메뉴 건너뛰기




Volumn 38, Issue , 2005, Pages 75-88

Transglutaminase and cell-survival signaling

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TRANSGLUTAMINASE 2;

EID: 14544304578     PISSN: 00796263     EISSN: None     Source Type: Book Series    
DOI: 10.1159/000084234     Document Type: Review
Times cited : (1)

References (100)
  • 2
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L, Graham RM: Transglutaminases: Crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 2003;4:140-156.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 3
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg CS, Birckbichler PJ, Rice RH: Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues. FASEB J 1991;5:3071-3077.
    • (1991) FASEB J , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 4
    • 0028946284 scopus 로고
    • Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: Identification of osteonectin as a major glutaminyl substrate
    • Aeschlimann D, Kaupp O, Paulsson M: Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: Identification of osteonectin as a major glutaminyl substrate. J Cell Biol 1995;129:881-892.
    • (1995) J Cell Biol , vol.129 , pp. 881-892
    • Aeschlimann, D.1    Kaupp, O.2    Paulsson, M.3
  • 5
    • 0037036409 scopus 로고    scopus 로고
    • Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb
    • Boehm JE, Singh U, Combs C, Antonyak MA, Cerione RA: Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb. J Biol Chem 2002;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
  • 6
    • 0022448196 scopus 로고
    • A role for transglutaminase in glucose-stimulated insulin release from the pancreatic beta-cell
    • Bungay PJ, Owen RA, Coutts IC, Griffin M: A role for transglutaminase in glucose-stimulated insulin release from the pancreatic beta-cell. Biochem J 1986;235:269-278.
    • (1986) Biochem J , vol.235 , pp. 269-278
    • Bungay, P.J.1    Owen, R.A.2    Coutts, I.C.3    Griffin, M.4
  • 7
    • 0035469864 scopus 로고    scopus 로고
    • Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin
    • Akimov SS, Belkin AM: Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood 2001;98:1567-1576.
    • (2001) Blood , vol.98 , pp. 1567-1576
    • Akimov, S.S.1    Belkin, A.M.2
  • 8
    • 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
    • Singh US, Pan J, Kao YL, Joshi S, Young KL, Baker KM: Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y Cells. J Biol Chem 2003;278:391-399.
    • (2003) J Biol Chem , vol.278 , pp. 391-399
    • Singh, U.S.1    Pan, J.2    Kao, Y.L.3    Joshi, S.4    Young, K.L.5    Baker, K.M.6
  • 9
    • 0035863525 scopus 로고    scopus 로고
    • Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells
    • Tucholski J, Lesort M, Johnson GV: Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells. Neuroscience 2001;102:481-491.
    • (2001) Neuroscience , vol.102 , pp. 481-491
    • Tucholski, J.1    Lesort, M.2    Johnson, G.V.3
  • 10
    • 0028129461 scopus 로고
    • Transfection of tissue transglutaminase into a highly malignant hamster fibrosarcoma leads to a reduced incidence of primary tumour growth
    • Johnson TS, Knight CR, el-Alaoui S, Mian S, Rees RC, Gentile V, Davies PJ, Griffin M: Transfection of tissue transglutaminase into a highly malignant hamster fibrosarcoma leads to a reduced incidence of primary tumour growth. Oncogene 1994;9:2935-2942.
    • (1994) Oncogene , vol.9 , pp. 2935-2942
    • Johnson, T.S.1    Knight, C.R.2    El-Alaoui, S.3    Mian, S.4    Rees, R.C.5    Gentile, V.6    Davies, P.J.7    Griffin, M.8
  • 14
    • 0028828698 scopus 로고
    • Identification and biochemical characterization of an 80 kilodalton GTP-binding/transglutaminase from rabbit liver nuclei
    • Singh US, Erickson JW, Cerione RA: Identification and biochemical characterization of an 80 kilodalton GTP-binding/transglutaminase from rabbit liver nuclei. Biochemistry 1995;34:15863-15871.
    • (1995) Biochemistry , vol.34 , pp. 15863-15871
    • Singh, U.S.1    Erickson, J.W.2    Cerione, R.A.3
  • 15
    • 0021126301 scopus 로고
    • Polyamine requirements for induction of HL-60 promyelocyte differentiation by leukocyte-conditioned medium and phorbol ester
    • Kufe DW, Griffin J, Mitchell T, Shafman T: Polyamine requirements for induction of HL-60 promyelocyte differentiation by leukocyte-conditioned medium and phorbol ester. Cancer Res 1984;44:4281-4284.
