메뉴 건너뛰기




Volumn 135, Issue 1-2, 2005, Pages 122-133

Tissue transglutaminase during mouse central nervous system development: Lack of alternative RNA processing and implications for its role(s) in murine models of neurotrauma and neurodegeneration

Author keywords

Alternative splicing; Cross linking; TGM2

Indexed keywords

MESSENGER RNA; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 18044379187     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbrainres.2004.12.009     Document Type: Article
Times cited : (10)

References (118)
  • 1
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • K.E. Achyuthan, and C.S. Greenberg Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity J. Biol. Chem. 262 1987 1901 1906
    • (1987) J. Biol. Chem. , vol.262 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 2
    • 0034839336 scopus 로고    scopus 로고
    • Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: A role in TGFbeta-dependent matrix deposition
    • S.S. Akimov, and A.M. Belkin Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: a role in TGFbeta-dependent matrix deposition J. Cell Sci. 114 2001 2989 3000
    • (2001) J. Cell Sci. , vol.114 , pp. 2989-3000
    • Akimov, S.S.1    Belkin, A.M.2
  • 3
    • 0029923459 scopus 로고    scopus 로고
    • Induction of tissue transglutaminase in rat superior cervical sympathetic ganglia following in vitro stimulation of retinoic acid
    • M. Ando, M. Yamauchi, K. Fujita, M. Kakita, and Y. Nagata Induction of tissue transglutaminase in rat superior cervical sympathetic ganglia following in vitro stimulation of retinoic acid Neurosci. Res. 24 1996 357 362
    • (1996) Neurosci. Res. , vol.24 , pp. 357-362
    • Ando, M.1    Yamauchi, M.2    Fujita, K.3    Kakita, M.4    Nagata, Y.5
  • 4
    • 0035823548 scopus 로고    scopus 로고
    • Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis
    • M.A. Antonyak, U.S. Singh, D.A. Lee, J.E. Boehm, C. Combs, M.M. Zgola, R.L. Page, and R.A. Cerione Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis J. Biol. Chem. 276 2001 33582 33587
    • (2001) J. Biol. Chem. , vol.276 , pp. 33582-33587
    • Antonyak, M.A.1    Singh, U.S.2    Lee, D.A.3    Boehm, J.E.4    Combs, C.5    Zgola, M.M.6    Page, R.L.7    Cerione, R.A.8
  • 5
    • 0031015814 scopus 로고    scopus 로고
    • The association of tissue transglutaminase with human recombinant tau results in the formation of insoluble filamentous structures
    • D.M. Appelt, and B.J. Balin The association of tissue transglutaminase with human recombinant tau results in the formation of insoluble filamentous structures Brain Res. 745 1997 21 31
    • (1997) Brain Res. , vol.745 , pp. 21-31
    • Appelt, D.M.1    Balin, B.J.2
  • 6
    • 3242861077 scopus 로고    scopus 로고
    • Localization of transglutaminase in hippocampal neurons: Implications for Alzheimer's disease
    • D.M. Appelt, G.C. Kopen, L.J. Boyne, and B.J. Balin Localization of transglutaminase in hippocampal neurons: implications for Alzheimer's disease J. Histochem. Cytochem. 44 1996 1421 1427
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 1421-1427
    • Appelt, D.M.1    Kopen, G.C.2    Boyne, L.J.3    Balin, B.J.4
  • 7
    • 1642336449 scopus 로고    scopus 로고
    • Validity of mouse models for the study of tissue transglutaminase in neurodegenerative diseases
    • C.D. Bailey, R.M. Graham, N. Nanda, P.J. Davies, and G.V. Johnson Validity of mouse models for the study of tissue transglutaminase in neurodegenerative diseases Mol. Cell. Neurosci. 25 2004 493 503
    • (2004) Mol. Cell. Neurosci. , vol.25 , pp. 493-503
    • Bailey, C.D.1    Graham, R.M.2    Nanda, N.3    Davies, P.J.4    Johnson, G.V.5
  • 9
    • 0037036409 scopus 로고    scopus 로고
    • Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb
    • J.E. Boehm, U. Singh, C. Combs, M.A. Antonyak, and R.A. Cerione Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb J. Biol. Chem. 277 2002 20127 20130
    • (2002) J. Biol. Chem. , vol.277 , pp. 20127-20130
    • Boehm, J.E.1    Singh, U.2    Combs, C.3    Antonyak, M.A.4    Cerione, R.A.5
  • 11
    • 0037019816 scopus 로고    scopus 로고
    • Specific methylation of the CpG-rich domains in the promoter of the human tissue transglutaminase gene
    • T. Cacciamani, S. Virgili, M. Centurelli, E. Bertoli, T. Eremenko, and P. Volpe Specific methylation of the CpG-rich domains in the promoter of the human tissue transglutaminase gene Gene 297 2002 103 112
    • (2002) Gene , vol.297 , pp. 103-112
    • Cacciamani, T.1    Virgili, S.2    Centurelli, M.3    Bertoli, E.4    Eremenko, T.5    Volpe, P.6
  • 14
    • 0035900751 scopus 로고    scopus 로고
    • Induction of cell cycle arrest and morphological differentiation by Nurr1 and retinoids in dopamine MN9D cells
    • D.S. Castro, E. Hermanson, B. Joseph, A. Wallen, P. Aarnisalo, A. Heller, and T. Perlmann Induction of cell cycle arrest and morphological differentiation by Nurr1 and retinoids in dopamine MN9D cells J. Biol. Chem. 276 2001 43277 43284
