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Volumn 278, Issue 24, 2011, Pages 4717-4739

Protein transamidation by transglutaminase 2 in cells: A disputed Ca 2+-dependent action of a multifunctional protein

Author keywords

Ca 2+ binding sites and regulation; intracellular activation; pathologic conditions; physiological processes; protein transamidation; splice variants; substrates; transglutaminase 2

Indexed keywords

6 (GAMMA GLUTAMYL)LYSINE; ALPHA SYNUCLEIN; AMPA RECEPTOR; BETA CRYSTALLIN; CALCIUM CHANNEL L TYPE; CALCIUM ION; CYCLIC GMP; CYTOKERATIN 18; CYTOKERATIN 8; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATE; HUNTINGTIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; POLYAMINE; PROTEIN DISULFIDE ISOMERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN KINASE; REACTIVE OXYGEN METABOLITE; RYANODINE RECEPTOR; VOLTAGE GATED CALCIUM CHANNEL;

EID: 82755161784     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08345.x     Document Type: Review
Times cited : (81)

References (176)
  • 1
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • DOI 10.1038/nrm1014
    • Lorand L, &, Graham RM, (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 4, 140-156. (Pubitemid 36172696)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.2 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 2
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • DOI 10.1016/S0968-0004(02)02182-5, PII S0968000402021825
    • Fesus L, &, Piacentini M, (2002) Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem Sci 27, 534-539. (Pubitemid 35279599)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 3
    • 78650961741 scopus 로고    scopus 로고
    • Factor XIII: Novel structural and functional aspects
    • Komáromi I, Bagoly Z, &, Muszbek L, (2011) Factor XIII: novel structural and functional aspects. J Thromb Haemost 9, 9-20.
    • (2011) J Thromb Haemost , vol.9 , pp. 9-20
    • Komáromi, I.1    Bagoly, Z.2    Muszbek, L.3
  • 4
    • 0032757460 scopus 로고    scopus 로고
    • Initiation of assembly of the cell envelope barrier structure of stratified squamous epithelia
    • Steinert PM, &, Marekov LN, (1999) Initiation of assembly of the cell envelope barrier structure of stratified squamous epithelia. Mol Biol Cell 10, 4247-4261.
    • (1999) Mol Biol Cell , vol.10 , pp. 4247-4261
    • Steinert, P.M.1    Marekov, L.N.2
  • 6
    • 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
    • Mishra S, &, Murphy LJ, (2004) Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. J Biol Chem 279, 23863-23868. (Pubitemid 38725242)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 8
    • 82755187317 scopus 로고    scopus 로고
    • Extracellular TG2: Emerging functions and regulation
    • Belkin AM, (2011) Extracellular TG2: emerging functions and regulation. FEBS J 278, 4704-4716.
    • (2011) FEBS J , vol.278 , pp. 4704-4716
    • Belkin, A.M.1
  • 10
    • 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
    • Peng X, Zhang Y, Zhang H, Graner S, Williams JF, Levitt ML, &, Lokshin A, (1999) Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3. FEBS Lett 446, 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
  • 12
    • 4644335421 scopus 로고    scopus 로고
    • Cell-surface-associated tissue transglutaminase is a target of MMP-2 proteolysis
    • DOI 10.1021/bi049266z
    • Belkin AM, Zemskov EA, Hang J, Akimov SS, Sikora S, &, Strongin AY, (2004) Cell-surface-associated tissue transglutaminase is a target of MMP-2 proteolysis. Biochemistry 43, 11760-11769. (Pubitemid 39277621)
    • (2004) Biochemistry , vol.43 , Issue.37 , pp. 11760-11769
    • Belkin, A.M.1    Zemskov, E.A.2    Hang, J.3    Akimov, S.S.4    Sikora, S.5    Strongin, A.Y.6
  • 13
    • 79955692581 scopus 로고    scopus 로고
    • Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes
    • Zemskov EA, Mikhailenko I, Hsia RC, Zaritskaya L, &, Belkin AM, (2011) Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes. PLoS ONE 6, e19414.
    • (2011) PLoS ONE , vol.6
    • Zemskov, E.A.1    Mikhailenko, I.2    Hsia, R.C.3    Zaritskaya, L.4    Belkin, A.M.5
  • 16
    • 0015777139 scopus 로고
    • Molecular and catalytic properties of transglutaminases
    • Folk JE, &, Chung S, (1973) Molecular and catalytic properties of transglutaminases. Adv Enzymol Relat Areas Mol Biol 38, 109-191.
    • (1973) Adv Enzymol Relat Areas Mol Biol , vol.38 , pp. 109-191
    • Folk, J.E.1    Chung, S.2
  • 18
    • 0023733194 scopus 로고
    • GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase
    • DOI 10.1016/0014-5793(88)80928-1
    • Bergamini CM, (1988) GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase. FEBS Lett 239, 255-258. (Pubitemid 18263458)
    • (1988) FEBS Letters , vol.239 , Issue.2 , pp. 255-258
    • Bergamini, C.M.1
  • 20
    • 0021322350 scopus 로고
    • The inhibition of glucose-stimulated insulin secretion by primary amines. A role for transglutaminase in the secretory mechanism
    • Bungay PJ, Potter JM, &, Griffin M, (1984) The inhibition of glucose-stimulated insulin secretion by primary amines. A role for transglutaminase in the secretory mechanism. Biochem J 219, 819-827. (Pubitemid 14141742)
    • (1984) Biochemical Journal , vol.219 , Issue.3 , pp. 819-827
    • Bungay, P.J.1    Potter, J.M.2    Griffin, M.3
  • 21
    • 0022330157 scopus 로고
    • Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein
    • Hand D, Bungay PJ, Elliott BM, &, Griffin M, (1985) Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein. Biosci Rep 5, 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
  • 29
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas DM, Strop P, Brunger AT, &, Khosla C, (2007) Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol 5, e327.
    • (2007) PLoS Biol , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 30
    • 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
    • Liu S, Cerione RA, &, Clardy J, (2002) Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci USA 99, 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
  • 31
    • 77954143820 scopus 로고    scopus 로고
    • Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate
    • Han BG, Cho JW, Cho YD, Jeong KC, Kim SY, &, Lee BI, (2010) Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate. Int J Biol Macromol 47, 190-195.