    • (1984) Cancer Res , vol.44 , pp. 4281-4284
    • Kufe, D.W.1    Griffin, J.2    Mitchell, T.3    Shafman, T.4
  • 16
    • 0021270287 scopus 로고
    • Involvement of spermidine in proliferation and differentiation of human promyelocytic leukemia cells
    • Sugiura M, Shafman T, Mitchell T, Griffin J, Kufe D: Involvement of spermidine in proliferation and differentiation of human promyelocytic leukemia cells. Blood 1984;63:1153-1158.
    • (1984) Blood , vol.63 , pp. 1153-1158
    • Sugiura, M.1    Shafman, T.2    Mitchell, T.3    Griffin, J.4    Kufe, D.5
  • 17
    • 0027412509 scopus 로고
    • Transglutaminase-catalyzed incorporation of polyamines into phospholipase A2
    • Tokyo
    • Cordella-Miele E, Miele L, Beninati S, Mukherjee AB: Transglutaminase- catalyzed incorporation of polyamines into phospholipase A2. J Biochem (Tokyo) 1993;113:164-173.
    • (1993) J Biochem , vol.113 , pp. 164-173
    • Cordella-Miele, E.1    Miele, L.2    Beninati, S.3    Mukherjee, A.B.4
  • 19
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • USA
    • Liu S, Cerione RA, Clardy J: Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci USA 2002;99:2743-2747.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 20
  • 22
    • 0032560573 scopus 로고    scopus 로고
    • 'Tissue' transglutaminase in cell death: A downstream or a multifunctional upstream effector?
    • Melino G, Piacentini M: 'Tissue' transglutaminase in cell death: A downstream or a multifunctional upstream effector? FEBS Lett 1998;430:59-63.
    • (1998) FEBS Lett , vol.430 , pp. 59-63
    • Melino, G.1    Piacentini, M.2
  • 23
    • 0030267458 scopus 로고    scopus 로고
    • Rho: Theme and variations
    • Ridley AJ: Rho: Theme and variations. Curr Biol 1996;6:1256-1264.
    • (1996) Curr Biol , vol.6 , pp. 1256-1264
    • Ridley, A.J.1
  • 24
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F: The GTPase superfamily: Conserved structure and molecular mechanism. Nature 1991;349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 25
    • 0029968827 scopus 로고    scopus 로고
    • Rho family GTPases: The cytoskeleton and beyond
    • Symons M: Rho family GTPases: The cytoskeleton and beyond. Trends Biochem Sci 1996;21:178-181.
    • (1996) Trends Biochem Sci , vol.21 , pp. 178-181
    • Symons, M.1
  • 26
    • 0030464444 scopus 로고    scopus 로고
    • How Ras-related proteins talk to their effectors
    • Wittinghofer A, Nassar N: How Ras-related proteins talk to their effectors. Trends Biochem Sci 1996;21:488-491.
    • (1996) Trends Biochem Sci , vol.21 , pp. 488-491
    • Wittinghofer, A.1    Nassar, N.2
  • 28
    • 0029121466 scopus 로고
    • In vitro binding assay for interactions of Rho and Rac with GTPase-activating proteins and effectors
    • Diekmann D, Hall A: In vitro binding assay for interactions of Rho and Rac with GTPase-activating proteins and effectors. Methods Enzymol 1995;256:207-215.
    • (1995) Methods Enzymol , vol.256 , pp. 207-215
    • Diekmann, D.1    Hall, A.2
  • 29
    • 0027470176 scopus 로고
    • Different structural organization of Ras and Rho effector domains
    • Self AJ, Paterson HF, Hall A: Different structural organization of Ras and Rho effector domains. Oncogene 1993;8:655-661.
    • (1993) Oncogene , vol.8 , pp. 655-661
    • Self, A.J.1    Paterson, H.F.2    Hall, A.3
  • 30
    • 0034928738 scopus 로고    scopus 로고
    • The insert region of RhoA is essential for Rho kinase activation and cellular transformation
    • Zong H, Kaibuchi K, Quilliam LA: The insert region of RhoA is essential for Rho kinase activation and cellular transformation. Mol Cell Biol 2001;21:5287-5298.