    • (2001) J. Biol. Chem. , vol.276 , pp. 43277-43284
    • Castro, D.S.1    Hermanson, E.2    Joseph, B.3    Wallen, A.4    Aarnisalo, P.5    Heller, A.6    Perlmann, T.7
  • 15
    • 0032866851 scopus 로고    scopus 로고
    • Tissue transglutaminase: An enzyme with a split personality
    • J.S. Chen, and K. Mehta Tissue transglutaminase: an enzyme with a split personality Int. J. Biochem. Cell Biol. 31 1999 817 836
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 817-836
    • Chen, J.S.1    Mehta, K.2
  • 16
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • P. Chomczynski, and N. Sacchi Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction Anal. Biochem. 162 1987 156 159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 17
    • 0031782683 scopus 로고    scopus 로고
    • Serpin=serine protease-like complexes within neurofilament conglomerates of motoneurons in amyotrophic lateral sclerosis
    • S.M. Chou, A. Taniguchi, H.S. Wang, and B.W. Festoff Serpin=serine protease-like complexes within neurofilament conglomerates of motoneurons in amyotrophic lateral sclerosis J. Neurol. Sci. 160 Suppl. 1 1998 S73 S79
    • (1998) J. Neurol. Sci. , vol.160 , Issue.SUPPL. 1
    • Chou, S.M.1    Taniguchi, A.2    Wang, H.S.3    Festoff, B.W.4
  • 18
    • 0034990512 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells
    • W. Chun, M. Lesort, J. Tucholski, P.W. Faber, M.E. MacDonald, C.A. Ross, and G.V. Johnson Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells Neurobiol. Dis. 8 2001 391 404
    • (2001) Neurobiol. Dis. , vol.8 , pp. 391-404
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Faber, P.W.4    MacDonald, M.E.5    Ross, C.A.6    Johnson, G.V.7
  • 19
    • 0035795406 scopus 로고    scopus 로고
    • Tissue transglutaminase does not contribute to the formation of mutant huntingtin aggregates
    • W. Chun, M. Lesort, J. Tucholski, C.A. Ross, and G.V. Johnson Tissue transglutaminase does not contribute to the formation of mutant huntingtin aggregates J. Cell Biol. 153 2001 25 34
    • (2001) J. Cell Biol. , vol.153 , pp. 25-34
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Ross, C.A.4    Johnson, G.V.5
  • 20
    • 0031564833 scopus 로고    scopus 로고
    • Apoptotic, injury-induced cell death in cultured mouse murine motor neurons
    • B.A. Citron, S.X. Zhang, I.V. Smirnova, and B.W. Festoff Apoptotic, injury-induced cell death in cultured mouse murine motor neurons Neurosci. Lett. 230 1997 25 28
    • (1997) Neurosci. Lett. , vol.230 , pp. 25-28
    • Citron, B.A.1    Zhang, S.X.2    Smirnova, I.V.3    Festoff, B.W.4
  • 21
    • 0033664631 scopus 로고    scopus 로고
    • Rapid upregulation of caspase-3 in rat spinal cord after injury: MRNA, protein, and cellular localization correlates with apoptotic cell death
    • B.A. Citron, P.M. Arnold, C. Sebastian, F. Qin, S. Malladi, S. Ameenuddin, M.E. Landis, and B.W. Festoff Rapid upregulation of caspase-3 in rat spinal cord after injury: mRNA, protein, and cellular localization correlates with apoptotic cell death Exp. Neurol. 166 2000 213 226
    • (2000) Exp. Neurol. , vol.166 , pp. 213-226
    • Citron, B.A.1    Arnold, P.M.2    Sebastian, C.3    Qin, F.4    Malladi, S.5    Ameenuddin, S.6    Landis, M.E.7    Festoff, B.W.8
  • 22
    • 0034309870 scopus 로고    scopus 로고
    • Regulation of the dual function tissue transglutaminase/Galpha(h) during murine neuromuscular development: Gene and enzyme isoform expression
    • B.A. Citron, E.J. Gregory, D.S. Steigerwalt, F. Qin, and B.W. Festoff Regulation of the dual function tissue transglutaminase/Galpha(h) during murine neuromuscular development: gene and enzyme isoform expression Neurochem. Int. 37 2000 337 349
    • (2000) Neurochem. Int. , vol.37 , pp. 337-349
    • Citron, B.A.1    Gregory, E.J.2    Steigerwalt, D.S.3    Qin, F.4    Festoff, B.W.5
  • 23
    • 0035793583 scopus 로고    scopus 로고
    • Intron-exon swapping of transglutaminase mRNA and neuronal tau aggregation in Alzheimer's disease
    • B.A. Citron, K.S. SantaCruz, P.J. Davies, and B.W. Festoff Intron-exon swapping of transglutaminase mRNA and neuronal tau aggregation in Alzheimer's disease J. Biol. Chem. 276 2001 3295 3301
    • (2001) J. Biol. Chem. , vol.276 , pp. 3295-3301
    • Citron, B.A.1    Santacruz, K.S.2    Davies, P.J.3    Festoff, B.W.4
  • 24
    • 0036135523 scopus 로고    scopus 로고
    • Protein crosslinking, tissue transglutaminase, alternative splicing and neurodegeneration
    • B.A. Citron, Z. Suo, K. SantaCruz, P.J. Davies, F. Qin, and B.W. Festoff Protein crosslinking, 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
  • 25
    • 0033012131 scopus 로고    scopus 로고
    • Pathogenesis of inclusion bodies in (CAG)n/Qn-expansion diseases with special reference to the role of tissue transglutaminase and to selective vulnerability
    • A.J. Cooper, K.F. Sheu, J.R. Burke, W.J. Strittmatter, V. Gentile, G. Peluso, and J.P. Blass Pathogenesis of inclusion bodies in (CAG)n/Qn-expansion diseases with special reference to the role of tissue transglutaminase and to selective vulnerability J. Neurochem. 72 1999 889 899
