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Volumn 46, Issue 1, 2007, Pages 1-36

Potential role of N-myristoyltransferase in cancer

Author keywords

Cancer; Heat shock cognate protein 70; Inhibitors; Lipid modification; Myristoylation; Myristoyltransferase

Indexed keywords

PROTEIN N MYRISTOYLTRANSFERASE;

EID: 33751298031     PISSN: 01637827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plipres.2006.05.002     Document Type: Review
Times cited : (90)

References (286)
  • 2
    • 0030592517 scopus 로고    scopus 로고
    • Lessons from hereditary colorectal cancer
    • Kinzler K.W., and Vogelstein B. Lessons from hereditary colorectal cancer. Cell 87 (1996) 159-170
    • (1996) Cell , vol.87 , pp. 159-170
    • Kinzler, K.W.1    Vogelstein, B.2
  • 3
    • 0033516320 scopus 로고    scopus 로고
    • Colorectal cancer: molecules and populations
    • Potter J.D. Colorectal cancer: molecules and populations. J Natl Cancer Inst 91 (1999) 916-932
    • (1999) J Natl Cancer Inst , vol.91 , pp. 916-932
    • Potter, J.D.1
  • 4
    • 0034907056 scopus 로고    scopus 로고
    • What we could do now: molecular pathology of colorectal cancer
    • Houlston R.S. What we could do now: molecular pathology of colorectal cancer. J Clin Pathol Mol Pathol 54 (2001) 206-214
    • (2001) J Clin Pathol Mol Pathol , vol.54 , pp. 206-214
    • Houlston, R.S.1
  • 5
    • 0034994538 scopus 로고    scopus 로고
    • Conventional catatonic and novel therapeutic concepts in colorectal cancer
    • Midgley R., and Kerr D. Conventional catatonic and novel therapeutic concepts in colorectal cancer. Expert Opin Invest Drugs 10 (2001) 1011-1019
    • (2001) Expert Opin Invest Drugs , vol.10 , pp. 1011-1019
    • Midgley, R.1    Kerr, D.2
  • 9
    • 0036781702 scopus 로고    scopus 로고
    • Myristoyl-CoA: protein N-myristoyltransferase: a novel molecular approach for cancer therapy
    • Selvakumar P., Pasha M.K., Ashakumary L., Dimmock J.R., and Sharma R.K. Myristoyl-CoA: protein N-myristoyltransferase: a novel molecular approach for cancer therapy. Int J Mol Med 10 (2002) 493-500
    • (2002) Int J Mol Med , vol.10 , pp. 493-500
    • Selvakumar, P.1    Pasha, M.K.2    Ashakumary, L.3    Dimmock, J.R.4    Sharma, R.K.5
  • 10
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • Farazi T.A., Waksman G., and Gordon J.I. The biology and enzymology of protein N-myristoylation. J Biol Chem 276 (2001) 39501-39504
    • (2001) J Biol Chem , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 11
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys Acta 1451 (1999) 1-16
    • (1999) Biochim. Biophys Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 12
    • 0030948184 scopus 로고    scopus 로고
    • Myristoylation
    • Boutin J.A. Myristoylation. Cell Signal 9 (1997) 15-35
    • (1997) Cell Signal , vol.9 , pp. 15-35
    • Boutin, J.A.1
  • 14
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey P.J. Protein lipidation in cell signaling. Science 268 (1995) 221-225
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 16
    • 0020201569 scopus 로고
    • 2-terminal blocking group of the catalytic subunit of cyclic AMP dependent protein kinase from bovine cardiac muscle
    • 2-terminal blocking group of the catalytic subunit of cyclic AMP dependent protein kinase from bovine cardiac muscle. Proc Natl Acad Sci USA 79 (1982) 6128-6131
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6128-6131
    • Carr, S.A.1    Biemann, K.2    Shozo, S.3    Pamelee, D.C.4    Titani, K.5
  • 17
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha J., Weiler S., Oh K.J., Wei M.C., and Korsmeyer S.J. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 290 (2000) 1761-1765
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 18
    • 0031818329 scopus 로고    scopus 로고
    • Ultrastructural localization of interferon-inducible double-stranded RNA-activated enzymes in human cells
    • Besse S., Rebouillat D., Marie I., Puvion-Dutilleul F., and Hovanessian A.G. Ultrastructural localization of interferon-inducible double-stranded RNA-activated enzymes in human cells. Exp Cell Res 239 (1998) 379-392
    • (1998) Exp Cell Res , vol.239 , pp. 379-392
    • Besse, S.1    Rebouillat, D.2    Marie, I.3    Puvion-Dutilleul, F.4    Hovanessian, A.G.5
  • 19
    • 0036290648 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence
    • Maurer-Stroh S., Eisenhaber B., and Eisenhaber F. N-terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence. J Mol Biol 317 (2002) 541-557
    • (2002) J Mol Biol , vol.317 , pp. 541-557
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 20
    • 0037440462 scopus 로고    scopus 로고
    • N-terminal modifications of the 19S regulatory particle subunits of the yeast proteasome
    • Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., and Hirano H. N-terminal modifications of the 19S regulatory particle subunits of the yeast proteasome. Arch Biochem Biophys 409 (2003) 341-348
    • (2003) Arch Biochem Biophys , vol.409 , pp. 341-348
    • Kimura, Y.1    Saeki, Y.2    Yokosawa, H.3    Polevoda, B.4    Sherman, F.5    Hirano, H.6
  • 21
    • 0034652143 scopus 로고    scopus 로고
    • Subcellular localization of proteasomes and their regulatory complexes in mammalian cells
    • Brooks P., Fuertes G., Murray R.Z., Bose S., Knecht E., Rechsteiner M.C., et al. Subcellular localization of proteasomes and their regulatory complexes in mammalian cells. Biochem J 346 (2000) 155-161
    • (2000) Biochem J , vol.346 , pp. 155-161
    • Brooks, P.1    Fuertes, G.2    Murray, R.Z.3    Bose, S.4    Knecht, E.5    Rechsteiner, M.C.6
  • 22
    • 0037109664 scopus 로고    scopus 로고
    • Rapsyn escorts the nicotinic acetylcholine receptor along the exocytic pathway via association with lipid rafts
    • Marchand S., Devillers-Thiery A., Pons S., Changeux J.P., and Cartaud J. Rapsyn escorts the nicotinic acetylcholine receptor along the exocytic pathway via association with lipid rafts. J Neurosci 22 (2002) 8891-8901
    • (2002) J Neurosci , vol.22 , pp. 8891-8901
    • Marchand, S.1    Devillers-Thiery, A.2    Pons, S.3    Changeux, J.P.4    Cartaud, J.5
  • 23
    • 0036151625 scopus 로고    scopus 로고
    • Conserved domains of the Nullo protein required for cell-surface localization and formation of adherens junctions
    • Hunter C., Sung P., Schejter E.D., and Wieschaus E. Conserved domains of the Nullo protein required for cell-surface localization and formation of adherens junctions. Mol Biol Cell 13 (2002) 146-157
    • (2002) Mol Biol Cell , vol.13 , pp. 146-157
    • Hunter, C.1    Sung, P.2    Schejter, E.D.3    Wieschaus, E.4
  • 24
    • 0033592709 scopus 로고    scopus 로고
    • WT p53 dependent expression of a membrane-associated isoform of adenylate kinase
    • Collavin L., Lazarevic D., Utrera R., Marzinotto S., Monte M., and Schneider C. WT p53 dependent expression of a membrane-associated isoform of adenylate kinase. Oncogene 18 (1999) 5879-5888
    • (1999) Oncogene , vol.18 , pp. 5879-5888
    • Collavin, L.1    Lazarevic, D.2    Utrera, R.3    Marzinotto, S.4    Monte, M.5    Schneider, C.6
  • 25
    • 0034700364 scopus 로고    scopus 로고
    • Molecular aspects of the cellular activities of ADP-ribosylation factors
    • Randazzo P.A., Nie Z., Miura K., and Hsu V.W. Molecular aspects of the cellular activities of ADP-ribosylation factors. Sci STKE 2000 (2000) RE1
    • (2000) Sci STKE , vol.2000
    • Randazzo, P.A.1    Nie, Z.2    Miura, K.3    Hsu, V.W.4
  • 26
    • 0036903977 scopus 로고    scopus 로고
    • A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1
    • Lin C.Y., Li C.C., Huang P.H., and Lee F.J. A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1. J Cell Sci 115 (2002) 4433-4445
    • (2002) J Cell Sci , vol.115 , pp. 4433-4445
    • Lin, C.Y.1    Li, C.C.2    Huang, P.H.3    Lee, F.J.4
  • 27
    • 0033578731 scopus 로고    scopus 로고
    • Characterization of the targeting, binding, and phosphorylation site domains of an A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog that are encoded by a single gene
    • Rossi E.A., Li Z., Feng H., and Rubin C.S. Characterization of the targeting, binding, and phosphorylation site domains of an A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog that are encoded by a single gene. J Biol Chem 274 (1999) 27201-27210
    • (1999) J Biol Chem , vol.274 , pp. 27201-27210
    • Rossi, E.A.1    Li, Z.2    Feng, H.3    Rubin, C.S.4
  • 28
    • 2642705036 scopus 로고    scopus 로고
    • A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive membrane events
    • Fraser I.D., Tavalin S.J., Lester L.B., Langeberg L.K., Westphal A.M., Dean R.A., et al. A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive membrane events. EMBO J 17 (1998) 2261-2272
    • (1998) EMBO J , vol.17 , pp. 2261-2272
    • Fraser, I.D.1    Tavalin, S.J.2    Lester, L.B.3    Langeberg, L.K.4    Westphal, A.M.5    Dean, R.A.6
  • 29
    • 0032555901 scopus 로고    scopus 로고
    • Annexin XIIIb associates with lipid microdomains to function in apical delivery
    • Lafont F., Lecat S., Verkade P., and Simons K. Annexin XIIIb associates with lipid microdomains to function in apical delivery. J Cell Biol 142 (1998) 1413-1427
    • (1998) J Cell Biol , vol.142 , pp. 1413-1427
    • Lafont, F.1    Lecat, S.2    Verkade, P.3    Simons, K.4
  • 30
    • 0036006051 scopus 로고    scopus 로고
    • An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum
    • Lu S.X., and Hrabak E.M. An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum. Plant Physiol 128 (2002) 1008-1021
    • (2002) Plant Physiol , vol.128 , pp. 1008-1021
    • Lu, S.X.1    Hrabak, E.M.2
  • 31
    • 0034986439 scopus 로고    scopus 로고
    • 2+- and myristoylation-dependent association of calcineurin with phosphatidylserine
    • 2+- and myristoylation-dependent association of calcineurin with phosphatidylserine. J Biochem 129 (2001) 835-841
    • (2001) J Biochem , vol.129 , pp. 835-841
    • Perrino, B.A.1    Martin, B.A.2
  • 32
    • 0032830852 scopus 로고    scopus 로고
    • 2+-binding protein p22 associates with microtubules in an N-myristoylation-dependent manner
    • 2+-binding protein p22 associates with microtubules in an N-myristoylation-dependent manner. Mol Biol Cell 10 (1999) 3473-3488
    • (1999) Mol Biol Cell , vol.10 , pp. 3473-3488
    • Timm, S.1    Titus, B.2    Bernd, K.3    Barroso, M.4
  • 33
    • 0033693383 scopus 로고    scopus 로고
    • A novel N-terminal domain directs membrane localization of mouse testis-specific calpastatin
    • Li S., and Goldberg E. A novel N-terminal domain directs membrane localization of mouse testis-specific calpastatin. Biol Reprod 63 (2000) 1594-1600
    • (2000) Biol Reprod , vol.63 , pp. 1594-1600
    • Li, S.1    Goldberg, E.2
  • 34
    • 0034695932 scopus 로고    scopus 로고
    • Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation
    • Pepperkok R., Hotz-Wagenblatt A., Konig N., Girod A., Bossemeyer D., and Kinzel V. Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation. J Cell Biol 148 (2000) 715-726
    • (2000) J Cell Biol , vol.148 , pp. 715-726
    • Pepperkok, R.1    Hotz-Wagenblatt, A.2    Konig, N.3    Girod, A.4    Bossemeyer, D.5    Kinzel, V.6
  • 35
    • 13144251141 scopus 로고    scopus 로고
    • Membrane targeting of cGMP-dependent protein kinase is required for cystic fibrosis transmembrane conductance regulator Cl-channel activation
    • Vaandrager A.B., Smolenski A., Tilly B.C., Houtsmuller A.B., Ehlert E.M., Bot A.G., et al. Membrane targeting of cGMP-dependent protein kinase is required for cystic fibrosis transmembrane conductance regulator Cl-channel activation. Proc Natl Acad Sci USA 95 (1998) 1466-1471
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1466-1471
    • Vaandrager, A.B.1    Smolenski, A.2    Tilly, B.C.3    Houtsmuller, A.B.4    Ehlert, E.M.5    Bot, A.G.6
  • 36
    • 0033553908 scopus 로고    scopus 로고
    • A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer's disease presenilin 2 protein
    • Stabler S.M., Ostrowski L.L., Janicki S.M., and Monteiro M.J. A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer's disease presenilin 2 protein. J Cell Biol 145 (1999) 1277-1292
    • (1999) J Cell Biol , vol.145 , pp. 1277-1292
    • Stabler, S.M.1    Ostrowski, L.L.2    Janicki, S.M.3    Monteiro, M.J.4
  • 37
    • 0043240190 scopus 로고    scopus 로고
    • Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen
    • Naik U.P., and Naik M.U. Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen. Blood 102 (2003) 1355-1362
    • (2003) Blood , vol.102 , pp. 1355-1362
    • Naik, U.P.1    Naik, M.U.2
  • 38
    • 0030920365 scopus 로고    scopus 로고
    • The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: a green fluorescent protein study
    • Liu J., Hughes T.E., and Sessa W.C. The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the Golgi region of cells: a green fluorescent protein study. J Cell Biol 137 (1997) 1525-1535
    • (1997) J Cell Biol , vol.137 , pp. 1525-1535
    • Liu, J.1    Hughes, T.E.2    Sessa, W.C.3
  • 39
    • 0033219896 scopus 로고    scopus 로고
    • Targeting and translocation of endothelial nitric oxide synthase
    • Michel T. Targeting and translocation of endothelial nitric oxide synthase. Braz J Med Biol Res 32 (1999) 1361-1366
    • (1999) Braz J Med Biol Res , vol.32 , pp. 1361-1366
    • Michel, T.1
  • 40
    • 0030589483 scopus 로고    scopus 로고
    • Role of N-myristoylation in targeting of band 4.2 (pallidin) in nonerythroid cells
    • Risinger M.A., Korsgren C., and Cohen C.M. Role of N-myristoylation in targeting of band 4.2 (pallidin) in nonerythroid cells. Exp Cell Res 229 (1996) 421-431
    • (1996) Exp Cell Res , vol.229 , pp. 421-431
    • Risinger, M.A.1    Korsgren, C.2    Cohen, C.M.3
  • 41
    • 0037376104 scopus 로고    scopus 로고
    • PACE-1, a novel protein that interacts with the C-terminal domain of ezrin
    • Sullivan A., Uff C.R., Isacke C.M., and Thorne R.F. PACE-1, a novel protein that interacts with the C-terminal domain of ezrin. Exp Cell Res 284 (2003) 224-238
    • (2003) Exp Cell Res , vol.284 , pp. 224-238
    • Sullivan, A.1    Uff, C.R.2    Isacke, C.M.3    Thorne, R.F.4
  • 42
    • 0142057020 scopus 로고    scopus 로고
    • Understanding the functions of plant disease resistance proteins
    • Martin G.B., Bogdanove A.J., and Sessa G. Understanding the functions of plant disease resistance proteins. Annu Rev Plant Biol 54 (2003) 23-61
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 23-61
    • Martin, G.B.1    Bogdanove, A.J.2    Sessa, G.3
  • 43
    • 0033560770 scopus 로고    scopus 로고
    • Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism
    • Godsel L.M., and Engman D.M. Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism. EMBO J 18 (1999) 2057-2065
    • (1999) EMBO J , vol.18 , pp. 2057-2065
    • Godsel, L.M.1    Engman, D.M.2
  • 44
    • 0031007608 scopus 로고    scopus 로고
    • Myristoylated and nonmyristoylated pools of sea urchin sperm flagellar creatine kinase exist side-by-side: myristoylation is necessary for efficient lipid association
    • Quest A.F., Harvey D.J., and McIlhinney R.A. Myristoylated and nonmyristoylated pools of sea urchin sperm flagellar creatine kinase exist side-by-side: myristoylation is necessary for efficient lipid association. Biochemistry 36 (1997) 6993-7002
    • (1997) Biochemistry , vol.36 , pp. 6993-7002
    • Quest, A.F.1    Harvey, D.J.2    McIlhinney, R.A.3
  • 45
    • 2342472611 scopus 로고    scopus 로고
    • Myristoylation of the fus1 protein is required for tumor suppression in human lung cancer cells
    • Uno F., Sasaki J., Nishizaki M., Carboni G., Xu K., Atkinson E.N., et al. Myristoylation of the fus1 protein is required for tumor suppression in human lung cancer cells. Cancer Res. 64 (2004) 2969-2976
    • (2004) Cancer Res. , vol.64 , pp. 2969-2976
    • Uno, F.1    Sasaki, J.2    Nishizaki, M.3    Carboni, G.4    Xu, K.5    Atkinson, E.N.6
  • 46
    • 0026518383 scopus 로고
    • Inhibitory effect of myristoylation on transrepression by FBR (Gag-Fos) protein
    • Kamata N., and Holt J.T. Inhibitory effect of myristoylation on transrepression by FBR (Gag-Fos) protein. Mol Cell Biol 12 (1992) 876-882
    • (1992) Mol Cell Biol , vol.12 , pp. 876-882
    • Kamata, N.1    Holt, J.T.2
  • 47
    • 0023109641 scopus 로고
    • Myristoylation is required for intracellular transport but not for assembly of D-type retrovirus capsids
    • Rhee S.S., and Hunter E. Myristoylation is required for intracellular transport but not for assembly of D-type retrovirus capsids. J Virol 61 (1987) 1045-1053
    • (1987) J Virol , vol.61 , pp. 1045-1053
    • Rhee, S.S.1    Hunter, E.2
  • 48
    • 0020650110 scopus 로고
    • Myristoyl amino-terminal acylation of murine retrovirus proteins: an unusual post-translational proteins modification
    • Henderson L.E., Krutzsch H.C., and Oroszlan S. Myristoyl amino-terminal acylation of murine retrovirus proteins: an unusual post-translational proteins modification. Proc Natl Acad Sci USA 80 (1983) 339-343
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 339-343
    • Henderson, L.E.1    Krutzsch, H.C.2    Oroszlan, S.3
  • 49
    • 0023864765 scopus 로고
    • Poorly expressed endogenous ecotropic provirus of DBA/2 mice encodes a mutant Pr65gag protein that is not myristoylated
    • Copeland N.G., Jenkins N.A., Nexo B., Schultz A.M., Rein A., Mikkelsen T., et al. Poorly expressed endogenous ecotropic provirus of DBA/2 mice encodes a mutant Pr65gag protein that is not myristoylated. J Virol 62 (1988) 479-487
    • (1988) J Virol , vol.62 , pp. 479-487
    • Copeland, N.G.1    Jenkins, N.A.2    Nexo, B.3    Schultz, A.M.4    Rein, A.5    Mikkelsen, T.6
  • 50
    • 0027528948 scopus 로고
    • Identification of proteolytic processing sites within the Gag and Pol polyproteins of feline immunodeficiency virus
    • Elder J.H., Schnolzer M., Hasselkus-Light C.S., Henson M., Lerner D.A., Phillips T.R., et al. Identification of proteolytic processing sites within the Gag and Pol polyproteins of feline immunodeficiency virus. J Virol 67 (1993) 1869-1876
    • (1993) J Virol , vol.67 , pp. 1869-1876
    • Elder, J.H.1    Schnolzer, M.2    Hasselkus-Light, C.S.3    Henson, M.4    Lerner, D.A.5    Phillips, T.R.6
  • 51
    • 0024474480 scopus 로고
    • Chemical characterization of p17gag from human immunodeficiency virus as an N-terminally myristoylated protein
    • Goddard C., Aquino A., Glazer R.I., and Felsted R.L. Chemical characterization of p17gag from human immunodeficiency virus as an N-terminally myristoylated protein. Eur J Biochem 182 (1989) 323-326
    • (1989) Eur J Biochem , vol.182 , pp. 323-326
    • Goddard, C.1    Aquino, A.2    Glazer, R.I.3    Felsted, R.L.4
  • 53
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M., and Ratner L. Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc Natl Acad Sci USA 87 (1990) 523-527
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 54
    • 0026937399 scopus 로고
    • Bacterial expression, purification, and in vitro N-myristoylation of HIV-1 p17gag
    • Burnette B., Kahn R., Glover C.J., and Felsted R.L. Bacterial expression, purification, and in vitro N-myristoylation of HIV-1 p17gag. Protein Expr Purif 3 (1992) 395-402
    • (1992) Protein Expr Purif , vol.3 , pp. 395-402
    • Burnette, B.1    Kahn, R.2    Glover, C.J.3    Felsted, R.L.4
  • 55
    • 0024009127 scopus 로고
    • Anti-myristoylation of gag proteins in human T-cell leukemia and human immunodeficiency viruses with N-myristoyl glycinal diethylacetal
    • Shoji S., Tashiro A., and Kubota Y. Anti-myristoylation of gag proteins in human T-cell leukemia and human immunodeficiency viruses with N-myristoyl glycinal diethylacetal. J Biochem 103 (1988) 747-749
    • (1988) J Biochem , vol.103 , pp. 747-749
    • Shoji, S.1    Tashiro, A.2    Kubota, Y.3
  • 56
    • 0026739681 scopus 로고
    • Myristoylation-dependent membrane targeting and release of the HTLV-I Gag precursor, Pr53gag, in yeast
    • Hayakawa T., Miyazaki T., Misumi Y., Kobayashi M., and Fujisawa Y. Myristoylation-dependent membrane targeting and release of the HTLV-I Gag precursor, Pr53gag, in yeast. Gene 119 (1992) 273-277
    • (1992) Gene , vol.119 , pp. 273-277
    • Hayakawa, T.1    Miyazaki, T.2    Misumi, Y.3    Kobayashi, M.4    Fujisawa, Y.5
  • 57
    • 0022408015 scopus 로고
    • Myristoylation of gag protein in human T-cell leukemia virus type-I and type-II
    • Ootsuyama Y., Shimotohno K., Miwa M., Oroszlan S., and Sugimura T. Myristoylation of gag protein in human T-cell leukemia virus type-I and type-II. Jpn J Cancer Res 76 (1985) 1132-1135
    • (1985) Jpn J Cancer Res , vol.76 , pp. 1132-1135
    • Ootsuyama, Y.1    Shimotohno, K.2    Miwa, M.3    Oroszlan, S.4    Sugimura, T.5
  • 58
    • 0025112947 scopus 로고
    • Structural role of the matrix protein of type D retroviruses in gag polyprotein stability and capsid assembly
    • Rhee S.S., and Hunter E. Structural role of the matrix protein of type D retroviruses in gag polyprotein stability and capsid assembly. J Virol 64 (1990) 4383-4389
    • (1990) J Virol , vol.64 , pp. 4383-4389
    • Rhee, S.S.1    Hunter, E.2
  • 59
    • 0024515364 scopus 로고
    • Unmyristoylated Moloney murine leukemia virus Pr65gag is excluded from virus assembly and maturation events
    • Schultz A.M., and Rein A. Unmyristoylated Moloney murine leukemia virus Pr65gag is excluded from virus assembly and maturation events. J Virol 63 (1989) 2370-2373
    • (1989) J Virol , vol.63 , pp. 2370-2373
    • Schultz, A.M.1    Rein, A.2
  • 61
    • 0028169915 scopus 로고
    • Myristylation of Pr60gag of the murine AIDS-defective virus is required to induce disease and notably for the expansion of its target cells