    • (2001) Mol Cell Biol , vol.21 , pp. 5287-5298
    • Zong, H.1    Kaibuchi, K.2    Quilliam, L.A.3
  • 31
    • 0033427140 scopus 로고    scopus 로고
    • Bacterial toxins inhibiting or activating small GTP-binding proteins
    • Boquet P: Bacterial toxins inhibiting or activating small GTP-binding proteins. Ann NY Acad Sci 1999;886:83-90.
    • (1999) Ann NY Acad Sci , vol.886 , pp. 83-90
    • Boquet, P.1
  • 33
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 a of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • Rittinger K, Walker PA, Eccleston JF, Smerdon SJ, Gamblin SJ: Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 1997;389:758-762.
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 34
    • 0030610785 scopus 로고    scopus 로고
    • Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt G, Sehr P, Wilm M, Selzer J, Mann M, Aktories K: Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 1997;387:725-729.
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 36
    • 0032577588 scopus 로고    scopus 로고
    • The Rho-deamidating cytotoxic necrotizing factor 1 from Escherichia coli possesses transglutaminase activity. Cysteine 866 and histidine 881 are essential for enzyme activity
    • Schmidt G, Selzer J, Lerm M, Aktories K: The Rho-deamidating cytotoxic necrotizing factor 1 from Escherichia coli possesses transglutaminase activity. Cysteine 866 and histidine 881 are essential for enzyme activity. J Biol Chem 1998;273:13669-13674.
    • (1998) J Biol Chem , vol.273 , pp. 13669-13674
    • Schmidt, G.1    Selzer, J.2    Lerm, M.3    Aktories, K.4
  • 37
    • 0035872859 scopus 로고    scopus 로고
    • Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2
    • Singh US, Kunar MT, Kao YL, Baker KM: Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2. EMBO J 2001;20:2413-2423.
    • (2001) EMBO J , vol.20 , pp. 2413-2423
    • Singh, U.S.1    Kunar, M.T.2    Kao, Y.L.3    Baker, K.M.4
  • 39
    • 0029911710 scopus 로고    scopus 로고
    • ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation
    • USA
    • Lechner C, Zahalka MA, Giot JF, Moller NP, Ullrich A: ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation. Proc Natl Acad Sci USA 1996;93:4355-4359.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 4355-4359
    • Lechner, C.1    Zahalka, M.A.2    Giot, J.F.3    Moller, N.P.4    Ullrich, A.5
  • 40
    • 0035281564 scopus 로고    scopus 로고
    • Regulation of gene expression by the small GTPase Rho through the ERK6 (p38 gamma) MAP kinase pathway
    • Marinissen MJ, Chiariello M, Gutkind JS: Regulation of gene expression by the small GTPase Rho through the ERK6 (p38 gamma) MAP kinase pathway. Genes Dev 2001;15:535-553.
    • (2001) Genes Dev , vol.15 , pp. 535-553
    • Marinissen, M.J.1    Chiariello, M.2    Gutkind, J.S.3
  • 42
    • 2942705910 scopus 로고    scopus 로고
    • Crystal structure of transglutaminase 3 in complex with GMP: Structural basis for nucleotide specificity
    • Ahvazi B, Boeshans KM, Steinert PM: Crystal structure of transglutaminase 3 in complex with GMP: Structural basis for nucleotide specificity. J Biol Chem 2004;279:26716-26725.
    • (2004) J Biol Chem , vol.279 , pp. 26716-26725
    • Ahvazi, B.1    Boeshans, K.M.2    Steinert, P.M.3
  • 45
    • 0033617199 scopus 로고    scopus 로고
    • Differential signaling by the thromboxane receptor isoforms via the novel GTP-binding protein, Gh
    • Vezza R, Habib A, FitzGerald GA: Differential signaling by the thromboxane receptor isoforms via the novel GTP-binding protein, Gh. J Biol Chem 1999;274:12774-12779.
    • (1999) J Biol Chem , vol.274 , pp. 12774-12779
    • Vezza, R.1    Habib, A.2    FitzGerald, G.A.3
  • 46
    • 0030004951 scopus 로고    scopus 로고
    • Oxytocin receptor couples to the 80 kDa Gh alpha family protein in human myometrium
    • Baek KJ, Kwon NS, Lee HS, Kim MS, Muralidhar P, Im MJ: Oxytocin receptor couples to the 80 kDa Gh alpha family protein in human myometrium. Biochem J 1996;315:739-744.
