 151 158
    • (2004) J. Neurosci. Methods , vol.134 , pp. 151-158
    • Johnson, G.V.1    LeShoure Jr., R.2
  • 61
    • 4944267025 scopus 로고    scopus 로고
    • Cross-linking of ubiquitin, HSP27, parkin, and α-synuclein by γ-glutamyl-ε-lysine bonds in Alzheimer's neurofibrillary tangles
    • Z. Nemes, B. Devreese, P.M. Steinert, J. Van Beeumen, and L. Fésüs Cross-linking of ubiquitin, HSP27, parkin, and α-synuclein by γ-glutamyl-ε-lysine bonds in Alzheimer's neurofibrillary tangles FASEB J. 18 2004 1135 1137
    • (2004) FASEB J. , vol.18 , pp. 1135-1137
    • Nemes, Z.1    Devreese, B.2    Steinert, P.M.3    Van Beeumen, J.4    Fésüs, L.5
  • 63
    • 0025778292 scopus 로고
    • Degradation of cells dying by apoptosis leads to accumulation of ε(γ-glutamyl)lysine isodipeptide in culture fluid and blood
    • L. Fésüs, E. Tarcsa, N. Kedei, F. Autuori, and M. Piacentini Degradation of cells dying by apoptosis leads to accumulation of ε(γ-glutamyl)lysine isodipeptide in culture fluid and blood FEBS Lett. 284 1991 109 112
    • (1991) FEBS Lett. , vol.284 , pp. 109-112
    • Fésüs, L.1    Tarcsa, E.2    Kedei, N.3    Autuori, F.4    Piacentini, M.5
  • 67
    • 0025196159 scopus 로고
    • Determination of ε(γ-glutamyl)lysine cross-link in proteins using phenylisothiocyanate derivatization and high-pressure liquid chromatographic separation
    • E. Tarcsa, and L. Fésüs Determination of ε(γ- glutamyl)lysine cross-link in proteins using phenylisothiocyanate derivatization and high-pressure liquid chromatographic separation Anal. Biochem. 186 1990 135 140
    • (1990) Anal. Biochem. , vol.186 , pp. 135-140
    • Tarcsa, E.1    Fésüs, L.2
  • 68
    • 0029050246 scopus 로고
    • The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope
    • P.M. Steinert, and L.N. Marekov The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope J. Biol. Chem. 270 1995 17702 17711
    • (1995) J. Biol. Chem. , vol.270 , pp. 17702-17711
    • Steinert, P.M.1    Marekov, L.N.2
  • 69
    • 0032852974 scopus 로고    scopus 로고
    • Rapid, single-step procedure for the identification of transglutaminase-mediated isopeptide cross-links in amino acid digests
    • M.L. Miller, and G.V. Johnson Rapid, single-step procedure for the identification of transglutaminase-mediated isopeptide cross-links in amino acid digests J. Chromatogr. B Biomed. Sci. Appl. 732 1999 65 72
    • (1999) J. Chromatogr. B Biomed. Sci. Appl. , vol.732 , pp. 65-72
    • Miller, M.L.1    Johnson, G.V.2
  • 70
    • 0026612802 scopus 로고
    • 726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes
    • 726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes J. Biol. Chem. 267 1992 11316 11321
    • (1992) J. Biol. Chem. , vol.267 , pp. 11316-11321
    • Aeschlimann, D.1    Paulsson, M.2    Mann, K.3
  • 71
    • 0032579370 scopus 로고    scopus 로고
    • Identification of transglutaminase-reactive residues in S100A11
    • N.A. Robinson, and R.L. Eckert Identification of transglutaminase- reactive residues in S100A11 J. Biol. Chem. 273 1998 2721 2728
    • (1998) J. Biol. Chem. , vol.273 , pp. 2721-2728
    • Robinson, N.A.1    Eckert, R.L.2
  • 75
    • 0034658383 scopus 로고    scopus 로고
    • Unique substrate specificities of two adjacent glutamine residues in EAQQIVM for transglutaminase: Identification and characterization of the reaction products by electrospray ionization tandem mass spectrometry
    • H. Sato, N. Yamada, N. Shimba, and Y. Takahara Unique substrate specificities of two adjacent glutamine residues in EAQQIVM for transglutaminase: identification and characterization of the reaction products by electrospray ionization tandem mass spectrometry Anal. Biochem. 281 2000 68 76
    • (2000) Anal. Biochem. , vol.281 , pp. 68-76
    • Sato, H.1    Yamada, N.2    Shimba, N.3    Takahara, Y.4
  • 76
    • 0034651790 scopus 로고    scopus 로고
    • Activation of rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizing toxin
    • M. Masuda, L. Betancourt, T. Matsuzawa, T. Kashimoto, T. Takao, Y. Shimonishi, and Y. Horiguchi Activation of rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizing toxin EMBO J. 19 2000 521 530
    • (2000) EMBO J. , vol.19 , pp. 521-530
    • Masuda, M.1    Betancourt, L.2    Matsuzawa, T.3    Kashimoto, T.4    Takao, T.5    Shimonishi, Y.6    Horiguchi, Y.7
  • 77
    • 0035894272 scopus 로고    scopus 로고
    • Broadband detection electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry to reveal enzymatically and chemically induced deamidation reactions within peptides
    • D.G. Schmid, F.D. von der Mulbe, B. Fleckenstein, T. Weinschenk, and G. Jung Broadband detection electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry to reveal enzymatically and chemically induced deamidation reactions within peptides Anal. Chem. 73 2001 6008 6013
