메뉴 건너뛰기




Volumn 133, Issue 3, 2012, Pages 392-410

Transglutaminase 2: Biology, relevance to neurodegenerative diseases and therapeutic implications

Author keywords

Alzheimer's disease; Huntington's disease; Neurodegenerative disease; Neuroprotection; Parkinson's disease; Protein aggregation; Transglutaminase 2

Indexed keywords

ACYLTRANSFERASE INHIBITOR; ALPHA SYNUCLEIN; BRAIN PROTEIN; CYSTAMINE; CYSTEINE; GLUTAMINE DERIVATIVE; GLUTEN; GUANOSINE TRIPHOSPHATASE; NEUROPROTECTIVE AGENT; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2 INHIBITOR; UNCLASSIFIED DRUG;

EID: 84856442248     PISSN: 01637258     EISSN: 1879016X     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2011.12.003     Document Type: Review
Times cited : (50)

References (277)
  • 2
    • 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 4 1987 1901 1906
    • (1987) J Biol Chem , vol.262 , Issue.4 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 3
    • 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 3 1995 881 892
    • (1995) J Cell Biol , vol.129 , Issue.3 , pp. 881-892
    • Aeschlimann, D.1    Kaupp, O.2    Paulsson, M.3
  • 4
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • D. Aeschlimann, and M. Paulsson Transglutaminases: protein cross-linking enzymes in tissues and body fluids Thromb Haemost 71 4 1994 402 415 (Pubitemid 24100662)
    • (1994) Thrombosis and Haemostasis , vol.71 , Issue.4 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 5
    • 34147161141 scopus 로고    scopus 로고
    • Tissue transglutaminase inhibits autophagy in pancreatic cancer cells
    • DOI 10.1158/1541-7786.MCR-06-0229
    • U. Akar, B. Ozpolat, K. Mehta, J. Fok, Y. Kondo, and G. Lopez-Berestein Tissue transglutaminase inhibits autophagy in pancreatic cancer cells Mol Cancer Res 5 3 2007 241 249 (Pubitemid 46569775)
    • (2007) Molecular Cancer Research , vol.5 , Issue.3 , pp. 241-249
    • Akar, U.1    Ozpolat, B.2    Mehta, K.3    Fok, J.4    Kondo, Y.5    Lopez-Berestein, G.6
  • 6
    • 0034839336 scopus 로고    scopus 로고
    • Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: A role in TGF-β-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 Pt 16 2001 2989 3000 (Pubitemid 32821537)
    • (2001) Journal of Cell Science , vol.114 , Issue.16 , pp. 2989-3000
    • Akimov, S.S.1    Belkin, A.M.2
  • 7
    • 0027249085 scopus 로고
    • Rapid and transient alterations in transglutaminase activity in rat superior cervical ganglia following denervation or axotomy
    • DOI 10.1016/0168-0102(93)90028-O
    • M. Ando, S. Kunii, T. Tatematsu, and Y. Nagata Rapid and transient alterations in transglutaminase activity in rat superior cervical ganglia following denervation or axotomy Neurosci Res 17 1 1993 47 52 (Pubitemid 23239269)
    • (1993) Neuroscience Research , vol.17 , Issue.1 , pp. 47-52
    • Ando, M.1    Kunii, S.2    Tatematsu, T.3    Nagata, Y.4
  • 8
    • 4644336256 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks 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 crosslinks in Parkinson's disease FASEB J 18 7 2004 932 934
    • (2004) FASEB J , vol.18 , Issue.7 , pp. 932-934
    • Andringa, G.1    Lam, K.Y.2    Chegary, M.3    Wang, X.4    Chase, T.N.5    Bennett, M.C.6
  • 10
    • 79953229234 scopus 로고    scopus 로고
    • Cancer cell-derived microvesicles induce transformation by transferring tissue transglutaminase and fibronectin to recipient cells
    • M.A. Antonyak, B. Li, L.K. Boroughs, J.L. Johnson, J.E. Druso, and K.L. Bryant Cancer cell-derived microvesicles induce transformation by transferring tissue transglutaminase and fibronectin to recipient cells Proc Natl Acad Sci U S A 108 12 2011 4852 4857
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.12 , pp. 4852-4857
    • Antonyak, M.A.1    Li, B.2    Boroughs, L.K.3    Johnson, J.L.4    Druso, J.E.5    Bryant, K.L.6
  • 11
    • 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, and M.M. Zgola Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis J Biol Chem 276 36 2001 33582 33587
    • (2001) J Biol Chem , vol.276 , Issue.36 , 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
  • 13
    • 0031015814 scopus 로고    scopus 로고
    • The association of tissue transglutaminase with human recombinant tau results in the formation of insoluble filamentous structures
    • DOI 10.1016/S0006-8993(96)01121-3, PII S0006899396011213
    • 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 1-2 1997 21 31 (Pubitemid 27055742)
    • (1997) Brain Research , vol.745 , Issue.1-2 , pp. 21-31
    • Appelt, D.M.1    Balin, B.J.2
  • 14
    • 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 12 1996 1421 1427
    • (1996) J Histochem Cytochem , vol.44 , Issue.12 , pp. 1421-1427
    • Appelt, D.M.1    Kopen, G.C.2    Boyne, L.J.3    Balin, B.J.4
  • 15
    • 0029592762 scopus 로고
    • Tetanus toxin inhibits neuroexocytosis even when its Zn(2+)-dependent protease activity is removed
    • A.C. Ashton, Y. Li, F. Doussau, U. Weller, G. Dougan, and B. Poulain Tetanus toxin inhibits neuroexocytosis even when its Zn(2+)-dependent protease activity is removed J Biol Chem 270 52 1995 31386 31390
    • (1995) J Biol Chem , vol.270 , Issue.52 , pp. 31386-31390
    • Ashton, A.C.1    Li, Y.2    Doussau, F.3    Weller, U.4    Dougan, G.5    Poulain, B.6
  • 16
    • 77958449984 scopus 로고    scopus 로고
    • Alpha-Synuclein: Membrane interactions and toxicity in Parkinson's disease
    • P.K. Auluck, G. Caraveo, and S. Lindquist alpha-Synuclein: membrane interactions and toxicity in Parkinson's disease Annu Rev Cell Dev Biol 26 2010 211 233
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 17
    • 0035937106 scopus 로고    scopus 로고
    • Phospholipase Cdelta1 is a guanine nucleotide exchanging factor for transglutaminase II (Galpha h) and promotes alpha 1B-adrenoreceptor-mediated GTP binding and intracellular calcium release
    • K.J. Baek, S. Kang, D. Damron, and M. Im Phospholipase Cdelta1 is a guanine nucleotide exchanging factor for transglutaminase II (Galpha h) and promotes alpha 1B-adrenoreceptor-mediated GTP binding and intracellular calcium release J Biol Chem 276 8 2001 5591 5597
    • (2001) J Biol Chem , vol.276 , Issue.8 , pp. 5591-5597
    • Baek, K.J.1    Kang, S.2    Damron, D.3    Im, M.4
  • 18
    • 1642336449 scopus 로고    scopus 로고
    • Validity of mouse models for the study of tissue transglutaminase in neurodegenerative diseases
    • DOI 10.1016/j.mcn.2003.11.016, PII S1044743103003725
    • 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 3 2004 493 503 (Pubitemid 38366414)
    • (2004) Molecular and Cellular Neuroscience , vol.25 , Issue.3 , pp. 493-503
    • Bailey, C.D.C.1    Graham, R.M.2    Nanda, N.3    Davies, P.J.A.4    Johnson, G.V.W.5
  • 19
    • 13244279859 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to disease progression in the R6/2 Huntington's disease mouse model via aggregate-independent mechanisms
    • DOI 10.1111/j.1471-4159.2004.02839.x
    • C.D. Bailey, and G.V. Johnson Tissue transglutaminase contributes to disease progression in the R6/2 Huntington's disease mouse model via aggregate-independent mechanisms J Neurochem 92 1 2005 83 92 (Pubitemid 40193511)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.1 , pp. 83-92
    • Bailey, C.D.C.1    Johnson, G.V.W.2
  • 20
    • 33746275522 scopus 로고    scopus 로고
    • The protective effects of cystamine in the R6/2 Huntington's disease mouse involve mechanisms other than the inhibition of tissue transglutaminase
    • DOI 10.1016/j.neurobiolaging.2005.04.001, PII S0197458005000965
    • C.D. Bailey, and G.V. Johnson The protective effects of cystamine in the R6/2 Huntington's disease mouse involve mechanisms other than the inhibition of tissue transglutaminase Neurobiol Aging 27 6 2006 871 879 (Pubitemid 44287905)
    • (2006) Neurobiology of Aging , vol.27 , Issue.6 , pp. 871-879
    • Bailey, C.D.C.1    Johnson, G.V.W.2
  • 21
    • 0035916311 scopus 로고    scopus 로고
    • Conformational changes in the nucleosome followed by the selective accessibility of histone glutamines in the transglutaminase reaction: Effects of ionic strength
    • DOI 10.1021/bi001575b
    • E. Ballestar, M. Boix-Chornet, and L. Franco Conformational changes in the nucleosome followed by the selective accessibility of histone glutamines in the transglutaminase reaction: effects of ionic strength Biochemistry 40 7 2001 1922 1929 (Pubitemid 32165660)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 1922-1929
    • Ballestar, E.1    Boix-Chornet, M.2    Franco, L.3
  • 22
    • 77649147161 scopus 로고    scopus 로고
    • Neurotransmission in Parkinson's disease: Beyond dopamine
    • P. Barone Neurotransmission in Parkinson's disease: beyond dopamine Eur J Neurol 17 3 2010 364 376
    • (2010) Eur J Neurol , vol.17 , Issue.3 , pp. 364-376
    • Barone, P.1
  • 24
    • 33746472503 scopus 로고    scopus 로고
    • +)-induced toxicity in differentiated human SH-SY5Y neuroblastoma cells
    • DOI 10.1016/j.neulet.2006.06.061, PII S0304394006006239
    • K.E. Beck, L.A. De Girolamo, M. Griffin, and E.E. Billett The role of tissue transglutaminase in 1-methyl-4-phenylpyridinium (MPP+)-induced toxicity in differentiated human SH-SY5Y neuroblastoma cells Neurosci Lett 405 1-2 2006 46 51 (Pubitemid 44142827)
    • (2006) Neuroscience Letters , vol.405 , Issue.1-2 , pp. 46-51
    • Beck, K.E.1    De Girolamo, L.A.2    Griffin, M.3    Billett, E.E.4
  • 26
    • 33744950386 scopus 로고    scopus 로고
    • Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity
    • DOI 10.1074/jbc.M600146200
    • G.E. Begg, S.R. Holman, P.H. Stokes, J.M. Matthews, R.M. Graham, and S.E. Iismaa Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity J Biol Chem 281 18 2006 12603 12609 (Pubitemid 43855349)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12603-12609
    • Begg, G.E.1    Holman, S.R.2    Stokes, P.H.3    Matthews, J.M.4    Graham, R.M.5    Iismaa, S.E.6
  • 27
    • 4143117776 scopus 로고    scopus 로고
    • The transglutaminase family: An overview. Minireview article
    • S. Beninati, and M. Piacentini The transglutaminase family: an overview: minireview article Amino Acids 26 4 2004 367 372 (Pubitemid 39093139)
    • (2004) Amino Acids , vol.26 , Issue.4 , pp. 367-372
    • Beninati, S.1    Piacentini, M.2
  • 28
    • 0023733194 scopus 로고
    • GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase
    • DOI 10.1016/0014-5793(88)80928-1
    • C.M. Bergamini GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase FEBS Lett 239 2 1988 255 258 (Pubitemid 18263458)
    • (1988) FEBS Letters , vol.239 , Issue.2 , pp. 255-258
    • Bergamini, C.M.1
  • 31
    • 0037036409 scopus 로고    scopus 로고
    • Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb
    • DOI 10.1074/jbc.C200147200
    • 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 23 2002 20127 20130 (Pubitemid 34967301)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.23 , pp. 20127-20130
    • Boehm, J.E.1    Singh, U.2    Combs, C.3    Antonyak, M.A.4    Cerione, R.A.5
  • 32
    • 0036453620 scopus 로고    scopus 로고
    • Cerebrospinal fluid tissue transglutaminase as a biochemical marker for Alzheimer's disease
    • DOI 10.1006/nbdi.2002.0535
    • R.M. Bonelli, A. Aschoff, G. Niederwieser, C. Heuberger, and G. Jirikowski Cerebrospinal fluid tissue transglutaminase as a biochemical marker for Alzheimer's disease Neurobiol Dis 11 1 2002 106 110 (Pubitemid 35435678)
    • (2002) Neurobiology of Disease , vol.11 , Issue.1 , pp. 106-110
    • Bonelli, R.M.1    Aschoff, A.2    Niederwieser, G.3    Heuberger, C.4    Jirikowski, G.5
  • 33
    • 33646421164 scopus 로고    scopus 로고
    • Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase
    • M. Borrell-Pages, J.M. Canals, F.P. Cordelieres, J.A. Parker, J.R. Pineda, and G. Grange Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase J Clin Invest 116 5 2006 1410 1424
    • (2006) J Clin Invest , vol.116 , Issue.5 , pp. 1410-1424
    • Borrell-Pages, M.1    Canals, J.M.2    Cordelieres, F.P.3    Parker, J.A.4    Pineda, J.R.5    Grange, G.6
  • 34
    • 0021232522 scopus 로고
    • Pantethine and cystamine deplete cystine from cystinotic fibroblasts via efflux of cysteamine-cysteine mixed disulfide
    • J.D. Butler, and M. Zatz Pantethine and cystamine deplete cystine from cystinotic fibroblasts via efflux of cysteamine-cysteine mixed disulfide J Clin Invest 74 2 1984 411 416 (Pubitemid 14053987)
    • (1984) Journal of Clinical Investigation , vol.74 , Issue.2 , pp. 411-416
    • Butler, D.J.1    Zatz, M.2
  • 35
    • 77953067720 scopus 로고    scopus 로고
    • Critical role of transglutaminase and other stress proteins during neurodegenerative processes
    • D. Caccamo, M. Curro, S. Condello, N. Ferlazzo, and R. Ientile Critical role of transglutaminase and other stress proteins during neurodegenerative processes Amino Acids 38 2 2010 653 658
    • (2010) Amino Acids , vol.38 , Issue.2 , pp. 653-658
    • Caccamo, D.1    Curro, M.2    Condello, S.3    Ferlazzo, N.4    Ientile, R.5
  • 36
    • 84861655173 scopus 로고    scopus 로고
    • Monitoring of transglutaminase2 under different oxidative stress conditions
    • 10.1007/s00726-011-1018-8
    • D. Caccamo, M. Curro, N. Ferlazzo, S. Condello, and R. Ientile Monitoring of transglutaminase2 under different oxidative stress conditions Amino Acids 2011 10.1007/s00726-011-1018-8
    • (2011) Amino Acids
    • Caccamo, D.1    Curro, M.2    Ferlazzo, N.3    Condello, S.4    Ientile, R.5
  • 38
    • 14644422536 scopus 로고    scopus 로고
    • Development of a mechanism-based assay for tissue transglutaminase - Results of a high-throughput screen and discovery of inhibitors
    • DOI 10.1016/j.ab.2004.09.047