    • (1996) Biochem J , vol.315 , pp. 739-744
    • Baek, K.J.1    Kwon, N.S.2    Lee, H.S.3    Kim, M.S.4    Muralidhar, P.5    Im, M.J.6
  • 47
    • 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: Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II. Biochemistry 1999;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
  • 48
    • 0029666275 scopus 로고    scopus 로고
    • Evidence that phospholipase delta1 is the effector in the Gh (transglutaminase II)-mediated signaling
    • Feng JF, Rhee SG, Im MJ: Evidence that phospholipase delta1 is the effector in the Gh (transglutaminase II)-mediated signaling. J Biol Chem 1996;271:16451-16454.
    • (1996) J Biol Chem , vol.271 , pp. 16451-16454
    • Feng, J.F.1    Rhee, S.G.2    Im, M.J.3
  • 49
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov SS, Krylov D, Fleischman LF, Belkin AM: Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J Cell Biol 2000;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
  • 50
    • 1342333140 scopus 로고    scopus 로고
    • Integrins in regulation of tissue development and function
    • Danen EH, Sonnenberg A: Integrins in regulation of tissue development and function. J Pathol 2003;201:632-641.
    • (2003) J Pathol , vol.201 , pp. 632-641
    • Danen, E.H.1    Sonnenberg, A.2
  • 51
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin AM, Akimov SS, Zaritskaya LS, Ratnikov BI, Deryugina EI, Strongin AY: Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J Biol Chem 2001;276:18415-18422.
    • (2001) J Biol Chem , vol.276 , pp. 18415-18422
    • Belkin, A.M.1    Akimov, S.S.2    Zaritskaya, L.S.3    Ratnikov, B.I.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 52
    • 0033544020 scopus 로고    scopus 로고
    • Tissue transglutaminase is an important player at the surface of human endothelial cells: Evidence for its externalization and its colocalization with the beta(1) integrin
    • Gaudry CA, Verderio E, Jones RA, Smith C, Griffin M: Tissue transglutaminase is an important player at the surface of human endothelial cells: Evidence for its externalization and its colocalization with the beta(1) integrin. Exp Cell Res 1999;252:104-113.
    • (1999) Exp Cell Res , vol.252 , pp. 104-113
    • Gaudry, C.A.1    Verderio, E.2    Jones, R.A.3    Smith, C.4    Griffin, M.5
  • 53
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • Lesort M, Attanavanich K, Zhang J, Johnson GV: Distinct nuclear localization and activity of tissue transglutaminase. J Biol Chem 1998;273:11991-11994.
    • (1998) J Biol Chem , vol.273 , pp. 11991-11994
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.4
  • 54
    • 0028231735 scopus 로고
    • Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers
    • Martinez J, Chalupowicz DG, Roush RK, Sheth A, Barsigian C: Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers. Biochemistry 1994;33:2538-2545.
    • (1994) Biochemistry , vol.33 , pp. 2538-2545
    • Martinez, J.1    Chalupowicz, D.G.2    Roush, R.K.3    Sheth, A.4    Barsigian, C.5
  • 55
    • 0024585067 scopus 로고
    • Complexation of fibronectin with tissue transglutaminase
    • Turner PM, Lorand L: Complexation of fibronectin with tissue transglutaminase. Biochemistry 1989;28:628-635.
    • (1989) Biochemistry , vol.28 , pp. 628-635
    • Turner, P.M.1    Lorand, L.2
  • 56
    • 0025885719 scopus 로고
    • Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme
    • Upchurch HF, Conway E, Patterson MK Jr, Maxwell MD: Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme. J Cell Physiol 1991;149:375-382.
    • (1991) J Cell Physiol , vol.149 , pp. 375-382
    • Upchurch, H.F.1    Conway, E.2    Patterson Jr., M.K.3    Maxwell, M.D.4
  • 57
    • 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
    • Singli US, Cerione RA: 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 1996;271: 27292-27298.
    • (1996) J Biol Chem , vol.271 , pp. 27292-27298
    • Singli, U.S.1    Cerione, R.A.2
  • 58
    • 0037177889 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase activity is required for retinoic acid-induced expression and activation of the tissue transglutaminase
    • Antonyak MA, Boehm JE, Cerione RA: Phosphoinositide 3-kinase activity is required for retinoic acid-induced expression and activation of the tissue transglutaminase. J Biol Chem 2002;277:14712-14716.