    • (2010) Int J Biol Macromol , vol.47 , pp. 190-195
    • Han, B.G.1    Cho, J.W.2    Cho, Y.D.3    Jeong, K.C.4    Kim, S.Y.5    Lee, B.I.6
  • 32
    • 0038606434 scopus 로고    scopus 로고
    • Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme
    • DOI 10.1074/jbc.M301162200
    • Ahvazi B, Boeshans KM, Idler W, Baxa U, &, Steinert PM, (2003) Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme. J Biol Chem 278, 23834-23841. (Pubitemid 36830209)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23834-23841
    • Ahvazi, B.1    Boeshans, K.M.2    Idler, W.3    Baxa, U.4    Steinert, P.M.5
  • 33
    • 2942575057 scopus 로고    scopus 로고
    • The emerging structural understanding of transglutaminase 3
    • DOI 10.1016/j.jsb.2004.03.009, PII S104784770400067X
    • Ahvazi B, Boeshans KM, &, Rastinejad F, (2004) The emerging structural understanding of transglutaminase 3. J Struct Biol 147, 200-207. (Pubitemid 38757515)
    • (2004) Journal of Structural Biology , vol.147 , Issue.2 , pp. 200-207
    • Ahvazi, B.1    Boeshans, K.M.2    Rastinejad, F.3
  • 36
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • DOI 10.1111/j.1742-4658.2005.05031.x
    • Zelensky AN, &, Gready JE, (2005) The C-type lectin-like domain superfamily. FEBS J 272, 6179-6217. (Pubitemid 41815610)
    • (2005) FEBS Journal , vol.272 , Issue.24 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 37
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • DOI 10.1038/nrm2328, PII NRM2328
    • Lemmon MA, (2008) Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9, 99-111. (Pubitemid 351158910)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 99-111
    • Lemmon, M.A.1
  • 38
    • 0012955959 scopus 로고    scopus 로고
    • Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1
    • DOI 10.1074/jbc.M208266200
    • Smallridge RS, Whiteman P, Werner JM, Campbell ID, Handford PA, &, Downing AK, (2003) Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1. J Biol Chem 278, 12199-12206. (Pubitemid 36800200)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12199-12206
    • Smallridge, R.S.1    Whiteman, P.2    Werner, J.M.3    Campbell, I.D.4    Handford, P.A.5    Downing, A.K.6
  • 40
    • 36048940286 scopus 로고    scopus 로고
    • Missense mutations in the TGM2 gene encoding transglutaminase 2 are found in patients with early-onset type 2 diabetes. Mutation in brief no. 982. Online
    • Porzio O, Massa O, Cunsolo V, Colombo C, Malaponti M, Bertuzzi F, Hansen T, Johansen A, Pedersen O, Meschi F, et al. (2007) Missense mutations in the TGM2 gene encoding transglutaminase 2 are found in patients with early-onset type 2 diabetes. Mutation in brief no. 982. Online. Hum Mutat 28, 1150.
    • (2007) Hum Mutat , vol.28 , pp. 1150
    • Porzio, O.1    Massa, O.2    Cunsolo, V.3    Colombo, C.4    Malaponti, M.5    Bertuzzi, F.6    Hansen, T.7    Johansen, A.8    Pedersen, O.9    Meschi, F.10
  • 42
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • Achyuthan KE, &, Greenberg CS, (1987) 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, 1901-1906.
    • (1987) J Biol Chem , vol.262 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 43
    • 0026754093 scopus 로고
    • Putative nucleotide binding sites of guinea pig liver transglutaminase
    • Takeuchi Y, Birckbichler PJ, Patterson MK Jr, &, Lee KN, (1992) Putative nucleotide binding sites of guinea pig liver transglutaminase. FEBS Lett 307, 177-180.
    • (1992) FEBS Lett , vol.307 , pp. 177-180
    • Takeuchi, Y.1    Birckbichler, P.J.2    Patterson, Jr.M.K.3    Lee, K.N.4
  • 44
    • 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
    • Lai TS, Slaughter TF, Peoples KA, Hettasch JM, &, Greenberg CS, (1998) 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, 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
  • 45
    • 0035942305 scopus 로고    scopus 로고
    • Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase
    • DOI 10.1021/bi002321t
    • Lai TS, Hausladen A, Slaughter TF, Eu JP, Stamler JS, &, Greenberg CS, (2001) Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase. Biochemistry 40, 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
  • 46
    • 37149029370 scopus 로고    scopus 로고
    • Calcium Signaling
    • DOI 10.1016/j.cell.2007.11.028, PII S0092867407015310
    • Clapham DE, (2007) Calcium signaling. Cell 131, 1047-1058. (Pubitemid 350258556)
    • (2007) Cell , vol.131 , Issue.6 , pp. 1047-1058
    • Clapham, D.E.1
  • 48
    • 46749147598 scopus 로고    scopus 로고
    • Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury
    • Siegel M, Strnad P, Watts RE, Choi K, Jabri B, Omary MB, &, Khosla C, (2008) Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury. PLoS ONE 3, e1861.
    • (2008) PLoS ONE , vol.3
    • Siegel, M.1    Strnad, P.2    Watts, R.E.3    Choi, K.4    Jabri, B.5    Omary, M.B.6    Khosla, C.7
  • 50
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • De Laurenzi V, &, Melino G, (2001) Gene disruption of tissue transglutaminase. Mol Cell Biol 21, 148-155.
    • (2001) Mol Cell Biol , vol.21 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2
  • 51
    • 0024471699 scopus 로고
    • Formation of N(ε)-(γ-glutamyl)-lysine isodipeptide in Chinese-hamster ovary cells
    • Fesus L, &, Tarcsa E, (1989) Formation of N epsilon-(gamma-glutamyl)- lysine isodipeptide in Chinese-hamster ovary cells. Biochem J 263, 843-848. (Pubitemid 19276464)
    • (1989) Biochemical Journal , vol.263 , Issue.3 , pp. 843-848
    • Fesus, L.1    Tarcsa, E.2
  • 52
    • 0026528787 scopus 로고
    • Presence and possible origin of epsilon(gamma-glutamyl)lysine isodipeptide in human plasma
    • Harsfalvi J, Tarcsa E, Udvardy M, Zajka G, Szarvas T, &, Fesus L, (1992) Presence and possible origin of epsilon(gamma-glutamyl)lysine isodipeptide in human plasma. Thromb Haemost 67, 60-62.
    • (1992) Thromb Haemost , vol.67 , pp. 60-62
    • Harsfalvi, J.1    Tarcsa, E.2    Udvardy, M.3    Zajka, G.4    Szarvas, T.5    Fesus, L.6
  • 53
    • 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
    • Nemes Z, Fésüs L, Egerházi A, Keszthelyi A, &, Degrell IM, (2001) N(epsilon)(gamma-glutamyl)lysine in cerebrospinal fluid marks Alzheimer type and vascular dementia. Neurobiol Aging 22, 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
  • 54
    • 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
    • Zhang J, Lesort M, Guttmann RP, &, Johnson GV, (1998) Modulation of the in situ activity of tissue transglutaminase by calcium and GTP. J Biol Chem 273, 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
  • 55
    • 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
    • Begg GE, Holman SR, Stokes PH, Matthews JM, Graham RM, &, Iismaa SE, (2006) Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity. J Biol Chem 281, 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
  • 56
    • 67651231435 scopus 로고    scopus 로고
    • The differential effects of R580A mutation on transamidation and GTP binding activity of rat and human type 2 transglutaminase
    • Ruan Q, Tucholski J, Gundemir S, &, Johnson Voll GV, (2008) The differential effects of R580A mutation on transamidation and GTP binding activity of rat and human type 2 transglutaminase. Int J Clin Exp Med 1, 248-259.
    • (2008) Int J Clin Exp Med , vol.1 , pp. 248-259
    • Ruan, Q.1    Tucholski, J.2    Gundemir, S.3    Johnson Voll, G.V.4
  • 57
    • 0023838641 scopus 로고
    • Free and protein-conjugated polyamines in mouse epidermal cells. Effect of high calcium and retinoic acid
    • Piacentini M, Martinet N, Beninati S, &, Folk JE, (1988) Free and protein-conjugated polyamines in mouse epidermal cells. Effect of high calcium and retinoic acid. J Biol Chem 263, 3790-3794. (Pubitemid 18078968)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.8 , pp. 3790-3794
    • Piacentini, M.1    Martinet, N.2    Beninati, S.3    Folk, J.E.4
  • 58
    • 82755187312 scopus 로고    scopus 로고
    • Novel roles for biogenic monamines: From monoamines in transglutaminase-mediated post-translational protein modification to monoaminylation deregulation diseases
    • Walther DJ, Stahlberg S, &, Vowinckel J, (2011) Novel roles for biogenic monamines: from monoamines in transglutaminase-mediated post-translational protein modification to monoaminylation deregulation diseases. FEBS J 278, 4740-4755.