    • A. Case, J. Ni, L.A. Yeh, and R.L. Stein Development of a mechanism-based assay for tissue transglutaminase-results of a high-throughput screen and discovery of inhibitors Anal Biochem 338 2 2005 237 244 (Pubitemid 40312587)
    • (2005) Analytical Biochemistry , vol.338 , Issue.2 , pp. 237-244
    • Case, A.1    Ni, J.2    Yeh, L.-A.3    Stein, R.L.4
  • 39
    • 33846601817 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor
    • DOI 10.1021/bi061787u
    • A. Case, and R.L. Stein Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor Biochemistry 46 4 2007 1106 1115 (Pubitemid 46184997)
    • (2007) Biochemistry , vol.46 , Issue.4 , pp. 1106-1115
    • Case, A.1    Stein, R.L.2
  • 40
    • 65449139544 scopus 로고    scopus 로고
    • Mitochondria, calcium and cell death: A deadly triad in neurodegeneration
    • F. Celsi, P. Pizzo, M. Brini, S. Leo, C. Fotino, and P. Pinton Mitochondria, calcium and cell death: a deadly triad in neurodegeneration Biochim Biophys Acta 1787 5 2009 335 344
    • (2009) Biochim Biophys Acta , vol.1787 , Issue.5 , pp. 335-344
    • Celsi, F.1    Pizzo, P.2    Brini, M.3    Leo, S.4    Fotino, C.5    Pinton, P.6
  • 41
    • 0023153692 scopus 로고
    • Posttranslational protein modification by polyamines in intact and regenerating nerves
    • DOI 10.1111/j.1471-4159.1987.tb05567.x
    • G. Chakraborty, T. Leach, M.F. Zanakis, J.A. Sturman, and N.A. Ingoglia Posttranslational protein modification by polyamines in intact and regenerating nerves J Neurochem 48 3 1987 669 675 (Pubitemid 17018691)
    • (1987) Journal of Neurochemistry , vol.48 , Issue.3 , pp. 669-675
    • Chakraborty, G.1    Leach, T.2    Zanakis, M.F.3
  • 42
    • 0032866851 scopus 로고    scopus 로고
    • Tissue transglutaminase: An enzyme with a split personality
    • DOI 10.1016/S1357-2725(99)00045-X, PII S135727259900045X
    • J.S. Chen, and K. Mehta Tissue transglutaminase: an enzyme with a split personality Int J Biochem Cell Biol 31 8 1999 817 836 (Pubitemid 29354079)
    • (1999) International Journal of Biochemistry and Cell Biology , vol.31 , Issue.8 , pp. 817-836
    • Chen, J.S.K.1    Mehta, K.2
  • 43
    • 0029657914 scopus 로고    scopus 로고
    • 1-adrenergic receptor signaling via G(h) is subtype specific and independent of its transglutaminase activity
    • DOI 10.1074/jbc.271.50.32385
    • S. Chen, F. Lin, S. Iismaa, K.N. Lee, P.J. Birckbichler, and R.M. Graham Alpha1-adrenergic receptor signaling via Gh is subtype specific and independent of its transglutaminase activity J Biol Chem 271 50 1996 32385 32391 (Pubitemid 26422281)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.50 , pp. 32385-32391
    • Chen, S.1    Lin, F.2    Iismaa, S.3    Lee, K.N.4    Birckbichler, P.J.5    Graham, R.M.6
  • 44
    • 70350630733 scopus 로고    scopus 로고
    • The emerging role of autophagy in Parkinson's disease
    • Z.H. Cheung, and N.Y. Ip The emerging role of autophagy in Parkinson's disease Mol Brain 2 2009 29
    • (2009) Mol Brain , vol.2 , pp. 29
    • Cheung, Z.H.1    Ip, N.Y.2
  • 45
    • 77957727111 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibits apoptosis induced by calcium- overload through down-regulation of Bax
    • S.Y. Cho, J.H. Lee, H.D. Bae, E.M. Jeong, G.Y. Jang, and C.W. Kim Transglutaminase 2 inhibits apoptosis induced by calcium- overload through down-regulation of Bax Exp Mol Med 42 9 2010 639 650
    • (2010) Exp Mol Med , vol.42 , Issue.9 , pp. 639-650
    • Cho, S.Y.1    Lee, J.H.2    Bae, H.D.3    Jeong, E.M.4    Jang, G.Y.5    Kim, C.W.6
  • 46
    • 17844391272 scopus 로고    scopus 로고
    • Chemistry and biology of dihydroisoxazole derivatives: Selective inhibitors of human transglutaminase 2
    • DOI 10.1016/j.chembiol.2005.02.007
    • K. Choi, M. Siegel, J.L. Piper, L. Yuan, E. Cho, and P. Strnad Chemistry and biology of dihydroisoxazole derivatives: selective inhibitors of human transglutaminase 2 Chem Biol 12 4 2005 469 475 (Pubitemid 40588922)
    • (2005) Chemistry and Biology , vol.12 , Issue.4 , pp. 469-475
    • Choi, K.1    Siegel, M.2    Piper, J.L.3    Yuan, L.4    Cho, E.5    Strnad, P.6    Omary, B.7    Rich, K.M.8    Khosla, C.9
  • 47
    • 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 5 2001 3295 3301
    • (2001) J Biol Chem , vol.276 , Issue.5 , pp. 3295-3301
    • Citron, B.A.1    Santacruz, K.S.2    Davies, P.J.3    Festoff, B.W.4
  • 48
    • 0036135523 scopus 로고    scopus 로고
    • Protein crosslinking, tissue transglutaminase, alternative splicing and neurodegeneration
    • DOI 10.1016/S0197-0186(01)00062-6, PII S0197018601000626
    • 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 1 2002 69 78 (Pubitemid 34003559)
    • (2002) Neurochemistry International , vol.40 , Issue.1 , pp. 69-78
    • Citron, B.A.1    Suo, Z.2    SantaCruz, K.3    Davies, P.J.A.4    Qin, F.5    Festoff, B.W.6
  • 50
    • 0033215063 scopus 로고    scopus 로고
    • Synucleins in synaptic plasticity and neurodegenerative disorders
    • DOI 10.1002/(SICI)1097-4547(19991001)58:1<120::AID-JNR12>3.0.CO;2-E
    • D.F. Clayton, and J.M. George Synucleins in synaptic plasticity and neurodegenerative disorders J Neurosci Res 58 1 1999 120 129 (Pubitemid 29463698)
    • (1999) Journal of Neuroscience Research , vol.58 , Issue.1 , pp. 120-129
    • Clayton, D.F.1    George, J.M.2
  • 52
    • 0036134811 scopus 로고    scopus 로고
    • n- expansion diseases?
    • DOI 10.1016/S0197-0186(01)00058-4, PII S0197018601000584
    • A.J. Cooper, T.M. Jeitner, V. Gentile, and J.P. Blass Cross linking of polyglutamine domains catalyzed by tissue transglutaminase is greatly favored with pathological-length repeats: does transglutaminase activity play a role in (CAG)(n)/Q(n)-expansion diseases? Neurochem Int 40 1 2002 53 67 (Pubitemid 34003558)
    • (2002) Neurochemistry International , vol.40 , Issue.1 , pp. 53-67
    • Cooper, A.J.L.1    Jeitner, T.M.2    Gentile, V.3    Blass, J.P.4
  • 53
    • 0030906890 scopus 로고    scopus 로고
    • Polyglutamine domains are substrates of tissue transglutaminase: Does transglutaminase play a role in expanded CAG/poly-Q neurodegenerative diseases?
    • A.J. Cooper, K.F. Sheu, J.R. Burke, O. Onodera, W.J. Strittmatter, and A.D. Roses Polyglutamine domains are substrates of tissue transglutaminase: does transglutaminase play a role in expanded CAG/poly-Q neurodegenerative diseases? J Neurochem 69 1 1997 431 434 (Pubitemid 27274202)
    • (1997) Journal of Neurochemistry , vol.69 , Issue.1 , pp. 431-434
    • Cooper, A.J.L.1    Sheu, K.-F.R.2    Burke, J.R.3    Onodera, O.4    Strittmatter, W.J.5    Roses, A.D.6    Blass, J.P.7
  • 55
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional Repression of PGC-1α by Mutant Huntingtin Leads to Mitochondrial Dysfunction and Neurodegeneration
    • DOI 10.1016/j.cell.2006.09.015, PII S0092867406012050
    • L. Cui, H. Jeong, F. Borovecki, C.N. Parkhurst, N. Tanese, and D. Krainc Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration Cell 127 1 2006 59 69 (Pubitemid 44466642)
    • (2006) Cell , vol.127 , Issue.1 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 58
    • 37349100874 scopus 로고    scopus 로고
    • GTP-binding-defective forms of tissue transglutaminase trigger cell death
    • DOI 10.1021/bi701422h
    • S. Datta, M.A. Antonyak, and R.A. Cerione GTP-binding-defective forms of tissue transglutaminase trigger cell death Biochemistry 46 51 2007 14819 14829 (Pubitemid 350308873)
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 14819-14829
    • Datta, S.1    Antonyak, M.A.2    Cerione, R.A.3
  • 59
    • 0033600124 scopus 로고    scopus 로고
    • The length of polyglutamine tract, its level of expression, the rate of degradation, and the transglutaminase activity influence the formation of intracellular aggregates
    • DOI 10.1006/bbrc.1999.0851
    • T. de Cristofaro, A. Affaitati, L. Cariello, E.V. Avvedimento, and S. Varrone The length of polyglutamine tract, its level of expression, the rate of degradation, and the transglutaminase activity influence the formation of intracellular aggregates Biochem Biophys Res Commun 260 1 1999 150 158 (Pubitemid 29351800)
    • (1999) Biochemical and Biophysical Research Communications , vol.260 , Issue.1 , pp. 150-158
    • De Cristofaro, T.1    Affaitati, A.2    Cariello, L.3    Avvedimento, E.V.4    Varrone, S.5
  • 60
    • 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 1 2001 148 155
    • (2001) Mol Cell Biol , vol.21 , Issue.1 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2
  • 61
    • 0036132253 scopus 로고    scopus 로고
    • Synthesis of dipeptide-bound epoxides and α,β-unsaturated amides as potential irreversible transglutaminase inhibitors
    • DOI 10.1016/S0968-0896(01)00292-9, PII S0968089601002929
    • P. de Macedo, C. Marrano, and J.W. Keillor Synthesis of dipeptide-bound epoxides and alpha, beta-unsaturated amides as potential irreversible transglutaminase inhibitors Bioorg Med Chem 10 2 2002 355 360 (Pubitemid 33121260)
    • (2002) Bioorganic and Medicinal Chemistry , vol.10 , Issue.2 , pp. 355-360
    • De Macedo, P.1    Marrano, C.2    Keillor, J.W.3
  • 63
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • P. Desplats, H.J. Lee, E.J. Bae, C. Patrick, E. Rockenstein, and L. Crews Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein Proc Natl Acad Sci U S A 106 31 2009 13010 13015
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.31 , pp. 13010-13015
    • Desplats, P.1    Lee, H.J.2    Bae, E.J.3    Patrick, C.4    Rockenstein, E.5    Crews, L.6
  • 65
    • 33646248382 scopus 로고    scopus 로고
    • CYTE-I-HD: Phase i dose finding and tolerability study of cysteamine (Cystagon) in Huntington's disease
    • R. Dubinsky, and C. Gray CYTE-I-HD: phase I dose finding and tolerability study of cysteamine (Cystagon) in Huntington's disease Mov Disord 21 4 2006 530 533
    • (2006) Mov Disord , vol.21 , Issue.4 , pp. 530-533
    • Dubinsky, R.1    Gray, C.2
  • 66
    • 15044349470 scopus 로고    scopus 로고
    • Structure-activity relationship study of novel tissue transglutaminase inhibitors
    • DOI 10.1016/j.bmcl.2005.02.005
    • E. Duval, A. Case, R.L. Stein, and G.D. Cuny Structure-activity relationship study of novel tissue transglutaminase inhibitors Bioorg Med Chem Lett 15 7 2005 1885 1889 (Pubitemid 40380753)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.7 , pp. 1885-1889
    • Duval, E.1    Case, A.2    Stein, R.L.3    Cuny, G.D.4
  • 67
    • 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, and A. Scaloni 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 10 1999 992 1001 (Pubitemid 29520801)
    • (1999) Cell Death and Differentiation , vol.6 , Issue.10 , 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
  • 68
    • 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 7 1993 4588 4591 (Pubitemid 23081563)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.7 , pp. 4588-4591
    • Facchiano, F.1    Benfenati, F.2    Valtorta, F.3    Luini, A.4
  • 69
    • 42049108832 scopus 로고    scopus 로고
    • Extracellular transglutaminase 2 activates beta-catenin signaling in calcifying vascular smooth muscle cells
    • L. Faverman, L. Mikhaylova, J. Malmquist, and M. Nurminskaya Extracellular transglutaminase 2 activates beta-catenin signaling in calcifying vascular smooth muscle cells FEBS Lett 582 10 2008 1552 1557
    • (2008) FEBS Lett , vol.582 , Issue.10 , pp. 1552-1557
    • Faverman, L.1    Mikhaylova, L.2    Malmquist, J.3    Nurminskaya, M.4
  • 70
    • 0033573849 scopus 로고    scopus 로고
    • Alpha 1B-adrenoceptor interacts with multiple sites of transglutaminase II: Characteristics of the interaction in binding and activation
    • J.F. Feng, C.D. Gray, and M.J. Im Alpha 1B-adrenoceptor interacts with multiple sites of transglutaminase II: characteristics of the interaction in binding and activation Biochemistry 38 7 1999 2224 2232
    • (1999) Biochemistry , vol.38 , Issue.7 , pp. 2224-2232
    • Feng, J.F.1    Gray, C.D.2    Im, M.J.3
  • 71
    • 0029666275 scopus 로고    scopus 로고
    • Evidence that phospholipase δ1 is the effector in the G(h) (transglutaminase II)-mediated signaling
    • DOI 10.1074/jbc.271.28.16451
    • J.F. Feng, S.G. Rhee, and M.J. Im Evidence that phospholipase delta1 is the effector in the Gh (transglutaminase II)-mediated signaling J Biol Chem 271 28 1996 16451 16454 (Pubitemid 26238993)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.28 , pp. 16451-16454
    • Feng, J.-F.1    Rhee, S.G.2    Im, M.-J.3
  • 72
    • 0032425260 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed protein cross-linking in the molecular program of apoptosis and its relationship to neuronal processes
    • DOI 10.1023/A:1020273903224
    • L. Fesus Transglutaminase-catalyzed protein cross-linking in the molecular program of apoptosis and its relationship to neuronal processes Cell Mol Neurobiol 18 6 1998 683 694 (Pubitemid 29012945)
    • (1998) Cellular and Molecular Neurobiology , vol.18 , Issue.6 , pp. 683-694
    • Fesus, L.1
  • 73
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • DOI 10.1016/S0968-0004(02)02182-5, PII S0968000402021825
    • L. Fesus, and M. Piacentini Transglutaminase 2: an enigmatic enzyme with diverse functions Trends Biochem Sci 27 10 2002 534 539 (Pubitemid 35279599)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 74
    • 20444363472 scopus 로고    scopus 로고
    • Transglutaminase 2 in the balance of cell death and survival
    • DOI 10.1016/j.febslet.2005.03.063, PII S0014579305004151
    • L. Fesus, and Z. Szondy Transglutaminase 2 in the balance of cell death and survival FEBS Lett 579 15 2005 3297 3302 (Pubitemid 40804677)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3297-3302
    • Fesus, L.1    Szondy, Z.2
  • 75
    • 0024471699 scopus 로고
    • Formation of N(ε)-(γ-glutamyl)-lysine isodipeptide in Chinese-hamster ovary cells