    • Huang M., and Jolicoeur P. Myristylation of Pr60gag of the murine AIDS-defective virus is required to induce disease and notably for the expansion of its target cells. J Virol 68 (1994) 5648-5655
    • (1994) J Virol , vol.68 , pp. 5648-5655
    • Huang, M.1    Jolicoeur, P.2
  • 62
    • 0027198787 scopus 로고
    • Assembly of the matrix protein of simian immunodeficiency virus into virus-like particles
    • Gonzalez S.A., Affranchino J.L., Gelderblom H.R., and Burny A. Assembly of the matrix protein of simian immunodeficiency virus into virus-like particles. Virology 194 (1993) 548-556
    • (1993) Virology , vol.194 , pp. 548-556
    • Gonzalez, S.A.1    Affranchino, J.L.2    Gelderblom, H.R.3    Burny, A.4
  • 63
    • 0027272237 scopus 로고
    • Inhibition of varicella-zoster virus replication by an inhibitor of protein myristoylation
    • Harper D.R., Gilbert R.L., Blunt C., and McIlhinney R.A. Inhibition of varicella-zoster virus replication by an inhibitor of protein myristoylation. J Gen Virol 74 (1993) 1181-1184
    • (1993) J Gen Virol , vol.74 , pp. 1181-1184
    • Harper, D.R.1    Gilbert, R.L.2    Blunt, C.3    McIlhinney, R.A.4
  • 64
    • 0024453409 scopus 로고
    • Evidence for attachment of fatty acid to varicella-zoster virus glycoproteins and effect of cerulenin on the maturation of varicella-zoster virus glycoproteins
    • Namazue J., Kato T., Okuno T., Shiraki K., and Yamanishi K. Evidence for attachment of fatty acid to varicella-zoster virus glycoproteins and effect of cerulenin on the maturation of varicella-zoster virus glycoproteins. Intervirology 30 (1989) 268-277
    • (1989) Intervirology , vol.30 , pp. 268-277
    • Namazue, J.1    Kato, T.2    Okuno, T.3    Shiraki, K.4    Yamanishi, K.5
  • 65
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr F.A., Puype M., Vandekerckhove J., and Warren G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91 (1997) 253-262
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 66
    • 0034423410 scopus 로고    scopus 로고
    • Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55
    • Kuo A., Zhong C., Lane W.S., and Derynck R. Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55. EMBO J 19 (2000) 6427-6439
    • (2000) EMBO J , vol.19 , pp. 6427-6439
    • Kuo, A.1    Zhong, C.2    Lane, W.S.3    Derynck, R.4
  • 67
    • 0037084502 scopus 로고    scopus 로고
    • Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex
    • Eberle H.B., Serrano R.L., Fullekrug J., Schlosser A., Lehmann W.D., Lottspeich F., et al. Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex. J Cell Sci 115 (2002) 827-838
    • (2002) J Cell Sci , vol.115 , pp. 827-838
    • Eberle, H.B.1    Serrano, R.L.2    Fullekrug, J.3    Schlosser, A.4    Lehmann, W.D.5    Lottspeich, F.6
  • 68
    • 0035952690 scopus 로고    scopus 로고
    • Regulation of G proteins by covalent modification
    • Chen C.A., and Manning D.R. Regulation of G proteins by covalent modification. Oncogene 20 (2001) 1643-1652
    • (2001) Oncogene , vol.20 , pp. 1643-1652
    • Chen, C.A.1    Manning, D.R.2
  • 69
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffett S., Brown D.A., and Linder M.E. Lipid-dependent targeting of G proteins into rafts. J Biol Chem 275 (2000) 2191-2198
    • (2000) J Biol Chem , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 70
    • 0037195270 scopus 로고    scopus 로고
    • Calcium- and myristoyl-dependent properties of guanylate cyclase-activating protein-1 and protein-2
    • Hwang J.Y., and Koch K.W. Calcium- and myristoyl-dependent properties of guanylate cyclase-activating protein-1 and protein-2. Biochemistry 41 (2002) 13021-13028
    • (2002) Biochemistry , vol.41 , pp. 13021-13028
    • Hwang, J.Y.1    Koch, K.W.2
  • 71
    • 0029977873 scopus 로고    scopus 로고
    • Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein
    • Hanakam F., Albrecht R., Eckerskorn C., Matzner M., and Gerisch G. Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein. EMBO J 15 (1996) 2935-2943
    • (1996) EMBO J , vol.15 , pp. 2935-2943
    • Hanakam, F.1    Albrecht, R.2    Eckerskorn, C.3    Matzner, M.4    Gerisch, G.5
  • 73
    • 0025036271 scopus 로고
    • Myristoylation and polylysine-mediated activation of the protein kinase domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10)
    • Chung T.D., Wymer J.P., Kulka M., Smith C.C., and Aurelian L. Myristoylation and polylysine-mediated activation of the protein kinase domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10). Virology 179 (1990) 168-178
    • (1990) Virology , vol.179 , pp. 168-178
    • Chung, T.D.1    Wymer, J.P.2    Kulka, M.3    Smith, C.C.4    Aurelian, L.5
  • 74
    • 0028141708 scopus 로고
    • Igloo, a GAP-43-related gene expressed in the developing nervous system of Drosophila
    • Neel V.A., and Young M.W. Igloo, a GAP-43-related gene expressed in the developing nervous system of Drosophila. Development 120 (1994) 2235-2243
    • (1994) Development , vol.120 , pp. 2235-2243
    • Neel, V.A.1    Young, M.W.2
  • 75
    • 0028822367 scopus 로고
    • Myristoylation of the hepatitis B virus large surface protein is essential for viral infectivity
    • Gripon P., Le Seyec J., Rumin S., and Guguen-Guillouzo C. Myristoylation of the hepatitis B virus large surface protein is essential for viral infectivity. Virology 213 (1995) 292-299
    • (1995) Virology , vol.213 , pp. 292-299
    • Gripon, P.1    Le Seyec, J.2    Rumin, S.3    Guguen-Guillouzo, C.4
  • 76
    • 0027968128 scopus 로고
    • Conditional lethal expression of the vaccinia virus L1R myristoylated protein reveals a role in virion assembly
    • Ravanello M.P., and Hruby D.E. Conditional lethal expression of the vaccinia virus L1R myristoylated protein reveals a role in virion assembly. J Virol 68 (1994) 6401-6410
    • (1994) J Virol , vol.68 , pp. 6401-6410
    • Ravanello, M.P.1    Hruby, D.E.2
  • 77
    • 0027340008 scopus 로고
    • 2-terminal peptide from the vaccinia virus L1R protein directs the myristoylation and virion envelope localization of a heterologous fusion protein
    • 2-terminal peptide from the vaccinia virus L1R protein directs the myristoylation and virion envelope localization of a heterologous fusion protein. J Biol Chem 268 (1993) 7585-7593
    • (1993) J Biol Chem , vol.268 , pp. 7585-7593
    • Ravanello, M.P.1    Franke, C.A.2    Hruby, D.E.3
  • 78
    • 0025202960 scopus 로고
    • Use of a cell-free system to identify the vaccinia virus L1R gene product as the major late myristoylated virion protein M25
    • Franke C.A., Wilson E.M., and Hruby D.E. Use of a cell-free system to identify the vaccinia virus L1R gene product as the major late myristoylated virion protein M25. J Virol 64 (1990) 5988-5996
    • (1990) J Virol , vol.64 , pp. 5988-5996
    • Franke, C.A.1    Wilson, E.M.2    Hruby, D.E.3
  • 79
    • 0025307422 scopus 로고
    • N myristoylation of the spleen necrosis virus matrix protein is required for correct association of the Gag polyprotein with intracellular membranes and for particle formation
    • Weaver T.A., and Panganiban A.T. N myristoylation of the spleen necrosis virus matrix protein is required for correct association of the Gag polyprotein with intracellular membranes and for particle formation. J Virol 64 (1990) 3995-4001
    • (1990) J Virol , vol.64 , pp. 3995-4001
    • Weaver, T.A.1    Panganiban, A.T.2
  • 80
  • 81
    • 0030469993 scopus 로고    scopus 로고
    • A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes
    • Borgese N., Aggujaro D., Carrera P., Pietrini G., and Bassetti M. A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes. J Cell Biol 135 (1996) 1501-1513
    • (1996) J Cell Biol , vol.135 , pp. 1501-1513
    • Borgese, N.1    Aggujaro, D.2    Carrera, P.3    Pietrini, G.4    Bassetti, M.5
  • 82
    • 0026487290 scopus 로고
    • Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction
    • Walker J.E., Arizmendi J.M., Dupuis A., Fearnley I.M., Finel M., Medd S.M., et al. Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction. J Mol Biol 226 (1992) 1051-1072
    • (1992) J Mol Biol , vol.226 , pp. 1051-1072
    • Walker, J.E.1    Arizmendi, J.M.2    Dupuis, A.3    Fearnley, I.M.4    Finel, M.5    Medd, S.M.6
  • 83
    • 0024390790 scopus 로고
    • The HIV-1 Gag precursor Pr55gag synthesized in yeast is myristoylated and targeted to the plasma membrane
    • Jacobs E., Gheysen D., Thines D., Francotte M., and de Wilde M. The HIV-1 Gag precursor Pr55gag synthesized in yeast is myristoylated and targeted to the plasma membrane. Gene 79 (1989) 71-81
    • (1989) Gene , vol.79 , pp. 71-81
    • Jacobs, E.1    Gheysen, D.2    Thines, D.3    Francotte, M.4    de Wilde, M.5
  • 84
  • 85
    • 0026092965 scopus 로고
    • Myristoylation of foot-and-mouth disease virus capsid protein precursors is independent of other viral proteins and occurs in both mammalian and insect cells
    • Belsham G.J., Abrams C.C., King A.M., Roosien J., and Vlak J.M. Myristoylation of foot-and-mouth disease virus capsid protein precursors is independent of other viral proteins and occurs in both mammalian and insect cells. J Gen Virol 72 (1991) 747-751
    • (1991) J Gen Virol , vol.72 , pp. 747-751
    • Belsham, G.J.1    Abrams, C.C.2    King, A.M.3    Roosien, J.4    Vlak, J.M.5
  • 86
    • 0027964371 scopus 로고
    • Protein glycosylation and myristoylation in Chlorella virus PBCV-1 and its antigenic variants
    • Que Q., Li Y., Wang I.N., Lane L.C., Chaney W.G., and Van Etten J.L. Protein glycosylation and myristoylation in Chlorella virus PBCV-1 and its antigenic variants. Virology 203 (1994) 320-327
    • (1994) Virology , vol.203 , pp. 320-327
    • Que, Q.1    Li, Y.2    Wang, I.N.3    Lane, L.C.4    Chaney, W.G.5    Van Etten, J.L.6
  • 87
    • 0034010126 scopus 로고    scopus 로고
    • A novel phosphatidylinositol-phospholipase C of Trypanosoma cruzi that is lipid modified and activated during trypomastigote to amastigote differentiation
    • Furuya T., Kashuba C., Docampo R., and Moreno S.N. A novel phosphatidylinositol-phospholipase C of Trypanosoma cruzi that is lipid modified and activated during trypomastigote to amastigote differentiation. J Biol Chem 275 (2000) 6428-6438
    • (2000) J Biol Chem , vol.275 , pp. 6428-6438
    • Furuya, T.1    Kashuba, C.2    Docampo, R.3    Moreno, S.N.4
  • 88
    • 0026013628 scopus 로고
    • Myristoylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly
    • Macrae D.R., Bruss V., and Ganem D. Myristoylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly. Virology 181 (1991) 359-363
    • (1991) Virology , vol.181 , pp. 359-363
    • Macrae, D.R.1    Bruss, V.2    Ganem, D.3
  • 89
    • 0025864197 scopus 로고
    • Myristoylation is involved in intracellular retention of hepatitis B virus envelope proteins
    • Prange R., Clemen A., and Streeck R.E. Myristoylation is involved in intracellular retention of hepatitis B virus envelope proteins. J Virol 65 (1991) 3919-3923
    • (1991) J Virol , vol.65 , pp. 3919-3923