    • (2011) FEBS J , vol.278 , pp. 4740-4755
    • Walther, D.J.1    Stahlberg, S.2    Vowinckel, J.3
  • 59
    • 0026585827 scopus 로고
    • The carboxy-terminal lysine of alpha B-crystallin is an amine-donor substrate for tissue transglutaminase
    • Groenen PJ, Bloemendal H, &, de Jong WW, (1992) The carboxy-terminal lysine of alpha B-crystallin is an amine-donor substrate for tissue transglutaminase. Eur J Biochem 205, 671-674.
    • (1992) Eur J Biochem , vol.205 , pp. 671-674
    • Groenen, P.J.1    Bloemendal, H.2    De Jong, W.W.3
  • 60
    • 77955816650 scopus 로고    scopus 로고
    • Identification of a preferred substrate peptide for transglutaminase 3 and detection of in situ activity in skin and hair follicles
    • Yamane A, Fukui M, Sugimura Y, Itoh M, Alea MP, Thomas V, El Alaoui S, Akiyama M, &, Hitomi K, (2010) Identification of a preferred substrate peptide for transglutaminase 3 and detection of in situ activity in skin and hair follicles. FEBS J 277, 3564-3574.
    • (2010) FEBS J , vol.277 , pp. 3564-3574
    • Yamane, A.1    Fukui, M.2    Sugimura, Y.3    Itoh, M.4    Alea, M.P.5    Thomas, V.6    El Alaoui, S.7    Akiyama, M.8    Hitomi, K.9
  • 61
    • 79953780725 scopus 로고    scopus 로고
    • In situ detection of active transglutaminases for keratinocyte-type (TGase 1) and tissue-type (TGase 2) using fluorescence-labeled highly reactive substrate peptides
    • Itoh M, Kawamoto T, Tatsukawa H, Kojima S, Yamanishi K, &, Hitomi K, (2011) In situ detection of active transglutaminases for keratinocyte-type (TGase 1) and tissue-type (TGase 2) using fluorescence-labeled highly reactive substrate peptides. J Histochem Cytochem 59, 180-187.
    • (2011) J Histochem Cytochem , vol.59 , pp. 180-187
    • Itoh, M.1    Kawamoto, T.2    Tatsukawa, H.3    Kojima, S.4    Yamanishi, K.5    Hitomi, K.6
  • 62
    • 79251542680 scopus 로고    scopus 로고
    • Dihydroisoxazole analogs for labeling and visualization of catalytically active transglutaminase 2
    • Dafik L, &, Khosla C, (2011) Dihydroisoxazole analogs for labeling and visualization of catalytically active transglutaminase 2. Chem Biol 18, 58-66.
    • (2011) Chem Biol , vol.18 , pp. 58-66
    • Dafik, L.1    Khosla, C.2
  • 63
    • 0025806439 scopus 로고
    • Transglutaminase activity and N epsilon (gamma glutamyl) lysine isopeptide levels during cell growth: An enzymic and immunological study
    • el Alaoui S, Legastelois S, Roch AM, Chantepie J, &, Quash G, (1991) Transglutaminase activity and N epsilon (gamma glutamyl) lysine isopeptide levels during cell growth: an enzymic and immunological study. Int J Cancer 48, 221-226.
    • (1991) Int J Cancer , vol.48 , pp. 221-226
    • El Alaoui, S.1    Legastelois, S.2    Roch, A.M.3    Chantepie, J.4    Quash, G.5
  • 64
    • 1542375349 scopus 로고    scopus 로고
    • Immunoblot analysis reveals that isopeptide antibodies do not specifically recognize the ε-(γ-glutamyl)lysine bonds formed by transglutaminase activity
    • DOI 10.1016/j.jneumeth.2003.11.006, PII S016502700300390X
    • Johnson GV, &, LeShoure R Jr, (2004) Immunoblot analysis reveals that isopeptide antibodies do not specifically recognize the epsilon-(gamma- glutamyl)lysine bonds formed by transglutaminase activity. J Neurosci Methods 134, 151-158. (Pubitemid 38299241)
    • (2004) Journal of Neuroscience Methods , vol.134 , Issue.2 , pp. 151-158
    • Johnson, G.V.W.1    LeShoure Jr., R.2
  • 66
    • 0033794508 scopus 로고    scopus 로고
    • Impaired mitochondrial function results in increased tissue transglutaminase activity in situ
    • Lesort M, Tucholski J, Zhang J, &, Johnson GV, (2000) Impaired mitochondrial function results in increased tissue transglutaminase activity in situ. J Neurochem 75, 1951-1961.
    • (2000) J Neurochem , vol.75 , pp. 1951-1961
    • Lesort, M.1    Tucholski, J.2    Zhang, J.3    Johnson, G.V.4
  • 67
    • 0026689033 scopus 로고
    • Identification of transglutaminase substrates in HT29 colon cancer cells: Use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe
    • Lee KN, Maxwell MD, Patterson MK Jr, Birckbichler PJ, &, Conway E, (1992) Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe. Biochim Biophys Acta 1136, 12-16.
    • (1992) Biochim Biophys Acta , vol.1136 , pp. 12-16
    • Lee, K.N.1    Maxwell, M.D.2    Patterson, Jr.M.K.3    Birckbichler, P.J.4    Conway, E.5
  • 68
    • 0021711157 scopus 로고
    • Alternative myelomonocytic differentiation of HL-60 reflects dual prospective potency of promyelocytes in human
    • DOI 10.1016/0008-8749(84)90340-X
    • Parwaresch MR, Radzun HJ, Bödewadt S, Frendel A, Sundström C, &, Lennert K, (1984) Alternative myelomonocytic differentiation of HL-60 reflects dual prospective potency of promyelocytes in human. Cell Immunol 89, 385-398. (Pubitemid 15198340)
    • (1984) Cellular Immunology , vol.89 , Issue.2 , pp. 385-398
    • Parwaresch, M.R.1    Radzun, H.J.2    Bodewadt, S.3
  • 69
    • 0022493523 scopus 로고
    • Identification of transglutaminase substrates in inside-out vesicles from human erythrocytes: Immunoblotting with anti-dansyl antibody
    • Lorand L, Murthy SN, Velasco PT, &, Karush F, (1986) Identification of transglutaminase substrates in inside-out vesicles from human erythrocytes: immunoblotting with anti-dansyl antibody. Biochem Biophys Res Commun 134, 685-689. (Pubitemid 16070551)
    • (1986) Biochemical and Biophysical Research Communications , vol.134 , Issue.2 , pp. 685-689
    • Lorand, L.1    Murthy, S.N.P.2    Velasco, P.T.3    Karush, F.4
  • 70
    • 2442607838 scopus 로고    scopus 로고
    • Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: Implications of transglutaminase 2 in age-related cataractogenesis
    • Shin DM, Jeon JH, Kim CW, Cho SY, Kwon JC, Lee HJ, Choi KH, Park SC, &, Kim IG, (2004) Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: implications of transglutaminase 2 in age-related cataractogenesis. J Biol Chem 279, 15032-15039.
    • (2004) J Biol Chem , vol.279 , pp. 15032-15039
    • Shin, D.M.1    Jeon, J.H.2    Kim, C.W.3    Cho, S.Y.4    Kwon, J.C.5    Lee, H.J.6    Choi, K.H.7    Park, S.C.8    Kim, I.G.9
  • 71
    • 1842332757 scopus 로고    scopus 로고
    • Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis
    • DOI 10.1074/jbc.272.33.20577
    • Nemes Z Jr, Adány R, Balázs M, Boross P, &, Fésüs L, (1997) Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis. J Biol Chem 272, 20577-20583. (Pubitemid 27355616)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.33 , pp. 20577-20583
    • Nemes Jr., Z.1    Adany, R.2    Balazs, M.3    Boross, P.4    Fesus, L.5
  • 73
    • 0031764609 scopus 로고    scopus 로고
    • DRPLA aggregation and transglutaminase, revisited
    • Lorand L, (1998) DRPLA aggregation and transglutaminase, revisited. Nat Genet 20, 231.