    • (2001) Anal. Chem. , vol.73 , pp. 6008-6013
    • Schmid, D.G.1    Von Der Mulbe, F.D.2    Fleckenstein, B.3    Weinschenk, T.4    Jung, G.5
  • 78
    • 0036136789 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase
    • S. Orru, M. Ruoppolo, S. Francese, L. Vitagliano, G. Marino, and C. Esposito Identification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase Protein Sci. 11 2002 137 146
    • (2002) Protein Sci. , vol.11 , pp. 137-146
    • Orru, S.1    Ruoppolo, M.2    Francese, S.3    Vitagliano, L.4    Marino, G.5    Esposito, C.6
  • 79
    • 0037216488 scopus 로고    scopus 로고
    • Structural characterization of transglutaminase-catalyzed cross-linking between glyceraldehyde 3-phosphate dehydrogenase and polyglutamine repeats
    • M. Ruoppolo, S. Orru, S. Francese, I. Caputo, and C. Esposito Structural characterization of transglutaminase-catalyzed cross-linking between glyceraldehyde 3-phosphate dehydrogenase and polyglutamine repeats Protein Sci. 12 2003 170 179
    • (2003) Protein Sci. , vol.12 , pp. 170-179
    • Ruoppolo, M.1    Orru, S.2    Francese, S.3    Caputo, I.4    Esposito, C.5
  • 80
    • 0037778904 scopus 로고    scopus 로고
    • Enzymatic modification of self-assembled peptide structures with tissue transglutaminase
    • J.H. Collier, and P.B. Messersmith Enzymatic modification of self-assembled peptide structures with tissue transglutaminase Bioconjug. Chem. 14 2003 748 755
    • (2003) Bioconjug. Chem. , vol.14 , pp. 748-755
    • Collier, J.H.1    Messersmith, P.B.2
  • 81
    • 0039004404 scopus 로고    scopus 로고
    • Cholesterol 3-sulfate interferes with cornified envelope assembly by diverting transglutaminase 1 activity from the formation of cross-links and esters to the hydrolysis of glutamine
    • Z. Nemes, M. Demény, L.N. Marekov, L. Fésüs, and P.M. Steinert Cholesterol 3-sulfate interferes with cornified envelope assembly by diverting transglutaminase 1 activity from the formation of cross-links and esters to the hydrolysis of glutamine J. Biol. Chem. 275 2000 2636 2646
    • (2000) J. Biol. Chem. , vol.275 , pp. 2636-2646
    • Nemes, Z.1    Demény, M.2    Marekov, L.N.3    Fésüs, L.4    Steinert, P.M.5
  • 83
    • 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
    • B. Fleckenstein, O. Molberg, S.W. Qiao, D.G. Schmid, F. vonder Mulbe, K. Elgstoen, G. Jung, and L.M. Sollid 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 2002 34109 34116
    • (2002) J. Biol. Chem. , vol.277 , pp. 34109-34116
    • Fleckenstein, B.1    Molberg, O.2    Qiao, S.W.3    Schmid, D.G.4    Vonder Mulbe, F.5    Elgstoen, K.6    Jung, G.7    Sollid, L.M.8
  • 85
    • 0037039447 scopus 로고    scopus 로고
    • High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: Implications for celiac sprue
    • J.L. Piper, G.M. Gray, and C. Khosla High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: implications for celiac sprue Biochemistry 41 2002 386 393
    • (2002) Biochemistry , vol.41 , pp. 386-393
    • Piper, J.L.1    Gray, G.M.2    Khosla, C.3
  • 88
    • 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
    • G. Schmidt, J. Selzer, M. Lerm, and K. Aktories 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. 273 1998 13669 13674
    • (1998) J. Biol. Chem. , vol.273 , pp. 13669-13674
    • Schmidt, G.1    Selzer, J.2    Lerm, M.3    Aktories, K.4
  • 89
    • 0018103258 scopus 로고
    • Cross-linking amino acids in collagen and elastin
    • R.B. Rucker, and J. Murray Cross-linking amino acids in collagen and elastin Am. J. Clin. Nutr. 31 1978 1221 1236
    • (1978) Am. J. Clin. Nutr. , vol.31 , pp. 1221-1236
    • Rucker, R.B.1    Murray, J.2
  • 90
    • 0020423677 scopus 로고
    • Retinoic acid induces transglutaminase activity but inhibits cornification of cultured epidermal cells
    • S.H. Yuspa, T. Ben, and P. Steinert Retinoic acid induces transglutaminase activity but inhibits cornification of cultured epidermal cells J. Biol. Chem. 257 1982 9906 9908
    • (1982) J. Biol. Chem. , vol.257 , pp. 9906-9908
    • Yuspa, S.H.1    Ben, T.2    Steinert, P.3
  • 91
    • 0001029638 scopus 로고
    • Microderivatization of peptides by placing a fixed positive charge at the N-terminus to modify high energy collision fragmentation
    • J.E. Vath, and K. Biemann Microderivatization of peptides by placing a fixed positive charge at the N-terminus to modify high energy collision fragmentation Int. J. Mass Spectrom. Ion Process. 100 1990 287 299
    • (1990) Int. J. Mass Spectrom. Ion Process. , vol.100 , pp. 287-299
    • Vath, J.E.1    Biemann, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.