메뉴 건너뛰기




Volumn 15, Issue 9, 2008, Pages 969-978

Identification of Chemical Inhibitors to Human Tissue Transglutaminase by Screening Existing Drug Libraries

Author keywords

CELLBIO; CHEMBIO

Indexed keywords

BLOOD CLOTTING FACTOR 13A; CALCIUM; ENZYME INHIBITOR; GUANOSINE TRIPHOSPHATE; NAPHTHOQUINONE; OCTOXINOL; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TISSUE TRANSGLUTAMINASE 2, HUMAN; TYRPHOSTIN;

EID: 51649127246     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2008.07.015     Document Type: Article
Times cited : (58)

References (56)
  • 1
    • 0141755338 scopus 로고    scopus 로고
    • Epidermal growth factor receptor is a common mediator of quinone-induced signaling leading to phosphorylation of connexin-43: role of glutathione and tyrosine phosphatases
    • Abdelmohsen K., Gerber P.A., von Montfort C., Sies H., and Klotz L.O. Epidermal growth factor receptor is a common mediator of quinone-induced signaling leading to phosphorylation of connexin-43: role of glutathione and tyrosine phosphatases. J. Biol. Chem. 278 (2003) 38360-38367
    • (2003) J. Biol. Chem. , vol.278 , pp. 38360-38367
    • Abdelmohsen, K.1    Gerber, P.A.2    von Montfort, C.3    Sies, H.4    Klotz, L.O.5
  • 2
    • 3042758862 scopus 로고    scopus 로고
    • Signaling effects of menadione: from tyrosine phosphatase inactivation to connexin phosphorylation
    • Abdelmohsen K., Patak P., Von Montfort C., Melchheier I., Sies H., and Klotz L.O. Signaling effects of menadione: from tyrosine phosphatase inactivation to connexin phosphorylation. Methods Enzymol. 378 (2004) 258-272
    • (2004) Methods Enzymol. , vol.378 , pp. 258-272
    • Abdelmohsen, K.1    Patak, P.2    Von Montfort, C.3    Melchheier, I.4    Sies, H.5    Klotz, L.O.6
  • 3
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • Achyuthan K.E., and Greenberg C.S. Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. J. Biol. Chem. 262 (1987) 1901-1906
    • (1987) J. Biol. Chem. , vol.262 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 4
    • 4644336256 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease
    • Andringa G., Lam K.Y., Chegary M., Wang X., Chase T.N., and Bennett M.C. Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease. FASEB J. 18 (2004) 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
  • 5
    • 4744351463 scopus 로고    scopus 로고
    • Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells
    • Antonyak M.A., Miller A.M., Jansen J.M., Boehm J.E., Balkman C.E., Wakshlag J.J., Page R.L., and Cerione R.A. Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells. J. Biol. Chem. 279 (2004) 41461-41467
    • (2004) J. Biol. Chem. , vol.279 , pp. 41461-41467
    • Antonyak, M.A.1    Miller, A.M.2    Jansen, J.M.3    Boehm, J.E.4    Balkman, C.E.5    Wakshlag, J.J.6    Page, R.L.7    Cerione, R.A.8
  • 6
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M., Mitra S., Schweitzer E.S., Segal M.R., and Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (2004) 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 7
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: an update
    • Bain J., McLauchlan H., Elliott M., and Cohen P. The specificities of protein kinase inhibitors: an update. Biochem. J. 371 (2003) 199-204
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 9
    • 0041570280 scopus 로고    scopus 로고
    • Kinetic analysis of the action of tissue transglutaminase on peptide and protein substrates
    • Case A., and Stein R.L. Kinetic analysis of the action of tissue transglutaminase on peptide and protein substrates. Biochemistry 42 (2003) 9466-9481
    • (2003) Biochemistry , vol.42 , pp. 9466-9481
    • Case, A.1    Stein, R.L.2
  • 10
    • 33846601817 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor
    • Case A., and Stein R.L. Kinetic analysis of the interaction of tissue transglutaminase with a nonpeptidic slow-binding inhibitor. Biochemistry 46 (2007) 1106-1115
    • (2007) Biochemistry , vol.46 , pp. 1106-1115
