메뉴 건너뛰기




Volumn 44, Issue 1, 2013, Pages 1-9

Transglutaminases: Future perspectives

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 8; CALCIUM ION; CATHEPSIN D; GUANOSINE TRIPHOSPHATE; ISOENZYME; N METHYL DEXTRO ASPARTIC ACID; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 1; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 3; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 4; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 84871953211     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-012-1431-7     Document Type: Review
Times cited : (14)

References (102)
  • 1
    • 0034530521 scopus 로고    scopus 로고
    • Involvement of transglutaminase in the receptor-mediated endocytosis of mouse peritoneal macrophages
    • 11145187 1:CAS:528:DC%2BD3cXos1ehs78%3D 10.1248/bpb.23.1511
    • Abe S, Yamashita K, Kohno H, Ohkubo Y (2000) Involvement of transglutaminase in the receptor-mediated endocytosis of mouse peritoneal macrophages. Biol Pharm Bull 23:1511-1513
    • (2000) Biol Pharm Bull , vol.23 , pp. 1511-1513
    • Abe, S.1    Yamashita, K.2    Kohno, H.3    Ohkubo, Y.4
  • 2
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion co-receptor for fibronectin
    • 10684262 1:CAS:528:DC%2BD3cXhsVOqsLg%3D 10.1083/jcb.148.4.825
    • Akimov SS, Krylov D, Fleischman LF, Belkin AM (2000) Tissue transglutaminase is an integrin-binding adhesion co-receptor for fibronectin. J Cell Biol 148:825-838
    • (2000) J Cell Biol , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 3
    • 33645396457 scopus 로고    scopus 로고
    • Transglutaminase activity regulates osteoblast differentiation and matrix mineralization in MC3T3-E1 osteoblast cultures
    • 16469487 1:CAS:528:DC%2BD28XjtFGhu7w%3D 10.1016/j.matbio.2005.11.001
    • Al-Jallad HF, Nakano Y, Chen JL, McMillan E, Lefebvre C, Kaartinen MT (2006) Transglutaminase activity regulates osteoblast differentiation and matrix mineralization in MC3T3-E1 osteoblast cultures. Matrix Biol 25:135-148
    • (2006) Matrix Biol , vol.25 , pp. 135-148
    • Al-Jallad, H.F.1    Nakano, Y.2    Chen, J.L.3    McMillan, E.4    Lefebvre, C.5    Kaartinen, M.T.6
  • 4
    • 33845489411 scopus 로고    scopus 로고
    • Two isoforms of tissue transglutaminase mediate opposing cellular fates
    • 17116873 1:CAS:528:DC%2BD28XhtlahtrzO 10.1073/pnas.0604844103
    • Antonyak MA, Jansen JM, Miller AM, Ly TK, Endo M, Cerione RA (2006) Two isoforms of tissue transglutaminase mediate opposing cellular fates. Proc Natl Acad Sci USA 103:18609-18614
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18609-18614
    • Antonyak, M.A.1    Jansen, J.M.2    Miller, A.M.3    Ly, T.K.4    Endo, M.5    Cerione, R.A.6
  • 5
    • 3242669145 scopus 로고    scopus 로고
    • Tie2/angiopoietin-1 signaling regulates hematopoietic stem cell quiescence in the bone marrow niche
    • 15260986 1:CAS:528:DC%2BD2cXmtlKntr4%3D 10.1016/j.cell.2004.07.004
    • Arai F, Hirao A, Ohmura M, Sato H, Matsuoka S, Takubo K, Ito K, Koh GY, Suda T (2004) Tie2/angiopoietin-1 signaling regulates hematopoietic stem cell quiescence in the bone marrow niche. Cell 118:149-161
    • (2004) Cell , vol.118 , pp. 149-161
    • Arai, F.1    Hirao, A.2    Ohmura, M.3    Sato, H.4    Matsuoka, S.5    Takubo, K.6    Ito, K.7    Koh, G.Y.8    Suda, T.9
  • 6
    • 84871981788 scopus 로고    scopus 로고
    • Recent advances in the development of tissue transglutaminase (TG2) inhibitors
    • 10.1007/s00726-011-1188-4 22160259
    • Badarau E, Collighan RJ, Griffin M (2011) Recent advances in the development of tissue transglutaminase (TG2) inhibitors. Amino Acids. doi: 10.1007/s00726-011-1188-4
    • (2011) Amino Acids
    • Badarau, E.1    Collighan, R.J.2    Griffin, M.3
  • 8
    • 0028955591 scopus 로고
    • Identification of a substrate site for transglutaminases on the human protein synthesis initiation factor 5A
    • 7848270 1:CAS:528:DyaK2MXjsFyhtr4%3D
    • Beninati S, Nicolini L, Jakus J, Passeggio A, Abbruzzese A (1995) Identification of a substrate site for transglutaminases on the human protein synthesis initiation factor 5A. Biochem J 305:725-728
    • (1995) Biochem J , vol.305 , pp. 725-728
    • Beninati, S.1    Nicolini, L.2    Jakus, J.3    Passeggio, A.4    Abbruzzese, A.5
  • 9
    • 0032538613 scopus 로고    scopus 로고
    • Tissue transglutaminase expression affects hypusine metabolism in BALB/c 3T3 cells
    • 9804167 1:CAS:528:DyaK1cXmslOnsL4%3D 10.1016/S0014-5793(98)01191-0
    • Beninati S, Gentile V, Caraglia M, Lentini A, Tagliaferri P, Abbruzzese A (1998) Tissue transglutaminase expression affects hypusine metabolism in BALB/c 3T3 cells. FEBS Lett 437:34-38
    • (1998) FEBS Lett , vol.437 , pp. 34-38
    • Beninati, S.1    Gentile, V.2    Caraglia, M.3    Lentini, A.4    Tagliaferri, P.5    Abbruzzese, A.6
  • 10
    • 62949123361 scopus 로고    scopus 로고
    • An overview of the first 50 years of transglutaminase research
    • 19039625 1:CAS:528:DC%2BD1MXjt1Cqtb4%3D 10.1007/s00726-008-0211-x
    • Beninati S, Bergamini CM, Piacentini M (2009) An overview of the first 50 years of transglutaminase research. Amino Acids 36:591-598
    • (2009) Amino Acids , vol.36 , pp. 591-598
    • Beninati, S.1    Bergamini, C.M.2    Piacentini, M.3
  • 11
    • 84942089176 scopus 로고    scopus 로고
    • In memoriam: John E. Folk (1925-2010) Doi: 10.1007/s00726-012-1367-y
    • Beninati S, Park MH, Wolff E, Fésüs L, Abbruzzese A, Chung SI, Carmassi F, Cocuzzi E, Trawick ML, Piacentini M (2012a) In memoriam: John E. Folk (1925-2010). Amino Acids Doi: 10.1007/s00726-012-1367-y
    • (2012) Amino Acids
    • Beninati S, P.1
  • 12
    • 84871943544 scopus 로고    scopus 로고
    • Expression of different forms of transglutaminases by immature cells of Helianthus tuberosus sprout apices
    • 10.1007/s00726-012-1411-y
    • Beninati S, Iorio RA, Tasco G, Serafini-Fracassini D, Casadio R, Del Duca S (2012b) Expression of different forms of transglutaminases by immature cells of Helianthus tuberosus sprout apices. Amino Acids. doi: 10.1007/s00726-012- 1411-y
    • (2012) Amino Acids
    • Beninati, S.1    Iorio, R.A.2    Tasco, G.3    Serafini-Fracassini, D.4    Casadio, R.5    Del Duca, S.6
  • 14
    • 0032886829 scopus 로고    scopus 로고
    • Tumor plasticity allows vasculogenic mimicry, a novel form of angiogenic switch. A rose by any other name?