    • L. Fesus, and E. Tarcsa Formation of N epsilon-(gamma-glutamyl)-lysine isodipeptide in Chinese-hamster ovary cells Biochem J 263 3 1989 843 848 (Pubitemid 19276464)
    • (1989) Biochemical Journal , vol.263 , Issue.3 , pp. 843-848
    • Fesus, L.1    Tarcsa, E.2
  • 76
    • 0023159034 scopus 로고
    • Induction and activation of tiussue transglutaminase during programmed cell death
    • DOI 10.1016/0014-5793(87)80430-1
    • L. Fesus, V. Thomazy, and A. Falus Induction and activation of tissue transglutaminase during programmed cell death FEBS Lett 224 1 1987 104 108 (Pubitemid 17159992)
    • (1987) FEBS Letters , vol.224 , Issue.1 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 78
    • 0019878161 scopus 로고
    • Gamma-Glutamylamine cyclotransferase. An enzyme involved in the catabolism of epsilon-(gamma-glutamyl)lysine and other gamma-glutamylamines
    • Spec No
    • M.L. Fink, and J.E. Folk gamma-Glutamylamine cyclotransferase. An enzyme involved in the catabolism of epsilon-(gamma-glutamyl)lysine and other gamma-glutamylamines Mol Cell Biochem 38 Pt 1 1981 59 67 Spec No
    • (1981) Mol Cell Biochem , vol.38 , Issue.PART 1 , pp. 59-67
    • Fink, M.L.1    Folk, J.E.2
  • 79
    • 0017680149 scopus 로고
    • The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases
    • J.E. Folk, and J.S. Finlayson The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases Adv Protein Chem 31 1977 1 133
    • (1977) Adv Protein Chem , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 81
    • 0037417220 scopus 로고    scopus 로고
    • Apoptosis and caspases in neurodegenerative diseases
    • DOI 10.1056/NEJMra022366
    • R.M. Friedlander Apoptosis and caspases in neurodegenerative diseases N Engl J Med 348 14 2003 1365 1375 (Pubitemid 36384105)
    • (2003) New England Journal of Medicine , vol.348 , Issue.14 , pp. 1365-1375
    • Friedlander, R.M.1
  • 82
    • 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 2-3 1991 331 334
    • (1991) Neuroscience , vol.43 , Issue.23 , pp. 331-334
    • Friedrich, P.1    Fesus, L.2    Tarcsa, E.3    Czeh, G.4
  • 83
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • B. Frost, R.L. Jacks, and M.I. Diamond Propagation of tau misfolding from the outside to the inside of a cell J Biol Chem 284 19 2009 12845 12852
    • (2009) J Biol Chem , vol.284 , Issue.19 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 84
    • 0033544020 scopus 로고    scopus 로고
    • 1 integrin
    • DOI 10.1006/excr.1999.4633
    • C.A. Gaudry, E. Verderio, R.A. Jones, C. Smith, and M. Griffin Tissue transglutaminase is an important player at the surface of human endothelial cells: evidence for its externalization and its colocalization with the beta(1) integrin Exp Cell Res 252 1 1999 104 113 (Pubitemid 29485130)
    • (1999) Experimental Cell Research , vol.252 , Issue.1 , pp. 104-113
    • Gaudry, C.A.1    Verderio, E.2    Jones, R.A.3    Smith, C.4    Griffin, M.5
  • 86
    • 0028220758 scopus 로고
    • The human tissue transglutaminase gene maps on chromosome 20q12 by in situ fluorescence hybridization
    • DOI 10.1006/geno.1994.1170
    • V. Gentile, P.J. Davies, and A. Baldini The human tissue transglutaminase gene maps on chromosome 20q12 by in situ fluorescence hybridization Genomics 20 2 1994 295 297 (Pubitemid 24108413)
    • (1994) Genomics , vol.20 , Issue.2 , pp. 295-297
    • Gentile, V.1    Davies, P.J.A.2    Baldini, A.3
  • 89
    • 0032522165 scopus 로고    scopus 로고
    • Tissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favored with long polyglutamine domains: A possible mechanism contributing to CAG-triplet diseases
    • DOI 10.1006/abbi.1998.0592
    • V. Gentile, C. Sepe, M. Calvani, M.A. Melone, R. Cotrufo, and A.J. Cooper Tissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favored with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases Arch Biochem Biophys 352 2 1998 314 321 (Pubitemid 28368600)
    • (1998) Archives of Biochemistry and Biophysics , vol.352 , Issue.2 , pp. 314-321
    • Gentile, V.1    Sepe, C.2    Calvani, M.3    Melone, M.A.B.4    Cotrufo, R.5    Cooper, A.J.L.6    Blass, J.P.7    Peluso, G.8
  • 90
    • 0026705663 scopus 로고
    • Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: Effects on cellular morphology and adhesion
    • V. Gentile, V. Thomazy, M. Piacentini, L. Fesus, and P.J. Davies Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: effects on cellular morphology and adhesion J Cell Biol 119 2 1992 463 474
    • (1992) J Cell Biol , vol.119 , Issue.2 , pp. 463-474
    • Gentile, V.1    Thomazy, V.2    Piacentini, M.3    Fesus, L.4    Davies, P.J.5
  • 91
    • 0025293021 scopus 로고
    • Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes
    • M.D. George, T.M. Vollberg, E.E. Floyd, J.P. Stein, and A.M. Jetten Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes J Biol Chem 265 19 1990 11098 11104
    • (1990) J Biol Chem , vol.265 , Issue.19 , pp. 11098-11104
    • George, M.D.1    Vollberg, T.M.2    Floyd, E.E.3    Stein, J.P.4    Jetten, A.M.5
  • 93
    • 0022203159 scopus 로고
    • Transglutaminase activity in rat brain: Characterization, distribution, and changes with age
    • DOI 10.1111/j.1471-4159.1985.tb07222.x
    • G.M. Gilad, and L.E. Varon Transglutaminase activity in rat brain: characterization, distribution, and changes with age J Neurochem 45 5 1985 1522 1526 (Pubitemid 16252593)
    • (1985) Journal of Neurochemistry , vol.45 , Issue.5 , pp. 1522-1526
    • Gilad, G.M.1    Varon, L.E.2
  • 94
    • 77954385676 scopus 로고    scopus 로고
    • The propagation of prion-like protein inclusions in neurodegenerative diseases
    • M. Goedert, F. Clavaguera, and M. Tolnay The propagation of prion-like protein inclusions in neurodegenerative diseases Trends Neurosci 33 7 2010 317 325
    • (2010) Trends Neurosci , vol.33 , Issue.7 , pp. 317-325
    • Goedert, M.1    Clavaguera, F.2    Tolnay, M.3
  • 95
    • 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 15 1991 3071 3077 (Pubitemid 21892867)
    • (1991) FASEB Journal , vol.5 , Issue.15 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 96
    • 0035951672 scopus 로고    scopus 로고
    • Three different human tau isoforms and rat neurofilament light, middle and heavy chain proteins are cellular substrates for transglutaminase
    • DOI 10.1016/S0304-3940(00)01714-6, PII S0304394000017146
    • 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 1 2001 9 12 (Pubitemid 32057202)
    • (2001) Neuroscience Letters , vol.298 , Issue.1 , pp. 9-12
    • Grierson, A.J.1    Johnson, G.V.W.2    Miller, C.C.J.3
  • 97
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • DOI 10.1042/BJ20021234
    • M. Griffin, R. Casadio, and C.M. Bergamini Transglutaminases: nature's biological glues Biochem J 368 Pt 2 2002 377 396 (Pubitemid 35454517)
    • (2002) Biochemical Journal , vol.368 , Issue.2 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 98
    • 0027424329 scopus 로고
    • Exposure of βH-crystallin to hydroxyl radicals enhances the transglutaminase-susceptibility of its existing amine-donor and amine-acceptor sites
    • P.J. Groenen, M. Seccia, R.H. Smulders, E. Gravela, K.H. Cheeseman, and H. Bloemendal Exposure of beta H-crystallin to hydroxyl radicals enhances the transglutaminase-susceptibility of its existing amine-donor and amine-acceptor sites Biochem J 295 Pt 2 1993 399 404 (Pubitemid 23315177)
    • (1993) Biochemical Journal , vol.295 , Issue.2 , pp. 399-404
    • Groenen, P.J.T.A.1    Seccia, M.2    Smulders, R.H.P.H.3    Gravela, E.4    Cheeseman, K.H.5    Bloemendal, H.6    De Jong, W.W.7
  • 100
    • 33846038743 scopus 로고    scopus 로고
    • Synthesis and evaluation of peptidic maleimides as transglutaminase inhibitors
    • DOI 10.1016/j.bmcl.2006.10.061, PII S0960894X06012418
    • D. Halim, K. Caron, and J.W. Keillor Synthesis and evaluation of peptidic maleimides as transglutaminase inhibitors Bioorg Med Chem Lett 17 2 2007 305 308 (Pubitemid 46073765)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.2 , pp. 305-308
    • Halim, D.1    Caron, K.2    Keillor, J.W.3
  • 101
    • 13944277614 scopus 로고    scopus 로고
    • Tau protien is cross-linked by transglutaminase in P301L tau transgenic mice
    • DOI 10.1523/JNEUROSCI.3263-04.2005
    • R.A. Halverson, J. Lewis, S. Frausto, M. Hutton, and N.A. Muma Tau protein is cross-linked by transglutaminase in P301L tau transgenic mice J Neurosci 25 5 2005 1226 1233 (Pubitemid 40268965)
    • (2005) Journal of Neuroscience , vol.25 , Issue.5 , pp. 1226-1233
    • Halverson, R.A.1    Lewis, J.2    Frausto, S.3    Hutton, M.4    Muma, N.A.5
  • 102
    • 0022330157 scopus 로고
    • Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein
    • D. Hand, P.J. Bungay, B.M. Elliott, and M. Griffin Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein Biosci Rep 5 12 1985 1079 1086 (Pubitemid 16141515)
    • (1985) Bioscience Reports , vol.5 , Issue.12 , pp. 1079-1086
    • Hand, D.1    Bungay, P.J.2    Elliott, B.M.3    Griffin, M.4
  • 103
    • 0032824155 scopus 로고    scopus 로고
    • Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis
    • Z.A. Haroon, J.M. Hettasch, T.S. Lai, M.W. Dewhirst, and C.S. Greenberg Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis FASEB J 13 13 1999 1787 1795 (Pubitemid 29473340)
    • (1999) FASEB Journal , vol.13 , Issue.13 , pp. 1787-1795
    • Haroon, Z.A.1    Hettasch, J.M.2    Lai, T.-S.3    Dewhirst, M.W.4    Greenberg, C.S.5
  • 105
    • 0037352689 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of gluten peptide analogs as selective inhibitors of human tissue transglutaminase
    • DOI 10.1016/S1074-5521(03)00045-0
    • F. Hausch, T. Halttunen, M. Maki, and C. Khosla Design, synthesis, and evaluation of gluten peptide analogs as selective inhibitors of human tissue transglutaminase Chem Biol 10 3 2003 225 231 (Pubitemid 36380279)
    • (2003) Chemistry and Biology , vol.10 , Issue.3 , pp. 225-231
    • Hausch, F.1    Halttunen, T.2    Maki, M.3    Khosla, C.4
  • 106
    • 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 1 1994 151 154
    • (1994) FEBS Lett , vol.349 , Issue.1 , pp. 151-154
    • Ho, G.J.1    Gregory, E.J.2    Smirnova, I.V.3    Zoubine, M.N.4    Festoff, B.W.5
  • 107
    • 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 45 1995 27058 27062
    • (1995) J Biol Chem , vol.270 , Issue.45 , pp. 27058-27062
    • Hwang, K.C.1    Gray, C.D.2    Sivasubramanian, N.3    Im, M.J.4
  • 109
    • 0030756529 scopus 로고    scopus 로고
    • The core domain of the tissue transglutaminase G(h) hydrolyzes GTP and ATP
    • DOI 10.1021/bi970545e
    • S.E. Iismaa, L. Chung, M.J. Wu, D.C. Teller, V.C. Yee, and R.M. Graham The core domain of the tissue transglutaminase Gh hydrolyzes GTP and ATP Biochemistry 36 39 1997 11655 11664 (Pubitemid 27424090)
    • (1997) Biochemistry , vol.36 , Issue.39 , pp. 11655-11664
    • Iismaa, S.E.1    Chung, L.2    Wu, M.-J.3    Teller, D.C.4    Yee, V.C.5    Graham, R.M.6
  • 110
    • 67651071286 scopus 로고    scopus 로고
    • Transglutaminases and disease: Lessons from genetically engineered mouse models and inherited disorders
    • S.E. Iismaa, B.M. Mearns, L. Lorand, and R.M. Graham Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders Physiol Rev 89 3 2009 991 1023
    • (2009) Physiol Rev , vol.89 , Issue.3 , pp. 991-1023
    • Iismaa, S.E.1    Mearns, B.M.2    Lorand, L.3    Graham, R.M.4
  • 111
    • 0034674770 scopus 로고    scopus 로고
    • GTP binding and signaling by G(h)/transglutaminase II involves distinct residues in a unique GTP-binding pocket
    • DOI 10.1074/jbc.M000583200
    • S.E. Iismaa, M.J. Wu, N. Nanda, W.B. Church, and R.M. Graham GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket J Biol Chem 275 24 2000 18259 18265 (Pubitemid 30414778)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18259-18265
    • Iismaa, S.E.1    Wu, M.-J.2    Nanda, N.3    Church, W.B.4    Graham, R.M.5
  • 112
    • 0033630190 scopus 로고    scopus 로고
    • High molecular weight transglutaminase inhibitor produced by a microorganism (Streptomyces lavendulae Y-200)
    • K. Ikura, K. Minami, C. Otomo, H. Hashimoto, S. Natsuka, and K. Oda High molecular weight transglutaminase inhibitor produced by a microorganism (Streptomyces lavendulae Y-200) Biosci Biotechnol Biochem 64 1 2000 116 124
    • (2000) Biosci Biotechnol Biochem , vol.64 , Issue.1 , pp. 116-124
    • Ikura, K.1    Minami, K.2    Otomo, C.3    Hashimoto, H.4    Natsuka, S.5    Oda, K.6
  • 114
    • 0027289153 scopus 로고
    • Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer β/A4 amyloid protein by transglutaminase
    • DOI 10.1016/0014-5793(93)81772-R
    • 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 1-3 1993 109 111 (Pubitemid 23200258)
    • (1993) FEBS Letters , vol.326 , Issue.1-3 , pp. 109-111
    • Ikura, K.1    Takahata, K.2    Sasaki, R.3
  • 115
    • 0024502917 scopus 로고
    • Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: Evidence for amino-terminal processing
    • DOI 10.1021/bi00431a054
    • K. Ikura, H. Yokota, R. Sasaki, and H. Chiba Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: evidence for amino-terminal processing Biochemistry 28 5 1989 2344 2348 (Pubitemid 19084464)
    • (1989) Biochemistry , vol.28 , Issue.5 , pp. 2344-2348
    • Ikura, K.1    Yokota, H.2    Sasaki, R.3    Chiba, H.4
  • 118
  • 119
    • 69849106959 scopus 로고    scopus 로고
    • Transglutaminase activation in neurodegenerative diseases
    • T.M. Jeitner, N.A. Muma, K.P. Battaile, and A.J. Cooper Transglutaminase activation in neurodegenerative diseases Future Neurol 4 4 2009 449 467
    • (2009) Future Neurol , vol.4 , Issue.4 , pp. 449-467
    • Jeitner, T.M.1    Muma, N.A.2    Battaile, K.P.3    Cooper, A.J.4
  • 121
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-28.