    • Case, A.1    Stein, R.L.2
  • 11
    • 34547770279 scopus 로고    scopus 로고
    • New uses for old drugs
    • Chong C.R., and Sullivan Jr. D.J. New uses for old drugs. Nature 448 (2007) 645-646
    • (2007) Nature , vol.448 , pp. 645-646
    • Chong, C.R.1    Sullivan Jr., D.J.2
  • 12
    • 33750735045 scopus 로고    scopus 로고
    • Importance of Ca(2+)-dependent transamidation activity in the protection afforded by tissue transglutaminase against doxorubicin-induced apoptosis
    • Datta S., Antonyak M.A., and Cerione R.A. Importance of Ca(2+)-dependent transamidation activity in the protection afforded by tissue transglutaminase against doxorubicin-induced apoptosis. Biochemistry 45 (2006) 13163-13174
    • (2006) Biochemistry , vol.45 , pp. 13163-13174
    • Datta, S.1    Antonyak, M.A.2    Cerione, R.A.3
  • 13
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., and Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351 (2000) 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 15
    • 0026325285 scopus 로고
    • Rapid uptake of tyrphostin into A431 human epidermoid cells is followed by delayed inhibition of epidermal growth factor (EGF)-stimulated EGF receptor tyrosine kinase activity
    • Faaland C.A., Mermelstein F.H., Hayashi J., and Laskin J.D. Rapid uptake of tyrphostin into A431 human epidermoid cells is followed by delayed inhibition of epidermal growth factor (EGF)-stimulated EGF receptor tyrosine kinase activity. Mol. Cell. Biol. 11 (1991) 2697-2703
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2697-2703
    • Faaland, C.A.1    Mermelstein, F.H.2    Hayashi, J.3    Laskin, J.D.4
  • 16
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation
    • Folk J.E. Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Adv. Enzymol. Relat. Areas Mol. Biol. 54 (1983) 1-56
    • (1983) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 17
    • 0026338017 scopus 로고
    • Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg C.S., Birckbichler P.J., and Rice R.H. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J. 5 (1991) 3071-3077
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 20
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj M.V., Becher M.W., Springer J.E., Chabas D., Youssef S., Pedotti R., Mitchell D., and Steinman L. Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat. Med. 8 (2002) 143-149
    • (2002) Nat. Med. , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8
  • 21
    • 0036735403 scopus 로고    scopus 로고
    • 2-Methyl-1,4-naphthoquinone, vitamin K(3), decreases gap-junctional intercellular communication via activation of the epidermal growth factor receptor/extracellular signal-regulated kinase cascade
    • Klotz L.O., Patak P., Ale-Agha N., Buchczyk D.P., Abdelmohsen K., Gerber P.A., von Montfort C., and Sies H. 2-Methyl-1,4-naphthoquinone, vitamin K(3), decreases gap-junctional intercellular communication via activation of the epidermal growth factor receptor/extracellular signal-regulated kinase cascade. Cancer Res. 62 (2002) 4922-4928
    • (2002) Cancer Res. , vol.62 , pp. 4922-4928
    • Klotz, L.O.1    Patak, P.2    Ale-Agha, N.3    Buchczyk, D.P.4    Abdelmohsen, K.5    Gerber, P.A.6    von Montfort, C.7    Sies, H.8
  • 22
    • 13544252480 scopus 로고    scopus 로고
    • Covalent blocking of fibril formation and aggregation of intracellular amyloidgenic proteins by transglutaminase-catalyzed intramolecular cross-linking
    • Konno T., Morii T., Hirata A., Sato S., Oiki S., and Ikura K. Covalent blocking of fibril formation and aggregation of intracellular amyloidgenic proteins by transglutaminase-catalyzed intramolecular cross-linking. Biochemistry 44 (2005) 2072-2079
    • (2005) Biochemistry , vol.44 , pp. 2072-2079
    • Konno, T.1    Morii, T.2    Hirata, A.3    Sato, S.4    Oiki, S.5    Ikura, K.6
  • 23
    • 0028138287 scopus 로고
    • Carboxyl-terminal truncation of recombinant factor XIII A-chains. Characterization of minimum structural requirement for transglutaminase activity