    • (1999) J. Neurochem. , vol.72 , pp. 889-899
    • Cooper, A.J.1    Sheu, K.F.2    Burke, J.R.3    Strittmatter, W.J.4    Gentile, V.5    Peluso, G.6    Blass, J.P.7
  • 26
    • 0024406903 scopus 로고
    • Hereditary disorders of the red cell membrane skeleton
    • K.A. Davies, and S.E. Lux Hereditary disorders of the red cell membrane skeleton Trends Genet. 5 1989 222 227
    • (1989) Trends Genet. , vol.5 , pp. 222-227
    • Davies, K.A.1    Lux, S.E.2
  • 27
    • 0021827570 scopus 로고
    • Retinoic acid-induced expression of tissue transglutaminase in human promyelocytic leukemia (HL-60) cells
    • P.J. Davies, M.P. Murtaugh, W.T. Moore Jr., G.S. Johnson, and D. Lucas Retinoic acid-induced expression of tissue transglutaminase in human promyelocytic leukemia (HL-60) cells J. Biol. Chem. 260 1985 5166 5174
    • (1985) J. Biol. Chem. , vol.260 , pp. 5166-5174
    • Davies, P.J.1    Murtaugh, M.P.2    Moore Jr., W.T.3    Johnson, G.S.4    Lucas, D.5
  • 28
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • V. De Laurenzi, and G. Melino Gene disruption of tissue transglutaminase Mol. Cell. Biol. 21 2001 148 155
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2
  • 30
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • J. Devereux, P. Haeberli, and O. Smithies A comprehensive set of sequence analysis programs for the VAX Nucleic Acids Res. 12 1984 387 395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 31
    • 0033120650 scopus 로고    scopus 로고
    • Essential roles of retinoic acid signaling in interdigital apoptosis and control of BMP-7 expression in mouse autopods
    • V. Dupe, N.B. Ghyselinck, V. Thomazy, L. Nagy, P.J. Davies, P. Chambon, and M. Mark Essential roles of retinoic acid signaling in interdigital apoptosis and control of BMP-7 expression in mouse autopods Dev. Biol. 208 1999 30 43
    • (1999) Dev. Biol. , vol.208 , pp. 30-43
    • Dupe, V.1    Ghyselinck, N.B.2    Thomazy, V.3    Nagy, L.4    Davies, P.J.5    Chambon, P.6    Mark, M.7
  • 34
    • 0032708946 scopus 로고    scopus 로고
    • Tissue transglutaminase is a caspase substrate during apoptosis. Cleavage causes loss of transamidating function and is a biochemical marker of caspase 3 activation
    • M. Fabbi, D. Marimpietri, S. Martini, C. Brancolini, A. Amoresano, A. Scaloni, A. Bargellesi, and E. Cosulich Tissue transglutaminase is a caspase substrate during apoptosis. Cleavage causes loss of transamidating function and is a biochemical marker of caspase 3 activation Cell Death Differ. 6 1999 992 1001
    • (1999) Cell Death Differ. , vol.6 , pp. 992-1001
    • Fabbi, M.1    Marimpietri, D.2    Martini, S.3    Brancolini, C.4    Amoresano, A.5    Scaloni, A.6    Bargellesi, A.7    Cosulich, E.8
  • 35
    • 0027480066 scopus 로고
    • Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase
    • F. Facchiano, F. Benfenati, F. Valtorta, and A. Luini Covalent modification of synapsin I by a tetanus toxin-activated transglutaminase J. Biol. Chem. 268 1993 4588 4591
    • (1993) J. Biol. Chem. , vol.268 , pp. 4588-4591
    • Facchiano, F.1    Benfenati, F.2    Valtorta, F.3    Luini, A.4
  • 36
    • 85030794792 scopus 로고    scopus 로고
    • Transglutaminases and their roles in development, degeneration, injury and regeneration of the nervous system
    • (in press).
    • B.W. Festoff, U. Singh, Transglutaminases and their roles in development, degeneration, injury and regeneration of the nervous system, Prog. Neurobiol. (in press).
    • Prog. Neurobiol.
    • Festoff, B.W.1    Singh, U.2
  • 37
    • 0034186091 scopus 로고    scopus 로고
    • Motor neuron cell death in wobbler mutant mice follows overexpression of the G-protein-coupled, protease-activated receptor for thrombin
    • B.W. Festoff, M.R. D'Andrea, B.A. Citron, R.M. Salcedo, I.V. Smirnova, and P. Andrade-Gordon Motor neuron cell death in wobbler mutant mice follows overexpression of the G-protein-coupled, protease-activated receptor for thrombin Mol. Med. 6 2000 410 429
    • (2000) Mol. Med. , vol.6 , pp. 410-429
    • Festoff, B.W.1    D'Andrea, M.R.2    Citron, B.A.3    Salcedo, R.M.4    Smirnova, I.V.5    Andrade-Gordon, P.6
  • 38
    • 0034796349 scopus 로고    scopus 로고
    • Plasticity and stabilization of neuromuscular and CNS synapses: Interactions between thrombin protease signaling pathways and tissue transglutaminase
    • B.W. Festoff, Z. Suo, and B.A. Citron Plasticity and stabilization of neuromuscular and CNS synapses: interactions between thrombin protease signaling pathways and tissue transglutaminase Int. Rev. Cytol. 211 2001 153 177
    • (2001) Int. Rev. Cytol. , vol.211 , pp. 153-177
    • Festoff, B.W.1    Suo, Z.2    Citron, B.A.3
  • 39
    • 0036312393 scopus 로고    scopus 로고
    • Injury-induced "switch" from GTP-regulated to novel GTP-independent isoform of tissue transglutaminase in the rat spinal cord