    • (1998) Nat Genet , vol.20 , pp. 231
    • Lorand, L.1
  • 75
    • 0026514824 scopus 로고
    • Microdomains of high calcium concentration in a presynaptic terminal
    • Llinas R, Sugimori M, &, Silver RB, (1992) Microdomains of high calcium concentration in a presynaptic terminal. Science 256, 677-679.
    • (1992) Science , vol.256 , pp. 677-679
    • Llinas, R.1    Sugimori, M.2    Silver, R.B.3
  • 79
    • 33748677687 scopus 로고    scopus 로고
    • Tissue-transglutaminase contributes to neutrophil granulocyte differentiation and functions
    • DOI 10.1182/blood-2004-02-007948
    • Balajthy Z, Csomós K, Vámosi G, Szántó A, Lanotte M, &, Fésüs L, (2006) Tissue-transglutaminase contributes to neutrophil granulocyte differentiation and functions. Blood 108, 2045-2054. (Pubitemid 44395020)
    • (2006) Blood , vol.108 , Issue.6 , pp. 2045-2054
    • Balajthy, Z.1    Csomos, K.2    Vamosi, G.3    Szanto, A.4    Lanotte, M.5    Fesus, L.6
  • 80
    • 78149461657 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to the all-trans retinoic acid induced differentiation syndrome phenotype in the NB4 model of acute promyelocytic leukemia
    • Csomós K, Német I, Fésüs L, &, Balajthy Z, (2010) Tissue transglutaminase contributes to the all-trans retinoic acid induced differentiation syndrome phenotype in the NB4 model of acute promyelocytic leukemia. Blood 116, 3933-3943.
    • (2010) Blood , vol.116 , pp. 3933-3943
    • Csomós, K.1    Német, I.2    Fésüs, L.3    Balajthy, Z.4
  • 82
    • 0027458695 scopus 로고
    • Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death)
    • Peitsch MC, Polzar B, Stephan H, Crompton T, MacDonald HR, Mannherz HG, &, Tschopp J, (1993) Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death). EMBO J 12, 371-377. (Pubitemid 23042417)
    • (1993) EMBO Journal , vol.12 , Issue.1 , pp. 371-377
    • Peitsch, M.C.1    Polzar, B.2    Stephan, H.3    Crompton, T.4    MacDonald, H.R.5    Mannherz, H.G.6    Tschopp, J.7
  • 83
    • 0028820202 scopus 로고
    • Mechanisms of phosphatidylserine exposure, a phagocyte recognition signal, on apoptotic T lymphocytes
    • Verhoven B, Schlegel RA, &, Williamson P, (1995) Mechanisms of phosphatidylserine exposure, a phagocyte recognition signal, on apoptotic T lymphocytes. J Exp Med 182, 1597-1601.
    • (1995) J Exp Med , vol.182 , pp. 1597-1601
    • Verhoven, B.1    Schlegel, R.A.2    Williamson, P.3
  • 84
    • 0023159034 scopus 로고
    • Induction and activation of tiussue transglutaminase during programmed cell death
    • DOI 10.1016/0014-5793(87)80430-1
    • Fesus L, Thomazy V, &, Falus A, (1987) Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett 224, 104-108. (Pubitemid 17159992)
    • (1987) FEBS Letters , vol.224 , Issue.1 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 85
    • 0024520475 scopus 로고
    • Apoptotic hepatocytes become insoluble in detergents and chaotropic agents as a result of transglutaminase action
    • DOI 10.1016/0014-5793(89)80210-8
    • Fesus L, Thomazy V, Autuori F, Ceru MP, Tarcsa E, &, Piacentini M, (1989) Apoptotic hepatocytes become insoluble in detergents and chaotropic agents as a result of transglutaminase action. FEBS Lett 245, 150-154. (Pubitemid 19076220)
    • (1989) FEBS Letters , vol.245 , Issue.1-2 , pp. 150-154
    • Fesus, L.1    Thomazy, V.2    Autuori, F.3    Ceru, M.P.4    Tarcsa, E.5    Piacentini, M.6
  • 87
    • 0038641718 scopus 로고    scopus 로고
    • Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: A mechanism for maintaining tissue integrity
    • DOI 10.1042/BJ20021949
    • Nicholas B, Smethurst P, Verderio E, Jones R, &, Griffin M, (2003) Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity. Biochem J 371, 413-422. (Pubitemid 36547624)
    • (2003) Biochemical Journal , vol.371 , Issue.2 , pp. 413-422
    • Nicholas, B.1    Smethurst, P.2    Verderio, E.3    Jones, R.4    Griffin, M.5
  • 88
    • 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
    • Fesus L, &, Szondy Z, (2005) Transglutaminase 2 in the balance of cell death and survival. FEBS Lett 579, 3297-3302. (Pubitemid 40804677)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3297-3302
    • Fesus, L.1    Szondy, Z.2
  • 89
    • 67651246845 scopus 로고    scopus 로고
    • Intracellular localization and conformational state of transglutaminase 2: Implications for cell death
    • Gundemir S, &, Johnson GV, (2009) Intracellular localization and conformational state of transglutaminase 2: implications for cell death. PLoS ONE 4, e6123.
    • (2009) PLoS ONE , vol.4
    • Gundemir, S.1    Johnson, G.V.2
  • 90
    • 82755187316 scopus 로고    scopus 로고
    • New insights into functions and localization of nuclear transglutaminase 2
    • Kuo TF, Tatsukawa H, &, Kojima S, (2011) New insights into functions and localization of nuclear transglutaminase 2. FEBS J 278, 4756-4767.
    • (2011) FEBS J , vol.278 , pp. 4756-4767
    • Kuo, T.F.1    Tatsukawa, H.2    Kojima, S.3
  • 91
    • 67650538098 scopus 로고    scopus 로고
    • Tissue transglutaminase is an essential participant in the epidermal growth factor-stimulated signaling pathway leading to cancer cell migration and invasion
    • Antonyak MA, Li B, Regan AD, Feng Q, Dusaban SS, &, Cerione RA, (2009) Tissue transglutaminase is an essential participant in the epidermal growth factor-stimulated signaling pathway leading to cancer cell migration and invasion. J Biol Chem 284, 17914-17925.
    • (2009) J Biol Chem , vol.284 , pp. 17914-17925
    • Antonyak, M.A.1    Li, B.2    Regan, A.D.3    Feng, Q.4    Dusaban, S.S.5    Cerione, R.A.6
  • 92
    • 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
    • Singh US, &, Cerione RA, (1996) 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, 27292-27298. (Pubitemid 26367282)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27292-27298
    • Singh, U.S.1    Cerione, R.A.2
  • 93
    • 0030997651 scopus 로고    scopus 로고
    • Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase
    • DOI 10.1074/jbc.272.26.16295
    • Lai TS, Bielawska A, Peoples KA, Hannun YA, &, Greenberg CS, (1997) Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase. J Biol Chem 272, 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
  • 94
    • 18344377027 scopus 로고    scopus 로고
    • A novel transglutaminase activator forms a complex with type 1 transglutaminase
    • DOI 10.1038/sj.onc.1208392
    • Sturniolo MT, Chandraratna RA, &, Eckert RL, (2005) A novel transglutaminase activator forms a complex with type 1 transglutaminase. Oncogene 24, 2963-2972. (Pubitemid 40675527)
    • (2005) Oncogene , vol.24 , Issue.18 , pp. 2963-2972
    • Sturniolo, M.T.1    Chandraratna, R.A.S.2    Eckert, R.L.3
  • 95
    • 0026655015 scopus 로고
    • Tetanus toxin potently stimulates tissue transglutaminase. A possible mechanism of neurotoxicity
    • Facchiano F, &, Luini A, (1992) Tetanus toxin potently stimulates tissue transglutaminase. A possible mechanism of neurotoxicity. J Biol Chem 267, 13267-13271.
