메뉴 건너뛰기




Volumn 15, Issue 5, 2010, Pages 478-487

A profiling platform for the characterization of transglutaminase 2 (TG2) inhibitors

Author keywords

Huntingtons disease; Mechanism of action; TG2; Tissue transglutaminase; Transamidation; Transglutaminase 2 inhibition

Indexed keywords

CYSTAMINE; CYSTEINE; ENZYME INHIBITOR; GUANINE NUCLEOTIDE; GUANOSINE TRIPHOSPHATE; HYDRAZIDE; HYDRAZIDE DERIVATIVE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2 INHIBITOR; PUTRESCINE; UNCLASSIFIED DRUG;

EID: 77953627403     PISSN: 10870571     EISSN: 1552454X     Source Type: Journal    
DOI: 10.1177/1087057110366035     Document Type: Article
Times cited : (67)

References (31)
  • 1
    • 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
  • 2
    • 0025010874 scopus 로고
    • A novel guanine nucleotide-binding protein coupled to the α1-adrenergic receptor
    • Im M-J., Riek P., Graham, R.: A novel guanine nucleotide-binding protein coupled to the α1-adrenergic receptor. J Biol Chem 1990 ; 265: 18952-18960.
    • (1990) J Biol Chem , vol.265 , pp. 18952-18960
    • Im, M.-J.1    Riek, P.2    Graham, R.3
  • 3
    • 0031890194 scopus 로고    scopus 로고
    • Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes
    • Lai T-S., Slaughter T., Peoples K., Hettasch J., Greenburg C.: Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. J Biol Chem 1998 ; 273: 1776-1781.
    • (1998) J Biol Chem , vol.273 , pp. 1776-1781
    • Lai, T.-S.1    Slaughter, T.2    Peoples, K.3    Hettasch, J.4    Greenburg, C.5
  • 4
    • 0042068233 scopus 로고    scopus 로고
    • A novel function of tissue-type transglutaminase: Protein disulfide isomerase
    • Hasegawa G., Suwa M., Ichikawa Y., Ohtsuka T., Kumagai S., Kikuchi M.,, et al. A novel function of tissue-type transglutaminase: protein disulfide isomerase. Biochem J 2003 ; 373: 793-803.
    • (2003) Biochem J , vol.373 , pp. 793-803
    • Hasegawa, G.1    Suwa, M.2    Ichikawa, Y.3    Ohtsuka, T.4    Kumagai, S.5    Kikuchi, M.6
  • 5
    • 3242861077 scopus 로고    scopus 로고
    • Localization of transglutaminase in hippocampal neurons: Implications for Alzheimers disease
    • Appelt DM, Kopen GC, Boyne LJ, Balin BJ: Localization of transglutaminase in hippocampal neurons: implications for Alzheimers disease. J Histochem Cytochem 1996 ; 44: 1421-1427.
    • (1996) J Histochem Cytochem , vol.44 , pp. 1421-1427
    • Appelt, D.M.1    Kopen, G.C.2    Boyne, L.J.3    Balin, B.J.4
  • 6
    • 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
  • 7
    • 33748957546 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes
    • Mastroberardino PG, Farrace M., Viti I., Pavone F., Fimia G., Melino G.,, et al. Tissue transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes. Biochimica et Biophysica Acta 2006 ; 1757: 1357-1365.
    • (2006) Biochimica et Biophysica Acta , vol.1757 , pp. 1357-1365
    • Mastroberardino, P.G.1    Farrace, M.2    Viti, I.3    Pavone, F.4    Fimia, G.5    Melino, G.6
  • 10
    • 34447286702 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitors and their therapeutic role in disease states
    • Siegel M., Khosla C.: Transglutaminase 2 inhibitors and their therapeutic role in disease states. Pharmacol Ther 2007 ; 115: 232-245.
    • (2007) Pharmacol Ther , vol.115 , pp. 232-245
    • Siegel, M.1    Khosla, C.2
  • 12
    • 0036715380 scopus 로고    scopus 로고
    • Tissue transglutaminase ablation reduces neuronal death and prolongs survival in a mouse model of Huntingtons disease
    • Mastroberardino PG, Iannicola C., Nardacci R., Bernassola F., DeLaurenzi V., Melino G.,, et al. Tissue transglutaminase ablation reduces neuronal death and prolongs survival in a mouse model of Huntingtons disease. Cell Death Differ 2002 ; 9: 873-880.
    • (2002) Cell Death Differ , vol.9 , pp. 873-880
    • Mastroberardino, P.G.1    Iannicola, C.2    Nardacci, R.3    Bernassola, F.4    Delaurenzi, V.5    Melino, G.6
  • 13
    • 13244279859 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to disease progression in the R6/2 Huntingtons disease mouse model via aggregate-independent mechanisms
    • Bailey C., Johnson G.: Tissue transglutaminase contributes to disease progression in the R6/2 Huntingtons disease mouse model via aggregate- independent mechanisms. J Neurochem 2005 ; 92: 83-92.
    • (2005) J Neurochem , vol.92 , pp. 83-92
    • Bailey, C.1    Johnson, G.2
  • 15
    • 8044259620 scopus 로고    scopus 로고
    • ETRO working party on factor XIII questionnaire on congenital FXIII deficiency in Europe: Status and perspective
    • Seitz R., Duckert F., Lopaciuk S., Muszbek L., Rodeghiero F., Seligsohn U.: ETRO working party on factor XIII questionnaire on congenital FXIII deficiency in Europe: status and perspective. Semin Thromb Hemost 1996 ; 22: 415-425.