    • B.W. Festoff, K. SantaCruz, P.M. Arnold, C.T. Sebastian, P.J. Davies, and B.A. Citron Injury-induced "switch" from GTP-regulated to novel GTP-independent isoform of tissue transglutaminase in the rat spinal cord J. Neurochem. 81 2002 708 718
    • (2002) J. Neurochem. , vol.81 , pp. 708-718
    • Festoff, B.W.1    Santacruz, K.2    Arnold, P.M.3    Sebastian, C.T.4    Davies, P.J.5    Citron, B.A.6
  • 40
    • 0029862039 scopus 로고    scopus 로고
    • Transglutaminase induction by various cell death and apoptosis pathways
    • L. Fesus, A. Madi, Z. Balajthy, Z. Nemes, and Z. Szondy Transglutaminase induction by various cell death and apoptosis pathways Experientia 52 1996 942 949
    • (1996) Experientia , vol.52 , pp. 942-949
    • Fesus, L.1    Madi, A.2    Balajthy, Z.3    Nemes, Z.4    Szondy, Z.5
  • 41
    • 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
  • 42
    • 0030690093 scopus 로고    scopus 로고
    • Organization and structure of the human tissue transglutaminase gene
    • B.M. Fraij, and R.A. Gonzales Organization and structure of the human tissue transglutaminase gene Biochim. Biophys. Acta 1354 1997 65 71
    • (1997) Biochim. Biophys. Acta , vol.1354 , pp. 65-71
    • Fraij, B.M.1    Gonzales, R.A.2
  • 43
    • 0026499522 scopus 로고
    • A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue
    • B.M. Fraij, P.J. Birckbichler, M.K. Patterson Jr., K.N. Lee, and R.A. Gonzales A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue J. Biol. Chem. 267 1992 22616 22623
    • (1992) J. Biol. Chem. , vol.267 , pp. 22616-22623
    • Fraij, B.M.1    Birckbichler, P.J.2    Patterson Jr., M.K.3    Lee, K.N.4    Gonzales, R.A.5
  • 44
    • 0029937589 scopus 로고    scopus 로고
    • A third human tissue transglutaminase homologue as a result of alternative gene transcripts
    • B.M. Fraij, and R.A. Gonzales A third human tissue transglutaminase homologue as a result of alternative gene transcripts Biochim. Biophys. Acta 1306 1996 63 74
    • (1996) Biochim. Biophys. Acta , vol.1306 , pp. 63-74
    • Fraij, B.M.1    Gonzales, R.A.2
  • 45
    • 0025822888 scopus 로고
    • Protein cross-linking by transglutaminase induced in long-term potentiation in the Ca1 region of hippocampal slices
    • P. Friedrich, L. Fesus, E. Tarcsa, and G. Czeh Protein cross-linking by transglutaminase induced in long-term potentiation in the Ca1 region of hippocampal slices Neuroscience 43 1991 331 334
    • (1991) Neuroscience , vol.43 , pp. 331-334
    • Friedrich, P.1    Fesus, L.2    Tarcsa, E.3    Czeh, G.4
  • 46
    • 0142121512 scopus 로고    scopus 로고
    • Experimental brain inflammation and neurodegeneration as model of Alzheimer's disease: Protective effects of selective COX-2 inhibitors
    • M.G. Giovannini, C. Scali, C. Prosperi, A. Bellucci, G. Pepeu, and F. Casamenti Experimental brain inflammation and neurodegeneration as model of Alzheimer's disease: protective effects of selective COX-2 inhibitors Int. J. Immunopathol. Pharmacol. 16 2003 31 40
    • (2003) Int. J. Immunopathol. Pharmacol. , vol.16 , pp. 31-40
    • Giovannini, M.G.1    Scali, C.2    Prosperi, C.3    Bellucci, A.4    Pepeu, G.5    Casamenti, F.6
  • 47
    • 0034906754 scopus 로고    scopus 로고
    • Alternative RNA splicing in the nervous system
    • P.J. Grabowski, and D.L. Black Alternative RNA splicing in the nervous system Prog. Neurobiol. 65 2001 289 308
    • (2001) Prog. Neurobiol. , vol.65 , pp. 289-308
    • Grabowski, P.J.1    Black, D.L.2
  • 48
    • 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
  • 49
    • 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
  • 50
    • 0035951672 scopus 로고    scopus 로고
    • Three different human tau isoforms and rat neurofilament light, middle and heavy chain proteins are cellular substrates for transglutaminase
    • A.J. Grierson, G.V. Johnson, and C.C. Miller Three different human tau isoforms and rat neurofilament light, middle and heavy chain proteins are cellular substrates for transglutaminase Neurosci. Lett. 298 2001 9 12
    • (2001) Neurosci. Lett. , vol.298 , pp. 9-12
    • Grierson, A.J.1    Johnson, G.V.2    Miller, C.C.3
  • 51
    • 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
  • 52
    • 0030600002 scopus 로고    scopus 로고
    • Glial-derived neurotrophic factor (GDNF) induced morphological differentiation of an immortalized monoclonal hybrid dopaminergic cell line of mesencephalic neuronal origin
    • A. Heller, S. Price, and L. Won Glial-derived neurotrophic factor (GDNF) induced morphological differentiation of an immortalized monoclonal hybrid dopaminergic cell line of mesencephalic neuronal origin Brain Res. 725 1996 132 136
    • (1996) Brain Res. , vol.725 , pp. 132-136
    • Heller, A.1    Price, S.2    Won, L.3
  • 53
    • 0035013377 scopus 로고    scopus 로고
    • Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse tissues and cell lines
    • K. Hitomi, Y. Horio, K. Ikura, K. Yamanishi, and M. Maki Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse tissues and cell lines Int. J. Biochem. Cell Biol. 33 2001 491 498