    • (2002) J Biol Chem , vol.277 , pp. 14712-14716
    • Antonyak, M.A.1    Boehm, J.E.2    Cerione, R.A.3
  • 59
    • 0038521257 scopus 로고    scopus 로고
    • Activation of the Ras-ERK pathway inhibits retinoic acid-induced stimulation of tissue transglutaminase expression in NIH3T3 cells
    • Antonyak MA, McNeill CJ, Wakshlag JJ, Boehm JE, Cerione RA: Activation of the Ras-ERK pathway inhibits retinoic acid-induced stimulation of tissue transglutaminase expression in NIH3T3 cells. J Biol Chem 2003;278:15859-15866.
    • (2003) J Biol Chem , vol.278 , pp. 15859-15866
    • Antonyak, M.A.1    McNeill, C.J.2    Wakshlag, J.J.3    Boehm, J.E.4    Cerione, R.A.5
  • 60
    • 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
    • Mishra S, Murphy LJ: Tissue transglutaminase has intrinsic kinase activity: Identification of transglutaminase 2 as an insulin-like growth factor binding protein-3 kinase. J Biol Chem 2004;279:23863-23868.
    • (2004) J Biol Chem , vol.279 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 61
    • 0035823548 scopus 로고    scopus 로고
    • Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis
    • Antonyak MA, Singh US, Lee DA, Boehm JE, Combs C, Zgola MM, Page RL, Cerione RA: Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis. J Biol Chem 2001;276:33582-33587.
    • (2001) J Biol Chem , vol.276 , pp. 33582-33587
    • Antonyak, M.A.1    Singh, U.S.2    Lee, D.A.3    Boehm, J.E.4    Combs, C.5    Zgola, M.M.6    Page, R.L.7    Cerione, R.A.8
  • 62
    • 1542335670 scopus 로고    scopus 로고
    • Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death
    • Milakovic T, Tucholski J, McCoy E, Johnson GV: Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death. J Biol Chem 2004;279:8715-8722.
    • (2004) J Biol Chem , vol.279 , pp. 8715-8722
    • Milakovic, T.1    Tucholski, J.2    McCoy, E.3    Johnson, G.V.4
  • 65
    • 0024418120 scopus 로고
    • The essential role of hypusine in eukaryotic translation initiation factor 4D (eIF-4D). Purification of eIF-4D and its precursors and comparison of their activities
    • Park MH: The essential role of hypusine in eukaryotic translation initiation factor 4D (eIF-4D). Purification of eIF-4D and its precursors and comparison of their activities. J Biol Chem 1989;264:18531-18535.
    • (1989) J Biol Chem , vol.264 , pp. 18531-18535
    • Park, M.H.1
  • 66
    • 0031890377 scopus 로고    scopus 로고
    • Identification of the eukaryotic initiation factor 5 a as a retinoic acid-stimulated cellular binding partner for tissue transglutaminase II
    • Singh US, Li Q, Cerione R: Identification of the eukaryotic initiation factor 5 A as a retinoic acid-stimulated cellular binding partner for tissue transglutaminase II. J Biol Chem 1998;273:1946-1950.
    • (1998) J Biol Chem , vol.273 , pp. 1946-1950
    • Singh, U.S.1    Li, Q.2    Cerione, R.3
  • 67
    • 0032809085 scopus 로고    scopus 로고
    • Nuclear pore localization and nucleocytoplasmic transport of eIF-5A: Evidence for direct interaction with the export receptor CRM1
    • Rosorius O, Reichart B, Kratzer F, Heger P, Dabauvalle MC, Hauber J: Nuclear pore localization and nucleocytoplasmic transport of eIF-5A: Evidence for direct interaction with the export receptor CRM1. J Cell Sci 1999;112:2369-2380.
    • (1999) J Cell Sci , vol.112 , pp. 2369-2380
    • Rosorius, O.1    Reichart, B.2    Kratzer, F.3    Heger, P.4    Dabauvalle, M.C.5    Hauber, J.6
  • 68
    • 0033060623 scopus 로고    scopus 로고
    • Evidence for specific nucleocytoplasmic transport pathways used by leucine-rich nuclear export signals
    • USA
    • Elfgang C, Rosorius O, Hofer L, Jaksche H, Hauber J, Bevec D: Evidence for specific nucleocytoplasmic transport pathways used by leucine-rich nuclear export signals. Proc Natl Acad Sci USA 1999;96:6229-6234.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 6229-6234
    • Elfgang, C.1    Rosorius, O.2    Hofer, L.3    Jaksche, H.4    Hauber, J.5    Bevec, D.6
  • 69
    • 0030863875 scopus 로고    scopus 로고
    • Interaction of eukaryotic initiation factor 5A with the human immunodeficiency virus type 1 Rev response element RNA and U6 snRNA requires deoxyhypusine or hypusine modification
    • Liu YP, Nemeroff M, Yan YP, Chen KY: Interaction of eukaryotic initiation factor 5A with the human immunodeficiency virus type 1 Rev response element RNA and U6 snRNA requires deoxyhypusine or hypusine modification. Biol Signals 1997;6:166-174.