    • 10487823 1:STN:280:DyaK1MvhvFalsA%3D%3D 10.1016/S0002-9440(10)65164-4
    • Bissell MJ (1999) Tumor plasticity allows vasculogenic mimicry, a novel form of angiogenic switch. A rose by any other name? Am J Pathol 155:675-679
    • (1999) Am J Pathol , vol.155 , pp. 675-679
    • Bissell, M.J.1
  • 15
    • 0025028980 scopus 로고
    • Patterns of food hypersensitivity during sixteen years of double-blind, placebo-controlled food challenges
    • 2213379 1:STN:280:DyaK3M%2FhtFyrsA%3D%3D 10.1016/S0022-3476(05)80689-4
    • Bock SA, Atkins FM (1990) Patterns of food hypersensitivity during sixteen years of double-blind, placebo-controlled food challenges. J Pediatr 117:561-567
    • (1990) J Pediatr , vol.117 , pp. 561-567
    • Bock, S.A.1    Atkins, F.M.2
  • 16
    • 0037036409 scopus 로고    scopus 로고
    • Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb
    • 11956182 1:CAS:528:DC%2BD38XkslWgsL8%3D 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
    • (2002) J Biol Chem , vol.277 , pp. 20127-20130
    • Boehm, J.E.1    Singh, U.2    Combs, C.3    Antonyak, M.A.4    Cerione, R.A.5
  • 17
    • 84871948925 scopus 로고    scopus 로고
    • Probing the specificity of gamma-glutamylamine cyclotransferase: An enzyme involved in the metabolism of transglutaminase-catalyzed protein crosslinks
    • 10.1007/s00726-011-1153-2 22120669
    • Bowser TE, Trawick ML (2011) Probing the specificity of gamma-glutamylamine cyclotransferase: an enzyme involved in the metabolism of transglutaminase-catalyzed protein crosslinks. Amino Acids. doi: 10.1007/s00726-011-1153-2
    • (2011) Amino Acids
    • Bowser, T.E.1    Trawick, M.L.2
  • 18
    • 84871944251 scopus 로고    scopus 로고
    • Tissue transglutaminase: A new target to reverse cancer drug resistance
    • 10.1007/s00726-011-1167-9 22130737
    • Budillon A, Carbone C, Di Gennaro E (2011) Tissue transglutaminase: a new target to reverse cancer drug resistance. Amino Acids. doi: 10.1007/s00726-011-1167-9
    • (2011) Amino Acids
    • Budillon, A.1    Carbone, C.2    Di Gennaro, E.3
  • 19
    • 84872001053 scopus 로고    scopus 로고
    • Transglutaminase 2 interaction with small heat shock proteins mediate cell survival upon excitotoxic stress
    • 10.1007/s00726-011-1083-z
    • Caccamo D, Condello S, Ferlazzo N, Currò M, Griffin M, Ientile R (2011) Transglutaminase 2 interaction with small heat shock proteins mediate cell survival upon excitotoxic stress. Amino Acids. doi: 10.1007/s00726-011- 1083-z
    • (2011) Amino Acids
    • Caccamo, D.1    Condello, S.2    Ferlazzo, N.3    Currò, M.4    Griffin, M.5    Ientile, R.6
  • 20
    • 84871966892 scopus 로고    scopus 로고
    • Anti-tissue transglutaminase antibodies activate intracellular tissue transglutaminase by modulating cytosolic Ca(2+) homeostasis
    • 10.1007/s00726-011-1120-y 22038180
    • Caputo I, Lepretti M, Secondo A, Martucciello S, Paolella G, Sblattero D, Barone MV, Esposito C (2011) Anti-tissue transglutaminase antibodies activate intracellular tissue transglutaminase by modulating cytosolic Ca(2+) homeostasis. Amino Acids. doi: 10.1007/s00726-011-1120-y
    • (2011) Amino Acids
    • Caputo, I.1    Lepretti, M.2    Secondo, A.3    Martucciello, S.4    Paolella, G.5    Sblattero, D.6    Barone, M.V.7    Esposito, C.8
  • 21
    • 0034467556 scopus 로고    scopus 로고
    • Post-translational modifications of eukaryotic initiation factor-5A (eIF-5A) as a new target for anti-cancer therapy
    • 10736626 1:CAS:528:DC%2BD3cXltFSjsLw%3D 10.1007/978-1-4757-3230-6-16
    • Caraglia M, Tagliaferri P, Budillon A, Abbruzzese A (1999) Post-translational modifications of eukaryotic initiation factor-5A (eIF-5A) as a new target for anti-cancer therapy. Adv Exp Med Biol 472:187-198
    • (1999) Adv Exp Med Biol , vol.472 , pp. 187-198
    • Caraglia, M.1    Tagliaferri, P.2    Budillon, A.3    Abbruzzese, A.4
  • 22
    • 84871992265 scopus 로고    scopus 로고
    • EIF5A isoforms and cancer: Two brothers for two functions?