    • Prange, R.1    Clemen, A.2    Streeck, R.E.3
  • 90
    • 12244260817 scopus 로고    scopus 로고
    • The postsynaptic density and dendritic raft localization of PSD-Zip70, which contains an N-myristoylation sequence and leucine-zipper motifs
    • Konno D., Ko J.A., Usui S., Hori K., Maruoka H., Inui M., et al. The postsynaptic density and dendritic raft localization of PSD-Zip70, which contains an N-myristoylation sequence and leucine-zipper motifs. J Cell Sci 115 (2002) 4695-4706
    • (2002) J Cell Sci , vol.115 , pp. 4695-4706
    • Konno, D.1    Ko, J.A.2    Usui, S.3    Hori, K.4    Maruoka, H.5    Inui, M.6
  • 91
    • 0035801358 scopus 로고    scopus 로고
    • Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana
    • Ueda T., Yamaguchi M., Uchimiya H., and Nakano A. Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana. EMBO J 20 (2001) 4730-4741
    • (2001) EMBO J , vol.20 , pp. 4730-4741
    • Ueda, T.1    Yamaguchi, M.2    Uchimiya, H.3    Nakano, A.4
  • 93
    • 0036758614 scopus 로고    scopus 로고
    • Reversible translocation and activity-dependent localization of the calcium-myristoyl switch protein VILIP-1 to different membrane compartments in living hippocampal neurons
    • Spilker C., Dresbach T., and Braunewell K.H. Reversible translocation and activity-dependent localization of the calcium-myristoyl switch protein VILIP-1 to different membrane compartments in living hippocampal neurons. J Neurosci 22 (2002) 7331-7339
    • (2002) J Neurosci , vol.22 , pp. 7331-7339
    • Spilker, C.1    Dresbach, T.2    Braunewell, K.H.3
  • 94
    • 0038644946 scopus 로고    scopus 로고
    • Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing
    • Lin S.S., Manchester J.K., and Gordon J.I. Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem 278 (2003) 13390-13397
    • (2003) J Biol Chem , vol.278 , pp. 13390-13397
    • Lin, S.S.1    Manchester, J.K.2    Gordon, J.I.3
  • 95
    • 0031657476 scopus 로고    scopus 로고
    • Control of cytoskeletal architecture by the src-suppressed C kinase substrate, SSeCKS
    • Gelman I.H., Lee K., Tombler E., Gordon R., and Lin X. Control of cytoskeletal architecture by the src-suppressed C kinase substrate, SSeCKS. Cell Motil Cytoskeleton 41 (1998) 1-17
    • (1998) Cell Motil Cytoskeleton , vol.41 , pp. 1-17
    • Gelman, I.H.1    Lee, K.2    Tombler, E.3    Gordon, R.4    Lin, X.5
  • 96
    • 0037468612 scopus 로고    scopus 로고
    • C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria
    • Utsumi T., Sakurai N., Nakano K., and Ishisaka R. C-terminal 15 kDa fragment of cytoskeletal actin is posttranslationally N-myristoylated upon caspase-mediated cleavage and targeted to mitochondria. FEBS Lett 539 (2003) 37-44
    • (2003) FEBS Lett , vol.539 , pp. 37-44
    • Utsumi, T.1    Sakurai, N.2    Nakano, K.3    Ishisaka, R.4
  • 98
    • 0036606184 scopus 로고    scopus 로고
    • IgA Fc receptor (FcalphaR) cross-linking recruits tyrosine kinases, phosphoinositide kinases and serine/threonine kinases to glycolipid rafts
    • Lang M.L., Chen Y.W., Shen L., Gao H., Lang G.A., Wade T.K., et al. IgA Fc receptor (FcalphaR) cross-linking recruits tyrosine kinases, phosphoinositide kinases and serine/threonine kinases to glycolipid rafts. Biochem J 364 (2002) 517-525
    • (2002) Biochem J , vol.364 , pp. 517-525
    • Lang, M.L.1    Chen, Y.W.2    Shen, L.3    Gao, H.4    Lang, G.A.5    Wade, T.K.6
  • 99
    • 0024843786 scopus 로고
    • Gene UL11 of herpes simplex virus type 1 encodes a virion protein which is myristoylated
    • MacLean C.A., Clark B., and McGeoch D.J. Gene UL11 of herpes simplex virus type 1 encodes a virion protein which is myristoylated. J Gen Virol 70 (1989) 3147-3157
    • (1989) J Gen Virol , vol.70 , pp. 3147-3157
    • MacLean, C.A.1    Clark, B.2    McGeoch, D.J.3
  • 100
    • 0026551254 scopus 로고
    • The myristoylated virion proteins of herpes simplex virus type 1: investigation of their role in the virus life cycle
    • MacLean C.A., Dolan A., Jamieson F.E., and McGeoch D.J. The myristoylated virion proteins of herpes simplex virus type 1: investigation of their role in the virus life cycle. J Gen Virol 73 (1992) 539-547
    • (1992) J Gen Virol , vol.73 , pp. 539-547
    • MacLean, C.A.1    Dolan, A.2    Jamieson, F.E.3    McGeoch, D.J.4
  • 101
    • 0027470177 scopus 로고
    • Structure, expression and chromosomal mapping of c-akt: relationship to v-akt and its implications
    • Bellacosa A., Franke T.F., Gonzalez-Portal M.E., Datta K., Taguchi T., Gardner J., et al. Structure, expression and chromosomal mapping of c-akt: relationship to v-akt and its implications. Oncogene 8 (1993) 745-754
    • (1993) Oncogene , vol.8 , pp. 745-754
    • Bellacosa, A.1    Franke, T.F.2    Gonzalez-Portal, M.E.3    Datta, K.4    Taguchi, T.5    Gardner, J.6
  • 102
    • 0030917789 scopus 로고    scopus 로고
    • Finkel-Biskis-Reilly mouse osteosarcoma virus v-fos inhibits the cellular response to ionizing radiation in a myristoylation-dependent manner
    • Abbott D.W., and Holt J.T. Finkel-Biskis-Reilly mouse osteosarcoma virus v-fos inhibits the cellular response to ionizing radiation in a myristoylation-dependent manner. J Biol Chem 272 (1997) 14005-14008
    • (1997) J Biol Chem , vol.272 , pp. 14005-14008
    • Abbott, D.W.1    Holt, J.T.2
  • 103
    • 0024483764 scopus 로고
    • Myristoylation of budgerigar fledgling disease virus capsid protein VP2
    • Schmidt M., Muller H., Schmidt M.F., and Rott R. Myristoylation of budgerigar fledgling disease virus capsid protein VP2. J Virol 63 (1989) 429-431
    • (1989) J Virol , vol.63 , pp. 429-431
    • Schmidt, M.1    Muller, H.2    Schmidt, M.F.3    Rott, R.4
  • 105
    • 0027328068 scopus 로고
    • Defect in entry and altered pathogenicity of a polyoma virus mutant blocked in VP2 myristoylation
    • Sahli R., Freund R., Dubensky T., Garcea R., Bronson R., and Benjamin T. Defect in entry and altered pathogenicity of a polyoma virus mutant blocked in VP2 myristoylation. Virology 192 (1993) 142-153
    • (1993) Virology , vol.192 , pp. 142-153
    • Sahli, R.1    Freund, R.2    Dubensky, T.3    Garcea, R.4    Bronson, R.5    Benjamin, T.6
  • 106
    • 0023113683 scopus 로고
    • Myristic acid is coupled to a structural protein of polyoma virus and SV40
    • Streuli C.H., and Griffin B.E. Myristic acid is coupled to a structural protein of polyoma virus and SV40. Nature 326 (1987) 619-622
    • (1987) Nature , vol.326 , pp. 619-622
    • Streuli, C.H.1    Griffin, B.E.2
  • 107
    • 0023198719 scopus 로고
    • Myristoylation of picornavirus capsid protein VP4 and its structural significance
    • Chow M., Newman J.F., Filman D., Hogle J.M., Rowlands D.J., and Brown F. Myristoylation of picornavirus capsid protein VP4 and its structural significance. Nature 327 (1987) 482-486
    • (1987) Nature , vol.327 , pp. 482-486
    • Chow, M.1    Newman, J.F.2    Filman, D.3    Hogle, J.M.4    Rowlands, D.J.5    Brown, F.6
  • 108
    • 0027164245 scopus 로고
    • Analysis of a potential myristoylation site in hepatitis A virus capsid protein VP4
    • Tesar M., Jia X.Y., Summers D.F., and Ehrenfeld E. Analysis of a potential myristoylation site in hepatitis A virus capsid protein VP4. Virology 194 (1993) 616-626
    • (1993) Virology , vol.194 , pp. 616-626
    • Tesar, M.1    Jia, X.Y.2    Summers, D.F.3    Ehrenfeld, E.4
  • 109
    • 0025773025 scopus 로고
    • Myristoylation is important at multiple stages in poliovirus assembly
    • Moscufo N., Simons J., and Chow M. Myristoylation is important at multiple stages in poliovirus assembly. J Virol 65 (1991) 2372-2380
    • (1991) J Virol , vol.65 , pp. 2372-2380
    • Moscufo, N.1    Simons, J.2    Chow, M.3
  • 111
    • 0024470776 scopus 로고
    • Role of myristoylation of poliovirus capsid protein VP4 as determined by site-directed mutagenesis of its N-terminal sequence
    • Marc D., Drugeon G., Haenni A.L., Girard M., and van der Werf S. Role of myristoylation of poliovirus capsid protein VP4 as determined by site-directed mutagenesis of its N-terminal sequence. EMBO J 8 (1989) 2661-2668
    • (1989) EMBO J , vol.8 , pp. 2661-2668
    • Marc, D.1    Drugeon, G.2    Haenni, A.L.3    Girard, M.4    van der Werf, S.5
  • 112
    • 0025082005 scopus 로고
    • Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles
    • Marc D., Masson G., Girard M., and van der Werf S. Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles. J Virol 64 (1990) 4099-4107
    • (1990) J Virol , vol.64 , pp. 4099-4107
    • Marc, D.1    Masson, G.2    Girard, M.3    van der Werf, S.4
  • 113
    • 0027256130 scopus 로고
    • A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole
    • Stack J.H., Herman P.K., Schu P.V., and Emr S.D. A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole. EMBO J 12 (1993) 2195-2204
    • (1993) EMBO J , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 114
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., and Emr S.D. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 3 (2002) 271-282
    • (2002) Dev Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 115
    • 0028936379 scopus 로고
    • The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm
    • Hanakam F., Eckerskorn C., Lottspeich F., Muller-Taubenberger A., Schafer W., and Gerish G. The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm. J Biol Chem 270 (1995) 596-602
    • (1995) J Biol Chem , vol.270 , pp. 596-602
    • Hanakam, F.1    Eckerskorn, C.2    Lottspeich, F.3    Muller-Taubenberger, A.4    Schafer, W.5    Gerish, G.6
  • 116
    • 0023868823 scopus 로고
    • 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase
    • Heuckeroth R.O., Towler D.A., Adams S.P., Glaser L., and Gordon J.I. 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase. J Biol Chem 263 (1988) 2127-2133
    • (1988) J Biol Chem , vol.263 , pp. 2127-2133
    • Heuckeroth, R.O.1    Towler, D.A.2    Adams, S.P.3    Glaser, L.4    Gordon, J.I.5
  • 117
    • 0026767886 scopus 로고
    • The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli
    • Wiegand R.C., Carr C., Minnerly J.C., Pauley A.M., Carron C.P., Langner C.A., et al. The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli. J Biol Chem 267 (1992) 8591-8598
    • (1992) J Biol Chem , vol.267 , pp. 8591-8598
    • Wiegand, R.C.1    Carr, C.2    Minnerly, J.C.3    Pauley, A.M.4    Carron, C.P.5    Langner, C.A.6
  • 118
    • 0028000667 scopus 로고
    • Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans
    • Lodge J.K., Johnson R.L., Weinberg R.A., and Gordon J.I. Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans. J Biol Chem 269 (1994) 2996-3009
    • (1994) J Biol Chem , vol.269 , pp. 2996-3009
    • Lodge, J.K.1    Johnson, R.L.2    Weinberg, R.A.3    Gordon, J.I.4
  • 119
    • 0023818374 scopus 로고
    • src. Identification of a myristoyl-CoA:glycylpeptide N-myristoyltransferase in rat tissues