    • (1992) J Biol Chem , vol.267 , pp. 13267-13271
    • Facchiano, F.1    Luini, A.2
  • 96
    • 0033578417 scopus 로고    scopus 로고
    • Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II
    • Feng JF, Readon M, Yadav SP, &, Im MJ, (1999) Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II. Biochemistry 38, 10743-10749.
    • (1999) Biochemistry , vol.38 , pp. 10743-10749
    • Feng, J.F.1    Readon, M.2    Yadav, S.P.3    Im, M.J.4
  • 97
    • 72149116712 scopus 로고    scopus 로고
    • Transglutaminase 2 regulates the GTPase-activating activity of Bcr
    • Yi SJ, Groffen J, &, Heisterkamp N, (2009) Transglutaminase 2 regulates the GTPase-activating activity of Bcr. J Biol Chem 284, 35645-35651.
    • (2009) J Biol Chem , vol.284 , pp. 35645-35651
    • Yi, S.J.1    Groffen, J.2    Heisterkamp, N.3
  • 99
    • 0021093255 scopus 로고
    • Interaction between tissue transglutaminase and phospholipid vesicles
    • Fésüs L, Horváth A, &, Hársfalvi J, (1983) Interaction between tissue transglutaminase and phospholipid vesicles. FEBS Lett 155, 1-5.
    • (1983) FEBS Lett , vol.155 , pp. 1-5
    • Fésüs, L.1    Horváth, A.2    Hársfalvi, J.3
  • 102
    • 77956916373 scopus 로고    scopus 로고
    • Transglutaminase 2: A multi-functional protein in multiple subcellular compartments
    • Park D, Choi SS, &, Ha KS, (2010) Transglutaminase 2: a multi-functional protein in multiple subcellular compartments. Amino Acids 39, 619-631.
    • (2010) Amino Acids , vol.39 , pp. 619-631
    • Park, D.1    Choi, S.S.2    Ha, K.S.3
  • 105
    • 70350437632 scopus 로고    scopus 로고
    • Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies
    • Nemes Z, Petrovski G, Aerts M, Sergeant K, Devreese B, &, Fésüs L, (2009) Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies. J Biol Chem 284, 27252-27264.
    • (2009) J Biol Chem , vol.284 , pp. 27252-27264
    • Nemes, Z.1    Petrovski, G.2    Aerts, M.3    Sergeant, K.4    Devreese, B.5    Fésüs, L.6
  • 106
    • 46149096244 scopus 로고    scopus 로고
    • Signaling mechanisms linking neuronal activity to gene expression and plasticity of the nervous system
    • Flavell SW, &, Greenberg ME, (2008) Signaling mechanisms linking neuronal activity to gene expression and plasticity of the nervous system. Annu Rev Neurosci 31, 563-590.
    • (2008) Annu Rev Neurosci , vol.31 , pp. 563-590
    • Flavell, S.W.1    Greenberg, M.E.2
  • 107
    • 52049106127 scopus 로고    scopus 로고
    • Multiple roles of calcium ions in the regulation of neurotransmitter release
    • Neher E, &, Sakaba T, (2008) Multiple roles of calcium ions in the regulation of neurotransmitter release. Neuron 59, 861-872.
    • (2008) Neuron , vol.59 , pp. 861-872
    • Neher, E.1    Sakaba, T.2
  • 109
    • 0026499522 scopus 로고
    • A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue
    • Fraij BM, Birckbichler PJ, Patterson MK Jr, Lee KN, &, Gonzales RA, (1992) A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue. J Biol Chem 267, 22616-22623.
    • (1992) J Biol Chem , vol.267 , pp. 22616-22623
    • Fraij, B.M.1    Birckbichler, P.J.2    Patterson, Jr.M.K.3    Lee, K.N.4    Gonzales, R.A.5
  • 110
    • 0030066233 scopus 로고    scopus 로고
    • GTP hydrolysis by human tissue transglutaminase homologue
    • DOI 10.1006/bbrc.1996.0009
    • Fraij BM, (1996) GTP hydrolysis by human tissue transglutaminase homologue. Biochem Biophys Res Commun 218, 45-49. (Pubitemid 26034486)
    • (1996) Biochemical and Biophysical Research Communications , vol.218 , Issue.1 , pp. 45-49
    • Fraij, B.M.1
  • 111
    • 0031013601 scopus 로고    scopus 로고
    • Expression of GTP-dependent and GTP-independent tissue-type transglutaminase in cytokine-treated rat brain astrocytes
    • Monsonego A, Shani Y, Friedmann I, Paas Y, Eizenberg O, &, Schwartz M, (1997) Expression of GTP-dependent and GTP-independent tissue-type transglutaminase in cytokine-treated rat brain astrocytes. J Biol Chem 272, 3724-3732.
    • (1997) J Biol Chem , vol.272 , pp. 3724-3732
    • Monsonego, A.1    Shani, Y.2    Friedmann, I.3    Paas, Y.4    Eizenberg, O.5    Schwartz, M.6
  • 112
    • 0029937589 scopus 로고    scopus 로고
    • A third human tissue transglutaminase homologue as a result of alternative gene transcripts
    • DOI 10.1016/0167-4781(95)00219-7
    • Fraij BM, &, Gonzales RA, (1996) A third human tissue transglutaminase homologue as a result of alternative gene transcripts. Biochim Biophys Acta 1306, 63-74. (Pubitemid 26120715)
    • (1996) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1306 , Issue.1 , pp. 63-74
    • Fraij, B.M.1    Gonzales, R.A.2
  • 113
    • 0035793583 scopus 로고    scopus 로고
    • Intron-exon swapping of transglutaminase mRNA and neuronal Tau aggregation in Alzheimer's disease
    • Citron BA, SantaCruz KS, Davies PJ, &, Festoff BW, (2001) Intron-exon swapping of transglutaminase mRNA and neuronal Tau aggregation in Alzheimer's disease. J Biol Chem 276, 3295-3301.