    • P. Jenner Oxidative stress in Parkinson's disease Ann Neurol 53 Suppl. 3 2003 S26 36 discussion S36-28.
    • (2003) Ann Neurol , vol.53 , Issue.SUPPL. 3 , pp. 26-36
    • Jenner, P.1
  • 122
    • 0029081997 scopus 로고
    • Residues in the synuclein consensus motif of the alpha-synuclein fragment, NAC, participate in transglutaminase-catalysed cross-linking to Alzheimer-disease amyloid beta A4 peptide
    • P.H. Jensen, E.S. Sorensen, T.E. Petersen, J. Gliemann, and L.K. Rasmussen Residues in the synuclein consensus motif of the alpha-synuclein fragment, NAC, participate in transglutaminase-catalysed cross-linking to Alzheimer-disease amyloid beta A4 peptide Biochem J 310 Pt 1 1995 91 94
    • (1995) Biochem J , vol.310 , Issue.PART 1 , pp. 91-94
    • Jensen, P.H.1    Sorensen, E.S.2    Petersen, T.E.3    Gliemann, J.4    Rasmussen, L.K.5
  • 123
    • 71449107433 scopus 로고    scopus 로고
    • The mechanism of transglutaminase 2 inhibition with glucosamine: Implications of a possible anti-inflammatory effect through transglutaminase inhibition
    • K.C. Jeong, K.O. Ahn, B.I. Lee, C.H. Lee, and S.Y. Kim The mechanism of transglutaminase 2 inhibition with glucosamine: implications of a possible anti-inflammatory effect through transglutaminase inhibition J Cancer Res Clin Oncol 136 1 2010 143 150
    • (2010) J Cancer Res Clin Oncol , vol.136 , Issue.1 , pp. 143-150
    • Jeong, K.C.1    Ahn, K.O.2    Lee, B.I.3    Lee, C.H.4    Kim, S.Y.5
  • 124
    • 0030998670 scopus 로고    scopus 로고
    • Transglutaminase activity is increased in Alzheimer's disease brain
    • DOI 10.1016/S0006-8993(96)01431-X, PII S000689939601431X
    • G.V. Johnson, T.M. Cox, J.P. Lockhart, M.D. Zinnerman, M.L. Miller, and R.E. Powers Transglutaminase activity is increased in Alzheimer's disease brain Brain Res 751 2 1997 323 329 (Pubitemid 27132565)
    • (1997) Brain Research , vol.751 , Issue.2 , pp. 323-329
    • Johnson, G.V.W.1    Cox, T.M.2    Lockhart, J.P.3    Zinnerman, M.D.4    Miller, M.L.5    Powers, R.E.6
  • 126
    • 0032014092 scopus 로고    scopus 로고
    • Transglutaminase action imitates Huntington's disease: Selective polymerization of huntingtin containing expanded polyglutamine
    • P. Kahlem, H. Green, and P. Djian Transglutaminase action imitates Huntington's disease: selective polymerization of Huntingtin containing expanded polyglutamine Mol Cell 1 4 1998 595 601 (Pubitemid 128374695)
    • (1998) Molecular Cell , vol.1 , Issue.4 , pp. 595-601
    • Kahlem, P.1    Green, H.2    Djian, P.3
  • 127
    • 0029856046 scopus 로고    scopus 로고
    • Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system
    • DOI 10.1073/pnas.93.25.14580
    • P. Kahlem, C. Terre, H. Green, and P. Djian Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: relevance to diseases of the nervous system Proc Natl Acad Sci U S A 93 25 1996 14580 14585 (Pubitemid 26419010)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.25 , pp. 14580-14585
    • Kahlem, P.1    Terre, C.2    Green, H.3    Djian, P.4
  • 128
    • 80052221634 scopus 로고    scopus 로고
    • Self-Assembly of Tissue Transglutaminase into Amyloid-Like Fibrils Using Physiological Concentration of Ca(2+)
    • H.R. Kalhor, V.F. Shahin, M.H. Fouani, and H. Hosseinkhani Self-Assembly of Tissue Transglutaminase into Amyloid-Like Fibrils Using Physiological Concentration of Ca(2+) Langmuir 27 17 2011 10776 10784
    • (2011) Langmuir , vol.27 , Issue.17 , pp. 10776-10784
    • Kalhor, H.R.1    Shahin, V.F.2    Fouani, M.H.3    Hosseinkhani, H.4
  • 129
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor protein-transgenic mice
    • M.D. Kane, W.J. Lipinski, M.J. Callahan, F. Bian, R.A. Durham, and R.D. Schwarz Evidence for seeding of beta -amyloid by intracerebral infusion of Alzheimer brain extracts in beta -amyloid precursor protein-transgenic mice J Neurosci 20 10 2000 3606 3611 (Pubitemid 30266223)
    • (2000) Journal of Neuroscience , vol.20 , Issue.10 , pp. 3606-3611
    • Kane, M.D.1    Lipinski, W.J.2    Callahan, M.J.3    Bian, F.4    Durham, R.A.5    Schwarz, R.D.6    Roher, A.E.7    Walker, L.C.8
  • 130
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • DOI 10.1038/nm0202-143
    • M.V. Karpuj, M.W. Becher, J.E. Springer, D. Chabas, S. Youssef, and R. Pedotti Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine Nat Med 8 2 2002 143 149 (Pubitemid 34155125)
    • (2002) Nature Medicine , vol.8 , Issue.2 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8
  • 132
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • K.B. Kegel, M. Kim, E. Sapp, C. McIntyre, J.G. Castano, and N. Aronin Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy J Neurosci 20 19 2000 7268 7278
    • (2000) J Neurosci , vol.20 , Issue.19 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6
  • 134
    • 57349187188 scopus 로고    scopus 로고
    • Glucosamine is an effective chemo-sensitizer via transglutaminase 2 inhibition
    • D.S. Kim, K.S. Park, K.C. Jeong, B.I. Lee, C.H. Lee, and S.Y. Kim Glucosamine is an effective chemo-sensitizer via transglutaminase 2 inhibition Cancer Lett 273 2 2009 243 249
    • (2009) Cancer Lett , vol.273 , Issue.2 , pp. 243-249
    • Kim, D.S.1    Park, K.S.2    Jeong, K.C.3    Lee, B.I.4    Lee, C.H.5    Kim, S.Y.6
  • 135
    • 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 43 1999 30715 30721
    • (1999) J Biol Chem , vol.274 , Issue.43 , pp. 30715-30721
    • Kim, S.Y.1    Grant, P.2    Lee, J.H.3    Pant, H.C.4    Steinert, P.M.5
  • 136
    • 70449709331 scopus 로고    scopus 로고
    • Functional significance of five noncanonical Ca2+-binding sites of human transglutaminase 2 characterized by site-directed mutagenesis
    • R. Kiraly, E. Csosz, T. Kurtan, S. Antus, K. Szigeti, and Z. Simon-Vecsei Functional significance of five noncanonical Ca2+-binding sites of human transglutaminase 2 characterized by site-directed mutagenesis FEBS J 276 23 2009 7083 7096
    • (2009) FEBS J , vol.276 , Issue.23 , pp. 7083-7096
    • Kiraly, R.1    Csosz, E.2    Kurtan, T.3    Antus, S.4    Szigeti, K.5    Simon-Vecsei, Z.6
  • 137
    • 13544252480 scopus 로고    scopus 로고
    • Covalent blocking of fibril formation and aggregation of intracellular amyloidgenic proteins by transglutaminase-catalyzed intramolecular cross-linking
    • DOI 10.1021/bi047722d
    • T. Konno, T. Morii, A. Hirata, S. Sato, S. Oiki, and K. Ikura Covalent blocking of fibril formation and aggregation of intracellular amyloidgenic proteins by transglutaminase-catalyzed intramolecular cross-linking Biochemistry 44 6 2005 2072 2079 (Pubitemid 40223634)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 2072-2079
    • Konno, T.1    Morii, T.2    Hirata, A.3    Sato, S.-I.4    Oiki, S.5    Ikura, K.6
  • 138
    • 0024417118 scopus 로고
    • Bovine aortic endothelial cell transglutaminase. Enzyme characterization and regulation of activity
    • G. Korner, D.E. Schneider, M.A. Purdon, and T.D. Bjornsson Bovine aortic endothelial cell transglutaminase. Enzyme characterization and regulation of activity Biochem J 262 2 1989 633 641 (Pubitemid 19228147)
    • (1989) Biochemical Journal , vol.262 , Issue.2 , pp. 633-641
    • Korner, G.1    Schneider, D.E.2    Purdon, M.A.3    Bjornsson, T.D.4
  • 141
    • 0030997651 scopus 로고    scopus 로고
    • Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase
    • DOI 10.1074/jbc.272.26.16295
    • T.S. Lai, A. Bielawska, K.A. Peoples, Y.A. Hannun, and C.S. Greenberg Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase J Biol Chem 272 26 1997 16295 16300 (Pubitemid 27276451)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.26 , pp. 16295-16300
    • Lai, T.-S.1    Bielawska, A.2    Peoples, K.A.3    Hannun, Y.A.4    Greenberg, C.S.5
  • 142
    • 0035942305 scopus 로고    scopus 로고
    • Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase
    • DOI 10.1021/bi002321t
    • T.S. Lai, A. Hausladen, T.F. Slaughter, J.P. Eu, J.S. Stamler, and C.S. Greenberg Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase Biochemistry 40 16 2001 4904 4910 (Pubitemid 32332535)
    • (2001) Biochemistry , vol.40 , Issue.16 , pp. 4904-4910
    • Lai, T.S.1    Hausladen, A.2    Slaughter, T.F.3    Eu, J.P.4    Stamler, J.S.5    Greenberg, C.S.6
  • 143
    • 51649127246 scopus 로고    scopus 로고
    • Identification of chemical inhibitors to human tissue transglutaminase by screening existing drug libraries
    • T.S. Lai, Y. Liu, T. Tucker, K.R. Daniel, D.C. Sane, and E. Toone Identification of chemical inhibitors to human tissue transglutaminase by screening existing drug libraries Chem Biol 15 9 2008 969 978
    • (2008) Chem Biol , vol.15 , Issue.9 , pp. 969-978
    • Lai, T.S.1    Liu, Y.2    Tucker, T.3    Daniel, K.R.4    Sane, D.C.5    Toone, E.6
  • 144
    • 0029856983 scopus 로고    scopus 로고
    • C-terminal deletion of human tissue transglutaminase enhances magnesium- dependent GTP/ATPase activity
    • DOI 10.1074/jbc.271.49.31191
    • T.S. Lai, T.F. Slaughter, C.M. Koropchak, Z.A. Haroon, and C.S. Greenberg C-terminal deletion of human tissue transglutaminase enhances magnesium-dependent GTP/ATPase activity J Biol Chem 271 49 1996 31191 31195 (Pubitemid 26408562)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.49 , pp. 31191-31195
    • Lai, T.-S.1    Slaughter, T.F.2    Koropchak, C.M.3    Haroon, Z.A.4    Greenberg, C.S.5
  • 145
    • 0031890194 scopus 로고    scopus 로고
    • Regulation of human tissue transglutaminase function by magnesium- nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP
    • DOI 10.1074/jbc.273.3.1776
    • T.S. Lai, T.F. Slaughter, K.A. Peoples, J.M. Hettasch, and C.S. Greenberg Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP J Biol Chem 273 3 1998 1776 1781 (Pubitemid 28133710)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.3 , pp. 1776-1781
    • Lai, T.-S.1    Slaughter, T.F.2    Peoples, K.A.3    Hettasch, J.M.4    Greenberg, C.S.5
  • 146
    • 1442348416 scopus 로고    scopus 로고
    • Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats
    • DOI 10.1046/j.1471-4159.2003.02249.x
    • T.S. Lai, T. Tucker, J.R. Burke, W.J. Strittmatter, and C.S. Greenberg Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats J Neurochem 88 5 2004 1253 1260 (Pubitemid 38280693)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.5 , pp. 1253-1260
    • Lai, T.-S.1    Tucker, T.2    Burke, J.R.3    Strittmatter, W.J.4    Greenberg, C.S.5
  • 147
    • 11144233953 scopus 로고    scopus 로고
    • Transglutaminase 2 induces nuclear factor-κB activation via a novel pathway in BV-2 microglia
    • DOI 10.1074/jbc.M407627200
    • J. Lee, Y.S. Kim, D.H. Choi, M.S. Bang, T.R. Han, and T.H. Joh Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia J Biol Chem 279 51 2004 53725 53735 (Pubitemid 40051881)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53725-53735
    • Lee, J.1    Kim, Y.-S.2    Choi, D.-H.3    Moon, S.B.4    Tai, R.H.5    Joh, T.H.6    Kim, S.-Y.7
  • 149
    • 0031049722 scopus 로고    scopus 로고
    • + channel by Gα(h) (transglutaminase II) in the vascular smooth muscle cell
    • DOI 10.1007/s004240050330