    • (1997) Biol Signals , vol.6 , pp. 166-174
    • Liu, Y.P.1    Nemeroff, M.2    Yan, Y.P.3    Chen, K.Y.4
  • 70
    • 0035951793 scopus 로고    scopus 로고
    • Hypusine is required for a sequence-specific interaction of eukaryotic initiation factor 5A with postsystematic evolution of ligands by exponential enrichment RNA
    • Xu A, Chen KY: Hypusine is required for a sequence-specific interaction of eukaryotic initiation factor 5A with postsystematic evolution of ligands by exponential enrichment RNA. J Biol Chem 2001;276:2555-2561.
    • (2001) J Biol Chem , vol.276 , pp. 2555-2561
    • Xu, A.1    Chen, K.Y.2
  • 71
    • 0034027295 scopus 로고    scopus 로고
    • Retinoic acid negatively regulates neuropeptide Y expression in human neuroblastoma cells
    • Magni P, Beretta E, Scaccianoce E, Motta M: Retinoic acid negatively regulates neuropeptide Y expression in human neuroblastoma cells. Neuropharmacology 2000;39:1628-1636.
    • (2000) Neuropharmacology , vol.39 , pp. 1628-1636
    • Magni, P.1    Beretta, E.2    Scaccianoce, E.3    Motta, M.4
  • 72
    • 0028955591 scopus 로고
    • Identification of a substrate site for transglutaminases on the human protein synthesis initiation factor 5A
    • Beninati S, Nicolini L, Jakus J, Passeggio A, Abbruzzese A: Identification of a substrate site for transglutaminases on the human protein synthesis initiation factor 5A. Biochem J 1995;305(Pt 3):725-728.
    • (1995) Biochem J , vol.305 , Issue.3 PART , pp. 725-728
    • Beninati, S.1    Nicolini, L.2    Jakus, J.3    Passeggio, A.4    Abbruzzese, A.5
  • 74
    • 2442607838 scopus 로고    scopus 로고
    • Cell-type specific activation of intracellular transglutaminase 2 by oxidative stress or UV 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: Cell-type specific activation of intracellular transglutaminase 2 by oxidative stress or UV irradiation: Implications of transglutaminase 2 in age-related cataractogenesis. J Biol Chem 2004;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
  • 75
    • 1942487316 scopus 로고    scopus 로고
    • Excitotoxin-induced changes in transglutaminase during differentiation of cerebellar granule cells
    • Caccamo D, Curro M, Cusumano G, Crisafulli G, Lentile R: Excitotoxin-induced changes in transglutaminase during differentiation of cerebellar granule cells. Amino Acids 2004;26:197-201.
    • (2004) Amino Acids , vol.26 , pp. 197-201
    • Caccamo, D.1    Curro, M.2    Cusumano, G.3    Crisafulli, G.4    Lentile, R.5
  • 76
    • 0037049234 scopus 로고    scopus 로고
    • NMDA-evoked excitotoxicity increases tissue transglutaminase in cerebellar granule cells
    • Lentile R, Caccamo D, Macaione V, Torre V, Macaione S: NMDA-evoked excitotoxicity increases tissue transglutaminase in cerebellar granule cells. Neuroscience 2002;115:723-729.
    • (2002) Neuroscience , vol.115 , pp. 723-729
    • Lentile, R.1    Caccamo, D.2    Macaione, V.3    Torre, V.4    Macaione, S.5
  • 77
    • 0032866851 scopus 로고    scopus 로고
    • Tissue transglutaminase: An enzyme with a split personality
    • Chen JS, Mehta K: Tissue transglutaminase: An enzyme with a split personality. Int J Biochem Cell Biol 1999;31:817-836.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 817-836
    • Chen, J.S.1    Mehta, K.2
  • 78
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin M, Casadio R, Bergamini CM: Transglutaminases: Nature's biological glues. Biochem J 2002;368:377-396.