    • (2001) J Biol Chem , vol.276 , pp. 3295-3301
    • Citron, B.A.1    Santacruz, K.S.2    Davies, P.J.3    Festoff, B.W.4
  • 114
    • 0036312393 scopus 로고    scopus 로고
    • Injury-induced 'switch' from GTP-regulated to novel GTP-independent isoform of tissue transglutaminase in the rat spinal cord
    • DOI 10.1046/j.1471-4159.2002.00850.x
    • Festoff BW, SantaCruz K, Arnold PM, Sebastian CT, Davies PJ, &, Citron BA, (2002) Injury-induced 'switch' from GTP-regulated to novel GTP-independent isoform of tissue transglutaminase in the rat spinal cord. J Neurochem 81, 708-718. (Pubitemid 34809300)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.4 , pp. 708-718
    • Festoff, B.W.1    Santa Cruz, K.2    Arnold, P.M.3    Sebastian, C.T.4    Davies, P.J.A.5    Citron, B.A.6
  • 115
    • 36849075155 scopus 로고    scopus 로고
    • Identification of two GTP-independent alternatively spliced forms of tissue transglutaminase in human leukocytes, vascular smooth muscle, and endothelial cells
    • DOI 10.1096/fj.06-7598com
    • Lai TS, Liu Y, Li W, &, Greenberg CS, (2007) Identification of two GTP-independent alternatively spliced forms of tissue transglutaminase in human leukocytes, vascular smooth muscle, and endothelial cells. FASEB J 21, 4131-4143. (Pubitemid 350232370)
    • (2007) FASEB Journal , vol.21 , Issue.14 , pp. 4131-4143
    • Lai, T.-S.1    Liu, Y.2    Li, W.3    Greenberg, C.S.4
  • 117
    • 17744412228 scopus 로고    scopus 로고
    • Two distinct classes of rat intestinal mucosal enzymes incorporating putrescine into protein
    • DOI 10.1016/S0014-5793(98)01062-X, PII S001457939801062X
    • Tsai YH, Lai WF, Wu YW, &, Johnson LR, (1998) Two distinct classes of rat intestinal mucosal enzymes incorporating putrescine into protein. FEBS Lett 435, 251-256. (Pubitemid 28435011)
    • (1998) FEBS Letters , vol.435 , Issue.2-3 , pp. 251-256
    • Tsai, Y.-H.1    Lai, W.-F.T.2    Wu, Y.-W.3    Johnson, L.R.4
  • 119
    • 77955271862 scopus 로고    scopus 로고
    • Coeliac disease autoantibodies mediate significant inhibition of tissue transglutaminase
    • Byrne G, Feighery C, Jackson J, &, Kelly J, (2010) Coeliac disease autoantibodies mediate significant inhibition of tissue transglutaminase. Clin Immunol 136, 426-431.
    • (2010) Clin Immunol , vol.136 , pp. 426-431
    • Byrne, G.1    Feighery, C.2    Jackson, J.3    Kelly, J.4
  • 120
    • 4944267025 scopus 로고    scopus 로고
    • Cross-linking of ubiquitin, HSP27, parkin, and α-synuclein by γ-glutamyl-ε-lysine bonds in Alzheimer's neurofibrillary tangles
    • DOI 10.1096/fj.04-1493fje
    • Nemes Z, Devreese B, Steinert PM, Van Beeumen J, &, Fésüs L, (2004) Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer's neurofibrillary tangles. FASEB J 18, 1135-1137. (Pubitemid 39561548)
    • (2004) FASEB Journal , vol.18 , Issue.10 , pp. 1135-1137
    • Nemes, Z.1    Devreese, B.2    Steinert, P.M.3    Van Beeumen, J.4    Fesus, L.5
  • 123
    • 47749113650 scopus 로고    scopus 로고
    • Aβ Plaques Lead to Aberrant Regulation of Calcium Homeostasis In Vivo Resulting in Structural and Functional Disruption of Neuronal Networks
    • DOI 10.1016/j.neuron.2008.06.008, PII S0896627308005011
    • Kuchibhotla KV, Goldman ST, Lattarulo CR, Wu HY, Hyman BT, &, Bacskai BJ, (2008) Abeta plaques lead to aberrant regulation of calcium homeostasis in vivo resulting in structural and functional disruption of neuronal networks. Neuron 59, 214-225. (Pubitemid 352033686)
    • (2008) Neuron , vol.59 , Issue.2 , pp. 214-225
    • Kuchibhotla, K.V.1    Goldman, S.T.2    Lattarulo, C.R.3    Wu, H.-Y.4    Hyman, B.T.5    Bacskai, B.J.6
  • 124
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny I, &, Mattson MP, (2008) Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci 31, 454-463.
    • (2008) Trends Neurosci , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 127
    • 79955665348 scopus 로고    scopus 로고
    • Aberrant subcellular neuronal calcium regulation in aging and Alzheimer's disease
    • Camandola S, &, Mattson MP, (2010) Aberrant subcellular neuronal calcium regulation in aging and Alzheimer's disease. Biochim Biophys Acta, 1813, 965-973.
    • (2010) Biochim Biophys Acta , vol.1813 , pp. 965-973
    • Camandola, S.1    Mattson, M.P.2
  • 128
    • 33947493213 scopus 로고    scopus 로고
    • Expansion of the calcium hypothesis of brain aging and Alzheimer's disease: Minding the store
    • DOI 10.1111/j.1474-9726.2007.00295.x
    • Thibault O, Gant JC, &, Landfield PW, (2007) Expansion of the calcium hypothesis of brain aging and Alzheimer's disease: minding the store. Aging Cell 6, 307-317. (Pubitemid 46785136)
    • (2007) Aging Cell , vol.6 , Issue.3 , pp. 307-317
    • Thibault, O.1    Gant, J.C.2    Landfield, P.W.3
  • 130
    • 43549111889 scopus 로고    scopus 로고
    • Elucidating a normal function of huntingtin by functional and microarray analysis of huntingtin-null mouse embryonic fibroblasts
    • Zhang H, Das S, Li QZ, Dragatsis I, Repa J, Zeitlin S, Hajnóczky G, &, Bezprozvanny I, (2008) Elucidating a normal function of huntingtin by functional and microarray analysis of huntingtin-null mouse embryonic fibroblasts. BMC Neurosci 9, 38.
    • (2008) BMC Neurosci , vol.9 , pp. 38
    • Zhang, H.1    Das, S.2    Li, Q.Z.3    Dragatsis, I.4    Repa, J.5    Zeitlin, S.6    Hajnóczky, G.7    Bezprozvanny, I.8
  • 131
    • 0041963057 scopus 로고    scopus 로고
    • Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1
    • DOI 10.1016/S0896-6273(03)00366-0
    • Tang TS, Tu H, Chan EY, Maximov A, Wang Z, Wellington CL, Hayden MR, &, Bezprozvanny I, (2003) Huntingtin and huntingtin-associated protein 1 influence neuronal calcium signaling mediated by inositol-(1,4,5) triphosphate receptor type 1. Neuron 39, 227-239. (Pubitemid 36897546)
    • (2003) Neuron , vol.39 , Issue.2 , pp. 227-239
    • Tang, T.-S.1    Tu, H.2    Chan, E.Y.W.3    Maximov, A.4    Wang, Z.5    Wellington, C.L.6    Hayden, M.R.7    Bezprozvanny, I.8
  • 132
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • DOI 10.1016/S0896-6273(02)00615-3
    • Zeron MM, Hansson O, Chen N, Wellington CL, Leavitt BR, Brundin P, Hayden MR, &, Raymond LA, (2002) Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron 33, 849-860. (Pubitemid 34246352)
    • (2002) Neuron , vol.33 , Issue.6 , pp. 849-860
    • Zeron, M.M.1    Hansson, O.2    Chen, N.3    Wellington, C.L.4    Leavitt, B.R.5    Brundin, P.6    Hayden, M.R.7    Raymond, L.A.8
  • 133
    • 59649118434 scopus 로고    scopus 로고
    • Neuroprotective effects of inositol 1,4,5-trisphosphate receptor C-terminal fragment in a Huntington's disease mouse model
    • Tang TS, Guo C, Wang H, Chen X, &, Bezprozvanny I, (2009) Neuroprotective effects of inositol 1,4,5-trisphosphate receptor C-terminal fragment in a Huntington's disease mouse model. J Neurosci 29, 1257-1266.