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 491-498
    • Hitomi, K.1    Horio, Y.2    Ikura, K.3    Yamanishi, K.4    Maki, M.5
  • 54
    • 0028177277 scopus 로고
    • Cross-linking of beta-amyloid protein precursor catalyzed by tissue transglutaminase
    • G.J. Ho, E.J. Gregory, I.V. Smirnova, M.N. Zoubine, and B.W. Festoff Cross-linking of beta-amyloid protein precursor catalyzed by tissue transglutaminase FEBS Lett. 349 1994 151 154
    • (1994) FEBS Lett. , vol.349 , pp. 151-154
    • Ho, G.J.1    Gregory, E.J.2    Smirnova, I.V.3    Zoubine, M.N.4    Festoff, B.W.5
  • 55
    • 0030576597 scopus 로고    scopus 로고
    • Superactivation of transglutaminase type 2 without change in enzyme level occurs during progressive neurodegeneration in the mnd mouse mutant
    • F.E. Holmes, and L.W. Haynes Superactivation of transglutaminase type 2 without change in enzyme level occurs during progressive neurodegeneration in the mnd mouse mutant Neurosci. Lett. 213 1996 185 188
    • (1996) Neurosci. Lett. , vol.213 , pp. 185-188
    • Holmes, F.E.1    Haynes, L.W.2
  • 56
    • 0037378023 scopus 로고    scopus 로고
    • Neuroinflammatory processes in Parkinson's disease
    • S. Hunot, and E.C. Hirsch Neuroinflammatory processes in Parkinson's disease Ann. Neurol. 53 Suppl. 3 2003 S49 S58 (discussion S58-60)
    • (2003) Ann. Neurol. , vol.53 , Issue.SUPPL. 3
    • Hunot, S.1    Hirsch, E.C.2
  • 57
    • 0028818837 scopus 로고
    • Interaction site of GTP binding Gh (transglutaminase II) with phospholipase C
    • K.C. Hwang, C.D. Gray, N. Sivasubramanian, and M.J. Im Interaction site of GTP binding Gh (transglutaminase II) with phospholipase C J. Biol. Chem. 270 1995 27058 27062
    • (1995) J. Biol. Chem. , vol.270 , pp. 27058-27062
    • Hwang, K.C.1    Gray, C.D.2    Sivasubramanian, N.3    Im, M.J.4
  • 59
    • 0027289153 scopus 로고
    • Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer beta/A4 amyloid protein by transglutaminase
    • K. Ikura, K. Takahata, and R. Sasaki Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer beta/A4 amyloid protein by transglutaminase FEBS Lett. 326 1993 109 111
    • (1993) FEBS Lett. , vol.326 , pp. 109-111
    • Ikura, K.1    Takahata, K.2    Sasaki, R.3
  • 61
    • 0033594894 scopus 로고    scopus 로고
    • Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei
    • M.V. Karpuj, H. Garren, H. Slunt, D.L. Price, J. Gusella, M.W. Becher, and L. Steinman Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei Proc. Natl. Acad. Sci. U. S. A. 96 1999 7388 7393
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7388-7393
    • Karpuj, M.V.1    Garren, H.2    Slunt, H.3    Price, D.L.4    Gusella, J.5    Becher, M.W.6    Steinman, L.7
  • 62
    • 0032749566 scopus 로고    scopus 로고
    • Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease
    • S.Y. Kim, P. Grant, J.H. Lee, H.C. Pant, and P.M. Steinert Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease J. Biol. Chem. 274 1999 30715 30721
    • (1999) J. Biol. Chem. , vol.274 , pp. 30715-30721
    • Kim, S.Y.1    Grant, P.2    Lee, J.H.3    Pant, H.C.4    Steinert, P.M.5
  • 64
    • 0028286547 scopus 로고
    • CDNA sequence, gene sequence, and properties of murine pallidin (band 4.2), the protein implicated in the murine pallid mutation
    • C. Korsgren, and C.M. Cohen cDNA sequence, gene sequence, and properties of murine pallidin (band 4.2), the protein implicated in the murine pallid mutation Genomics 21 1994 478 485
    • (1994) Genomics , vol.21 , pp. 478-485
    • Korsgren, C.1    Cohen, C.M.2
  • 67
    • 0032585519 scopus 로고    scopus 로고
    • Isolation and characterization of brain-specific transglutaminases from rat
    • S.J. Kwak, S.Y. Kim, Y.S. Kim, K.Y. Song, I.G. Kim, and S.C. Park Isolation and characterization of brain-specific transglutaminases from rat Exp. Mol. Med. 30 1998 177 185
    • (1998) Exp. Mol. Med. , vol.30 , pp. 177-185
    • Kwak, S.J.1    Kim, S.Y.2    Kim, Y.S.3    Song, K.Y.4    Kim, I.G.5    Park, S.C.6
  • 68
    • 0032742674 scopus 로고    scopus 로고
    • Tissue transglutaminase is increased in Huntington's disease brain
    • M. Lesort, W. Chun, G.V. Johnson, and R.J. Ferrante Tissue transglutaminase is increased in Huntington's disease brain J. Neurochem. 73 1999 2018 2027
    • (1999) J. Neurochem. , vol.73 , pp. 2018-2027
    • Lesort, M.1    Chun, W.2    Johnson, G.V.3    Ferrante, R.J.4
  • 69
    • 0034257067 scopus 로고    scopus 로고
    • Tissue transglutaminase: A possible role in neurodegenerative diseases
    • M. Lesort, J. Tucholski, M.L. Miller, and G.V. Johnson Tissue transglutaminase: a possible role in neurodegenerative diseases Prog. Neurobiol. 61 2000 439 463
    • (2000) Prog. Neurobiol. , vol.61 , pp. 439-463
    • Lesort, M.1    Tucholski, J.2    Miller, M.L.3    Johnson, G.V.4
  • 70
    • 0036134809 scopus 로고    scopus 로고
    • Does tissue transglutaminase play a role in Huntington's disease?