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 80
    • 0025293021 scopus 로고
    • Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes
    • George MD, Vollberg TM, Floyd EE, Stein JP, Jetten AM: Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes. J Biol Chem 1990;265:11098-11104.
    • (1990) J Biol Chem , vol.265 , pp. 11098-11104
    • George, M.D.1    Vollberg, T.M.2    Floyd, E.E.3    Stein, J.P.4    Jetten, A.M.5
  • 81
    • 0035403504 scopus 로고    scopus 로고
    • Interleukin-1 induces pro-mineralizing activity of cartilage tissue transglutaminase and factor XIIIa
    • Johnson K, Hashimoto S, Lotz M, Pritzker K, Terkeltaub R: Interleukin-1 induces pro-mineralizing activity of cartilage tissue transglutaminase and factor XIIIa. Am J Pathol 2001;159:149-163.
    • (2001) Am J Pathol , vol.159 , pp. 149-163
    • Johnson, K.1    Hashimoto, S.2    Lotz, M.3    Pritzker, K.4    Terkeltaub, R.5
  • 83
    • 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
    • Ritter SJ, Davies PJ: 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 1998;273:12798-12806.
    • (1998) J Biol Chem , vol.273 , pp. 12798-12806
    • Ritter, S.J.1    Davies, P.J.2
  • 84
    • 0021827570 scopus 로고
    • Retinoic acid-induced expression of tissue transglutaminase in human promyelocytic leukemia (HL-60) cells
    • Davies PJ, Murtaugh MP, Moore WT Jr, Johnson GS, Lucas D: Retinoic acid-induced expression of tissue transglutaminase in human promyelocytic leukemia (HL-60) cells. J Biol Chem 1985;260:5166-5174.
    • (1985) J Biol Chem , vol.260 , pp. 5166-5174
    • Davies, P.J.1    Murtaugh, M.P.2    Moore Jr., W.T.3    Johnson, G.S.4    Lucas, D.5
  • 85
    • 0033865893 scopus 로고    scopus 로고
    • The role of retinoic acid receptors in neurite outgrowth from different populations of embryonic mouse dorsal root ganglia
    • Corcoran J, Shroot B, Pizzey J, Maden M: The role of retinoic acid receptors in neurite outgrowth from different populations of embryonic mouse dorsal root ganglia. J Cell Sci 2000;113(Pt 14):2567-2574.
    • (2000) J Cell Sci , vol.113 , Issue.14 PART , pp. 2567-2574
    • Corcoran, J.1    Shroot, B.2    Pizzey, J.3    Maden, M.4
  • 86
  • 87
    • 0032604220 scopus 로고    scopus 로고
    • Retinoids in nonmammalian embryos
    • Maden M: Retinoids in nonmammalian embryos. Methods Mol Biol 1999;97:491-509.
    • (1999) Methods Mol Biol , vol.97 , pp. 491-509
    • Maden, M.1
  • 88
    • 17144466005 scopus 로고    scopus 로고
    • Regulation of retinoic acid signaling in the embryonic nervous system: A master differentiation factor
    • McCaffery P, Drager UC: Regulation of retinoic acid signaling in the embryonic nervous system: A master differentiation factor. Cytokine Growth Factor Rev 2000;11:233-249.
    • (2000) Cytokine Growth Factor Rev , vol.11 , pp. 233-249
    • McCaffery, P.1    Drager, U.C.2
  • 89
    • 0028168007 scopus 로고
    • Genetic analysis of RXR alpha developmental function: Convergence of RXR and RAR signaling pathways in heart and eye morphogenesis
    • Kastner P, Grondona JM, Mark M, Gansmuller A, LeMeur M, Decimo D, Vonesch JL, Dolle P, Chambon P: Genetic analysis of RXR alpha developmental function: Convergence of RXR and RAR signaling pathways in heart and eye morphogenesis. Cell 1994;78:987-1003.
    • (1994) Cell , vol.78 , pp. 987-1003
    • Kastner, P.1    Grondona, J.M.2    Mark, M.3    Gansmuller, A.4    LeMeur, M.5    Decimo, D.6    Vonesch, J.L.7    Dolle, P.8    Chambon, P.9
  • 90
    • 0036832158 scopus 로고    scopus 로고
    • Retinoid signalling in the development of the central nervous system
    • Maden M: Retinoid signalling in the development of the central nervous system. Nat Rev Neurosci 2002;3:843-853.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 843-853
    • Maden, M.1
  • 91
    • 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
    • Nagy L, Saydak M, Shipley N, Lu S, Basilion JP, Yan ZH, Syka P, Chandraratna RA, Stein JP, Heyman RA, Davies PJ: 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 1996;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
  • 92
    • 0030863635 scopus 로고    scopus 로고
    • Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis
    • Oliverio S, Amendola A, Di Sano F, Farrace MG, Fesus L, Nemes Z, Piredda L, Spinedi A, Piacentini M: Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis. Mol Cell Biol 1997;17:6040-6048.