    • src. Identification of a myristoyl-CoA:glycylpeptide N-myristoyltransferase in rat tissues. Biochem J 250 (1988) 485-491
    • (1988) Biochem J , vol.250 , pp. 485-491
    • Glover, C.J.1    Goddard, C.2    Felsted, R.L.3
  • 120
    • 0026649910 scopus 로고
    • Demonstration of multiple forms of bovine brain myristoyl CoA:protein N-myristoyltransferase
    • King M.J., and Sharma R.K. Demonstration of multiple forms of bovine brain myristoyl CoA:protein N-myristoyltransferase. Mol Cell Biochem 133 (1992) 77-81
    • (1992) Mol Cell Biochem , vol.133 , pp. 77-81
    • King, M.J.1    Sharma, R.K.2
  • 121
    • 0030175053 scopus 로고    scopus 로고
    • Overexpression of human N-myristoyltransferase utilizing a T7 polymerase gene expression system
    • Raju R.V., Datla R.S., and Sharma R.K. Overexpression of human N-myristoyltransferase utilizing a T7 polymerase gene expression system. Prot Exp Pur 7 (1996) 431-437
    • (1996) Prot Exp Pur , vol.7 , pp. 431-437
    • Raju, R.V.1    Datla, R.S.2    Sharma, R.K.3
  • 122
    • 0032524623 scopus 로고    scopus 로고
    • Genetic and biochemical studies establish that the fungicidal effect of a fully depeptidized inhibitor of Cryptococcus neoformans myristoyl-CoA:protein N-myristoyltransferase (NMT) is NMT-dependent
    • Lodge J.K., Jackson-Machelski E., Higgins M., McWherter C.A., Sikorski J.A., Devadas B., et al. Genetic and biochemical studies establish that the fungicidal effect of a fully depeptidized inhibitor of Cryptococcus neoformans myristoyl-CoA:protein N-myristoyltransferase (NMT) is NMT-dependent. J Biol Chem 273 (1998) 12482-12491
    • (1998) J Biol Chem , vol.273 , pp. 12482-12491
    • Lodge, J.K.1    Jackson-Machelski, E.2    Higgins, M.3    McWherter, C.A.4    Sikorski, J.A.5    Devadas, B.6
  • 123
    • 0031045971 scopus 로고    scopus 로고
    • Sequence and expression of Drosophila myristoyl-CoA: protein N-myristoyl transferase: evidence for proteolytic processing and membrane localisation
    • Ntwasa M., Egerton M., and Gay N.J. Sequence and expression of Drosophila myristoyl-CoA: protein N-myristoyl transferase: evidence for proteolytic processing and membrane localisation. J Cell Sci 110 (1997) 149-156
    • (1997) J Cell Sci , vol.110 , pp. 149-156
    • Ntwasa, M.1    Egerton, M.2    Gay, N.J.3
  • 124
    • 0028362006 scopus 로고
    • Purification and properties of bovine spleen N-myristoyl-CoA protein:N-myristoyltransferase
    • Raju R.V., Kalra J., and Sharma R.K. Purification and properties of bovine spleen N-myristoyl-CoA protein:N-myristoyltransferase. J Biol Chem 269 (1994) 12080-12083
    • (1994) J Biol Chem , vol.269 , pp. 12080-12083
    • Raju, R.V.1    Kalra, J.2    Sharma, R.K.3
  • 125
    • 0031543496 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of bovine spleen myristoyl CoA:protein N-myristoyltransferase
    • Raju R.V., Anderson J.W., Datla R.S., and Sharma R.K. Molecular cloning and biochemical characterization of bovine spleen myristoyl CoA:protein N-myristoyltransferase. Arch Biochem Biophys 348 (1997) 134-142
    • (1997) Arch Biochem Biophys , vol.348 , pp. 134-142
    • Raju, R.V.1    Anderson, J.W.2    Datla, R.S.3    Sharma, R.K.4
  • 127
    • 0034737580 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization, and biochemical characterization of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis thaliana
    • Qi Q., Rajala R.V., Anderson W., Jiang C., Rozwadowski K., Selvaraj G., et al. Molecular cloning, genomic organization, and biochemical characterization of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis thaliana. J Biol Chem 275 (2000) 9673-9683
    • (2000) J Biol Chem , vol.275 , pp. 9673-9683
    • Qi, Q.1    Rajala, R.V.2    Anderson, W.3    Jiang, C.4    Rozwadowski, K.5    Selvaraj, G.6
  • 128
    • 15444381259 scopus 로고    scopus 로고
    • Molecular characterization of a gene encoding N-myristoyl transferase (NMT) from Triticum aestivum (bread wheat)
    • Dumonceaux T., Rajala R.V., Sharma R., Selvaraj G., and Datla R. Molecular characterization of a gene encoding N-myristoyl transferase (NMT) from Triticum aestivum (bread wheat). Genome 47 (2004) 1036-1042
    • (2004) Genome , vol.47 , pp. 1036-1042
    • Dumonceaux, T.1    Rajala, R.V.2    Sharma, R.3    Selvaraj, G.4    Datla, R.5
  • 129
    • 1842452641 scopus 로고    scopus 로고
    • Myristoyl-CoA:protein N-myristoyltransferases: isoform identification and gene expression in retina
    • Rundle D.R., Rajala R.V., Alvarez R.A., and Anderson R.E. Myristoyl-CoA:protein N-myristoyltransferases: isoform identification and gene expression in retina. Mol Vis 10 (2004) 177-185
    • (2004) Mol Vis , vol.10 , pp. 177-185
    • Rundle, D.R.1    Rajala, R.V.2    Alvarez, R.A.3    Anderson, R.E.4
  • 130
    • 0035996358 scopus 로고    scopus 로고
    • Characterization of Type I and Type II myristoyl-CoA:protein N-myristoyltransferases with the Acyl-CoAs found on heterogeneously acylated retinal proteins
    • Rundle D.R., Rajala R.V., and Anderson R.E. Characterization of Type I and Type II myristoyl-CoA:protein N-myristoyltransferases with the Acyl-CoAs found on heterogeneously acylated retinal proteins. Exp Eye Res 75 (2002) 87-97
    • (2002) Exp Eye Res , vol.75 , pp. 87-97
    • Rundle, D.R.1    Rajala, R.V.2    Anderson, R.E.3
  • 131
    • 33751299699 scopus 로고    scopus 로고
    • Selvakumar P, Lakshmikuttyamma A, Sharma RK. Characterization of bovine testis N-myristoyltransferase 2 [in preparation].
  • 132
    • 33646264311 scopus 로고    scopus 로고
    • Identification and characterization of recombinant and native rat myristoyl-CoA: protein N-myristoyltransferases
    • Rioux V., Beauchamp E., Pedrono F., Daval S., Molle D., Catheline D., et al. Identification and characterization of recombinant and native rat myristoyl-CoA: protein N-myristoyltransferases. Mol Cell Biochem 286 (2006) 161-170
    • (2006) Mol Cell Biochem , vol.286 , pp. 161-170
    • Rioux, V.1    Beauchamp, E.2    Pedrono, F.3    Daval, S.4    Molle, D.5    Catheline, D.6
  • 133
    • 0032549571 scopus 로고    scopus 로고
    • A second mammalian N-myristoyltransferase
    • Giang D.K., and Cravatt B.F. A second mammalian N-myristoyltransferase. J Biol Chem 273 (1998) 6595-6598
    • (1998) J Biol Chem , vol.273 , pp. 6595-6598
    • Giang, D.K.1    Cravatt, B.F.2
  • 134
    • 0025776359 scopus 로고
    • N-myristoyl-transferase activity in cancer cells. Solubilization, specificity and enzymatic inhibition of a N-myristoyl transferase from L1210 microsomes
    • Boutin J.A., Clarenc J.P., Ferry G., Ernould A.P., Remond G., Vincent M., et al. N-myristoyl-transferase activity in cancer cells. Solubilization, specificity and enzymatic inhibition of a N-myristoyl transferase from L1210 microsomes. Eur J Biochem 201 (1991) 257-263
    • (1991) Eur J Biochem , vol.201 , pp. 257-263
    • Boutin, J.A.1    Clarenc, J.P.2    Ferry, G.3    Ernould, A.P.4    Remond, G.5    Vincent, M.6
  • 135
    • 0022476767 scopus 로고
    • Protein fatty acid acylation: enzymatic synthesis of an N-myristoylglycyl peptide
    • Towler D., and Glaser L. Protein fatty acid acylation: enzymatic synthesis of an N-myristoylglycyl peptide. Proc Natl Acad Sci USA 83 (1986) 2812-2816
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2812-2816
    • Towler, D.1    Glaser, L.2
  • 136
    • 0029097024 scopus 로고
    • Characterization and cellular localization of human myristoyl-CoA: protein N-myristoyltransferase
    • McIlhinney R.A. Characterization and cellular localization of human myristoyl-CoA: protein N-myristoyltransferase. Biochem Soc Trans 23 (1995) 549-553
    • (1995) Biochem Soc Trans , vol.23 , pp. 549-553
    • McIlhinney, R.A.1
  • 137
    • 0029876931 scopus 로고    scopus 로고
    • Immunocytochemical characterization and subcellular localization of human myristoyl-CoA: protein N-myristoyltransferase in HeLa cells
    • McIlhinney R.A., and McGlone K. Immunocytochemical characterization and subcellular localization of human myristoyl-CoA: protein N-myristoyltransferase in HeLa cells. Exp Cell Res 223 (1996) 348-356
    • (1996) Exp Cell Res , vol.223 , pp. 348-356
    • McIlhinney, R.A.1    McGlone, K.2
  • 138
    • 0025359849 scopus 로고
    • Structural and functional studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase produced in Escherichia coli. Evidence for an acyl-enzyme intermediate
    • Rudnick D.A., McWherter C.A., Adams S.P., Ropson I.J., Duronio R.J., and Gordon J.I. Structural and functional studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase produced in Escherichia coli. Evidence for an acyl-enzyme intermediate. J Biol Chem 265 (1990) 13370-13378
    • (1990) J Biol Chem , vol.265 , pp. 13370-13378
    • Rudnick, D.A.1    McWherter, C.A.2    Adams, S.P.3    Ropson, I.J.4    Duronio, R.J.5    Gordon, J.I.6
  • 139
    • 0025834950 scopus 로고
    • Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase
    • Rudnick D.A., McWherter C.A., Rocque W.J., Lennon P.J., Getman D.P., and Gordon J.I. Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. J Biol Chem 266 (1991) 9732-9739
    • (1991) J Biol Chem , vol.266 , pp. 9732-9739
    • Rudnick, D.A.1    McWherter, C.A.2    Rocque, W.J.3    Lennon, P.J.4    Getman, D.P.5    Gordon, J.I.6
  • 140
    • 0028244655 scopus 로고
    • Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands
    • Bhatnagar R.S., Jackson-Machelski E., McWherter C.A., and Gordon J.I. Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands. J Biol Chem 269 (1994) 11045-11053
    • (1994) J Biol Chem , vol.269 , pp. 11045-11053
    • Bhatnagar, R.S.1    Jackson-Machelski, E.2    McWherter, C.A.3    Gordon, J.I.4
  • 142
    • 0026544934 scopus 로고
    • Mutations of human myristoyl CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae
    • Duronio R.J., Reed S.I., and Gordon J.I. Mutations of human myristoyl CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 89 (1992) 4129-4133
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4129-4133
    • Duronio, R.J.1    Reed, S.I.2    Gordon, J.I.3
  • 143
    • 0028298347 scopus 로고
    • Characterization of polyhistidine-tagged form of human myristoyl-CoA:protein N-myristoyltransferase produced in Escherichia coli
    • McIlhinney R.A., Patel P.B., and McGlone K. Characterization of polyhistidine-tagged form of human myristoyl-CoA:protein N-myristoyltransferase produced in Escherichia coli. Eur J Biochem 222 (1994) 137-146
    • (1994) Eur J Biochem , vol.222 , pp. 137-146
    • McIlhinney, R.A.1    Patel, P.B.2    McGlone, K.3
  • 144
    • 0030031394 scopus 로고    scopus 로고
    • Expression of human N-myristoyltransferase in Escherichia coli. Comparison with N-myristoyltransferases expressed in different tissues
    • Raju R.V., Datla R.S., and Sharma R.K. Expression of human N-myristoyltransferase in Escherichia coli. Comparison with N-myristoyltransferases expressed in different tissues. Mol Cell Biochem 155 (1996) 69-76
    • (1996) Mol Cell Biochem , vol.155 , pp. 69-76