    • 10.1007/s00726-011-1182-x 22139412
    • Caraglia M, Park MH, Wolff EC, Marra M, Abbruzzese A (2011) eIF5A isoforms and cancer: two brothers for two functions? Amino Acids. doi: 10.1007/s00726-011-1182-x
    • (2011) Amino Acids
    • Caraglia, M.1    Park, M.H.2    Wolff, E.C.3    Marra, M.4    Abbruzzese, A.5
  • 23
    • 67650928193 scopus 로고    scopus 로고
    • Tissue transglutaminase promotes or suppresses tumors depending on cell context
    • 19528447 1:CAS:528:DC%2BD1MXos1Wnu74%3D
    • Chhabra A, Verma A, Mehta K (2009) Tissue transglutaminase promotes or suppresses tumors depending on cell context. Anticancer Res 29:1909-1919
    • (2009) Anticancer Res , vol.29 , pp. 1909-1919
    • Chhabra, A.1    Verma, A.2    Mehta, K.3
  • 24
    • 0035793583 scopus 로고    scopus 로고
    • Intron-exon swapping of transglutaminase mRNA and neuronal Tau aggregation in Alzheimer's disease
    • 11013236 1:CAS:528:DC%2BD3MXhtFWju70%3D 10.1074/jbc.M004776200
    • 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
  • 25
    • 14644403713 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the proangiogenic effect of factor XIII
    • 15618543 1:CAS:528:DC%2BD2MXhtl2ktbg%3D 10.1161/01.ATV.0000154137.21230. 80
    • Dardik R, Loscalzo J, Eskaraev R, Inbal A (2005) Molecular mechanisms underlying the proangiogenic effect of factor XIII. Arterioscler Thromb Vasc Biol 25:526-532
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 526-532
    • Dardik, R.1    Loscalzo, J.2    Eskaraev, R.3    Inbal, A.4
  • 26
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • 11113189 10.1128/MCB.21.1.148-155.2001
    • 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
  • 27
    • 84871998866 scopus 로고    scopus 로고
    • Tissue-specific responses to loss of transglutaminase 2
    • 10.1007/s00726-011-1183-9
    • Deasey S, Shanmugasundaram S, Nurminskaya M (2011) Tissue-specific responses to loss of transglutaminase 2. Amino Acids. doi: 10.1007/s00726-011- 1183-9
    • (2011) Amino Acids
    • Deasey, S.1    Shanmugasundaram, S.2    Nurminskaya, M.3
  • 28
    • 62949245813 scopus 로고    scopus 로고
    • Transglutaminases and their substrates in biology and human diseases: 50 years of growing
    • 18597041 1:CAS:528:DC%2BD1MXjt1CqtLw%3D 10.1007/s00726-008-0124-8
    • Facchiano A, Facchiano F (2009) Transglutaminases and their substrates in biology and human diseases: 50 years of growing. Amino Acids 36:599-614
    • (2009) Amino Acids , vol.36 , pp. 599-614
    • Facchiano, A.1    Facchiano, F.2
  • 29
    • 0037254694 scopus 로고    scopus 로고
    • Active sequences collection (ASC) database: A new tool to assign functions to protein sequences
    • 12520027 1:CAS:528:DC%2BD3sXhvFSmtb8%3D 10.1093/nar/gkg042
    • Facchiano AM, Facchiano A, Facchiano F (2003) Active sequences collection (ASC) database: a new tool to assign functions to protein sequences. Nucleic Acids Res 31:379-382
    • (2003) Nucleic Acids Res , vol.31 , pp. 379-382
    • Facchiano, A.M.1    Facchiano, A.2    Facchiano, F.3
  • 32
    • 0032519925 scopus 로고    scopus 로고
    • Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF
    • 9466984 1:CAS:528:DyaK1cXht1Wrt70%3D 10.1172/JCI1112
    • Fadok VA, Bratton DL, Konowal A, Freed PW, Westcott JY, Henson PM (1998) Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine/paracrine mechanisms involving TGF-beta, PGE2, and PAF. J Clin Invest 101:890-898
    • (1998) J Clin Invest , vol.101 , pp. 890-898
    • Fadok, V.A.1    Bratton, D.L.2    Konowal, A.3    Freed, P.W.4    Westcott, J.Y.5    Henson, P.M.6
  • 33
    • 77951911179 scopus 로고    scopus 로고
    • Regulation of autophagy in mammals and its interplay with apoptosis
    • 20165902 1:CAS:528:DC%2BC3cXltVyksbc%3D 10.1007/s00018-010-0284-z
    • Fimia GM, Piacentini M (2010) Regulation of autophagy in mammals and its interplay with apoptosis. Cell Mol Life Sci 67(10):1581-1588
    • (2010) Cell Mol Life Sci , vol.67 , Issue.10 , pp. 1581-1588
    • Fimia, G.M.1    Piacentini, M.2
  • 34
    • 0019878161 scopus 로고
    • γ-Glutamylamine cyclotransferase. An enzyme involved in the catabolism of epsilon-(gamma-glutamyl) lysine and other gamma-glutamylamines
    • 6117008 1:CAS:528:DyaL3MXlvVaru7k%3D 10.1007/BF00235688
    • Fink ML, Folk JE (1981) γ-Glutamylamine cyclotransferase. An enzyme involved in the catabolism of epsilon-(gamma-glutamyl) lysine and other gamma-glutamylamines. Mol Cell Biochem 38:59-67
    • (1981) Mol Cell Biochem , vol.38 , pp. 59-67
    • Fink, M.L.1    Folk, J.E.2
  • 35
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase catalyzed epsilon-(gamma-glutamyl) lysine bond formation
    • 6133417 1:CAS:528:DyaL3sXhsFKrsLo%3D
    • Folk JE (1983) Mechanism and basis for specificity of transglutaminase catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Adv Enzymol Relat Areas Mol Biol 54:1-56
    • (1983) Adv Enzymol Relat Areas Mol Biol , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 36
    • 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
    • 5928192 1:CAS:528:DyaF28XltV2nu7g%3D
    • 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
  • 38
    • 62949131510 scopus 로고    scopus 로고
    • Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin
    • 18604470 1:CAS:528:DC%2BD1MXjt1Cqt7k%3D 10.1007/s00726-008-0125-7
    • Forsprecher J, Wang Z, Nelea V, Kaartinen MT (2009) Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin. Amino Acids 36:747-753
    • (2009) Amino Acids , vol.36 , pp. 747-753
    • Forsprecher, J.1    Wang, Z.2    Nelea, V.3    Kaartinen, M.T.4
  • 39
    • 84871960316 scopus 로고    scopus 로고
    • Retinoids produced by macrophages engulfing apoptotic cells contribute to the appearance of transglutaminase 2 in apoptotic thymocytes
    • 10.1007/s00726-011-1119-4 21997537
    • Garabuczi E, Kiss B, Felszeghy S, Tsay GJ, Fésüs L, Szondy Z (2011) Retinoids produced by macrophages engulfing apoptotic cells contribute to the appearance of transglutaminase 2 in apoptotic thymocytes. Amino Acids. doi: 10.1007/s00726-011-1119-4
    • (2011) Amino Acids
    • Garabuczi, E.1    Kiss, B.2    Felszeghy, S.3    Tsay, G.J.4    Fésüs, L.5    Szondy, Z.6
  • 40
    • 9944246963 scopus 로고    scopus 로고
    • Tumour angiogenesis: Vascular growth and survival
    • 15563307 10.1111/j.1600-0463.2004.apm11207-0804.x