    • M. Lesort, W. Chun, J. Tucholski, and G.V. Johnson Does tissue transglutaminase play a role in Huntington's disease? Neurochem. Int. 40 2002 37 52
    • (2002) Neurochem. Int. , vol.40 , pp. 37-52
    • Lesort, M.1    Chun, W.2    Tucholski, J.3    Johnson, G.V.4
  • 71
    • 0037423204 scopus 로고    scopus 로고
    • Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders
    • M. Lesort, M. Lee, J. Tucholski, and G.V. Johnson Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders J. Biol. Chem. 278 2003 3825 3830
    • (2003) J. Biol. Chem. , vol.278 , pp. 3825-3830
    • Lesort, M.1    Lee, M.2    Tucholski, J.3    Johnson, G.V.4
  • 72
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • S. Liu, R.A. Cerione, and J. Clardy Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity Proc. Natl. Acad. Sci. U. S. A. 99 2002 2743 2747
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 73
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • L. Lorand, and R.M. Graham Transglutaminases: crosslinking 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
  • 74
    • 0022575415 scopus 로고
    • Transglutaminase and neuronal differentiation
    • R.B. Maccioni, and N.W. Seeds Transglutaminase and neuronal differentiation Mol. Cell. Biochem. 69 1986 161 168
    • (1986) Mol. Cell. Biochem. , vol.69 , pp. 161-168
    • MacCioni, R.B.1    Seeds, N.W.2
  • 76
    • 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
  • 77
    • 0037251917 scopus 로고    scopus 로고
    • New weapons against inflammation: Dual inhibitors of phospholipase A2 and transglutaminase
    • L. Miele New weapons against inflammation: dual inhibitors of phospholipase A2 and transglutaminase J. Clin. Invest. 111 2003 19 21
    • (2003) J. Clin. Invest. , vol.111 , pp. 19-21
    • Miele, L.1
  • 78
    • 0022627398 scopus 로고
    • Transglutaminase and the neuronal cytoskeleton in Alzheimer's disease
    • C.C. Miller, and B.H. Anderton Transglutaminase and the neuronal cytoskeleton in Alzheimer's disease J. Neurochem. 46 1986 1912 1922
    • (1986) J. Neurochem. , vol.46 , pp. 1912-1922
    • Miller, C.C.1    Anderton, B.H.2
  • 79
    • 0031013601 scopus 로고    scopus 로고
    • Expression of GTP-dependent and GTP-independent tissue-type transglutaminase in cytokine-treated rat brain astrocytes
    • A. Monsonego, Y. Shani, I. Friedmann, Y. Paas, O. Eizenberg, and M. Schwartz Expression of GTP-dependent and GTP-independent tissue-type transglutaminase in cytokine-treated rat brain astrocytes J. Biol. Chem. 272 1997 3724 3732
    • (1997) J. Biol. Chem. , vol.272 , pp. 3724-3732
    • Monsonego, A.1    Shani, Y.2    Friedmann, I.3    Paas, Y.4    Eizenberg, O.5    Schwartz, M.6
  • 80
    • 0032475924 scopus 로고    scopus 로고
    • GTP-dependent conformational changes associated with the functional switch between Galpha and cross-linking activities in brain-derived tissue transglutaminase
    • A. Monsonego, I. Friedmann, Y. Shani, M. Eisenstein, and M. Schwartz GTP-dependent conformational changes associated with the functional switch between Galpha and cross-linking activities in brain-derived tissue transglutaminase J. Mol. Biol. 282 1998 713 720
    • (1998) J. Mol. Biol. , vol.282 , pp. 713-720
    • Monsonego, A.1    Friedmann, I.2    Shani, Y.3    Eisenstein, M.4    Schwartz, M.5
  • 81
    • 0040041521 scopus 로고    scopus 로고
    • Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase
    • S.N. Murthy, J.H. Wilson, T.J. Lukas, J. Kuret, and L. Lorand Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase J. Neurochem. 71 1998 2607 2614
    • (1998) J. Neurochem. , vol.71 , pp. 2607-2614
    • Murthy, S.N.1    Wilson, J.H.2    Lukas, T.J.3    Kuret, J.4    Lorand, L.5
  • 82
    • 0001298461 scopus 로고    scopus 로고
    • The promoter of the mouse tissue transglutaminase gene directs tissue-specific, retinoid-regulated and apoptosis-linked expression
    • L. Nagy, V.A. Thomazy, M.M. Saydak, J.P. Stein, and P.J. Davies The promoter of the mouse tissue transglutaminase gene directs tissue-specific, retinoid-regulated and apoptosis-linked expression Cell Death Differ. 4 1997 534 547
    • (1997) Cell Death Differ. , vol.4 , pp. 534-547
    • Nagy, L.1    Thomazy, V.A.2    Saydak, M.M.3    Stein, J.P.4    Davies, P.J.5
  • 83
    • 0028176166 scopus 로고
    • Gh: A GTP-binding protein with transglutaminase activity and receptor signaling function
    • H. Nakaoka, D.M. Perez, K.J. Baek, T. Das, A. Husain, K. Misono, M.J. Im, and R.M. Graham Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function Science 264 1994 1593 1596
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 85
    • 0038641718 scopus 로고    scopus 로고
    • Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: A mechanism for maintaining tissue integrity
    • B. Nicholas, P. Smethurst, E. Verderio, R. Jones, and M. Griffin Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity Biochem. J. 371 2003 413 422
    • (2003) Biochem. J. , vol.371 , pp. 413-422
    • Nicholas, B.1    Smethurst, P.2    Verderio, E.3    Jones, R.4    Griffin, M.5
  • 86
    • 0024913973 scopus 로고
    • Use of image analysis to quantitate changes in form of mitochondrial DNA after x-irradiation