    • M.Y. Lee, S. Chung, H.W. Bang, K.J. Baek, and D. Uhm Modulation of large conductance Ca2+-activated K+ channel by Galphah (transglutaminase II) in the vascular smooth muscle cell Pflugers Arch 433 5 1997 671 673 (Pubitemid 27093131)
    • (1997) Pflugers Archiv European Journal of Physiology , vol.433 , Issue.5 , pp. 671-673
    • Lee, M.-Y.1    Chung, S.2    Bang, H.-W.3    Baek, K.J.4    Uhm, D.-Y.5
  • 150
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • DOI 10.1074/jbc.273.20.11991
    • M. Lesort, K. Attanavanich, J. Zhang, and G.V. Johnson Distinct nuclear localization and activity of tissue transglutaminase J Biol Chem 273 20 1998 11991 11994 (Pubitemid 28240553)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.20 , pp. 11991-11994
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.W.4
  • 151
    • 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 5 1999 2018 2027 (Pubitemid 29491816)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.5 , pp. 2018-2027
    • Lesort, M.1    Chun, W.2    Johnson, G.V.W.3    Ferrante, R.J.4
  • 152
    • 0037423204 scopus 로고    scopus 로고
    • Cystamine inhibits caspase activity: Implications for the treatment of polyglutamine disorders
    • DOI 10.1074/jbc.M205812200
    • 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 6 2003 3825 3830 (Pubitemid 36801110)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 3825-3830
    • Lesort, M.1    Lee, M.2    Tucholski, J.3    Johnson, G.V.W.4
  • 153
    • 0034257067 scopus 로고    scopus 로고
    • Tissue transglutaminase: A possible role in neurodegenerative diseases
    • DOI 10.1016/S0301-0082(99)00052-0, PII S0301008299000520
    • M. Lesort, J. Tucholski, M.L. Miller, and G.V. Johnson Tissue transglutaminase: a possible role in neurodegenerative diseases Prog Neurobiol 61 5 2000 439 463 (Pubitemid 30169054)
    • (2000) Progress in Neurobiology , vol.61 , Issue.5 , pp. 439-463
    • Lesort, M.1    Tucholski, J.2    Miller, M.L.3    Johnson, G.V.W.4
  • 154
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • DOI 10.1073/pnas.042454899
    • 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 5 2002 2743 2747 (Pubitemid 34240531)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.5 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 155
    • 0026514824 scopus 로고
    • Microdomains of high calcium concentration in a presynaptic terminal
    • R. Llinas, M. Sugimori, and R.B. Silver Microdomains of high calcium concentration in a presynaptic terminal Science 256 5057 1992 677 679
    • (1992) Science , vol.256 , Issue.5057 , pp. 677-679
    • Llinas, R.1    Sugimori, M.2    Silver, R.B.3
  • 156
    • 0031764609 scopus 로고    scopus 로고
    • DRPLA aggregation and transglutaminase, revisited
    • L. Lorand DRPLA aggregation and transglutaminase, revisited Nat Genet 20 3 1998 231
    • (1998) Nat Genet , vol.20 , Issue.3 , pp. 231
    • Lorand, L.1
  • 158
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • DOI 10.1038/nrm1014
    • L. Lorand, and R.M. Graham Transglutaminases: crosslinking enzymes with pleiotropic functions Nat Rev Mol Cell Biol 4 2 2003 140 156 (Pubitemid 36172696)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.2 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 159
    • 0032077093 scopus 로고    scopus 로고
    • Novel inhibitors against the transglutaminase-catalysed crosslinking of lens proteins
    • DOI 10.1006/exer.1997.0463
    • L. Lorand, A.M. Stern, and P.T. Velasco Novel inhibitors against the transglutaminase-catalysed crosslinking of lens proteins Exp Eye Res 66 5 1998 531 536 (Pubitemid 28267123)
    • (1998) Experimental Eye Research , vol.66 , Issue.5 , pp. 531-536
    • Lorand, L.1    Stern, A.M.2    Velasco, P.T.3
  • 161
    • 77956396747 scopus 로고    scopus 로고
    • Defective CFTR induces aggresome formation and lung inflammation in cystic fibrosis through ROS-mediated autophagy inhibition
    • A. Luciani, V.R. Villella, S. Esposito, N. Brunetti-Pierri, D. Medina, and C. Settembre Defective CFTR induces aggresome formation and lung inflammation in cystic fibrosis through ROS-mediated autophagy inhibition Nat Cell Biol 12 9 2010 863 875
    • (2010) Nat Cell Biol , vol.12 , Issue.9 , pp. 863-875
    • Luciani, A.1    Villella, V.R.2    Esposito, S.3    Brunetti-Pierri, N.4    Medina, D.5    Settembre, C.6
  • 162
    • 72149119358 scopus 로고    scopus 로고
    • Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
    • K.C. Luk, C. Song, P. O'Brien, A. Stieber, J.R. Branch, and K.R. Brunden Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells Proc Natl Acad Sci U S A 106 47 2009 20051 20056
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.47 , pp. 20051-20056
    • Luk, K.C.1    Song, C.2    O'Brien, P.3    Stieber, A.4    Branch, J.R.5    Brunden, K.R.6
  • 164
    • 0035656107 scopus 로고    scopus 로고
    • Synthesis and evaluation of novel dipeptide-bound 1,2,4-thiadiazoles as irreversible inhibitors of guinea pig liver transglutaminase
    • C. Marrano, P. de Macedo, P. Gagnon, D. Lapierre, C. Gravel, and J.W. Keillor Synthesis and evaluation of novel dipeptide-bound 1,2,4-thiadiazoles as irreversible inhibitors of guinea pig liver transglutaminase Bioorg Med Chem 9 12 2001 3231 3241
    • (2001) Bioorg Med Chem , vol.9 , Issue.12 , pp. 3231-3241
    • Marrano, C.1    De MacEdo, P.2    Gagnon, P.3    Lapierre, D.4    Gravel, C.5    Keillor, J.W.6
  • 165
    • 0034951866 scopus 로고    scopus 로고
    • Evaluation of novel dipeptide-bound α,β-unsaturated amides and epoxides as irreversible inhibitors of guinea pig liver transglutaminase
    • DOI 10.1016/S0968-0896(01)00101-8, PII S0968089601001018
    • C. Marrano, P. de Macedo, and J.W. Keillor Evaluation of novel dipeptide-bound alpha, beta-unsaturated amides and epoxides as irreversible inhibitors of guinea pig liver transglutaminase Bioorg Med Chem 9 7 2001 1923 1928 (Pubitemid 32655022)
    • (2001) Bioorganic and Medicinal Chemistry , vol.9 , Issue.7 , pp. 1923-1928
    • Marrano, C.1    De Macedo, P.2    Keillor, J.W.3
  • 166
    • 33745755214 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed reactions responsible for the pathogenesis of celiac disease and neurodegenerative diseases: From basic biochemistry to clinic
    • A. Martin, G. Romito, I. Pepe, G. De Vivo, M.R. Merola, and A. Limatola Transglutaminase-catalyzed reactions responsible for the pathogenesis of celiac disease and neurodegenerative diseases: from basic biochemistry to clinic Curr Med Chem 13 16 2006 1895 1902
    • (2006) Curr Med Chem , vol.13 , Issue.16 , pp. 1895-1902
    • Martin, A.1    Romito, G.2    Pepe, I.3    De Vivo, G.4    Merola, M.R.5    Limatola, A.6
  • 167
    • 0028231735 scopus 로고
    • Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers
    • J. Martinez, D.G. Chalupowicz, R.K. Roush, A. Sheth, and C. Barsigian Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers Biochemistry 33 9 1994 2538 2545 (Pubitemid 24099661)
    • (1994) Biochemistry , vol.33 , Issue.9 , pp. 2538-2545
    • Martinez, J.1    Chalupowicz, D.G.2    Roush, R.K.3    Sheth, A.4    Barsigian, C.5
  • 170
    • 77958614199 scopus 로고    scopus 로고
    • Type 2 transglutaminase in Huntington's disease: A double-edged sword with clinical potential
    • P.G. Mastroberardino, and M. Piacentini Type 2 transglutaminase in Huntington's disease: a double-edged sword with clinical potential J Intern Med 268 5 2010 419 431
    • (2010) J Intern Med , vol.268 , Issue.5 , pp. 419-431
    • Mastroberardino, P.G.1    Piacentini, M.2
  • 171
    • 77956949459 scopus 로고    scopus 로고
    • Inhibition of transglutaminase 2 mitigates transcriptional dysregulation in models of Huntington disease
    • S.J. McConoughey, M. Basso, Z.V. Niatsetskaya, S.F. Sleiman, N.A. Smirnova, and B.C. Langley Inhibition of transglutaminase 2 mitigates transcriptional dysregulation in models of Huntington disease EMBO Mol Med 2 9 2010 349 370
    • (2010) EMBO Mol Med , vol.2 , Issue.9 , pp. 349-370
    • McConoughey, S.J.1    Basso, M.2    Niatsetskaya, Z.V.3    Sleiman, S.F.4    Smirnova, N.A.5    Langley, B.C.6
  • 173
    • 0033525041 scopus 로고    scopus 로고
    • Regulation of the transglutaminase I gene. Identification of DNA elements involved in its transcriptional control in tracheobronchial epithelial cells
    • DOI 10.1074/jbc.274.6.3887
    • A. Medvedev, N.A. Saunders, H. Matsuura, A. Chistokhina, and A.M. Jetten Regulation of the transglutaminase I gene. Identification of DNA elements involved in its transcriptional control in tracheobronchial epithelial cells J Biol Chem 274 6 1999 3887 3896 (Pubitemid 29077239)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.6 , pp. 3887-3896
    • Medvedev, A.1    Saunders, N.A.2    Matsuura, H.3    Chistokhina, A.4    Jetten, A.M.5
  • 174
    • 32844467408 scopus 로고    scopus 로고
    • Tissue transglutaminase: From biological glue to cell survival cues
    • K. Mehta, J.Y. Fok, and L.S. Mangala Tissue transglutaminase: from biological glue to cell survival cues Front Biosci 11 2006 173 185 (Pubitemid 43253484)
    • (2006) Frontiers in Bioscience , vol.11 , pp. 173-185
    • Mehta, K.1    Fok, J.Y.2    Mangala, L.S.3
  • 175
    • 0030071518 scopus 로고    scopus 로고
    • Activation of retinoid receptors RARα and RXRα induces differentiation and apoptosis, respectively, in HL-60 cells
    • K. Mehta, T. McQueen, N. Neamati, S. Collins, and M. Andreeff Activation of retinoid receptors RAR alpha and RXR alpha induces differentiation and apoptosis, respectively, in HL-60 cells Cell Growth Differ 7 2 1996 179 186 (Pubitemid 26049826)
    • (1996) Cell Growth and Differentiation , vol.7 , Issue.2 , pp. 179-186
    • Mehta, K.1    McQueen, T.2    Neamati, N.3    Collins, S.4    Andreeff, M.5
  • 178
    • 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 1-2 1995 27 31
    • (1995) FEBS Lett , vol.370 , Issue.12 , pp. 27-31
    • Mian, S.1    El Alaoui, S.2    Lawry, J.3    Gentile, V.4    Davies, P.J.5    Griffin, M.6
  • 179
    • 34547110814 scopus 로고    scopus 로고
    • Transglutaminase 2 kinase activity facilitates protein kinase A-induced phosphorylation of retinoblastoma protein
    • DOI 10.1074/jbc.M607413200
    • S. Mishra, G. Melino, and L.J. Murphy Transglutaminase 2 kinase activity facilitates protein kinase A-induced phosphorylation of retinoblastoma protein J Biol Chem 282 25 2007 18108 18115 (Pubitemid 47100203)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18108-18115
    • Mishra, S.1    Melino, G.2    Murphy, L.J.3
  • 180
    • 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
    • DOI 10.1074/jbc.M311919200
    • S. Mishra, and L.J. Murphy Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase J Biol Chem 279 23 2004 23863 23868 (Pubitemid 38725242)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 181
    • 28444488402 scopus 로고    scopus 로고
    • The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity
    • DOI 10.1016/j.bbrc.2005.11.071, PII S0006291X05025982
    • S. Mishra, and L.J. Murphy The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity Biochem Biophys Res Commun 339 2 2006 726 730 (Pubitemid 41739727)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.2 , pp. 726-730