    • Giatromanolaki A, Sivridis E, Koukourakis MI (2004) Tumour angiogenesis: vascular growth and survival. APMIS 112:431-440
    • (2004) APMIS , vol.112 , pp. 431-440
    • Giatromanolaki, A.1    Sivridis, E.2    Koukourakis, M.I.3
  • 41
    • 0035980007 scopus 로고    scopus 로고
    • Evolution of transglutaminase genes: Identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z
    • 11390390 1:CAS:528:DC%2BD3MXmvFCmuro%3D 10.1074/jbc.M102553200
    • Grenard P, Bates MK, Aeschlimann D (2001) Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z. J Biol Chem 276:33066-33078
    • (2001) J Biol Chem , vol.276 , pp. 33066-33078
    • Grenard, P.1    Bates, M.K.2    Aeschlimann, D.3
  • 42
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • 12366374 1:CAS:528:DC%2BD38XovF2jt78%3D 10.1042/BJ20021234
    • Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: nature's biological glues. Biochem J 368:377-396
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 43
    • 40849085396 scopus 로고    scopus 로고
    • Substrate-bound insulin-like growth factor (IGF)-I-IGF binding protein-vitronectin-stimulated breast cell migration is enhanced by coactivation of the phosphatidylinositide 3-kinase/AKT pathway by (alpha)v-integrins and the IGF-I receptor
    • 18079201 1:CAS:528:DC%2BD1cXisVaqtrs%3D 10.1210/en.2007-0740
    • Hollier BG, Kricker JA, Van Lonkhuyzen DR, Leavesley DI, Upton Z (2008) Substrate-bound insulin-like growth factor (IGF)-I-IGF binding protein-vitronectin-stimulated breast cell migration is enhanced by coactivation of the phosphatidylinositide 3-kinase/AKT pathway by (alpha)v-integrins and the IGF-I receptor. Endocrinology 149:1075-1090
    • (2008) Endocrinology , vol.149 , pp. 1075-1090
    • Hollier, B.G.1    Kricker, J.A.2    Van Lonkhuyzen, D.R.3    Leavesley, D.I.4    Upton, Z.5
  • 46
    • 45449119171 scopus 로고    scopus 로고
    • Increased levels of γ-Glutamyl amines in Huntington disease CSF
    • 18422943 1:CAS:528:DC%2BD1cXot1Ohuro%3D 10.1111/j.1471-4159.2008.05350.x
    • Jeitner TM, Matson WR, Folk JE, Blass JP, Cooper AJL (2008) Increased levels of γ-Glutamyl amines in Huntington disease CSF. J Neurochem 106:37-44
    • (2008) J Neurochem , vol.106 , pp. 37-44
    • Jeitner, T.M.1    Matson, W.R.2    Folk, J.E.3    Blass, J.P.4    Cooper, A.J.L.5
  • 48
    • 84871960505 scopus 로고    scopus 로고
    • γ-Glutamylamines and neurodegenerative diseases
    • 10.1007/s00726-011-1209-3 22407484
    • Jeitner TM, Battaile K, Cooper AJ (2012) γ-Glutamylamines and neurodegenerative diseases. Amino Acids. doi: 10.1007/s00726-011-1209-3
    • (2012) Amino Acids
    • Jeitner, T.M.1    Battaile, K.2    Cooper, A.J.3
  • 49
    • 84871975618 scopus 로고    scopus 로고
    • The role of TG2 in ECV304-related vasculogenic mimicry
    • 10.1007/s00726-011-1214-6 22231926
    • Jones RA, Wang Z, Dookie S, Griffin M (2012) The role of TG2 in ECV304-related vasculogenic mimicry. Amino Acids. doi: 10.1007/s00726-011-1214-6
    • (2012) Amino Acids
    • Jones, R.A.1    Wang, Z.2    Dookie, S.3    Griffin, M.4
  • 50
    • 0036894649 scopus 로고    scopus 로고
    • Tissue transglutaminase and its substrates in bone
    • 12469910 1:CAS:528:DC%2BD38XpsV2lsL4%3D 10.1359/jbmr.2002.17.12.2161
    • Kaartinen MT, El-Maadawy S, Räsänen NH, McKee MD (2002) Tissue transglutaminase and its substrates in bone. J Bone Miner Res 17:2161-2173
    • (2002) J Bone Miner Res , vol.17 , pp. 2161-2173
    • Kaartinen, M.T.1    El-Maadawy, S.2    Räsänen, N.H.3    McKee, M.D.4
  • 51
    • 79953182314 scopus 로고    scopus 로고
    • Insulin-like growth factor-I:vitronectin complex-induced changes in gene expression effect breast cell survival and migration
    • 21303956 1:CAS:528:DC%2BC3MXkvVOktrw%3D 10.1210/en.2010-0897
    • Kashyap AS, Hollier BG, Manton KJ, Satyamoorthy K, Leavesley DI, Upton Z (2011) Insulin-like growth factor-I:vitronectin complex-induced changes in gene expression effect breast cell survival and migration. Endocrinology 152:1388-1401
    • (2011) Endocrinology , vol.152 , pp. 1388-1401
    • Kashyap, A.S.1    Hollier, B.G.2    Manton, K.J.3    Satyamoorthy, K.4    Leavesley, D.I.5    Upton, Z.6
  • 52
    • 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
    • 10521460 1:CAS:528:DyaK1MXntVSmtL4%3D 10.1074/jbc.274.43.30715
    • Kim SY, Grant P, Lee JH, Pant HC, Steinert PM (1999) 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 274:30715-30721
    • (1999) J Biol Chem , vol.274 , pp. 30715-30721
    • Kim, S.Y.1    Grant, P.2    Lee, J.H.3    Pant, H.C.4    Steinert, P.M.5
  • 53
    • 84871955140 scopus 로고    scopus 로고
    • Depletion of cathepsin D by transglutaminase 2 through protein cross-linking promotes cell survival
    • 10.1007/s00726-011-1089-6
    • Kim SJ, Kim KH, Ahn ER, Yoo BC, Kim SY (2011) Depletion of cathepsin D by transglutaminase 2 through protein cross-linking promotes cell survival. Amino Acids. doi: 10.1007/s00726-011-1089-6
    • (2011) Amino Acids
    • Kim, S.J.1    Kim, K.H.2    Ahn, E.R.3    Yoo, B.C.4    Kim, S.Y.5
  • 54
    • 84871943950 scopus 로고    scopus 로고
    • Polymorphism of transglutaminase 2: Unusually low frequency of genomic variants with deficient functions
    • 10.1007/s00726-011-1194-6 22160262
    • Király R, Barta E, Fésüs L (2011) Polymorphism of transglutaminase 2: unusually low frequency of genomic variants with deficient functions. Amino Acids. doi: 10.1007/s00726-011-1194-6
    • (2011) Amino Acids
    • Király, R.1    Barta, E.2    Fésüs, L.3
  • 55
    • 38349076498 scopus 로고    scopus 로고
    • Retinoid receptor-activating ligands are produced within the mouse thymus during postnatal development
    • 18085670 1:CAS:528:DC%2BD1cXhvVOnsbk%3D 10.1002/eji.200737342
    • Kiss I, Rühl R, Szegezdi E, Fritzsche B, Tóth B, Pongrácz J, Perlmann T, Fésüs L, Szondy Z (2008) Retinoid receptor-activating ligands are produced within the mouse thymus during postnatal development. Eur J Immunol 38:147-155
    • (2008) Eur J Immunol , vol.38 , pp. 147-155
    • Kiss, I.1    Rühl, R.2    Szegezdi, E.3    Fritzsche, B.4    Tóth, B.5    Pongrácz, J.6    Perlmann, T.7    Fésüs, L.8    Szondy, Z.9
  • 56
    • 84871994461 scopus 로고    scopus 로고
    • Tissue transglutaminase, inflammation, and cancer: How intimate is the relationship?