    • (1997) Mol Cell Biol , vol.17 , pp. 6040-6048
    • Oliverio, S.1    Amendola, A.2    Di Sano, F.3    Farrace, M.G.4    Fesus, L.5    Nemes, Z.6    Piredda, L.7    Spinedi, A.8    Piacentini, M.9
  • 94
    • 2442676613 scopus 로고    scopus 로고
    • Tissue transglutaminase triggers oligomerization and activation of dual leucine zipper-bearing kinase in calphostin C-treated cells to facilitate apoptosis
    • Robitaille K, Daviau A, Tucholski J, Johnson GV, Rancourt C, Blouin R: Tissue transglutaminase triggers oligomerization and activation of dual leucine zipper-bearing kinase in calphostin C-treated cells to facilitate apoptosis. Cell Death Differ 2004;11:542-549.
    • (2004) Cell Death Differ , vol.11 , pp. 542-549
    • Robitaille, K.1    Daviau, A.2    Tucholski, J.3    Johnson, G.V.4    Rancourt, C.5    Blouin, R.6
  • 95
    • 0031893826 scopus 로고    scopus 로고
    • Modulation of the in situ activity of tissue transglutaminase by calcium and GTP
    • Zhang J, Lesort M, Guttmarm RP, Johnson GV: Modulation of the in situ activity of tissue transglutaminase by calcium and GTP. J Biol Chem 1998;273:2288-2295.
    • (1998) J Biol Chem , vol.273 , pp. 2288-2295
    • Zhang, J.1    Lesort, M.2    Guttmarm, R.P.3    Johnson, G.V.4
  • 96
    • 0037101970 scopus 로고    scopus 로고
    • Function and regulation of CREB family transcription factors in the nervous system
    • Lonze BE, Ginty DD: Function and regulation of CREB family transcription factors in the nervous system. Neuron 2002;35:605-623.
    • (2002) Neuron , vol.35 , pp. 605-623
    • Lonze, B.E.1    Ginty, D.D.2
  • 97
    • 0037171782 scopus 로고    scopus 로고
    • Apoptosis, axonal growth defects, and degeneration of peripheral neurons in mice lacking CREB
    • Lonze BE, Riccio A, Cohen S, Ginty DD: Apoptosis, axonal growth defects, and degeneration of peripheral neurons in mice lacking CREB. Neuron 2002;34:371-385.
    • (2002) Neuron , vol.34 , pp. 371-385
    • Lonze, B.E.1    Riccio, A.2    Cohen, S.3    Ginty, D.D.4
  • 98
    • 0034722057 scopus 로고    scopus 로고
    • Stabilization of neuntes in cerebellar granule cells by transglutaminase activity: Identification of midkine and galectin-3 as substrates
    • Mahoney SA, Wilkinson M, Smith S, Haynes LW: Stabilization of neuntes in cerebellar granule cells by transglutaminase activity: Identification of midkine and galectin-3 as substrates. Neuroscience 2000;101:141-155.
    • (2000) Neuroscience , vol.101 , pp. 141-155
    • Mahoney, S.A.1    Wilkinson, M.2    Smith, S.3    Haynes, L.W.4
  • 99
    • 4644336256 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease
    • Andringa G, Lam KY, Chegary M, Wang X, Chase TN, Bennett MC: Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease. FASEB J, 2004;18:932-934.
    • (2004) FASEB J , vol.18 , pp. 932-934
    • Andringa, G.1    Lam, K.Y.2    Chegary, M.3    Wang, X.4    Chase, T.N.5    Bennett, M.C.6
  • 100
    • 0034990512 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells
    • Chun W, Lesort M, Tucholski J, Faber PW, MacDonald ME, Ross CA, Johnson GV: Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells. Neurobiol Dis 2001;8:391-404.
    • (2001) Neurobiol Dis , vol.8 , pp. 391-404
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Faber, P.W.4    MacDonald, M.E.5    Ross, C.A.6    Johnson, G.V.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.