    • Mishra, S.1    Murphy, L.J.2
  • 183
    • 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 6 1997 3724 3732
    • (1997) J Biol Chem , vol.272 , Issue.6 , pp. 3724-3732
    • Monsonego, A.1    Shani, Y.2    Friedmann, I.3    Paas, Y.4    Eizenberg, O.5    Schwartz, M.6
  • 184
    • 71549121663 scopus 로고    scopus 로고
    • Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-beta oligomers
    • B.D. Moore, V. Rangachari, W.M. Tay, N.M. Milkovic, and T.L. Rosenberry Biophysical analyses of synthetic amyloid-beta(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-beta oligomers Biochemistry 48 49 2009 11796 11806
    • (2009) Biochemistry , vol.48 , Issue.49 , pp. 11796-11806
    • Moore, B.D.1    Rangachari, V.2    Tay, W.M.3    Milkovic, N.M.4    Rosenberry, T.L.5
  • 186
    • 79955456732 scopus 로고    scopus 로고
    • Mutant huntingtin causes defective actin remodeling during stress: Defining a new role for transglutaminase 2 in neurodegenerative disease
    • L. Munsie, N. Caron, R.S. Atwal, I. Marsden, E.J. Wild, and J.R. Bamburg Mutant huntingtin causes defective actin remodeling during stress: defining a new role for transglutaminase 2 in neurodegenerative disease Hum Mol Genet 20 10 2011 1937 1951
    • (2011) Hum Mol Genet , vol.20 , Issue.10 , pp. 1937-1951
    • Munsie, L.1    Caron, N.2    Atwal, R.S.3    Marsden, I.4    Wild, E.J.5    Bamburg, J.R.6
  • 188
    • 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 6 1998 2607 2614 (Pubitemid 28531274)
    • (1998) Journal of Neurochemistry , vol.71 , Issue.6 , pp. 2607-2614
    • Murthy, S.N.P.1    Wilson, J.H.2    Lukas, T.J.3    Kuret, J.4    Lorand, L.5
  • 189
    • 0030051022 scopus 로고    scopus 로고
    • Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter
    • L. Nagy, M. Saydak, N. Shipley, S. Lu, J.P. Basilion, and Z.H. Yan Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter J Biol Chem 271 8 1996 4355 4365
    • (1996) J Biol Chem , vol.271 , Issue.8 , pp. 4355-4365
    • Nagy, L.1    Saydak, M.2    Shipley, N.3    Lu, S.4    Basilion, J.P.5    Yan, Z.H.6
  • 190
    • 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 7 1997 534 547 (Pubitemid 127680688)
    • (1997) Cell Death and Differentiation , vol.4 , Issue.7 , pp. 534-547
    • Nagy, L.1    Thomazy, V.A.2    Saydak, M.M.3    Stein, J.P.4    Davies, P.J.A.5
  • 191
    • 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, and K. Misono Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function Science 264 5165 1994 1593 1596
    • (1994) Science , vol.264 , Issue.5165 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6
  • 194
    • 0034743767 scopus 로고    scopus 로고
    • ε(γ-glutamyl)lysine in cerebrospinal fluid marks Alzheimer type and vascular dementia
    • DOI 10.1016/S0197-4580(01)00224-X, PII S019745800100224X
    • Z. Nemes, L. Fesus, A. Egerhazi, A. Keszthelyi, and I.M. Degrell N(epsilon)(gamma-glutamyl)lysine in cerebrospinal fluid marks Alzheimer type and vascular dementia Neurobiol Aging 22 3 2001 403 406 (Pubitemid 32510911)
    • (2001) Neurobiology of Aging , vol.22 , Issue.3 , pp. 403-406
    • Nemes, Z.1    Fesus, L.2    Egerhazi, A.3    Keszthelyi, A.4    Degrell, I.M.5
  • 195
    • 70350437632 scopus 로고    scopus 로고
    • Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies
    • Z. Nemes, G. Petrovski, M. Aerts, K. Sergeant, B. Devreese, and L. Fesus Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies J Biol Chem 284 40 2009 27252 27264
    • (2009) J Biol Chem , vol.284 , Issue.40 , pp. 27252-27264
    • Nemes, Z.1    Petrovski, G.2    Aerts, M.3    Sergeant, K.4    Devreese, B.5    Fesus, L.6
  • 196
    • 57649178442 scopus 로고    scopus 로고
    • Oxidative stress and energy crises in neuronal dysfunction
    • D.G. Nicholls Oxidative stress and energy crises in neuronal dysfunction Ann N Y Acad Sci 1147 2008 53 60
    • (2008) Ann N y Acad Sci , vol.1147 , pp. 53-60
    • Nicholls, D.G.1
  • 197
    • 0030974902 scopus 로고    scopus 로고
    • Latent transforming growth factor-β binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-β
    • DOI 10.1083/jcb.136.5.1151
    • I. Nunes, P.E. Gleizes, C.N. Metz, and D.B. Rifkin Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta J Cell Biol 136 5 1997 1151 1163 (Pubitemid 27131745)
    • (1997) Journal of Cell Biology , vol.136 , Issue.5 , pp. 1151-1163
    • Nunes, I.1    Gleizes, P.-E.2    Metz, C.N.3    Rifkin, D.B.4
  • 199
  • 200
    • 33750514359 scopus 로고    scopus 로고
    • Synthesis and evaluation of peptidic irreversible inhibitors of tissue transglutaminase
    • DOI 10.1016/j.bmc.2006.09.011, PII S0968089606007279
    • C. Pardin, S.M. Gillet, and J.W. Keillor Synthesis and evaluation of peptidic irreversible inhibitors of tissue transglutaminase Bioorg Med Chem 14 24 2006 8379 8385 (Pubitemid 44667551)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.24 , pp. 8379-8385
    • Pardin, C.1    Gillet, S.M.F.G.2    Keillor, J.W.3
  • 201
    • 48249124215 scopus 로고    scopus 로고
    • Cinnamoyl inhibitors of tissue transglutaminase
    • C. Pardin, J.N. Pelletier, W.D. Lubell, and J.W. Keillor Cinnamoyl inhibitors of tissue transglutaminase J Org Chem 73 15 2008 5766 5775
    • (2008) J Org Chem , vol.73 , Issue.15 , pp. 5766-5775
    • Pardin, C.1    Pelletier, J.N.2    Lubell, W.D.3    Keillor, J.W.4
  • 202
    • 50449111031 scopus 로고    scopus 로고
    • Reversible and competitive cinnamoyl triazole inhibitors of tissue transglutaminase
    • C. Pardin, I. Roy, W.D. Lubell, and J.W. Keillor Reversible and competitive cinnamoyl triazole inhibitors of tissue transglutaminase Chem Biol Drug Des 72 3 2008 189 196
    • (2008) Chem Biol Drug des , vol.72 , Issue.3 , pp. 189-196
    • Pardin, C.1    Roy, I.2    Lubell, W.D.3    Keillor, J.W.4
  • 203
    • 77956916373 scopus 로고    scopus 로고
    • Transglutaminase 2: A multi-functional protein in multiple subcellular compartments
    • D. Park, S.S. Choi, and K.S. Ha Transglutaminase 2: a multi-functional protein in multiple subcellular compartments Amino Acids 39 3 2010 619 631
    • (2010) Amino Acids , vol.39 , Issue.3 , pp. 619-631
    • Park, D.1    Choi, S.S.2    Ha, K.S.3
  • 205
    • 79957822028 scopus 로고    scopus 로고
    • TNF-alpha mediated NF-kappaB activation is constantly extended by transglutaminase 2
    • K.S. Park, D.S. Kim, C. Ko, S.J. Lee, S.H. Oh, and S.Y. Kim TNF-alpha mediated NF-kappaB activation is constantly extended by transglutaminase 2 Front Biosci (Elite Ed) 3 2011 341 354
    • (2011) Front Biosci (Elite Ed) , vol.3 , pp. 341-354
    • Park, K.S.1    Kim, D.S.2    Ko, C.3    Lee, S.J.4    Oh, S.H.5    Kim, S.Y.6
  • 206
    • 0025092129 scopus 로고
    • Transglutaminase activity in reversible cerebral ischemia in the rat
    • W. Paschen, G. Rohn, and R. Schmidt-Kastner Transglutaminase activity in reversible cerebral ischemia in the rat Neurosci Lett 110 1-2 1990 232 236 (Pubitemid 20059583)
    • (1990) Neuroscience Letters , vol.110 , Issue.1-2 , pp. 232-236
    • Paschen, W.1    Rohn, G.2    Schmidt-Kastner, R.3
  • 207
    • 0032988045 scopus 로고    scopus 로고
    • Interaction of tissue transglutaminase with nuclear transport protein importin-α3
    • DOI 10.1016/S0014-5793(99)00018-6, PII S0014579399000186
    • X. Peng, Y. Zhang, H. Zhang, S. Graner, J.F. Williams, and M.L. Levitt Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3 FEBS Lett 446 1 1999 35 39 (Pubitemid 29127245)
    • (1999) FEBS Letters , vol.446 , Issue.1 , pp. 35-39
    • Peng, X.1    Zhang, Y.2    Zhang, H.3    Graner, S.4    Williams, J.F.5    Levitt, M.L.6    Lokshin, A.7
  • 208
    • 0026786093 scopus 로고
    • Phenotype-specific "tissue" transglutaminase regulation in human neuroblastoma cells in response to retinoic acid: Correlation with cell death by apoptosis
    • M. Piacentini, M. Annicchiarico-Petruzzelli, S. Oliverio, L. Piredda, J.L. Biedler, and E. Melino Phenotype-specific "tissue" transglutaminase regulation in human neuroblastoma cells in response to retinoic acid: correlation with cell death by apoptosis Int J Cancer 52 2 1992 271 278
    • (1992) Int J Cancer , vol.52 , Issue.2 , pp. 271-278
    • Piacentini, M.1    Annicchiarico-Petruzzelli, M.2    Oliverio, S.3    Piredda, L.4    Biedler, J.L.5    Melino, E.6
  • 209
    • 0026693929 scopus 로고
    • In vivo and in vitro induction of 'tissue' transglutaminase in rat hepatocytes by retinoic acid
    • M. Piacentini, M.P. Ceru, L. Dini, M. Di Rao, L. Piredda, and V. Thomazy In vivo and in vitro induction of 'tissue' transglutaminase in rat hepatocytes by retinoic acid Biochim Biophys Acta 1135 2 1992 171 179
    • (1992) Biochim Biophys Acta , vol.1135 , Issue.2 , pp. 171-179
    • Piacentini, M.1    Ceru, M.P.2    Dini, L.3    Di Rao, M.4    Piredda, L.5    Thomazy, V.6
  • 210
    • 0001911727 scopus 로고
    • Tissue transglutaminase in cells undergoing apoptosis
    • L.D. Tomei, F.O. Cope, Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • M. Piacentini, P.J.A. Davies, and L. Fesus Tissue transglutaminase in cells undergoing apoptosis L.D. Tomei, F.O. Cope, Apoptosis II: The Molecular Basis of Apoptosis in Disease 1994 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 143 163
    • (1994) Apoptosis II: The Molecular Basis of Apoptosis in Disease , pp. 143-163
    • Piacentini, M.1    Davies, P.J.A.2    Fesus, L.3
  • 212
    • 0025728132 scopus 로고
    • The expression of "tissue" transglutaminase in two human cancer cell lines is related with the programmed cell death (apoptosis)
    • M. Piacentini, L. Fesus, M.G. Farrace, L. Ghibelli, L. Piredda, and G. Melino The expression of "tissue" transglutaminase in two human cancer cell lines is related with the programmed cell death (apoptosis) Eur J Cell Biol 54 2 1991 246 254
    • (1991) Eur J Cell Biol , vol.54 , Issue.2 , pp. 246-254
    • Piacentini, M.1    Fesus, L.2    Farrace, M.G.3    Ghibelli, L.4    Piredda, L.5    Melino, G.6
  • 214
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • D.M. Pinkas, P. Strop, A.T. Brunger, and C. Khosla Transglutaminase 2 undergoes a large conformational change upon activation PLoS Biol 5 12 2007 e327
    • (2007) PLoS Biol , vol.5 , Issue.12 , pp. 327
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 215
    • 0037039447 scopus 로고    scopus 로고
    • High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: Implications for Celiac Sprue
    • DOI 10.1021/bi011715x
    • 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 1 2002 386 393 (Pubitemid 34049414)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 386-393
    • Piper, J.L.1    Gray, G.M.2    Khosla, C.3
  • 218
    • 0003631524 scopus 로고    scopus 로고
    • 3 rd ed Sinauer Associates Sunderland, Mass
    • D. Purves Neuroscience 3 rd ed 2004 Sinauer Associates Sunderland, Mass
    • (2004) Neuroscience
    • Purves, D.1
  • 219
    • 0032802769 scopus 로고    scopus 로고
    • HLA binding and T cell recognition of a tissue transglutaminase-modified gliadin epitope
    • DOI 10.1002/(SICI)1521-4141(199908)29:08<2506::AID-IMMU2506>3.0. CO;2-9