    • 10.1007/s00726-011-1139-0
    • Kumar S, Mehta K (2011) Tissue transglutaminase, inflammation, and cancer: how intimate is the relationship? Amino Acids. doi: 10.1007/s00726-011- 1139-0
    • (2011) Amino Acids
    • Kumar, S.1    Mehta, K.2
  • 57
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • 19240129 1:CAS:528:DC%2BD1MXivF2ntrg%3D 10.1101/gad.1758709
    • Legate KR, Wickstrom SA, Fassler R (2009) Genetic and cell biological analysis of integrin outside-in signaling. Genes Dev 23:397-418
    • (2009) Genes Dev , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickstrom, S.A.2    Fassler, R.3
  • 58
    • 39049087558 scopus 로고    scopus 로고
    • Impairment of the metastatic activity of melanoma cells by transglutaminase-catalyzed incorporation of polyamines into laminin and matrigel
    • 17356804 1:CAS:528:DC%2BD1cXkvFWmsro%3D 10.1007/s00726-007-0505-4
    • Lentini A, Provenzano B, Caraglia M, Shevchenko A, Abbruzzese A, Beninati S (2008) Impairment of the metastatic activity of melanoma cells by transglutaminase-catalyzed incorporation of polyamines into laminin and matrigel. Amino Acids 34:251-256
    • (2008) Amino Acids , vol.34 , pp. 251-256
    • Lentini, A.1    Provenzano, B.2    Caraglia, M.3    Shevchenko, A.4    Abbruzzese, A.5    Beninati, S.6
  • 59
    • 79955995168 scopus 로고    scopus 로고
    • Spermidine delays eye lens opacification in vitro by suppressing transglutaminase-catalyzed crystallin cross-linking
    • 21287398 1:CAS:528:DC%2BC3MXhsVCit7o%3D 10.1007/s10930-011-9311-7
    • Lentini A, Tabolacci C, Mattioli P, Provenzano B, Beninati S (2011) Spermidine delays eye lens opacification in vitro by suppressing transglutaminase-catalyzed crystallin cross-linking. Protein J 30:109-114
    • (2011) Protein J , vol.30 , pp. 109-114
    • Lentini, A.1    Tabolacci, C.2    Mattioli, P.3    Provenzano, B.4    Beninati, S.5
  • 61
    • 67650892240 scopus 로고    scopus 로고
    • Memory and the NMDA receptors
    • 19605837 1:CAS:528:DC%2BD1MXos1Wrtro%3D 10.1056/NEJMcibr0902052
    • Li F, Tsien JZ (2009) Memory and the NMDA receptors. N Engl J Med 361:302-303
    • (2009) N Engl J Med , vol.361 , pp. 302-303
    • Li, F.1    Tsien, J.Z.2
  • 62
    • 49249086117 scopus 로고    scopus 로고
    • Age-related changes in polyamines in memory associated brain structures in rats
    • 18621105 1:CAS:528:DC%2BD1cXhtVSgtbbL 10.1016/j.neuroscience.2008.06.033
    • Liu P, Gupta N, Jing Y, Zhang H (2008) Age-related changes in polyamines in memory associated brain structures in rats. Neuroscience 155:789-796
    • (2008) Neuroscience , vol.155 , pp. 789-796
    • Liu, P.1    Gupta, N.2    Jing, Y.3    Zhang, H.4
  • 63
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • 12563291 1:CAS:528:DC%2BD3sXnsFaqtg%3D%3D 10.1038/nrm1014
    • Lorand L, Graham RM (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 4:140-156
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 64
    • 34247153086 scopus 로고    scopus 로고
    • Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells
    • 17043648 1:CAS:528:DC%2BD2sXktVChtr0%3D 10.1038/sj.onc.1210035
    • Mangala LS, Fok JY, Zorrilla-Calancha IR, Verma A, Mehta K (2007) Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells. Oncogene 26:2459-2470
    • (2007) Oncogene , vol.26 , pp. 2459-2470
    • Mangala, L.S.1    Fok, J.Y.2    Zorrilla-Calancha, I.R.3    Verma, A.4    Mehta, K.5
  • 65
    • 84871960070 scopus 로고    scopus 로고
    • Possible involvement of transglutaminase-catalyzed reactions in the physiopathology of neurodegenerative diseases
    • 10.1007/s00726-011-1081-1
    • Martin A, Giuliano A, Collaro D, De Vivo G, Sedia C, Serretiello E, Gentile V (2011) Possible involvement of transglutaminase-catalyzed reactions in the physiopathology of neurodegenerative diseases. Amino Acids. doi: 10.1007/s00726-011-1081-1
    • (2011) Amino Acids
    • Martin, A.1    Giuliano, A.2    Collaro, D.3    De Vivo, G.4    Sedia, C.5    Serretiello, E.6    Gentile, V.7
  • 66
    • 0033593593 scopus 로고    scopus 로고
    • Troponin i degradation and covalent complex formation accompanies myocardial ischemia/reperfusion injury
    • 9915770 1:CAS:528:DyaK1MXmslGisQ%3D%3D 10.1161/01.RES.84.1.9
    • McDonough JL, Arrell DK, Van Eyk JE (1999) Troponin I degradation and covalent complex formation accompanies myocardial ischemia/reperfusion injury. Circ Res 84:9-20
    • (1999) Circ Res , vol.84 , pp. 9-20
    • McDonough, J.L.1    Arrell, D.K.2    Van Eyk, J.E.3
  • 67
    • 0031013601 scopus 로고    scopus 로고
    • Expression of GTP-dependent and GTP-independent tissue-type transglutaminase in cytokine-treated rat brain astrocytes
    • 9013629 1:CAS:528:DyaK2sXhtFCitro%3D 10.1074/jbc.272.6.3724
    • 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
  • 68
    • 0023903858 scopus 로고
    • Enhanced tumour necrosis factor and interleukin-1 in fulminant hepatic failure