    • Lai T.S., Achyuthan K.E., Santiago M.A., and Greenberg G.S. Carboxyl-terminal truncation of recombinant factor XIII A-chains. Characterization of minimum structural requirement for transglutaminase activity. J. Biol. Chem. 269 (1994) 24596-24601
    • (1994) J. Biol. Chem. , vol.269 , pp. 24596-24601
    • Lai, T.S.1    Achyuthan, K.E.2    Santiago, M.A.3    Greenberg, G.S.4
  • 24
    • 0031890194 scopus 로고    scopus 로고
    • Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP
    • Lai T.S., Slaughter T.F., Peoples K.A., Hettasch J.M., and Greenberg C.S. Regulation of human tissue transglutaminase function by magnesium-nucleotide complexes. Identification of distinct binding sites for Mg-GTP and Mg-ATP. J. Biol. Chem. 273 (1998) 1776-1781
    • (1998) J. Biol. Chem. , vol.273 , pp. 1776-1781
    • Lai, T.S.1    Slaughter, T.F.2    Peoples, K.A.3    Hettasch, J.M.4    Greenberg, C.S.5
  • 25
    • 1442348416 scopus 로고    scopus 로고
    • Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats
    • Lai T.S., Tucker T., Burke J.R., Strittmatter W.J., and Greenberg C.S. Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats. J. Neurochem. 88 (2004) 1253-1260
    • (2004) J. Neurochem. , vol.88 , pp. 1253-1260
    • Lai, T.S.1    Tucker, T.2    Burke, J.R.3    Strittmatter, W.J.4    Greenberg, C.S.5
  • 26
    • 0042919084 scopus 로고    scopus 로고
    • The anticancer effects of vitamin K
    • Lamson D.W., and Plaza S.M. The anticancer effects of vitamin K. Altern. Med. Rev. 8 (2003) 303-318
    • (2003) Altern. Med. Rev. , vol.8 , pp. 303-318
    • Lamson, D.W.1    Plaza, S.M.2
  • 27
    • 0041809012 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B inhibition: opportunities and challenges
    • Liu G. Protein tyrosine phosphatase 1B inhibition: opportunities and challenges. Curr. Med. Chem. 10 (2003) 1407-1421
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1407-1421
    • Liu, G.1
  • 28
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • Liu S., Cerione R.A., and Clardy J. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 2743-2747
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 29
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., and Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4 (2003) 140-156
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 30
    • 1542327277 scopus 로고    scopus 로고
    • Inhibitors of JAKs/STATs and the kinases: a possible new cluster of drugs
    • Luo C., and Laaja P. Inhibitors of JAKs/STATs and the kinases: a possible new cluster of drugs. Drug Discov. Today 9 (2004) 268-275
    • (2004) Drug Discov. Today , vol.9 , pp. 268-275
    • Luo, C.1    Laaja, P.2
  • 31
    • 39749124295 scopus 로고    scopus 로고
    • Type 2 transglutaminase in neurodegenerative diseases: the mitochondrial connection
    • Malorni W., Farrace M.G., Rodolfo C., and Piacentini M. Type 2 transglutaminase in neurodegenerative diseases: the mitochondrial connection. Curr. Pharm. Des. 14 (2008) 278-288
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 278-288
    • Malorni, W.1    Farrace, M.G.2    Rodolfo, C.3    Piacentini, M.4
  • 33
    • 0035720628 scopus 로고    scopus 로고
    • Fluorescence approaches to study G protein mechanisms
    • McEwen D.P., Gee K.R., Kang H.C., and Neubig R.R. Fluorescence approaches to study G protein mechanisms. Methods Enzymol. 344 (2002) 403-420
    • (2002) Methods Enzymol. , vol.344 , pp. 403-420
    • McEwen, D.P.1    Gee, K.R.2    Kang, H.C.3    Neubig, R.R.4
  • 35
    • 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., and Murphy L.J. Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. J. Biol. Chem. 279 (2004) 23863-23868
    • (2004) J. Biol. Chem. , vol.279 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 36
    • 51649099917 scopus 로고    scopus 로고
    • Mishra, S., and Murphy, L.J. (2004b). Transglutaminase has intrinsic kinase activity. United States Patent 7090971.