    • H. Quarsten, O. Molberg, L. Fugger, S.N. McAdam, and L.M. Sollid HLA binding and T cell recognition of a tissue transglutaminase-modified gliadin epitope Eur J Immunol 29 8 1999 2506 2514 (Pubitemid 29378121)
    • (1999) European Journal of Immunology , vol.29 , Issue.8 , pp. 2506-2514
    • Quarsten, H.1    Molberg, O.2    Fugger, L.3    McAdam, S.N.4    Sollid, L.M.5
  • 220
    • 0028144630 scopus 로고
    • 2M receptor
    • DOI 10.1016/0014-5793(94)80356-0
    • L.K. Rasmussen, E.S. Sorensen, T.E. Petersen, J. Gliemann, and P.H. Jensen Identification of glutamine and lysine residues in Alzheimer amyloid beta A4 peptide responsible for transglutaminase-catalysed homopolymerization and cross-linking to alpha 2M receptor FEBS Lett 338 2 1994 161 166 (Pubitemid 24064957)
    • (1994) FEBS Letters , vol.338 , Issue.2 , pp. 161-166
    • Rasmussen, L.K.1
  • 221
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • P.H. Ren, J.E. Lauckner, I. Kachirskaia, J.E. Heuser, R. Melki, and R.R. Kopito Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates Nat Cell Biol 11 2 2009 219 225
    • (2009) Nat Cell Biol , vol.11 , Issue.2 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 222
    • 0032557461 scopus 로고    scopus 로고
    • Identification of a transforming growth factor-β1/bone morphogenetic protein 4 (TGF-β1/BMP4) response element within the mouse tissue transglutaminase gene promoter
    • DOI 10.1074/jbc.273.21.12798
    • S.J. Ritter, and P.J. Davies Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter J Biol Chem 273 21 1998 12798 12806 (Pubitemid 28246835)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.21 , pp. 12798-12806
    • Ritter, S.J.1    Davies, P.J.A.2
  • 223
    • 34249808244 scopus 로고    scopus 로고
    • Transglutaminase 2 in neurodegenerative disorders
    • DOI 10.2741/2111
    • Q. Ruan, and G.V. Johnson Transglutaminase 2 in neurodegenerative disorders Front Biosci 12 2007 891 904 (Pubitemid 46846864)
    • (2007) Frontiers in Bioscience , vol.12 , Issue.3 , pp. 891-904
    • Ruan, Q.1    Johnson, G.V.W.2
  • 224
    • 24144442640 scopus 로고    scopus 로고
    • Tissue transglutaminase (TG2) acting as G protein protects hepatocytes against Fas-mediated cell death in mice
    • DOI 10.1002/hep.20812
    • Z. Sarang, P. Molnar, T. Nemeth, S. Gomba, T. Kardon, and G. Melino Tissue transglutaminase (TG2) acting as G protein protects hepatocytes against Fas-mediated cell death in mice Hepatology 42 3 2005 578 587 (Pubitemid 41233650)
    • (2005) Hepatology , vol.42 , Issue.3 , pp. 578-587
    • Sarang, Z.1    Molnar, P.2    Nemeth, T.3    Gomba, S.4    Kardon, T.5    Melino, G.6    Cotecchia, S.7    Fesus, L.8    Szondy, Z.9
  • 225
    • 67349196431 scopus 로고    scopus 로고
    • Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: Implications for the pathogenesis of Parkinson disease
    • A.W. Schmid, D. Chiappe, V. Pignat, V. Grimminger, I. Hang, and M. Moniatte Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease J Biol Chem 284 19 2009 13128 13142
    • (2009) J Biol Chem , vol.284 , Issue.19 , pp. 13128-13142
    • Schmid, A.W.1    Chiappe, D.2    Pignat, V.3    Grimminger, V.4    Hang, I.5    Moniatte, M.6
  • 227
    • 34447286702 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitors and their therapeutic role in disease states
    • DOI 10.1016/j.pharmthera.2007.05.003, PII S0163725807000885
    • M. Siegel, and C. Khosla Transglutaminase 2 inhibitors and their therapeutic role in disease states Pharmacol Ther 115 2 2007 232 245 (Pubitemid 47042912)
    • (2007) Pharmacology and Therapeutics , vol.115 , Issue.2 , pp. 232-245
    • Siegel, M.1    Khosla, C.2
  • 228
    • 34447647295 scopus 로고    scopus 로고
    • Structure-based design of α-amido aldehyde containing gluten peptide analogues as modulators of HLA-DQ2 and transglutaminase 2
    • DOI 10.1016/j.bmc.2007.06.020, PII S0968089607005433
    • M. Siegel, J. Xia, and C. Khosla Structure-based design of alpha-amido aldehyde containing gluten peptide analogues as modulators of HLA-DQ2 and transglutaminase 2 Bioorg Med Chem 15 18 2007 6253 6261 (Pubitemid 47088951)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.18 , pp. 6253-6261
    • Siegel, M.1    Xia, J.2    Khosla, C.3
  • 229
    • 0036134831 scopus 로고    scopus 로고
    • Transglutaminase bonds in neurofibrillary tangles and paired helical filament tau early in Alzheimer's disease
    • DOI 10.1016/S0197-0186(01)00061-4, PII S0197018601000614
    • 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 1 2002 17 30 (Pubitemid 34003555)
    • (2002) Neurochemistry International , vol.40 , Issue.1 , pp. 17-30
    • Singer, S.M.1    Zainelli, G.M.2    Norlund, M.A.3    Lee, J.M.4    Muma, N.A.5
  • 230
    • 0029861050 scopus 로고    scopus 로고
    • Biochemical effects of retinoic acid on GTP-binding protein/ transglutaminases in HeLa cells: Stimulation of GTP-binding and transglutaminase activity, membrane association, and phosphatidylinositol lipid turnover
    • DOI 10.1074/jbc.271.44.27292
    • U.S. Singh, and R.A. Cerione Biochemical effects of retinoic acid on GTP-binding Protein/Transglutaminases in HeLa cells. Stimulation of GTP-binding and transglutaminase activity, membrane association, and phosphatidylinositol lipid turnover J Biol Chem 271 44 1996 27292 27298 (Pubitemid 26367282)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27292-27298
    • Singh, U.S.1    Cerione, R.A.2
  • 231
    • 0028828698 scopus 로고
    • Identification and biochemical characterization of an 80 kilodalton GTP-binding/transglutaminase from rabbit liver nuclei
    • U.S. Singh, J.W. Erickson, and R.A. Cerione Identification and biochemical characterization of an 80 kilodalton GTP-binding/transglutaminase from rabbit liver nuclei Biochemistry 34 48 1995 15863 15871
    • (1995) Biochemistry , vol.34 , Issue.48 , pp. 15863-15871
    • Singh, U.S.1    Erickson, J.W.2    Cerione, R.A.3
  • 232
    • 0035872859 scopus 로고    scopus 로고
    • Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2
    • DOI 10.1093/emboj/20.10.2413
    • 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 10 2001 2413 2423 (Pubitemid 32452859)
    • (2001) EMBO Journal , vol.20 , Issue.10 , pp. 2413-2423
    • Singh, U.S.1    Kunar, M.T.2    Kao, Y.-L.3    Baker, K.M.4
  • 233
    • 0021838059 scopus 로고
    • Subcellular localization of a membrane-associated transglutaminase activity in rat liver
    • DOI 10.1016/0003-9861(85)90554-5
    • C.W. Slife, M.D. Dorsett, G.T. Bouquett, A. Register, E. Taylor, and S. Conroy Subcellular localization of a membrane-associated transglutaminase activity in rat liver Arch Biochem Biophys 241 2 1985 329 336 (Pubitemid 15023261)
    • (1985) Archives of Biochemistry and Biophysics , vol.241 , Issue.2 , pp. 329-336
    • Slife, C.W.1    Dorsett, M.D.2    Bouquett, G.T.3
  • 234
    • 0033597861 scopus 로고    scopus 로고
    • Cardiac specific overexpression of transglutaminase II (G(h)) results in a unique hypertrophy phenotype independent of phospholipase C activation
    • K. Small, J.F. Feng, J. Lorenz, E.T. Donnelly, A. Yu, and M.J. Im Cardiac specific overexpression of transglutaminase II (G(h)) results in a unique hypertrophy phenotype independent of phospholipase C activation J Biol Chem 274 30 1999 21291 21296
    • (1999) J Biol Chem , vol.274 , Issue.30 , pp. 21291-21296
    • Small, K.1    Feng, J.F.2    Lorenz, J.3    Donnelly, E.T.4    Yu, A.5    Im, M.J.6
  • 235
    • 0030032813 scopus 로고    scopus 로고
    • Measurement of tissue transglutaminase activity in a permeabilized cell system: Its regulation by Ca2+ and nucleotides
    • P.A. Smethurst, and M. Griffin Measurement of tissue transglutaminase activity in a permeabilized cell system: its regulation by Ca2+ and nucleotides Biochem J 313 Pt 3 1996 803 808
    • (1996) Biochem J , vol.313 , Issue.PART 3 , pp. 803-808
    • Smethurst, P.A.1    Griffin, M.2
  • 236
    • 0037252190 scopus 로고    scopus 로고
    • Novel transglutaminase inhibitors reverse the inflammation of allergic conjunctivitis
    • DOI 10.1172/JCI200315937
    • 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 1 2003 121 128 (Pubitemid 36134855)
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.1 , pp. 121-128
    • Sohn, J.1    Kim, T.-I.2    Yoon, Y.-H.3    Kim, J.-Y.4    Kim, S.-Y.5
  • 237
    • 39149116708 scopus 로고    scopus 로고
    • Therapeutic attenuation of mitochondrial dysfunction and oxidative stress in neurotoxin models of Parkinson's disease
    • E.C. Stack, J.L. Ferro, J. Kim, S.J. Del Signore, S. Goodrich, and S. Matson Therapeutic attenuation of mitochondrial dysfunction and oxidative stress in neurotoxin models of Parkinson's disease Biochim Biophys Acta 1782 3 2008 151 162
    • (2008) Biochim Biophys Acta , vol.1782 , Issue.3 , pp. 151-162
    • Stack, E.C.1    Ferro, J.L.2    Kim, J.3    Del Signore, S.J.4    Goodrich, S.5    Matson, S.6
  • 238
    • 33645988884 scopus 로고    scopus 로고
    • Pharmacologic transglutaminase inhibition attenuates drug-primed liver hypertrophy but not Mallory body formation
    • P. Strnad, M. Siegel, D.M. Toivola, K. Choi, J.C. Kosek, and C. Khosla Pharmacologic transglutaminase inhibition attenuates drug-primed liver hypertrophy but not Mallory body formation FEBS Lett 580 9 2006 2351 2357
    • (2006) FEBS Lett , vol.580 , Issue.9 , pp. 2351-2357
    • Strnad, P.1    Siegel, M.2    Toivola, D.M.3    Choi, K.4    Kosek, J.C.5    Khosla, C.6
  • 239
    • 77952322840 scopus 로고    scopus 로고
    • Effects of cysteamine on MPTP-induced dopaminergic neurodegeneration in mice
    • L. Sun, S. Xu, M. Zhou, C. Wang, Y. Wu, and P. Chan Effects of cysteamine on MPTP-induced dopaminergic neurodegeneration in mice Brain Res 1335 2010 74 82
    • (2010) Brain Res , vol.1335 , pp. 74-82
    • Sun, L.1    Xu, S.2    Zhou, M.3    Wang, C.4    Wu, Y.5    Chan, P.6
  • 242
    • 77958091268 scopus 로고    scopus 로고
    • Transglutaminase 2 expression induced by lipopolysaccharide stimulation together with NO synthase induction in cultured astrocytes
    • K. Takano, K. Shiraiwa, M. Moriyama, and Y. Nakamura Transglutaminase 2 expression induced by lipopolysaccharide stimulation together with NO synthase induction in cultured astrocytes Neurochem Int 57 7 2010 812 818
    • (2010) Neurochem Int , vol.57 , Issue.7 , pp. 812-818
    • Takano, K.1    Shiraiwa, K.2    Moriyama, M.3    Nakamura, Y.4
  • 243
    • 0026754093 scopus 로고
    • Putative nucleotide binding sites of guinea pig liver transglutaminase
    • Y. Takeuchi, P.J. Birckbichler, M.K. Patterson Jr., and K.N. Lee Putative nucleotide binding sites of guinea pig liver transglutaminase FEBS Lett 307 2 1992 177 180
    • (1992) FEBS Lett , vol.307 , Issue.2 , pp. 177-180
    • Takeuchi, Y.1    Birckbichler, P.J.2    Patterson, Jr.M.K.3    Lee, K.N.4
  • 244
    • 65249179547 scopus 로고    scopus 로고
    • Role of transglutaminase 2 in liver injury via cross-linking and silencing of transcription factor Sp1
    • e1710.
    • H. Tatsukawa, Y. Fukaya, G. Frampton, A. Martinez-Fuentes, K. Suzuki, and T.F. Kuo Role of transglutaminase 2 in liver injury via cross-linking and silencing of transcription factor Sp1 Gastroenterology 136 5 2009 1783 1795 e1710.