    • 2898700 1:STN:280:DyaL1c3mtVGmtQ%3D%3D 10.1016/S0140-6736(88)90006-2
    • Muto Y, Nouri-Aria KT, Meager A, Alexander GJ, Eddleston AL, Williams R (1988) Enhanced tumour necrosis factor and interleukin-1 in fulminant hepatic failure. Lancet 2:72-74
    • (1988) Lancet , vol.2 , pp. 72-74
    • Muto, Y.1    Nouri-Aria, K.T.2    Meager, A.3    Alexander, G.J.4    Eddleston, A.L.5    Williams, R.6
  • 69
    • 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
    • 8626785 1:CAS:528:DyaK28XhtlSmtL0%3D 10.1074/jbc.271.27.16323
    • Nagy L, Saydak M, Shipley N, Lu S, Basilion JP, Yan ZH, Syka P, Chandraratna RA, Stein JP, Heyman RA, Davies PJ (1996) 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 271:4355-4365
    • (1996) J Biol Chem , vol.271 , pp. 4355-4365
    • Nagy, L.1    Saydak, M.2    Shipley, N.3    Lu, S.4    Basilion, J.P.5    Yan, Z.H.6    Syka, P.7    Chandraratna, R.A.8    Stein, J.P.9    Heyman, R.A.10    Davies, P.J.11
  • 70
    • 0035827627 scopus 로고    scopus 로고
    • Targeted inactivation of Gh/tissue transglutaminase II
    • 11274171 1:CAS:528:DC%2BD3MXktlKnu70%3D 10.1074/jbc.M010846200
    • Nanda N, Iismaa SE, Owens WA, Husain A, Mackay F, Graham RM (2001) Targeted inactivation of Gh/tissue transglutaminase II. J Biol Chem 276:20673-20678
    • (2001) J Biol Chem , vol.276 , pp. 20673-20678
    • Nanda, N.1    Iismaa, S.E.2    Owens, W.A.3    Husain, A.4    MacKay, F.5    Graham, R.M.6
  • 71
    • 84857427521 scopus 로고    scopus 로고
    • Cellular functions of tissue transglutaminase
    • 22364871 1:CAS:528:DC%2BC38XhsFKgsL3K 10.1016/B978-0-12-394305-7.00001-X
    • Nurminskaya MV, Belkin AM (2012) Cellular functions of tissue transglutaminase. Int Rev Cell Mol Biol 294:1-97
    • (2012) Int Rev Cell Mol Biol , vol.294 , pp. 1-97
    • Nurminskaya, M.V.1    Belkin, A.M.2
  • 72
    • 32844467767 scopus 로고    scopus 로고
    • Transglutaminases in mineralized tissues
    • 16368540 1:CAS:528:DC%2BD28XislSns7o%3D 10.2741/1907
    • Nurminskaya M, Kaartinen MT (2006) Transglutaminases in mineralized tissues. Front Biosci 11:1591-1606
    • (2006) Front Biosci , vol.11 , pp. 1591-1606
    • Nurminskaya, M.1    Kaartinen, M.T.2
  • 73
    • 60749093017 scopus 로고    scopus 로고
    • Assay-related issues in the measurement of cardiac troponins
    • 19168041 1:CAS:528:DC%2BD1MXisFahur0%3D 10.1016/j.cca.2008.12.037
    • Panteghini M (2009) Assay-related issues in the measurement of cardiac troponins. Clin Chim Acta 402:88-93
    • (2009) Clin Chim Acta , vol.402 , pp. 88-93
    • Panteghini, M.1
  • 74
    • 33845951183 scopus 로고    scopus 로고
    • Transglutaminase 2 mediates polymer formation of I-kappaBalpha through C-terminal glutamine cluster
    • 16987813 1:CAS:528:DC%2BD28XhtF2gtbnP 10.1074/jbc.M604150200
    • 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
  • 75
    • 84871971104 scopus 로고    scopus 로고
    • Identification of human salivary transglutaminases
    • 10.1007/s00726-011-1142-5 22080209
    • Perez Alea M, Thomas V, Martin G, El Alaoui S (2011) Identification of human salivary transglutaminases. Amino Acids. doi: 10.1007/s00726-011-1142-5
    • (2011) Amino Acids
    • Perez Alea, M.1    Thomas, V.2    Martin, G.3    El Alaoui, S.4
  • 76
    • 84872000567 scopus 로고    scopus 로고
    • Expression of transglutaminase-2 isoforms in normal human tissues and cancer cell lines: Dysregulation of alternative slicing in cancer
    • 10.1007/s00726-011-1127-4 22089883
    • Phatak VM, Croft SM, Rameshaiah Setty SG, Scarpellini A, Hughes DC, Rees R, McArdle S, Verderio EA (2011) Expression of transglutaminase-2 isoforms in normal human tissues and cancer cell lines: dysregulation of alternative slicing in cancer. Amino Acids. doi: 10.1007/s00726-011-1127-4
    • (2011) Amino Acids
    • Phatak, V.M.1    Croft, S.M.2    Rameshaiah Setty, S.G.3    Scarpellini, A.4    Hughes, D.C.5    Rees, R.6    McArdle, S.7    Verderio, E.A.8
  • 77
    • 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 25:2788-2796
    • (2007) PLoS Biol , vol.25 , pp. 2788-2796
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 78
    • 84871947298 scopus 로고    scopus 로고
    • Transglutaminase-mediated modification of ovomucoid: Effects on its trypsin inhibitory activity and antigenic properties
    • 10.1007/s00726-011-1155-0 22105613
    • Porta R, Giosafatto CV, di Pierro P, Sorrentino A, Mariniello L (2011) Transglutaminase-mediated modification of ovomucoid: effects on its trypsin inhibitory activity and antigenic properties. Amino Acids. doi: 10.1007/s00726-011-1155-0
    • (2011) Amino Acids
    • Porta, R.1    Giosafatto, C.V.2    Di Pierro, P.3    Sorrentino, A.4    Mariniello, L.5
  • 79
    • 0026690364 scopus 로고
    • Distinct proliferative and differentiated stages of murine MC-3T3-E1 culture; An in vitro model of osteoblast development
    • 1414487 1:STN:280:DyaK3s%2FjsVCgsw%3D%3D 10.1002/jbmr.5650070613