    • (2009) J Neurosci , vol.29 , pp. 1257-1266
    • Tang, T.S.1    Guo, C.2    Wang, H.3    Chen, X.4    Bezprozvanny, I.5
  • 135
    • 33845933438 scopus 로고    scopus 로고
    • Mutant Huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: Functional consequences
    • DOI 10.1074/jbc.M603845200
    • Milakovic T, Quintanilla RA, &, Johnson GV, (2006) Mutant huntingtin expression induces mitochondrial calcium handling defects in clonal striatal cells: functional consequences. J Biol Chem 281, 34785-34795. (Pubitemid 46036517)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 34785-34795
    • Milakovic, T.1    Quintanilla, R.A.2    Johnson, G.V.W.3
  • 136
    • 0037768767 scopus 로고    scopus 로고
    • c dynamics in spontaneously firing dopamine neurons of the rat substantia nigra pars compacta
    • DOI 10.1242/jcs.00481
    • Choi YM, Kim SH, Uhm DY, &, Park MK, (2003) Glutamate-mediated [Ca2+]c dynamics in spontaneously firing dopamine neurons of the rat substantia nigra pars compacta. J Cell Sci 116 (Pt 13), 2665-2675. (Pubitemid 36857220)
    • (2003) Journal of Cell Science , vol.116 , Issue.13 , pp. 2665-2675
    • Choi, Y.M.1    Kim, S.H.2    Uhm, D.Y.3    Park, M.K.4
  • 137
    • 34548657565 scopus 로고    scopus 로고
    • Calcium, ageing, and neuronal vulnerability in Parkinson's disease
    • DOI 10.1016/S1474-4422(07)70246-6, PII S1474442207702466
    • Surmeier DJ, (2007) Calcium, ageing, and neuronal vulnerability in Parkinson's disease. Lancet Neurol 6, 933-938. (Pubitemid 47405004)
    • (2007) Lancet Neurology , vol.6 , Issue.10 , pp. 933-938
    • Surmeier, D.J.1
  • 138
    • 34247210109 scopus 로고    scopus 로고
    • Transglutaminase 2 Regulates Mallory Body Inclusion Formation and Injury-Associated Liver Enlargement
    • DOI 10.1053/j.gastro.2007.02.020, PII S0016508507003678
    • Strnad P, Harada M, Siegel M, Terkeltaub RA, Graham RM, Khosla C, &, Omary MB, (2007) Transglutaminase 2 regulates mallory body inclusion formation and injury-associated liver enlargement. Gastroenterology 132, 1515-1526. (Pubitemid 46627586)
    • (2007) Gastroenterology , vol.132 , Issue.4 , pp. 1515-1526
    • Strnad, P.1    Harada, M.2    Siegel, M.3    Terkeltaub, R.A.4    Graham, R.M.5    Khosla, C.6    Omary, M.B.7
  • 139
    • 34249859423 scopus 로고    scopus 로고
    • Ethanol induced mitochondria injury and permeability transition pore opening: Role of mitochondria in alcoholic liver disease
    • Yan M, Zhu P, Liu HM, Zhang HT, &, Liu L, (2007) Ethanol induced mitochondria injury and permeability transition pore opening: role of mitochondria in alcoholic liver disease. World J Gastroenterol 13, 2352-2356. (Pubitemid 46860738)
    • (2007) World Journal of Gastroenterology , vol.13 , Issue.16 , pp. 2352-2356
    • Yan, M.1    Zhu, P.2    Liu, H.-M.3    Zhang, H.-T.4    Liu, L.5
  • 141
    • 0021022139 scopus 로고
    • β-Crystallin: Endogenous substrate of lens transglutaminase. Characterization of the acyl-donor site in the βB(p) chain
    • Berbers GA, Bentlage HC, Brans AM, Bloemendal H, &, de Jong WW, (1983) beta-Crystallin: endogenous substrate of lens transglutaminase. Characterization of the acyl-donor site in the beta Bp chain. Eur J Biochem 135, 315-320. (Pubitemid 14237953)
    • (1983) European Journal of Biochemistry , vol.135 , Issue.2 , pp. 315-320
    • Berbers, G.A.M.1    Bentlage, H.C.M.2    Brans, A.M.M.3
  • 147
    • 0014011698 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: Identification of a functional cysteine essential for activity
    • Folk JE, &, Cole PW, (1966) Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity. J Biol Chem 241, 5518-5525.
    • (1966) J Biol Chem , vol.241 , pp. 5518-5525
    • Folk, J.E.1    Cole, P.W.2
  • 149
    • 0037036409 scopus 로고    scopus 로고
    • Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb
    • DOI 10.1074/jbc.C200147200
    • Boehm JE, Singh U, Combs C, Antonyak MA, &, Cerione RA, (2002) Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb. J Biol Chem 277, 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
  • 150
    • 0035863525 scopus 로고    scopus 로고
    • Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells
    • DOI 10.1016/S0306-4522(00)00482-6, PII S0306452200004826
    • Tucholski J, Lesort M, &, Johnson GV, (2001) Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells. Neuroscience 102, 481-491. (Pubitemid 32126502)
    • (2001) Neuroscience , vol.102 , Issue.2 , pp. 481-491
    • Tucholski, J.1    Lesort, M.2    Johnson, G.V.W.3
  • 151
    • 0037414822 scopus 로고    scopus 로고
    • Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells
    • DOI 10.1074/jbc.M206361200
    • Singh US, Pan J, Kao YL, Joshi S, Young KL, &, Baker KM, (2003) Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells. J Biol Chem 278, 391-399. (Pubitemid 36043588)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 391-399
    • Singh, U.S.1    Pan, J.2    Kao, Y.-L.3    Joshi, S.4    Young, K.L.5    Baker, K.M.6
  • 152
    • 77950468903 scopus 로고    scopus 로고
    • Opposing effects of two tissue transglutaminase protein isoforms in neuroblastoma cell differentiation
    • Tee AE, Marshall GM, Liu PY, Xu N, Haber M, Norris MD, Iismaa SE, &, Liu T, (2010) Opposing effects of two tissue transglutaminase protein isoforms in neuroblastoma cell differentiation. J Biol Chem 285, 3561-3567.
    • (2010) J Biol Chem , vol.285 , pp. 3561-3567
    • Tee, A.E.1    Marshall, G.M.2    Liu, P.Y.3    Xu, N.4    Haber, M.5    Norris, M.D.6    Iismaa, S.E.7    Liu, T.8
  • 153
    • 67650179228 scopus 로고    scopus 로고
    • Tissue transglutaminase regulates matrix metalloproteinase-2 in ovarian cancer by modulating cAMP-response element-binding protein activity
    • Satpathy M, Shao M, Emerson R, Donner DB, &, Matei D, (2009) Tissue transglutaminase regulates matrix metalloproteinase-2 in ovarian cancer by modulating cAMP-response element-binding protein activity. J Biol Chem 284, 15390-15399.