    • R.R. O'Neill, L.G. Mitchell, C.R. Merril, and W.S. Rasband Use of image analysis to quantitate changes in form of mitochondrial DNA after x-irradiation Appl. Theor. Electrophor. 1 1989 163 167
    • (1989) Appl. Theor. Electrophor. , vol.1 , pp. 163-167
    • O'Neill, R.R.1    Mitchell, L.G.2    Merril, C.R.3    Rasband, W.S.4
  • 87
  • 88
    • 0027243955 scopus 로고
    • Localization and activity of transglutaminase, a retinoid-inducible protein, in developing rat spinal cord
    • M.J. Perry, and L.W. Haynes Localization and activity of transglutaminase, a retinoid-inducible protein, in developing rat spinal cord Int. J. Dev. Neurosci. 11 1993 325 337
    • (1993) Int. J. Dev. Neurosci. , vol.11 , pp. 325-337
    • Perry, M.J.1    Haynes, L.W.2
  • 91
    • 1042290533 scopus 로고    scopus 로고
    • Tissue transglutaminase-the key player in celiac disease: A review
    • S. Reif, and A. Lerner Tissue transglutaminase-the key player in celiac disease: a review Autoimmun. Rev. 3 2004 40 45
    • (2004) Autoimmun. Rev. , vol.3 , pp. 40-45
    • Reif, S.1    Lerner, A.2
  • 92
    • 0031228921 scopus 로고    scopus 로고
    • Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development
    • J.C. Schittny, M. Paulsson, C. Vallan, P.H. Burri, N. Kedei, and D. Aeschlimann Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development Am. J. Respir. Cell Mol. Biol. 17 1997 334 343
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 334-343
    • Schittny, J.C.1    Paulsson, M.2    Vallan, C.3    Burri, P.H.4    Kedei, N.5    Aeschlimann, D.6
  • 93
    • 0036135509 scopus 로고    scopus 로고
    • Introducing transglutaminase into the study of Alzheimer's disease. a personal look back
    • D.J. Selkoe Introducing transglutaminase into the study of Alzheimer's disease. A personal look back Neurochem. Int. 40 2002 13 16
    • (2002) Neurochem. Int. , vol.40 , pp. 13-16
    • Selkoe, D.J.1
  • 94
    • 0000831917 scopus 로고
    • Brain transglutaminase: In vitro crosslinking of human neurofilament proteins into insoluble polymers
    • D.J. Selkoe, C. Abraham, and Y. Ihara Brain transglutaminase: in vitro crosslinking of human neurofilament proteins into insoluble polymers Proc. Natl. Acad. Sci. U. S. A. 79 1982 6070 6074
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 6070-6074
    • Selkoe, D.J.1    Abraham, C.2    Ihara, Y.3
  • 95
    • 0034791419 scopus 로고    scopus 로고
    • Transactivation via RAR/RXR-Sp1 interaction: Characterization of binding between Sp1 and GC box motif
    • J. Shimada, Y. Suzuki, S.J. Kim, P.C. Wang, M. Matsumura, and S. Kojima Transactivation via RAR/RXR-Sp1 interaction: characterization of binding between Sp1 and GC box motif Mol. Endocrinol. 15 2001 1677 1692
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1677-1692
    • Shimada, J.1    Suzuki, Y.2    Kim, S.J.3    Wang, P.C.4    Matsumura, M.5    Kojima, S.6
  • 96
    • 0035872859 scopus 로고    scopus 로고
    • Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2
    • U.S. Singh, M.T. Kunar, Y.L. Kao, and K.M. Baker Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2 EMBO J. 20 2001 2413 2423
    • (2001) EMBO J. , vol.20 , pp. 2413-2423
    • Singh, U.S.1    Kunar, M.T.2    Kao, Y.L.3    Baker, K.M.4
  • 97
    • 0037414822 scopus 로고    scopus 로고
    • Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells
    • U.S. Singh, J. Pan, Y.L. Kao, S. Joshi, K.L. Young, and K.M. Baker Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells J. Biol. Chem. 278 2003 391 399
    • (2003) J. Biol. Chem. , vol.278 , pp. 391-399
    • Singh, U.S.1    Pan, J.2    Kao, Y.L.3    Joshi, S.4    Young, K.L.5    Baker, K.M.6
  • 99
    • 0031814260 scopus 로고    scopus 로고
    • Calcium mobilization and protease-activated receptor cleavage after thrombin stimulation in motor neurons
    • I.V. Smirnova, S. Vamos, T. Wiegmann, B.A. Citron, P.M. Arnold, and B.W. Festoff Calcium mobilization and protease-activated receptor cleavage after thrombin stimulation in motor neurons J. Mol. Neurosci. 10 1998 31 44
    • (1998) J. Mol. Neurosci. , vol.10 , pp. 31-44
    • Smirnova, I.V.1    Vamos, S.2    Wiegmann, T.3    Citron, B.A.4    Arnold, P.M.5    Festoff, B.W.6
  • 100
    • 0031813736 scopus 로고    scopus 로고
    • Thrombin is an extracellular signal that activates intracellular death protease pathways inducing apoptosis in model motor neurons
    • I.V. Smirnova, S.X. Zhang, B.A. Citron, P.M. Arnold, and B.W. Festoff Thrombin is an extracellular signal that activates intracellular death protease pathways inducing apoptosis in model motor neurons J. Neurobiol. 36 1998 64 80
    • (1998) J. Neurobiol. , vol.36 , pp. 64-80
    • Smirnova, I.V.1    Zhang, S.X.2    Citron, B.A.3    Arnold, P.M.4    Festoff, B.W.5
  • 101
    • 0034958701 scopus 로고    scopus 로고
    • Neuroprotective signal transduction in model motor neurons exposed to thrombin: G-protein modulation effects on neurite outgrowth, Ca(2+) mobilization, and apoptosis
    • I.V. Smirnova, B.A. Citron, P.M. Arnold, and B.W. Festoff Neuroprotective signal transduction in model motor neurons exposed to thrombin: G-protein modulation effects on neurite outgrowth, Ca(2+) mobilization, and apoptosis J. Neurobiol. 48 2001 87 100
    • (2001) J. Neurobiol. , vol.48 , pp. 87-100