    • Quarles LD, Yohay DA, Lever LW, Caton R, Wenstrup RJ (1992) Distinct proliferative and differentiated stages of murine MC-3T3-E1 culture; an in vitro model of osteoblast development. J Bone Miner Res 7:683-692
    • (1992) J Bone Miner Res , vol.7 , pp. 683-692
    • Quarles, L.D.1    Yohay, D.A.2    Lever, L.W.3    Caton, R.4    Wenstrup, R.J.5
  • 80
    • 78650153633 scopus 로고    scopus 로고
    • Tumour vascularization via endothelial differentiation of glioblastoma stem-like cells
    • 21102434 1:CAS:528:DC%2BC3cXhsVGhsr%2FJ 10.1038/nature09557
    • Ricci-Vitiani L, Pallini R, Biffoni M, Todaro M, Invernici G et al (2010) Tumour vascularization via endothelial differentiation of glioblastoma stem-like cells. Nature 468:824-828
    • (2010) Nature , vol.468 , pp. 824-828
    • Ricci-Vitiani, L.1    Pallini, R.2    Biffoni, M.3    Todaro, M.4    Invernici, G.5
  • 81
    • 0032557461 scopus 로고    scopus 로고
    • Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter
    • 9582307 1:CAS:528:DyaK1cXjsVertbY%3D 10.1074/jbc.273.21.12798
    • Ritter SJ, Davies PJ (1998) 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):12798-12806
    • (1998) J Biol Chem , vol.273 , Issue.21 , pp. 12798-12806
    • Ritter, S.J.1    Davies, P.J.2
  • 82
    • 34548157657 scopus 로고    scopus 로고
    • Roles of transglutaminases in cardiac and vascular diseases
    • 17127261 1:CAS:528:DC%2BD28Xht1OnsbnN 10.2741/2253
    • Sane DC, Kontos JL, Greenberg CS (2007) Roles of transglutaminases in cardiac and vascular diseases. Front Biosci 12:2530-2545
    • (2007) Front Biosci , vol.12 , pp. 2530-2545
    • Sane, D.C.1    Kontos, J.L.2    Greenberg, C.S.3
  • 84
    • 0000719659 scopus 로고
    • An enzymically catalyzed incorporation of amines into proteins
    • 13471608 1:CAS:528:DyaG2sXptFekuw%3D%3D 10.1016/0006-3002(57)90512-7
    • Sarkar NK, Clarke DD, Waelsch H (1957) An enzymically catalyzed incorporation of amines into proteins. Biochim Biophys Acta 25:451-452
    • (1957) Biochim Biophys Acta , vol.25 , pp. 451-452
    • Sarkar, N.K.1    Clarke, D.D.2    Waelsch, H.3
  • 86
    • 0017902345 scopus 로고
    • 2+-induced cross-linking of membrane proteins in intact human erythrocytes
    • 28146 1:CAS:528:DyaE1cXksFOiu7k%3D 10.1021/bi00606a022
    • 2+-induced cross-linking of membrane proteins in intact human erythrocytes. Biochemistry 17:2598-2604
    • (1978) Biochemistry , vol.17 , pp. 2598-2604
    • Siefring Jr., G.E.1    Apostol, A.B.2    Velasco, P.T.3    Lorand, L.4
  • 87
  • 88
    • 82955250010 scopus 로고    scopus 로고
    • Celiac disease and transglutaminase 2: A model for posttranslational modification of antigens and HLA association in the pathogenesis of autoimmune disorders
    • 21917438 1:CAS:528:DC%2BC3MXhsFOhtLjI 10.1016/j.coi.2011.08.006
    • Sollid LM, Jabri B (2011) Celiac disease and transglutaminase 2: a model for posttranslational modification of antigens and HLA association in the pathogenesis of autoimmune disorders. Curr Opin Immunol 23:732-738
    • (2011) Curr Opin Immunol , vol.23 , pp. 732-738
    • Sollid, L.M.1    Jabri, B.2
  • 89
    • 84871986798 scopus 로고    scopus 로고
    • The side chain of glutamine 13 is the acyl-donor amino acid modified by type 2 transglutaminase in subunit T of the native rabbit skeletal muscle troponin complex
    • 10.1007/s00726-011-1144-3
    • Squerzanti M, Cervellati C, Ura B, Mischiati C, Pucci P, Annunziata S, Iannone C, Casadio R, Bergamini CM, Esposito C (2011) The side chain of glutamine 13 is the acyl-donor amino acid modified by type 2 transglutaminase in subunit T of the native rabbit skeletal muscle troponin complex. Amino Acids. doi: 10.1007/s00726-011-1144-3
    • (2011) Amino Acids
    • Squerzanti, M.1    Cervellati, C.2    Ura, B.3    Mischiati, C.4    Pucci, P.5    Annunziata, S.6    Iannone, C.7    Casadio, R.8    Bergamini, C.M.9    Esposito, C.10
  • 90
    • 84868633053 scopus 로고    scopus 로고
    • Treatment-induced damage to the microenvironment promotes prostate cancer therapy resistance through WNT16B
    • 10.1038/nm.2890
    • Sun Y, Campisi J, Higano C, Beer TM, Porter P, Coleman I, True L, Nelson PS (2012) Treatment-induced damage to the microenvironment promotes prostate cancer therapy resistance through WNT16B. Nat Med. doi: 10.1038/nm.2890
    • (2012) Nat Med
    • Sun, Y.1    Campisi, J.2    Higano, C.3    Beer, T.M.4    Porter, P.5    Coleman, I.6    True, L.7    Nelson, P.S.8
  • 92
    • 84861694176 scopus 로고    scopus 로고
    • Evidences for a role of protein cross-links in transglutaminase-related disease
    • 21800260 1:CAS:528:DC%2BC38Xhtlyqtb4%3D 10.1007/s00726-011-1011-2
    • Tabolacci C, Lentini A, Provenzano B, Beninati S (2012) Evidences for a role of protein cross-links in transglutaminase-related disease. Amino Acids 42:975-986
    • (2012) Amino Acids , vol.42 , pp. 975-986
    • Tabolacci, C.1    Lentini, A.2    Provenzano, B.3    Beninati, S.4