    • Raju, R.V.1    Datla, R.S.2    Sharma, R.K.3
  • 145
    • 0029095573 scopus 로고
    • Identification and characterization of multiple forms of bovine brain N-myristoyltransferase
    • Glover C.J., and Felsted R.L. Identification and characterization of multiple forms of bovine brain N-myristoyltransferase. J Biol Chem 270 (1995) 23226-23233
    • (1995) J Biol Chem , vol.270 , pp. 23226-23233
    • Glover, C.J.1    Felsted, R.L.2
  • 146
    • 0023931431 scopus 로고
    • Myristoyl CoA:protein N-myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities
    • Towler D.A., Adams S.P., Eubanks S.R., Towery D.S., Jackson-Machelski E., Glaser L., et al. Myristoyl CoA:protein N-myristoyltransferase activities from rat liver and yeast possess overlapping yet distinct peptide substrate specificities. J Biol Chem 263 (1988) 1784-1790
    • (1988) J Biol Chem , vol.263 , pp. 1784-1790
    • Towler, D.A.1    Adams, S.P.2    Eubanks, S.R.3    Towery, D.S.4    Jackson-Machelski, E.5    Glaser, L.6
  • 147
    • 0027095974 scopus 로고
    • Studies of the catalytic activities and substrate specificities of Saccharomyces cerevisiae myristoyl-coenzyme A: protein N-myristoyltransferase deletion mutants and human/yeast Nmt chimeras in Escherichia coli and S. cerevisiae
    • Rudnick D.A., Johnson R.L., and Gordon J.I. Studies of the catalytic activities and substrate specificities of Saccharomyces cerevisiae myristoyl-coenzyme A: protein N-myristoyltransferase deletion mutants and human/yeast Nmt chimeras in Escherichia coli and S. cerevisiae. J Biol Chem 267 (1992) 23852-23861
    • (1992) J Biol Chem , vol.267 , pp. 23852-23861
    • Rudnick, D.A.1    Johnson, R.L.2    Gordon, J.I.3
  • 148
    • 0027464939 scopus 로고
    • Purification and partial sequencing of myristoyl CoA:protein N-myristoyltransferase from bovine brain
    • McIlhinney R.A., McGlone K., and Willis A.C. Purification and partial sequencing of myristoyl CoA:protein N-myristoyltransferase from bovine brain. Biochem J 290 (1993) 405-410
    • (1993) Biochem J , vol.290 , pp. 405-410
    • McIlhinney, R.A.1    McGlone, K.2    Willis, A.C.3
  • 149
    • 0030459645 scopus 로고    scopus 로고
    • Biochemical studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase mutants
    • Zhang L., Jackson-Machelski E., and Gordon J.I. Biochemical studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase mutants. J Biol Chem 271 (1996) 33131-33140
    • (1996) J Biol Chem , vol.271 , pp. 33131-33140
    • Zhang, L.1    Jackson-Machelski, E.2    Gordon, J.I.3
  • 150
    • 0031733246 scopus 로고    scopus 로고
    • Recombinant bovine spleen myristoyl-CoA:protein N-myristoyltransferase
    • Raju R.V., Datla R.S., Kakkar R., and Sharma R.K. Recombinant bovine spleen myristoyl-CoA:protein N-myristoyltransferase. Mol Cell Biochem 189 (1998) 91-97
    • (1998) Mol Cell Biochem , vol.189 , pp. 91-97
    • Raju, R.V.1    Datla, R.S.2    Kakkar, R.3    Sharma, R.K.4
  • 152
    • 0030657584 scopus 로고    scopus 로고
    • Human N-myristoyltransferase amino-terminal domain involved in targeting enzyme to the ribosomal subcellular fraction
    • Glover C.J., Hartman K.D., and Felsted R.L. Human N-myristoyltransferase amino-terminal domain involved in targeting enzyme to the ribosomal subcellular fraction. J Biol Chem 272 (1997) 28680-28689
    • (1997) J Biol Chem , vol.272 , pp. 28680-28689
    • Glover, C.J.1    Hartman, K.D.2    Felsted, R.L.3
  • 153
    • 0027253206 scopus 로고
    • Myristoyl CoA:protein N-myristoyltransferase activity in cancer cells. Purification and characterization of a cytosolic isoform from the murine leukaemia cell line L1210
    • Boutin J.A., Ferry G., Renould A.P., Maes P., Remound G., and Vincent M. Myristoyl CoA:protein N-myristoyltransferase activity in cancer cells. Purification and characterization of a cytosolic isoform from the murine leukaemia cell line L1210. Eur J Biochem 214 (1993) 853-867
    • (1993) Eur J Biochem , vol.214 , pp. 853-867
    • Boutin, J.A.1    Ferry, G.2    Renould, A.P.3    Maes, P.4    Remound, G.5    Vincent, M.6
  • 154
    • 0028072831 scopus 로고
    • Fatty acyl transfer by human N-myristoyltransferase is dependent upon conserved cysteine and histidine residues
    • Pesecks S.M., and Resh M.D. Fatty acyl transfer by human N-myristoyltransferase is dependent upon conserved cysteine and histidine residues. J Biol Chem 269 (1994) 30888-30892
    • (1994) J Biol Chem , vol.269 , pp. 30888-30892
    • Pesecks, S.M.1    Resh, M.D.2
  • 155
    • 0032143539 scopus 로고    scopus 로고
    • Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme
    • McIlhinney R.A., Young K., Egerton M., Camble R., White A., and Soloviev M. Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme. Biochem J 333 (1998) 491-495
    • (1998) Biochem J , vol.333 , pp. 491-495
    • McIlhinney, R.A.1    Young, K.2    Egerton, M.3    Camble, R.4    White, A.5    Soloviev, M.6
  • 156
    • 0033551201 scopus 로고    scopus 로고
    • Genomic organization of human N-myristoyltransferase-1
    • Raju R.V., Datla R.S., and Sharma R.K. Genomic organization of human N-myristoyltransferase-1. Biochem Biophys Res Commun 257 (1999) 284-288
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 284-288
    • Raju, R.V.1    Datla, R.S.2    Sharma, R.K.3
  • 157
    • 0028670723 scopus 로고
    • Mechanisms of action of NIP71 on N-myristoyltransferase activity
    • King M.J., and Sharma R.K. Mechanisms of action of NIP71 on N-myristoyltransferase activity. Mol Cell Biochem 141 (1994) 79-86
    • (1994) Mol Cell Biochem , vol.141 , pp. 79-86
    • King, M.J.1    Sharma, R.K.2
  • 158
    • 0029926690 scopus 로고    scopus 로고
    • N-Myristoyltransferase activity in rabbit intestine
    • Magnuson B., Raju R.V., and Sharma R.K. N-Myristoyltransferase activity in rabbit intestine. Biochim Biophys Acta 1300 (1996) 119-124
    • (1996) Biochim Biophys Acta , vol.1300 , pp. 119-124
    • Magnuson, B.1    Raju, R.V.2    Sharma, R.K.3
  • 159
    • 0031846663 scopus 로고    scopus 로고
    • Myristoyl-CoA:protein N-myristoyltransferase from bovine cardiac muscle. Molecular cloning, kinetic analysis, and in vitro proteolytic cleavage by m-calpain
    • Raju R.V., Kakkar R., Datla R.S., Radhi J.M., and Sharma R.K. Myristoyl-CoA:protein N-myristoyltransferase from bovine cardiac muscle. Molecular cloning, kinetic analysis, and in vitro proteolytic cleavage by m-calpain. Exp Cell Res 241 (1998) 23-35
    • (1998) Exp Cell Res , vol.241 , pp. 23-35
    • Raju, R.V.1    Kakkar, R.2    Datla, R.S.3    Radhi, J.M.4    Sharma, R.K.5
  • 160
    • 0024461910 scopus 로고
    • A simplified assay for the enzyme responsible for the attachment of myristic acid to the N-terminal glycine residue of proteins, myristoyl-CoA:glycylpeptide N-myristoyltransferase
    • McIlhinney R.A., and McGlone K. A simplified assay for the enzyme responsible for the attachment of myristic acid to the N-terminal glycine residue of proteins, myristoyl-CoA:glycylpeptide N-myristoyltransferase. Biochem J 263 (1989) 387-391
    • (1989) Biochem J , vol.263 , pp. 387-391
    • McIlhinney, R.A.1    McGlone, K.2
  • 161
    • 0027276545 scopus 로고
    • A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase
    • Rocque W.J., McWherter C.A., Wood D.C., and Gordon J.I. A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. J Biol Chem 268 (1993) 9964-9971
    • (1993) J Biol Chem , vol.268 , pp. 9964-9971
    • Rocque, W.J.1    McWherter, C.A.2    Wood, D.C.3    Gordon, J.I.4
  • 162
    • 0016369228 scopus 로고
    • Destabilization of membranes with chaotropic ions
    • Hatefi Y., and Hanstein W.G. Destabilization of membranes with chaotropic ions. Methods Enzymol 31 (1974) 770-790
    • (1974) Methods Enzymol , vol.31 , pp. 770-790
    • Hatefi, Y.1    Hanstein, W.G.2
  • 163
    • 0014448296 scopus 로고
    • N-Acylsarcosines as inhibitors of respiration and glycolysis and glycolytic enzymes
    • Nicalau J., and Bacila M. N-Acylsarcosines as inhibitors of respiration and glycolysis and glycolytic enzymes. Arch Biochem Biophys 129 (1969)
    • (1969) Arch Biochem Biophys , vol.129 , pp. 357-361
    • Nicalau, J.1    Bacila, M.2
  • 164
    • 0028953366 scopus 로고
    • Myristoyl CoA:protein N-myristoyltransferase: subcellular localization, activation and kinetic behavior in the presence of organic solvents
    • Rajala R.V., and Sharma R.K. Myristoyl CoA:protein N-myristoyltransferase: subcellular localization, activation and kinetic behavior in the presence of organic solvents. Biochem Biophys Res Commun 208 (1995) 617-623
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 617-623
    • Rajala, R.V.1    Sharma, R.K.2
  • 165
    • 0028929461 scopus 로고
    • Ethanol enhances the stimulatory effects of insulin and insulin like growth factor-1 on DNA synthesis in NIH 3T3 fibroblasts
    • Tomono M., and Kiss Z. Ethanol enhances the stimulatory effects of insulin and insulin like growth factor-1 on DNA synthesis in NIH 3T3 fibroblasts. Biochem Biophys Res Commun 208 (1995) 63-67
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 63-67
    • Tomono, M.1    Kiss, Z.2
  • 166
    • 0023507408 scopus 로고
    • Ethanol: an enhancer of major histocompatibility complex antigen expression
    • Parent L.J., Ehrlich R., Marls L., and Singer D.S. Ethanol: an enhancer of major histocompatibility complex antigen expression. FASEB J 1 (1987) 469-473
    • (1987) FASEB J , vol.1 , pp. 469-473
    • Parent, L.J.1    Ehrlich, R.2    Marls, L.3    Singer, D.S.4
  • 167
    • 0018718811 scopus 로고
    • Stimulation of glycogen phosphorylase kinase from rabbit skeletal muscle by organic solvents
    • Singh T.J., and Wang J.I.-I. Stimulation of glycogen phosphorylase kinase from rabbit skeletal muscle by organic solvents. J Biol Chem 254 (1979) 8466-8472
    • (1979) J Biol Chem , vol.254 , pp. 8466-8472
    • Singh, T.J.1    Wang, J.I.-I.2
  • 168
    • 0032552973 scopus 로고    scopus 로고
    • Effects of l-histidine and its structural analogues on human N-myristoyltransferase activity and importance of EEVEH amino acid sequence for enzyme activity
    • Raju R.V., Datla R.S., Warrington R.C., and Sharma R.K. Effects of l-histidine and its structural analogues on human N-myristoyltransferase activity and importance of EEVEH amino acid sequence for enzyme activity. Biochemistry 37 (1998) 14928-14936
    • (1998) Biochemistry , vol.37 , pp. 14928-14936
    • Raju, R.V.1    Datla, R.S.2    Warrington, R.C.3    Sharma, R.K.4
  • 169
    • 0035576809 scopus 로고    scopus 로고
    • Novel target genes of the Ah (dioxin) receptor: transcriptional induction of N-myristoyltransferase 2
    • Kolluri S.K., Balduf C., Hofmann M., and Gottlicher M. Novel target genes of the Ah (dioxin) receptor: transcriptional induction of N-myristoyltransferase 2. Cancer Res 61 (2001) 8534-8539
    • (2001) Cancer Res , vol.61 , pp. 8534-8539