    • (2009) Gastroenterology , vol.136 , Issue.5 , pp. 1783-1795
    • Tatsukawa, H.1    Fukaya, Y.2    Frampton, G.3    Martinez-Fuentes, A.4    Suzuki, K.5    Kuo, T.F.6
  • 245
    • 0017196752 scopus 로고
    • Cystinosis. Intracellular cystine depletion by aminothiols in vitro and in vivo
    • J.G. Thoene, R.G. Oshima, J.C. Crawhall, D.L. Olson, and J.A. Schneider Cystinosis. Intracellular cystine depletion by aminothiols in vitro and in vivo J Clin Invest 58 1 1976 180 189
    • (1976) J Clin Invest , vol.58 , Issue.1 , pp. 180-189
    • Thoene, J.G.1    Oshima, R.G.2    Crawhall, J.C.3    Olson, D.L.4    Schneider, J.A.5
  • 246
    • 0024597647 scopus 로고
    • Differential expression of tissue transglutaminase in human cells. An immunohistochemical study
    • V. Thomazy, and L. Fesus Differential expression of tissue transglutaminase in human cells. An immunohistochemical study Cell Tissue Res 255 1 1989 215 224 (Pubitemid 19017924)
    • (1989) Cell and Tissue Research , vol.255 , Issue.1 , pp. 215-224
    • Thomazy, V.1    Fesus, L.2
  • 248
    • 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 5 1999 1871 1880 (Pubitemid 29491800)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.5 , pp. 1871-1880
    • Tucholski, J.1    Kuret, J.2    Johnson, G.V.W.3
  • 249
    • 33645310662 scopus 로고    scopus 로고
    • Tissue transglutaminase overexpression in the brain potentiates calcium-induced hippocampal damage
    • J. Tucholski, K.A. Roth, and G.V. Johnson Tissue transglutaminase overexpression in the brain potentiates calcium-induced hippocampal damage J Neurochem 97 2 2006 582 594
    • (2006) J Neurochem , vol.97 , Issue.2 , pp. 582-594
    • Tucholski, J.1    Roth, K.A.2    Johnson, G.V.3
  • 250
    • 0025885719 scopus 로고
    • Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme
    • H.F. Upchurch, E. Conway, M.K. Patterson Jr., and M.D. Maxwell Localization of cellular transglutaminase on the extracellular matrix after wounding: characteristics of the matrix bound enzyme J Cell Physiol 149 3 1991 375 382 (Pubitemid 21910202)
    • (1991) Journal of Cellular Physiology , vol.149 , Issue.3 , pp. 375-382
    • Upchurch, H.F.1    Conway, E.2    Patterson Jr., M.K.3    Maxwell, M.D.4
  • 252
    • 77956226230 scopus 로고    scopus 로고
    • Gene-environment interactions in Parkinson's disease and other forms of parkinsonism
    • J.M. Vance, S. Ali, W.G. Bradley, C. Singer, and D.A. Di Monte Gene-environment interactions in Parkinson's disease and other forms of parkinsonism Neurotoxicology 31 5 2010 598 602
    • (2010) Neurotoxicology , vol.31 , Issue.5 , pp. 598-602
    • Vance, J.M.1    Ali, S.2    Bradley, W.G.3    Singer, C.4    Di Monte, D.A.5
  • 253
    • 0031869591 scopus 로고    scopus 로고
    • Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: Effects on the processing of fibronectin, cell attachment, and cell death
    • DOI 10.1006/excr.1997.3874
    • E. Verderio, B. Nicholas, S. Gross, and M. Griffin Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: effects on the processing of fibronectin, cell attachment, and cell death Exp Cell Res 239 1 1998 119 138 (Pubitemid 28368484)
    • (1998) Experimental Cell Research , vol.239 , Issue.1 , pp. 119-138
    • Verderio, E.1    Nicholas, B.2    Gross, S.3    Griffin, M.4
  • 254
    • 79955673727 scopus 로고    scopus 로고
    • Blockade of enzyme activity inhibits tissue transglutaminase-mediated transamidation of alpha-synuclein in a cellular model of Parkinson's disease
    • R. Verhaar, C.A. Jongenelen, M. Gerard, V. Baekelandt, A.M. Van Dam, and M.M. Wilhelmus Blockade of enzyme activity inhibits tissue transglutaminase- mediated transamidation of alpha-synuclein in a cellular model of Parkinson's disease Neurochem Int 58 7 2011 785 793
    • (2011) Neurochem Int , vol.58 , Issue.7 , pp. 785-793
    • Verhaar, R.1    Jongenelen, C.A.2    Gerard, M.3    Baekelandt, V.4    Van Dam, A.M.5    Wilhelmus, M.M.6
  • 255
    • 0026499659 scopus 로고
    • Expression of retinoic acid nuclear receptors and tissue transglutaminase is altered in various tissues of rats fed a vitamin A-deficient diet
    • A.K. Verma, A. Shoemaker, R. Simsiman, M. Denning, and R.D. Zachman Expression of retinoic acid nuclear receptors and tissue transglutaminase is altered in various tissues of rats fed a vitamin A-deficient diet J Nutr 122 11 1992 2144 2152
    • (1992) J Nutr , vol.122 , Issue.11 , pp. 2144-2152
    • Verma, A.K.1    Shoemaker, A.2    Simsiman, R.3    Denning, M.4    Zachman, R.D.5
  • 256
    • 7244254372 scopus 로고    scopus 로고
    • Elevated concentration of cerebrospinal fluid tissue transglutaminase in Parkinson's disease indicating apoptosis
    • DOI 10.1002/mds.20197
    • I. Vermes, E.N. Steur, G.F. Jirikowski, and C. Haanen Elevated concentration of cerebrospinal fluid tissue transglutaminase in Parkinson's disease indicating apoptosis Mov Disord 19 10 2004 1252 1254 (Pubitemid 39429976)
    • (2004) Movement Disorders , vol.19 , Issue.10 , pp. 1252-1254
    • Vermes, I.1    Jansen Steur, E.N.H.2    Jirikowski, G.F.3    Haanen, C.4
  • 257
    • 0033617199 scopus 로고    scopus 로고
    • Differential signaling by the thromboxane receptor isoforms via the novel GTP-binding protein, Gh
    • R. Vezza, A. Habib, and G.A. FitzGerald Differential signaling by the thromboxane receptor isoforms via the novel GTP-binding protein, Gh J Biol Chem 274 18 1999 12774 12779
    • (1999) J Biol Chem , vol.274 , Issue.18 , pp. 12774-12779
    • Vezza, R.1    Habib, A.2    Fitzgerald, G.A.3
  • 258
    • 0031052563 scopus 로고    scopus 로고
    • Retinoblastoma protein in growth suppression and death protection
    • DOI 10.1016/S0959-437X(97)80107-4
    • J.Y. Wang Retinoblastoma protein in growth suppression and death protection Curr Opin Genet Dev 7 1 1997 39 45 (Pubitemid 27092762)
    • (1997) Current Opinion in Genetics and Development , vol.7 , Issue.1 , pp. 39-45
    • Wang, J.Y.1
  • 259
    • 15944409947 scopus 로고    scopus 로고
    • Cerebral PET imaging and histological evidence of transglutaminase inhibitor cystamine induced neuroprotection in transgenic R6/2 mouse model of Huntington's disease
    • DOI 10.1016/j.jns.2004.12.011
    • X. Wang, A. Sarkar, F. Cicchetti, M. Yu, A. Zhu, and K. Jokivarsi Cerebral PET imaging and histological evidence of transglutaminase inhibitor cystamine induced neuroprotection in transgenic R6/2 mouse model of Huntington's disease J Neurol Sci 231 1-2 2005 57 66 (Pubitemid 40439235)
    • (2005) Journal of the Neurological Sciences , vol.231 , Issue.1-2 , pp. 57-66
    • Wang, X.1    Sarkar, A.2    Cicchetti, F.3    Yu, M.4    Zhu, A.5    Jokivarsi, K.6    Saint-Pierre, M.7    Brownell, A.-L.8
  • 260
    • 33845501601 scopus 로고    scopus 로고
    • Structure-activity relationship analysis of the selective inhibition of transglutaminase 2 by dihydroisoxazoles
    • DOI 10.1021/jm060839a
    • R.E. Watts, M. Siegel, and C. Khosla Structure-activity relationship analysis of the selective inhibition of transglutaminase 2 by dihydroisoxazoles J Med Chem 49 25 2006 7493 7501 (Pubitemid 44913408)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.25 , pp. 7493-7501
    • Watts, R.E.1    Siegel, M.2    Khosla, C.3
  • 261
    • 43049140462 scopus 로고    scopus 로고
    • Tissue transglutaminase: A novel pharmacological target in preventing toxic protein aggregation in neurodegenerative diseases
    • M.M. Wilhelmus, A.M. van Dam, and B. Drukarch Tissue transglutaminase: a novel pharmacological target in preventing toxic protein aggregation in neurodegenerative diseases Eur J Pharmacol 585 2-3 2008 464 472
    • (2008) Eur J Pharmacol , vol.585 , Issue.23 , pp. 464-472
    • Wilhelmus, M.M.1    Van Dam, A.M.2    Drukarch, B.3
  • 262
    • 79251589371 scopus 로고    scopus 로고
    • Presence of tissue transglutaminase in granular endoplasmic reticulum is characteristic of melanized neurons in Parkinson's disease brain
    • M.M. Wilhelmus, R. Verhaar, G. Andringa, J.G. Bol, P. Cras, and L. Shan Presence of tissue transglutaminase in granular endoplasmic reticulum is characteristic of melanized neurons in Parkinson's disease brain Brain Pathol 21 2 2010 130 139
    • (2010) Brain Pathol , vol.21 , Issue.2 , pp. 130-139
    • Wilhelmus, M.M.1    Verhaar, R.2    Andringa, G.3    Bol, J.G.4    Cras, P.5    Shan, L.6
  • 263
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • C.M. Wischik, M. Novak, H.C. Thogersen, P.C. Edwards, M.J. Runswick, and R. Jakes Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease Proc Natl Acad Sci U S A 85 12 1988 4506 4510
    • (1988) Proc Natl Acad Sci U S A , vol.85 , Issue.12 , pp. 4506-4510
    • Wischik, C.M.1    Novak, M.2    Thogersen, H.C.3    Edwards, P.C.4    Runswick, M.J.5    Jakes, R.6
  • 264
    • 33244472849 scopus 로고    scopus 로고
    • Inhibition of HLA-DQ2-mediated antigen presentation by analogues of a high affinity 33-residue peptide from α2-gliadin
    • DOI 10.1021/ja056423o
    • J. Xia, M. Siegel, E. Bergseng, L.M. Sollid, and C. Khosla Inhibition of HLA-DQ2-mediated antigen presentation by analogues of a high affinity 33-residue peptide from alpha2-gliadin J Am Chem Soc 128 6 2006 1859 1867 (Pubitemid 43277324)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.6 , pp. 1859-1867
    • Xia, J.1    Siegel, M.2    Bergseng, E.3    Sollid, L.M.4    Khosla, C.5
  • 265
    • 30644459554 scopus 로고    scopus 로고
    • Tissue transglutaminase serves as an inhibitor of apoptosis by cross-linking caspase 3 in thapsigargin-treated cells
    • DOI 10.1128/MCB.26.2.569-579.2006
    • H. Yamaguchi, and H.G. Wang Tissue transglutaminase serves as an inhibitor of apoptosis by cross-linking caspase 3 in thapsigargin-treated cells Mol Cell Biol 26 2 2006 569 579 (Pubitemid 43089769)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.2 , pp. 569-579
    • Yamaguchi, H.1    Wang, H.-G.2
  • 267
    • 33644668017 scopus 로고    scopus 로고
    • Tissue transglutaminase 2 inhibition promotes cell death and chemosensitivity in glioblastomas
    • L. Yuan, K. Choi, C. Khosla, X. Zheng, R. Higashikubo, and M.R. Chicoine Tissue transglutaminase 2 inhibition promotes cell death and chemosensitivity in glioblastomas Mol Cancer Ther 4 9 2005 1293 1302
    • (2005) Mol Cancer Ther , vol.4 , Issue.9 , pp. 1293-1302
    • Yuan, L.1    Choi, K.2    Khosla, C.3    Zheng, X.4    Higashikubo, R.5    Chicoine, M.R.6
  • 268
    • 79959837759 scopus 로고    scopus 로고
    • Novel chemo-sensitizing agent, ERW1227B, impairs cellular motility and enhances cell death in glioblastomas
    • L. Yuan, T.C. Holmes, R.E. Watts, C. Khosla, T.J. Broekelmann, and R. Mecham Novel chemo-sensitizing agent, ERW1227B, impairs cellular motility and enhances cell death in glioblastomas J Neurooncol 103 2 2011 207 219
    • (2011) J Neurooncol , vol.103 , Issue.2 , pp. 207-219
    • Yuan, L.1    Holmes, T.C.2    Watts, R.E.3    Khosla, C.4    Broekelmann, T.J.5    Mecham, R.6
  • 269
    • 34247349128 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy
    • DOI 10.1038/sj.onc.1210048, PII 1210048
    • L. Yuan, M. Siegel, K. Choi, C. Khosla, C.R. Miller, and E.N. Jackson Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy Oncogene 26 18 2007 2563 2573 (Pubitemid 46632005)
    • (2007) Oncogene , vol.26 , Issue.18 , pp. 2563-2573
    • Yuan, L.1    Siegel, M.2    Choi, K.3    Khosla, C.4    Miller, C.R.5    Jackson, E.N.6    Piwnica-Worms, D.7    Rich, K.M.8
  • 272
    • 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 11 2000 983 989
    • (2000) J Neuropathol Exp Neurol , vol.59 , Issue.11 , pp. 983-989
    • Zemaitaitis, M.O.1    Lee, J.M.2    Troncoso, J.C.3    Muma, N.A.4
  • 273
    • 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 1 1998 240 247 (Pubitemid 28292555)
    • (1998) Journal of Neurochemistry , vol.71 , Issue.1 , pp. 240-247
    • Zhang, J.1    Guttmann, R.P.2    Johnson, G.V.W.3
  • 274
    • 0031893826 scopus 로고    scopus 로고
    • Modulation of the in situ activity of tissue transglutaminase by calcium and GTP
    • DOI 10.1074/jbc.273.4.2288
    • J. Zhang, M. Lesort, R.P. Guttmann, and G.V. Johnson Modulation of the in situ activity of tissue transglutaminase by calcium and GTP J Biol Chem 273 4 1998 2288 2295 (Pubitemid 28069282)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 2288-2295
    • Zhang, J.1    Lesort, M.2    Guttmann, R.P.3    Johnson, G.V.W.4
  • 275
    • 0028947023 scopus 로고
    • Evidence for the involvement of retinoic acid receptor RAR alpha-dependent signaling pathway in the induction of tissue transglutaminase and apoptosis by retinoids
    • L.X. Zhang, K.J. Mills, M.I. Dawson, S.J. Collins, and A.M. Jetten Evidence for the involvement of retinoic acid receptor RAR alpha-dependent signaling pathway in the induction of tissue transglutaminase and apoptosis by retinoids J Biol Chem 270 11 1995 6022 6029
    • (1995) J Biol Chem , vol.270 , Issue.11 , pp. 6022-6029
    • Zhang, L.X.1    Mills, K.J.2    Dawson, M.I.3    Collins, S.J.4    Jetten, A.M.5
  • 276
    • 0030959139 scopus 로고    scopus 로고
    • Pharmacologic inhibition of transglutaminase-induced cross-linking of Alzheimer's amyloid β-peptide
    • DOI 10.1016/S0024-3205(97)00288-9, PII S0024320597002889
    • W. Zhang, B.R. Johnson, and T.D. Bjornsson Pharmacologic inhibition of transglutaminase-induced cross-linking of Alzheimer's amyloid beta-peptide Life Sci 60 25 1997 2323 2332 (Pubitemid 27237244)
    • (1997) Life Sciences , vol.60 , Issue.25 , pp. 2323-2332
    • Zhang, W.1    Johnson, B.R.2    Bjornsson, T.D.3
  • 277
    • 0031690048 scopus 로고    scopus 로고
    • Immunohistochemical demonstration of tissue transglutaminase in amyloid plaques
    • DOI 10.1007/s004010050910
    • W. Zhang, B.R. Johnson, D.E. Suri, J. Martinez, and T.D. Bjornsson Immunohistochemical demonstration of tissue transglutaminase in amyloid plaques Acta Neuropathol 96 4 1998 395 400 (Pubitemid 28451145)
    • (1998) Acta Neuropathologica , vol.96 , Issue.4 , pp. 395-400
    • Zhang, W.1    Johnson, B.R.2    Suri, D.E.3    Martinez, J.4    Bjornsson, T.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.