  • 93
    • 84871942751 scopus 로고    scopus 로고
    • Transglutaminase 2 as a biomarker of osteoarthritis: An update
    • 10.1007/s00726-011-1181-y 22139411
    • Tarantino U, Ferlosio A, Arcuri G, Spagnoli LG, Orlandi A (2011) Transglutaminase 2 as a biomarker of osteoarthritis: an update. Amino Acids. doi: 10.1007/s00726-011-1181-y
    • (2011) Amino Acids
    • Tarantino, U.1    Ferlosio, A.2    Arcuri, G.3    Spagnoli, L.G.4    Orlandi, A.5
  • 94
    • 0033771879 scopus 로고    scopus 로고
    • Differentiate or die: The view from Montreal
    • 11279548 1:CAS:528:DC%2BD3cXnslWjur4%3D 10.1038/sj.cdd.4400723
    • Thiele CJ, Gore S, Collins S, Waxman S, Miller W (2000) Differentiate or die: the view from Montreal. Cell Death Differ 7:1014-1017
    • (2000) Cell Death Differ , vol.7 , pp. 1014-1017
    • Thiele, C.J.1    Gore, S.2    Collins, S.3    Waxman, S.4    Miller, W.5
  • 96
    • 84859712314 scopus 로고    scopus 로고
    • Hippocampal polyamine levels and transglutaminase activity are paralleling spatial memory retrieval in the C57BL/6 J mouse
    • 10.1002/hipo.22016 1:CAS:528:DC%2BC38XlsFOntr4%3D
    • Tiboldi A, Lentini A, Provenzano B, Tabolacci C, Höger H, Beninati S, Lubec G (2012) Hippocampal polyamine levels and transglutaminase activity are paralleling spatial memory retrieval in the C57BL/6 J mouse. Hippocampus 5:1068-1074
    • (2012) Hippocampus , vol.5 , pp. 1068-1074
    • Tiboldi, A.1    Lentini, A.2    Provenzano, B.3    Tabolacci, C.4    Höger, H.5    Beninati, S.6    Lubec, G.7
  • 97
    • 84871945231 scopus 로고    scopus 로고
    • γ-Tocopherol inhibits human prostate cancer cell proliferation by up-regulation of transglutaminase 2 and down-regulation of cyclins
    • 10.1007/s00726-012-1278-y 20981458
    • Torricelli P, Caraglia M, Abbruzzese A, Beninati S (2011) γ-Tocopherol inhibits human prostate cancer cell proliferation by up-regulation of transglutaminase 2 and down-regulation of cyclins. Amino Acids. doi: 10.1007/s00726-012-1278-y
    • (2011) Amino Acids
    • Torricelli, P.1    Caraglia, M.2    Abbruzzese, A.3    Beninati, S.4
  • 98
    • 34548848815 scopus 로고    scopus 로고
    • Tissue transglutaminase-mediated chemoresistance in cancer cells
    • 17662645 1:CAS:528:DC%2BD2sXhtFWhs7zK 10.1016/j.drup.2007.06.002
    • Verma A, Mehta K (2007) Tissue transglutaminase-mediated chemoresistance in cancer cells. Drug Resist Updat 10:144-151
    • (2007) Drug Resist Updat , vol.10 , pp. 144-151
    • Verma, A.1    Mehta, K.2
  • 99
    • 84871991783 scopus 로고    scopus 로고
    • Transglutaminase 2 and Factor XIII catalyze distinct substrates in differentiating osteoblastic cell line: Utility of highly reactive substrate peptides
    • 10.1007/s00726-011-1131-8
    • Watanabe K, Tsunoda K, Itoh M, Fukui M, Mori H, Hitomi K (2011) Transglutaminase 2 and Factor XIII catalyze distinct substrates in differentiating osteoblastic cell line: utility of highly reactive substrate peptides. Amino Acids. doi: 10.1007/s00726-011-1131-8
    • (2011) Amino Acids
    • Watanabe, K.1    Tsunoda, K.2    Itoh, M.3    Fukui, M.4    Mori, H.5    Hitomi, K.6
  • 100
    • 0034068838 scopus 로고    scopus 로고
    • IgE-binding activity to enzyme-digested ovomucoid distinguishes between patients with contact urticaria to egg with and without overt symptoms on ingestion
    • 10858989 1:CAS:528:DC%2BD3cXktVCns7w%3D 10.1034/j.1398-9995.2000.00430.x
    • Yamada K, Urisu A, Kakami M, Koyama H, Tokuda R, Wada E, Kondo Y, Ando H, Morita Y, Torii S (2000) IgE-binding activity to enzyme-digested ovomucoid distinguishes between patients with contact urticaria to egg with and without overt symptoms on ingestion. Allergy 55:565-569
    • (2000) Allergy , vol.55 , pp. 565-569
    • Yamada, K.1    Urisu, A.2    Kakami, M.3    Koyama, H.4    Tokuda, R.5    Wada, E.6    Kondo, Y.7    Ando, H.8    Morita, Y.9    Torii, S.10
  • 101
    • 84871952778 scopus 로고    scopus 로고
    • Divergent results induced by different types of septic shock in transglutaminase 2 knockout mice
    • 10.1007/s00726-012-1412-x 23053022
    • Yoo H, Ahn ER, Kim SJ, Lee SH, Oh SH, Kim SY (2012) Divergent results induced by different types of septic shock in transglutaminase 2 knockout mice. Amino Acids. doi: 10.1007/s00726-012-1412-x
    • (2012) Amino Acids
    • Yoo, H.1    Ahn, E.R.2    Kim, S.J.3    Lee, S.H.4    Oh, S.H.5    Kim, S.Y.6
  • 102
    • 32844466022 scopus 로고    scopus 로고
    • The role of tissue transglutaminase in cell-matrix interactions
    • 16146797 1:CAS:528:DC%2BD2MXhtlSrurfK 10.2741/1863
    • Zemskov EA, Janiak A, Hang J, Waghray A, Belkin AM (2006) The role of tissue transglutaminase in cell-matrix interactions. Front Biosci 11:1057-1076
    • (2006) Front Biosci , vol.11 , pp. 1057-1076
    • Zemskov, E.A.1    Janiak, A.2    Hang, J.3    Waghray, A.4    Belkin, A.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.