    • Smirnova, I.V.1    Citron, B.A.2    Arnold, P.M.3    Festoff, B.W.4
  • 103
    • 0037252190 scopus 로고    scopus 로고
    • Novel transglutaminase inhibitors reverse the inflammation of allergic conjunctivitis
    • J. Sohn, T.I. Kim, Y.H. Yoon, J.Y. Kim, and S.Y. Kim Novel transglutaminase inhibitors reverse the inflammation of allergic conjunctivitis J. Clin. Invest. 111 2003 121 128
    • (2003) J. Clin. Invest. , vol.111 , pp. 121-128
    • Sohn, J.1    Kim, T.I.2    Yoon, Y.H.3    Kim, J.Y.4    Kim, S.Y.5
  • 104
    • 0141733132 scopus 로고    scopus 로고
    • Rapid tau aggregation and delayed hippocampal neuronal death induced by persistent thrombin signaling
    • Z. Suo, M. Wu, B.A. Citron, R.E. Palazzo, and B.W. Festoff Rapid tau aggregation and delayed hippocampal neuronal death induced by persistent thrombin signaling J. Biol. Chem. 278 2003 37681 37689
    • (2003) J. Biol. Chem. , vol.278 , pp. 37681-37689
    • Suo, Z.1    Wu, M.2    Citron, B.A.3    Palazzo, R.E.4    Festoff, B.W.5
  • 105
    • 0027998377 scopus 로고
    • Tumour necrosis factor alpha and interleukin-1 beta induce specific subunits of NFKB to bind the HIV-1 enhancer: Characterisation of transcription factors controlling human immunodeficiency virus type 1 gene expression in neural cells
    • S. Swingler, A. Morris, and A. Easton Tumour necrosis factor alpha and interleukin-1 beta induce specific subunits of NFKB to bind the HIV-1 enhancer: characterisation of transcription factors controlling human immunodeficiency virus type 1 gene expression in neural cells Biochem. Biophys. Res. Commun. 203 1994 623 630
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 623-630
    • Swingler, S.1    Morris, A.2    Easton, A.3
  • 109
    • 0032744527 scopus 로고    scopus 로고
    • Tau is modified by tissue transglutaminase in situ: Possible functional and metabolic effects of polyamination
    • J. Tucholski, J. Kuret, and G.V. Johnson Tau is modified by tissue transglutaminase in situ: possible functional and metabolic effects of polyamination J. Neurochem. 73 1999 1871 1880
    • (1999) J. Neurochem. , vol.73 , pp. 1871-1880
    • Tucholski, J.1    Kuret, J.2    Johnson, G.V.3
  • 110
    • 0036319364 scopus 로고    scopus 로고
    • Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner
    • J. Tucholski, and G.V. Johnson Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner J. Neurochem. 81 2002 780 791
    • (2002) J. Neurochem. , vol.81 , pp. 780-791
    • Tucholski, J.1    Johnson, G.V.2
  • 111
    • 0038035231 scopus 로고    scopus 로고
    • Tissue transglutaminase directly regulates adenylyl cyclase resulting in enhanced cAMP-response element-binding protein (CREB) activation
    • J. Tucholski, and G.V. Johnson Tissue transglutaminase directly regulates adenylyl cyclase resulting in enhanced cAMP-response element-binding protein (CREB) activation J. Biol. Chem. 278 2003 26838 26843
    • (2003) J. Biol. Chem. , vol.278 , pp. 26838-26843
    • Tucholski, J.1    Johnson, G.V.2
  • 112
    • 0035863525 scopus 로고    scopus 로고
    • Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells
    • J. Tucholski, M. Lesort, and G.V. Johnson Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells Neuroscience 102 2001 481 491
    • (2001) Neuroscience , vol.102 , pp. 481-491
    • Tucholski, J.1    Lesort, M.2    Johnson, G.V.3
  • 113
    • 0033636349 scopus 로고    scopus 로고
    • Molecular mechanism of monocyte predominant infiltration in chronic inflammation: Mediation by a novel monocyte chemotactic factor, S19 ribosomal protein dimer
    • T. Yamamoto Molecular mechanism of monocyte predominant infiltration in chronic inflammation: mediation by a novel monocyte chemotactic factor, S19 ribosomal protein dimer Pathol. Int. 50 2000 863 871
    • (2000) Pathol. Int. , vol.50 , pp. 863-871
    • Yamamoto, T.1
  • 114
    • 0007607636 scopus 로고    scopus 로고
    • Retinoic acid induction of the tissue transglutaminase promoter is mediated by a novel response element
    • Z.H. Yan, S. Noonan, L. Nagy, P.J. Davies, and J.P. Stein Retinoic acid induction of the tissue transglutaminase promoter is mediated by a novel response element Mol. Cell. Endocrinol. 120 1996 203 212
    • (1996) Mol. Cell. Endocrinol. , vol.120 , pp. 203-212
    • Yan, Z.H.1    Noonan, S.2    Nagy, L.3    Davies, P.J.4    Stein, J.P.5
  • 116
    • 0033764710 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking of tau proteins in progressive supranuclear palsy
    • M.O. Zemaitaitis, J.M. Lee, J.C. Troncoso, and N.A. Muma Transglutaminase-induced cross-linking of tau proteins in progressive supranuclear palsy J. Neuropathol. Exp. Neurol. 59 2000 983 989
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , pp. 983-989
    • Zemaitaitis, M.O.1    Lee, J.M.2    Troncoso, J.C.3    Muma, N.A.4
  • 117
    • 0031866960 scopus 로고    scopus 로고
    • Tissue transglutaminase is an in situ substrate of calpain: Regulation of activity
    • J. Zhang, R.P. Guttmann, and G.V. Johnson Tissue transglutaminase is an in situ substrate of calpain: regulation of activity J. Neurochem. 71 1998 240 247
    • (1998) J. Neurochem. , vol.71 , pp. 240-247
    • Zhang, J.1    Guttmann, R.P.2    Johnson, G.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.