    • Mishra, S., and Murphy, L.J. (2004b). Transglutaminase has intrinsic kinase activity. United States Patent 7090971.
  • 37
    • 28444488402 scopus 로고    scopus 로고
    • The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity
    • Mishra S., and Murphy L.J. The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity. Biochem. Biophys. Res. Commun. 339 (2006) 726-730
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 726-730
    • Mishra, S.1    Murphy, L.J.2
  • 38
    • 34147106950 scopus 로고    scopus 로고
    • Transglutaminase is linked to neurodegenerative diseases
    • Muma N.A. Transglutaminase is linked to neurodegenerative diseases. J. Neuropathol. Exp. Neurol. 66 (2007) 258-263
    • (2007) J. Neuropathol. Exp. Neurol. , vol.66 , pp. 258-263
    • Muma, N.A.1
  • 39
    • 0032718477 scopus 로고    scopus 로고
    • Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP
    • Murthy S.N., Lomasney J.W., Mak E.C., and Lorand L. Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 11815-11819
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11815-11819
    • Murthy, S.N.1    Lomasney, J.W.2    Mak, E.C.3    Lorand, L.4
  • 41
    • 0028176166 scopus 로고
    • Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka H., Perez D.M., Baek K.J., Das T., Husain A., Misono K., Im M.J., and Graham R.M. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 264 (1994) 1593-1596
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 42
    • 0031048034 scopus 로고    scopus 로고
    • Epidermal growth factor receptor signaling cascade as target for tyrphostin (RG 50864) in epithelial cells. Paradoxical effects on mitogen-activated protein kinase kinase and mitogen-activated protein kinase activities
    • Nowak F., Jacquemin-Sablon A., and Pierre J. Epidermal growth factor receptor signaling cascade as target for tyrphostin (RG 50864) in epithelial cells. Paradoxical effects on mitogen-activated protein kinase kinase and mitogen-activated protein kinase activities. Biochem. Pharmacol. 53 (1997) 287-298
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 287-298
    • Nowak, F.1    Jacquemin-Sablon, A.2    Pierre, J.3
  • 43
    • 0028291204 scopus 로고
    • Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules
    • Pedersen L.C., Yee V.C., Bishop P.D., Le Trong I., Teller D.C., and Stenkamp R.E. Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Protein Sci. 3 (1994) 1131-1135
    • (1994) Protein Sci. , vol.3 , pp. 1131-1135
    • Pedersen, L.C.1    Yee, V.C.2    Bishop, P.D.3    Le Trong, I.4    Teller, D.C.5    Stenkamp, R.E.6
  • 44
    • 18044369361 scopus 로고    scopus 로고
    • Novel hydroxyl naphthoquinones with potent Cdc25 antagonizing and growth inhibitory properties
    • Peyregne V.P., Kar S., Ham S.W., Wang M., Wang Z., and Carr B.I. Novel hydroxyl naphthoquinones with potent Cdc25 antagonizing and growth inhibitory properties. Mol. Cancer Ther. 4 (2005) 595-602
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 595-602
    • Peyregne, V.P.1    Kar, S.2    Ham, S.W.3    Wang, M.4    Wang, Z.5    Carr, B.I.6
  • 45