    • Kolluri, S.K.1    Balduf, C.2    Hofmann, M.3    Gottlicher, M.4
  • 170
    • 0342474487 scopus 로고
    • Heteroatom-substituted fatty acid analogs as substrates for N-myristoyltransferase: an approach for studying both the enzymology and function of protein acylation
    • Heuckeroth R.O., Glaser L., and Gordon J.I. Heteroatom-substituted fatty acid analogs as substrates for N-myristoyltransferase: an approach for studying both the enzymology and function of protein acylation. Proc Natl Acad Sci USA 85 (1988) 8795-8799
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8795-8799
    • Heuckeroth, R.O.1    Glaser, L.2    Gordon, J.I.3
  • 172
    • 0024327018 scopus 로고
    • S-(2-oxopentadecyl)-CoA, a nonhydrolyzable analogue of myristoyl-CoA, is a potent inhibitor of myristoyl-CoA:protein N-myristoyltransferase
    • Paige L.A., Zheng G.Q., DeFrees S.A., Cassady J.M., and Geahlen R.L. S-(2-oxopentadecyl)-CoA, a nonhydrolyzable analogue of myristoyl-CoA, is a potent inhibitor of myristoyl-CoA:protein N-myristoyltransferase. J Med Chem 32 (1989) 1665-1667
    • (1989) J Med Chem , vol.32 , pp. 1665-1667
    • Paige, L.A.1    Zheng, G.Q.2    DeFrees, S.A.3    Cassady, J.M.4    Geahlen, R.L.5
  • 173
    • 0025245802 scopus 로고
    • Metabolic activation of 2-substituted derivatives of myristic acid to form potent inhibitors of myristoyl CoA:protein N-myristoyltransferase
    • Paige L.A., Zheng G.Q., DeFrees S.A., Cassady J.M., and Geahlen R.L. Metabolic activation of 2-substituted derivatives of myristic acid to form potent inhibitors of myristoyl CoA:protein N-myristoyltransferase. Biochemistry 29 (1990) 10566-10573
    • (1990) Biochemistry , vol.29 , pp. 10566-10573
    • Paige, L.A.1    Zheng, G.Q.2    DeFrees, S.A.3    Cassady, J.M.4    Geahlen, R.L.5
  • 174
    • 0023109534 scopus 로고
    • Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyltransferase
    • Towler D.A., Eubanks S.R., Towery D.S., Adams S.P., and Glaser L. Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyltransferase. J Biol Chem 262 (1987) 1030-1036
    • (1987) J Biol Chem , vol.262 , pp. 1030-1036
    • Towler, D.A.1    Eubanks, S.R.2    Towery, D.S.3    Adams, S.P.4    Glaser, L.5
  • 175
    • 0028357644 scopus 로고
    • Synthesis of myristoyl CoA analogues and myristoyl peptides as inhibitors of myristoyl CoA:protein N-myristoyltransferase
    • Zheng G.Q., Hu X., Cassady J.M., Paige L.A., and Geahlen R.L. Synthesis of myristoyl CoA analogues and myristoyl peptides as inhibitors of myristoyl CoA:protein N-myristoyltransferase. J Pharm Sci 83 (1994) 233-238
    • (1994) J Pharm Sci , vol.83 , pp. 233-238
    • Zheng, G.Q.1    Hu, X.2    Cassady, J.M.3    Paige, L.A.4    Geahlen, R.L.5
  • 176
    • 0029071405 scopus 로고
    • Design and syntheses of potent and selective dipeptide inhibitors of Candida albicans myristoyl-CoA:protein N-myristoyltransferase
    • Devadas B., Zupec M.E., Freeman S.K., Brown D.L., Nagarajan S., Sikorski J.A., et al. Design and syntheses of potent and selective dipeptide inhibitors of Candida albicans myristoyl-CoA:protein N-myristoyltransferase. J Med Chem 38 (1995) 1837-1840
    • (1995) J Med Chem , vol.38 , pp. 1837-1840
    • Devadas, B.1    Zupec, M.E.2    Freeman, S.K.3    Brown, D.L.4    Nagarajan, S.5    Sikorski, J.A.6
  • 177
    • 0036808337 scopus 로고    scopus 로고
    • Development of an enzyme-linked immunosorbent assay for measurement of activity of myristoyl-coenzyme A:protein N-myristoyltransferase
    • Takamune N., Hamada H., Sugawara H., Misumi S., and Shoji S. Development of an enzyme-linked immunosorbent assay for measurement of activity of myristoyl-coenzyme A:protein N-myristoyltransferase. Anal Biochem 309 (2002) 137-142
    • (2002) Anal Biochem , vol.309 , pp. 137-142
    • Takamune, N.1    Hamada, H.2    Sugawara, H.3    Misumi, S.4    Shoji, S.5
  • 178
    • 0036051790 scopus 로고    scopus 로고
    • Antifungals targeted to protein modification: focus on protein N-myristoyltransferase
    • Georgopapadakou N.H. Antifungals targeted to protein modification: focus on protein N-myristoyltransferase. Expert Opin Investig Drugs 11 (2002) 1117-1125
    • (2002) Expert Opin Investig Drugs , vol.11 , pp. 1117-1125
    • Georgopapadakou, N.H.1
  • 179
    • 17944387642 scopus 로고    scopus 로고
    • Design and synthesis of novel benzofurans as a new class of antifungal agents targeting fungal N-myristoyltransferase
    • Kawasaki K., Masubuchi M., Morikami K., Sogabe S., Aoyama T., Ebiike H., et al. Design and synthesis of novel benzofurans as a new class of antifungal agents targeting fungal N-myristoyltransferase. Bioorg Med Chem Lett 13 (2003) 87-91
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 87-91
    • Kawasaki, K.1    Masubuchi, M.2    Morikami, K.3    Sogabe, S.4    Aoyama, T.5    Ebiike, H.6
  • 180
    • 0027172905 scopus 로고
    • Identification, purification and characterization of a membrane-associated N-myristoyltransferase inhibitor protein from bovine brain
    • King M.J., and Sharma R.K. Identification, purification and characterization of a membrane-associated N-myristoyltransferase inhibitor protein from bovine brain. Biochem J 291 (1993) 635-639
    • (1993) Biochem J , vol.291 , pp. 635-639
    • King, M.J.1    Sharma, R.K.2
  • 181
    • 0034647954 scopus 로고    scopus 로고
    • Expression of N-myristoyltransferase inhibitor protein and its relationship to c-Src levels in human colon cancer cell lines
    • Rajala R.V., Dehm S., Bi X., Bonham K., and Sharma R.K. Expression of N-myristoyltransferase inhibitor protein and its relationship to c-Src levels in human colon cancer cell lines. Biochem Biophys Res Commun 273 (2000) 1116-1120
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 1116-1120
    • Rajala, R.V.1    Dehm, S.2    Bi, X.3    Bonham, K.4    Sharma, R.K.5
  • 183
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., and Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92 (1998) 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 186
    • 0023201302 scopus 로고
    • Mutant p53 proteins bind hsp 72/73 cellular heat shock-related proteins in SV40-transformed monkey cells
    • Sturzbecher H.W., Chumakov P., Welch W.J., and Jenkins J.R. Mutant p53 proteins bind hsp 72/73 cellular heat shock-related proteins in SV40-transformed monkey cells. Oncogene 1 (1987) 201-211
    • (1987) Oncogene , vol.1 , pp. 201-211
    • Sturzbecher, H.W.1    Chumakov, P.2    Welch, W.J.3    Jenkins, J.R.4
  • 187
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny M.V., Toretsky J., Bohen S., and Neckers L. Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc Natl Acad Sci USA 93 (1996) 8379-8383
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 188
    • 0024271276 scopus 로고
    • Specific interaction between a subset of the p53 protein family and heat shock proteins hsp72/hsc73 in a human osteosarcoma cell line
    • Ehrhart J.C., Duthu A., Ullrich S., Appella E., and May P. Specific interaction between a subset of the p53 protein family and heat shock proteins hsp72/hsc73 in a human osteosarcoma cell line. Oncogene 3 (1988) 595-603
    • (1988) Oncogene , vol.3 , pp. 595-603
    • Ehrhart, J.C.1    Duthu, A.2    Ullrich, S.3    Appella, E.4    May, P.5
  • 189
    • 0035801391 scopus 로고    scopus 로고
    • Hsp70 interactions with the p53 tumour suppressor protein
    • Zylicz M., King F.W., and Wawrzynow A. Hsp70 interactions with the p53 tumour suppressor protein. EMBO J 20 (2001) 4634-4638
    • (2001) EMBO J , vol.20 , pp. 4634-4638
    • Zylicz, M.1    King, F.W.2    Wawrzynow, A.3
  • 191
    • 3242724279 scopus 로고    scopus 로고
    • The prognostic value of both neuron-specific enolase (NSE) and Cyfra21-1 in small cell lung cancer
    • Ando S., Suzuki M., Yamamoto N., Iida T., and Kimura H. The prognostic value of both neuron-specific enolase (NSE) and Cyfra21-1 in small cell lung cancer. Anticancer Res 24 (2004) 1941-1946
    • (2004) Anticancer Res , vol.24 , pp. 1941-1946
    • Ando, S.1    Suzuki, M.2    Yamamoto, N.3    Iida, T.4    Kimura, H.5
  • 192
    • 0030591169 scopus 로고    scopus 로고
    • Reduction of oncoprotein transformation in vitro by albumin
    • Raju R.V., Datla R.S., and Sharma R.K. Reduction of oncoprotein transformation in vitro by albumin. J Natl Cancer Inst 88 (1996) 556-557
    • (1996) J Natl Cancer Inst , vol.88 , pp. 556-557
    • Raju, R.V.1    Datla, R.S.2    Sharma, R.K.3
  • 193
    • 0018750411 scopus 로고
    • Albumin-deficient rat mutant
    • Nagase S., Shimamune K., and Shumiya S. Albumin-deficient rat mutant. Science 205 (1979) 590-591
    • (1979) Science , vol.205 , pp. 590-591
    • Nagase, S.1    Shimamune, K.2    Shumiya, S.3
  • 194
    • 0023777906 scopus 로고
    • Chemical carcinogenesis in analbuminmic rats
    • Kakizoe T., and Sugimura T. Chemical carcinogenesis in analbuminmic rats. Jpn J Cancer Res 79 (1988) 775-784
    • (1988) Jpn J Cancer Res , vol.79 , pp. 775-784
    • Kakizoe, T.1    Sugimura, T.2
  • 195
    • 0027434270 scopus 로고
    • Elevated N-myristoyltransferase activity is reversed by sodium orthovanadate in streptozotocin-induced diabetic rat
    • King M.J., Pugazhenthi S., Khandelwal R.L., and Sharma R.K. Elevated N-myristoyltransferase activity is reversed by sodium orthovanadate in streptozotocin-induced diabetic rat. Biochem Biophys Acta 1165 (1993) 259-262
    • (1993) Biochem Biophys Acta , vol.1165 , pp. 259-262
    • King, M.J.1    Pugazhenthi, S.2    Khandelwal, R.L.3    Sharma, R.K.4
  • 200
    • 15144355281 scopus 로고    scopus 로고
    • Design and synthesis of novel imidazole-substituted dipeptide amides as potent and selective inhibitors of Candida albicans myristoyl CoA:protein N-myristoyltransferase and identification of related tripeptide inhibitors with mechanism-based antifungal activity
    • Devadas B., Freeman S.K., Zupec M.E., Lu H.F., Nagarajan S.R., Kishore N.S., et al. Design and synthesis of novel imidazole-substituted dipeptide amides as potent and selective inhibitors of Candida albicans myristoyl CoA:protein N-myristoyltransferase and identification of related tripeptide inhibitors with mechanism-based antifungal activity. J Med Chem 40 (1997) 2609-2625
    • (1997) J Med Chem , vol.40 , pp. 2609-2625
    • Devadas, B.1    Freeman, S.K.2    Zupec, M.E.3    Lu, H.F.4    Nagarajan, S.R.5    Kishore, N.S.6
  • 201
    • 0030499038 scopus 로고    scopus 로고
    • l-Histidinol reverses resistance to cisplatinum and other antineoplastics in a tumorigenic epithelial cell line
    • Warrington R.C., Fang W.D., and Zhang L.U. l-Histidinol reverses resistance to cisplatinum and other antineoplastics in a tumorigenic epithelial cell line. Anticancer Res 16 (1996) 3641-3646
    • (1996) Anticancer Res , vol.16 , pp. 3641-3646
    • Warrington, R.C.1    Fang, W.D.2    Zhang, L.U.3
  • 202
    • 0027495237 scopus 로고
    • Modulation of anticancer drug toxicity by l-histidinol: root for improving human cancer chemotherapy?