    • (2009) J Biol Chem , vol.284 , pp. 15390-15399
    • Satpathy, M.1    Shao, M.2    Emerson, R.3    Donner, D.B.4    Matei, D.5
  • 154
    • 0038035231 scopus 로고    scopus 로고
    • Tissue transglutaminase directly regulates adenylyl cyclase resulting in enhanced cAMP-response element-binding protein (CREB) activation
    • DOI 10.1074/jbc.M303683200
    • Tucholski J, &, Johnson GV, (2003) Tissue transglutaminase directly regulates adenylyl cyclase resulting in enhanced cAMP-response element-binding protein (CREB) activation. J Biol Chem 278, 26838-26843. (Pubitemid 36876834)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26838-26843
    • Tucholski, J.1    Johnson, G.V.W.2
  • 155
    • 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
    • Singh US, Kunar MT, Kao YL, &, Baker KM, (2001) Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2. EMBO J 20, 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
  • 156
    • 0023830062 scopus 로고
    • Transglutaminase-catalysed cross-linking of proteins phosphorylated in the intact glucose-stimulated pancreatic β-cell
    • DOI 10.1016/0167-4889(88)90011-0
    • Owen RA, Bungay PJ, Hussain M, &, Griffin M, (1988) Transglutaminase-catalysed cross-linking of proteins phosphorylated in the intact glucose-stimulated pancreatic beta-cell. Biochim Biophys Acta 968, 220-230. (Pubitemid 18078339)
    • (1988) Biochimica et Biophysica Acta - Molecular Cell Research , vol.968 , Issue.2 , pp. 220-230
    • Owen, R.A.1    Bungay, P.J.2    Hussain, M.3    Griffin, M.4
  • 157
    • 79952486896 scopus 로고    scopus 로고
    • Phospholipase C, Ca(2+), and calmodulin signaling are required for 5-HT(2A) receptor-mediated transamidation of Rac1 by transglutaminase
    • Dai Y, Dudek NL, Li Q, &, Muma NA, (2010) Phospholipase C, Ca(2+), and calmodulin signaling are required for 5-HT(2A) receptor-mediated transamidation of Rac1 by transglutaminase. Psychopharmacology (Berl), 213, 403-412.
    • (2010) Psychopharmacology (Berl) , vol.213 , pp. 403-412
    • Dai, Y.1    Dudek, N.L.2    Li, Q.3    Muma, N.A.4
  • 159
    • 79751530304 scopus 로고    scopus 로고
    • Bcr is a substrate for transglutaminase 2 cross-linking activity
    • Yi SJ, Groffen J, &, Heisterkamp N, (2011) Bcr is a substrate for transglutaminase 2 cross-linking activity. BMC Biochem 12, 8.
    • (2011) BMC Biochem , vol.12 , pp. 8
    • Yi, S.J.1    Groffen, J.2    Heisterkamp, N.3
  • 160
    • 79953270842 scopus 로고    scopus 로고
    • Inhibition of transglutaminase 2 attenuates contractility of pregnant human myometrium
    • Alcock J, Warren AY, Goodson YJ, Hill SJ, Khan RN, &, Lymn JS, (2011) Inhibition of transglutaminase 2 attenuates contractility of pregnant human myometrium. Biol Reprod 84, 646-653.
    • (2011) Biol Reprod , vol.84 , pp. 646-653
    • Alcock, J.1    Warren, A.Y.2    Goodson, Y.J.3    Hill, S.J.4    Khan, R.N.5    Lymn, J.S.6
  • 161
    • 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
    • Lee J, Kim YS, Choi DH, Bang MS, Han TR, Joh TH, &, Kim SY, (2004) Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia. J Biol Chem 279, 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
  • 162
    • 33845951183 scopus 로고    scopus 로고
    • Transglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster
    • Park SS, Kim JM, Kim DS, Kim IH, &, Kim SY, (2006) Transglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster. J Biol Chem 281, 34965-34972.
    • (2006) J Biol Chem , vol.281 , pp. 34965-34972
    • Park, S.S.1    Kim, J.M.2    Kim, D.S.3    Kim, I.H.4    Kim, S.Y.5
  • 163
    • 77955841190 scopus 로고    scopus 로고
    • I-kappaBalpha depletion by transglutaminase 2 and mu-calpain occurs in parallel with the ubiquitin-proteasome pathway
    • Kim DS, Han BG, Park KS, Lee BI, Kim SY, &, Bae CD, (2010) I-kappaBalpha depletion by transglutaminase 2 and mu-calpain occurs in parallel with the ubiquitin-proteasome pathway. Biochem Biophys Res Commun 399, 300-306.
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 300-306
    • Kim, D.S.1    Han, B.G.2    Park, K.S.3    Lee, B.I.4    Kim, S.Y.5    Bae, C.D.6
  • 166
    • 79957822028 scopus 로고    scopus 로고
    • TNF-alpha mediated NF-kappaB activation is constantly extended by transglutaminase 2
    • Park KS, Kim DS, Ko C, Lee SJ, Oh SH, &, Kim SY, (2011) TNF-alpha mediated NF-kappaB activation is constantly extended by transglutaminase 2. Front Biosci 3, 341-354.
    • (2011) Front Biosci , 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
  • 168
    • 33750735045 scopus 로고    scopus 로고
    • 2+-dependent transamidation activity in the protection afforded by tissue transglutaminase against doxorubicin-induced apoptosis
    • DOI 10.1021/bi0606795
    • Datta S, Antonyak MA, &, Cerione RA, (2006) Importance of Ca(2+)-dependent transamidation activity in the protection afforded by tissue transglutaminase against doxorubicin-induced apoptosis. Biochemistry 45, 13163-13174. (Pubitemid 44707677)
    • (2006) Biochemistry , vol.45 , Issue.44 , pp. 13163-13174
    • Datta, S.1    Antonyak, M.A.2    Cerione, R.A.3
  • 169
    • 0026612914 scopus 로고
    • High amount of epsilon-(gamma-glutamyl)lysine cross-links in Mallory bodies
    • Zatloukal K, Fesus L, Denk H, Tarcsa E, Spurej G, &, Böck G, (1992) High amount of epsilon-(gamma-glutamyl)lysine cross-links in Mallory bodies. Lab Invest 66, 774-777.
    • (1992) Lab Invest , vol.66 , pp. 774-777
    • Zatloukal, K.1    Fesus, L.2    Denk, H.3    Tarcsa, E.4    Spurej, G.5    Böck, G.6
  • 173
    • 0037902355 scopus 로고    scopus 로고
    • Activation of in situ tissue transglutaminase by intracellular reactive oxygen species
    • Lee ZW, Kwon SM, Kim SW, Yi SJ, Kim YM, &, Ha KS, (2003) Activation of in situ tissue transglutaminase by intracellular reactive oxygen species. Biochem Biophys Res Commun 305, 633-640.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 633-640
    • Lee, Z.W.1    Kwon, S.M.2    Kim, S.W.3    Yi, S.J.4    Kim, Y.M.5    Ha, K.S.6
  • 174
    • 76549112005 scopus 로고    scopus 로고
    • EGF potentiated oncogenesis requires a tissue transglutaminase-dependent signaling pathway leading to Src activation
    • Li B, Antonyak MA, Druso JE, Cheng L, Nikitin AY, &, Cerione RA, (2010) EGF potentiated oncogenesis requires a tissue transglutaminase-dependent signaling pathway leading to Src activation. Proc Natl Acad Sci USA 107, 1408-1413.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1408-1413
    • Li, B.1    Antonyak, M.A.2    Druso, J.E.3    Cheng, L.4    Nikitin, A.Y.5    Cerione, R.A.6
  • 176
    • 77953726947 scopus 로고    scopus 로고
    • Inhibition of tissue transglutaminase sensitizes TRAIL-resistant lung cancer cells through upregulation of death receptor 5
    • Frese-Schaper M, Schardt JA, Sakai T, Carboni GL, Schmid RA, &, Frese S, (2010) Inhibition of tissue transglutaminase sensitizes TRAIL-resistant lung cancer cells through upregulation of death receptor 5. FEBS Lett 584, 2867-2871.
    • (2010) FEBS Lett , vol.584 , pp. 2867-2871
    • Frese-Schaper, M.1    Schardt, J.A.2    Sakai, T.3    Carboni, G.L.4    Schmid, R.A.5    Frese, S.6


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