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas D.M., Strop P., Brunger A.T., and Khosla C. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 5 (2007) e327
    • (2007) PLoS Biol. , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 46
    • 33846322227 scopus 로고    scopus 로고
    • Protein transduction domain-mediated delivery of QBP1 suppresses polyglutamine-induced neurodegeneration in vivo
    • Popiel H.A., Nagai Y., Fujikake N., and Toda T. Protein transduction domain-mediated delivery of QBP1 suppresses polyglutamine-induced neurodegeneration in vivo. Mol. Ther. 15 (2007) 303-309
    • (2007) Mol. Ther. , vol.15 , pp. 303-309
    • Popiel, H.A.1    Nagai, Y.2    Fujikake, N.3    Toda, T.4
  • 48
    • 0026660488 scopus 로고
    • A microtiter plate transglutaminase assay utilizing 5-(biotinamido)pentylamine as substrate
    • Slaughter T.F., Achyuthan K.E., Lai T.S., and Greenberg C.S. A microtiter plate transglutaminase assay utilizing 5-(biotinamido)pentylamine as substrate. Anal. Biochem. 205 (1992) 166-171
    • (1992) Anal. Biochem. , vol.205 , pp. 166-171
    • Slaughter, T.F.1    Achyuthan, K.E.2    Lai, T.S.3    Greenberg, C.S.4
  • 49
    • 0035920212 scopus 로고    scopus 로고
    • Potentiation of insulin-related signal transduction by a novel protein-tyrosine phosphatase inhibitor, Et-3,4-dephostatin, on cultured 3T3-L1 adipocytes
    • Suzuki T., Hiroki A., Watanabe T., Yamashita T., Takei I., and Umezawa K. Potentiation of insulin-related signal transduction by a novel protein-tyrosine phosphatase inhibitor, Et-3,4-dephostatin, on cultured 3T3-L1 adipocytes. J. Biol. Chem. 276 (2001) 27511-27518
    • (2001) J. Biol. Chem. , vol.276 , pp. 27511-27518
    • Suzuki, T.1    Hiroki, A.2    Watanabe, T.3    Yamashita, T.4    Takei, I.5    Umezawa, K.6
  • 50
  • 51
    • 0032744527 scopus 로고    scopus 로고
    • Tau is modified by tissue transglutaminase in situ: possible functional and metabolic effects of polyamination
    • Tucholski J., Kuret J., and Johnson G.V. Tau is modified by tissue transglutaminase in situ: possible functional and metabolic effects of polyamination. J. Neurochem. 73 (1999) 1871-1880
    • (1999) J. Neurochem. , vol.73 , pp. 1871-1880
    • Tucholski, J.1    Kuret, J.2    Johnson, G.V.3
  • 53
    • 0037205484 scopus 로고    scopus 로고
    • Identification of epidermal growth factor receptor as a target of Cdc25A protein phosphatase
    • Wang Z., Wang M., Lazo J.S., and Carr B.I. Identification of epidermal growth factor receptor as a target of Cdc25A protein phosphatase. J. Biol. Chem. 277 (2002) 19470-19475
    • (2002) J. Biol. Chem. , vol.277 , pp. 19470-19475
    • Wang, Z.1    Wang, M.2    Lazo, J.S.3    Carr, B.I.4
  • 56
    • 0027936113 scopus 로고
    • Inhibition of GTP-utilizing enzymes by tyrphostins
    • Wolbring G., Hollenberg M.D., and Schnetkamp P.P. Inhibition of GTP-utilizing enzymes by tyrphostins. J. Biol. Chem. 269 (1994) 22470-22472
    • (1994) J. Biol. Chem. , vol.269 , pp. 22470-22472
    • Wolbring, G.1    Hollenberg, M.D.2    Schnetkamp, P.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.