    • (1996) Semin Thromb Hemost , vol.22 , pp. 415-425
    • Seitz, R.1    Duckert, F.2    Lopaciuk, S.3    Muszbek, L.4    Rodeghiero, F.5    Seligsohn, U.6
  • 17
    • 15044349470 scopus 로고    scopus 로고
    • Structure-activity relationship study of novel tissue transglutaminase inhibitors
    • DOI 10.1016/j.bmcl.2005.02.005
    • Duval E., Case A., Stein R., Cuny G.: Structure-activity relationship study of novel tissue transglutaminase inhibitors. Bioorg Med Chem Lett 2005 ; 15: 1885-1889. (Pubitemid 40380753)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.7 , pp. 1885-1889
    • Duval, E.1    Case, A.2    Stein, R.L.3    Cuny, G.D.4
  • 18
    • 51649127246 scopus 로고    scopus 로고
    • Identification of chemical inhibitors to human tissue transglutaminase by screening existing drug libraries
    • Lai T-S., Liu Y., Tucker T., Daniel K., Sane D., Toone E.,, et al. Identification of chemical inhibitors to human tissue transglutaminase by screening existing drug libraries. Chem Biol 2008 ; 15: 969-978.
    • (2008) Chem Biol , vol.15 , pp. 969-978
    • Lai, T.-S.1    Liu, Y.2    Tucker, T.3    Daniel, K.4    Sane, D.5    Toone, E.6
  • 20
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas D., Strop P., Brunger A., Khosla C.: Transglutaminase 2 undergoes a large conformational change upon activation. PLOS Biol 2007 ; 5: 2788-2796.
    • (2007) PLOS Biol , vol.5 , pp. 2788-2796
    • Pinkas, D.1    Strop, P.2    Brunger, A.3    Khosla, C.4
  • 21
    • 0034951866 scopus 로고    scopus 로고
    • Evaluation of novel dipeptide-bound α,β-unsaturated amides and epoxides as irreversible inhibitors of guinea pig liver transglutaminase
    • Marrano C., deMacedo P., Keillor J.: Evaluation of novel dipeptide-bound α,β-unsaturated amides and epoxides as irreversible inhibitors of guinea pig liver transglutaminase. Bioorg Med Chem 2001 ; 9: 1923-1928.
    • (2001) Bioorg Med Chem , vol.9 , pp. 1923-1928
    • Marrano, C.1    Demacedo, P.2    Keillor, J.3
  • 22
    • 33846601817 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor
    • Case A., Stein R.: Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor. Biochemistry 2007 ; 46: 1106-1115.
    • (2007) Biochemistry , vol.46 , pp. 1106-1115
    • Case, A.1    Stein, R.2
  • 24
    • 34250174215 scopus 로고    scopus 로고
    • Type 2 transglutaminase differentially modulates striatal cell death in the presence of wild type or mutant huntingtin
    • Ruan Q., Quintanilla RA, Johnson GV: Type 2 transglutaminase differentially modulates striatal cell death in the presence of wild type or mutant huntingtin. J Neurochem 2007 ; 102: 25-36.
    • (2007) J Neurochem , vol.102 , pp. 25-36
    • Ruan, Q.1    Quintanilla, R.A.2    Johnson, G.V.3
  • 25
    • 33751217716 scopus 로고    scopus 로고
    • The role of the informatics framework in early lead discovery
    • Fay N.: The role of the informatics framework in early lead discovery. Drug Discov Today 2006 ; 11: 1075-1084.
    • (2006) Drug Discov Today , vol.11 , pp. 1075-1084
    • Fay, N.1
  • 27
    • 3042531037 scopus 로고    scopus 로고
    • Ghα/tissue transglutaminase 2: An emerging G protein in signal transduction
    • Mhaouty-Kodja S.: Ghα/tissue transglutaminase 2: an emerging G protein in signal transduction. Biol Cell 2004 ; 96: 363-367.
    • (2004) Biol Cell , vol.96 , pp. 363-367
    • Mhaouty-Kodja, S.1
  • 28
    • 0034608860 scopus 로고    scopus 로고
    • Nucleotide binding by the erythrocyte transglutaminase/Gh protein, probed with fluorescent analogs of GTP and GDP
    • Murthy SNP, Lorand, L.: Nucleotide binding by the erythrocyte transglutaminase/Gh protein, probed with fluorescent analogs of GTP and GDP. Proc Natl Acad Sci USA 2000 ; 97: 7744-7747.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7744-7747
    • Murthy, S.N.P.1    Lorand, L.2
  • 29
    • 0033215059 scopus 로고    scopus 로고
    • A continuous spectrophotometric linked enzyme assay for transglutaminase activity
    • Day N., Keillor J.: A continuous spectrophotometric linked enzyme assay for transglutaminase activity. Anal Biochem 1999 ; 274: 141-144.
    • (1999) Anal Biochem , vol.274 , pp. 141-144
    • Day, N.1    Keillor, J.2
  • 31
    • 0028227785 scopus 로고
    • Selective putrescine export is regulated by insulin and ornithine in Reuber H35 hepatoma cells
    • Hawel L., Tjandrawinata R., Byus C.: Selective putrescine export is regulated by insulin and ornithine in Reuber H35 hepatoma cells. Biochimica et Biophysica Acta 1994 ; 1222: 15-26.
    • (1994) Biochimica et Biophysica Acta , vol.1222 , pp. 15-26
    • Hawel, L.1    Tjandrawinata, R.2    Byus, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.