    • Warrington R.C. Modulation of anticancer drug toxicity by l-histidinol: root for improving human cancer chemotherapy?. Drugs Future 18 (1993) 743-749
    • (1993) Drugs Future , vol.18 , pp. 743-749
    • Warrington, R.C.1
  • 203
    • 0036181978 scopus 로고    scopus 로고
    • Cytotoxic 1,4-bis(2-oxo-1-cycloalkylmethylene)benzenes and related compounds
    • Dimmock J.R., Jha A., Kumar P., Zello G.A., Quail J.W., Oloo E.O., et al. Cytotoxic 1,4-bis(2-oxo-1-cycloalkylmethylene)benzenes and related compounds. Eur J Med Chem 37 (2002) 35-44
    • (2002) Eur J Med Chem , vol.37 , pp. 35-44
    • Dimmock, J.R.1    Jha, A.2    Kumar, P.3    Zello, G.A.4    Quail, J.W.5    Oloo, E.O.6
  • 204
    • 0029893137 scopus 로고    scopus 로고
    • Coenzyme A dependent myristoylation and demyristoylation in the regulation of bovine spleen N-myristoyltransferase
    • Raju R.V., and Sharma R.K. Coenzyme A dependent myristoylation and demyristoylation in the regulation of bovine spleen N-myristoyltransferase. Mol Cell Biochem 158 (1996) 107-113
    • (1996) Mol Cell Biochem , vol.158 , pp. 107-113
    • Raju, R.V.1    Sharma, R.K.2
  • 205
    • 0015523212 scopus 로고
    • Reversible inhibition by histidinol of protein synthesis in human cells at the activation of histidine
    • Hansen B.S., Vaughan M.H., and Wang L. Reversible inhibition by histidinol of protein synthesis in human cells at the activation of histidine. J Biol Chem 247 (1972) 3854-3857
    • (1972) J Biol Chem , vol.247 , pp. 3854-3857
    • Hansen, B.S.1    Vaughan, M.H.2    Wang, L.3
  • 206
    • 0021270554 scopus 로고
    • Histidinol-mediated improvement in the specificity of 1-beta-d-arabinofuranosylcytosine and 5-fluorouracil in L 1210 leukemia-bearing mice
    • Warrington R.C., Muzyka T.G., and Fang W.D. Histidinol-mediated improvement in the specificity of 1-beta-d-arabinofuranosylcytosine and 5-fluorouracil in L 1210 leukemia-bearing mice. Cancer Res 44 (1984) 2929-2935
    • (1984) Cancer Res , vol.44 , pp. 2929-2935
    • Warrington, R.C.1    Muzyka, T.G.2    Fang, W.D.3
  • 207
    • 0021868965 scopus 로고
    • Histidinol-mediated enhancement of the specificity of two anticancer drugs in mice bearing leukemic bone marrow disease
    • Warrington R.C., and Fang W.D. Histidinol-mediated enhancement of the specificity of two anticancer drugs in mice bearing leukemic bone marrow disease. J Natl Cancer Inst 74 (1985) 1071-1077
    • (1985) J Natl Cancer Inst , vol.74 , pp. 1071-1077
    • Warrington, R.C.1    Fang, W.D.2
  • 208
    • 0023258650 scopus 로고
    • Effects of l-histidinol on the susceptibility of P815 mastocytoma cells to selected anticancer drugs in vitro and in DBA/2J mice
    • Warrington R.C., Cheng I., and Fang W.D. Effects of l-histidinol on the susceptibility of P815 mastocytoma cells to selected anticancer drugs in vitro and in DBA/2J mice. J Natl Cancer Inst 78 (1987) 1177-1183
    • (1987) J Natl Cancer Inst , vol.78 , pp. 1177-1183
    • Warrington, R.C.1    Cheng, I.2    Fang, W.D.3
  • 209
    • 0024386273 scopus 로고
    • l-Histidinol improves the selectivity and efficacy of alkylating agents and daunomycin in mice with P388 leukaemia
    • Warrington R.C., and Fang W.D. l-Histidinol improves the selectivity and efficacy of alkylating agents and daunomycin in mice with P388 leukaemia. Br J Cancer 60 (1989) 652-656
    • (1989) Br J Cancer , vol.60 , pp. 652-656
    • Warrington, R.C.1    Fang, W.D.2
  • 210
    • 0026333923 scopus 로고
    • Improved treatment of disseminated B16f10 melanoma in mice with anticancer drugs in combination with l-histidinol
    • Warrington R.C., and Fang W.D. Improved treatment of disseminated B16f10 melanoma in mice with anticancer drugs in combination with l-histidinol. Anticancer Res 11 (1991) 1869-1874
    • (1991) Anticancer Res , vol.11 , pp. 1869-1874
    • Warrington, R.C.1    Fang, W.D.2
  • 211
    • 0026863906 scopus 로고
    • l-Histidinol in experimental cancer chemotherapy: improving the selectivity and efficacy of anticancer drugs, eliminating metastatic disease and reversing the multidrug-resistant phenotype
    • Warrington R.C. l-Histidinol in experimental cancer chemotherapy: improving the selectivity and efficacy of anticancer drugs, eliminating metastatic disease and reversing the multidrug-resistant phenotype. Biochem Cell Biol 70 (1992) 365-375
    • (1992) Biochem Cell Biol , vol.70 , pp. 365-375
    • Warrington, R.C.1
  • 213
    • 0034687246 scopus 로고    scopus 로고
    • Sequential cytotoxicity: a theory evaluated using novel 2-[4-(3-aryl-2-propenoyloxy)phenylmethylene]cyclohexanones and related compounds
    • Dimmock J.R., Kandepu N.M., Nazarali A.J., Motaganahalli N.L., Kowalchuk T.P., Pugazhenthi U., et al. Sequential cytotoxicity: a theory evaluated using novel 2-[4-(3-aryl-2-propenoyloxy)phenylmethylene]cyclohexanones and related compounds. J Med Chem 43 (2000) 3933-3940
    • (2000) J Med Chem , vol.43 , pp. 3933-3940
    • Dimmock, J.R.1    Kandepu, N.M.2    Nazarali, A.J.3    Motaganahalli, N.L.4    Kowalchuk, T.P.5    Pugazhenthi, U.6
  • 216
    • 0033064746 scopus 로고    scopus 로고
    • Potentiation of the cytostatic effect of melphalan on colorectal cancer hepatic metastases by infusion of buthionine sulfoximine (BSO) in the rat: enhanced tumor glutathione depletion by infusion of BSO in the hepatic artery
    • Vahrmeijer A.L., van Dierendonck J.H., Schutrups J., van de Velde C.J., and Mulder G.J. Potentiation of the cytostatic effect of melphalan on colorectal cancer hepatic metastases by infusion of buthionine sulfoximine (BSO) in the rat: enhanced tumor glutathione depletion by infusion of BSO in the hepatic artery. Cancer Chemother Pharmacol 44 (1999) 111-116
    • (1999) Cancer Chemother Pharmacol , vol.44 , pp. 111-116
    • Vahrmeijer, A.L.1    van Dierendonck, J.H.2    Schutrups, J.3    van de Velde, C.J.4    Mulder, G.J.5
  • 217
    • 0023270590 scopus 로고
    • The role of glutathione in radiation and drug induced cytotoxicity
    • Mitchell J.B., and Russo A. The role of glutathione in radiation and drug induced cytotoxicity. Br J Cancer Suppl 8 (1987) 96-104
    • (1987) Br J Cancer Suppl , vol.8 , pp. 96-104
    • Mitchell, J.B.1    Russo, A.2
  • 218
    • 0034103531 scopus 로고    scopus 로고
    • N,N-diethyl-2-[4-(phenylmethyl)phenoxy]ethanamine (DPPE) a chemopotentiating and cytoprotective agent in clinical trials: interaction with histamine at cytochrome P450 3A4 and other isozymes that metabolize antineoplastic drugs
    • Brandes L.J., Queen G.M., and LaBella F.S. N,N-diethyl-2-[4-(phenylmethyl)phenoxy]ethanamine (DPPE) a chemopotentiating and cytoprotective agent in clinical trials: interaction with histamine at cytochrome P450 3A4 and other isozymes that metabolize antineoplastic drugs. Cancer Chemother Pharmacol 45 (2000) 298-304
    • (2000) Cancer Chemother Pharmacol , vol.45 , pp. 298-304
    • Brandes, L.J.1    Queen, G.M.2    LaBella, F.S.3
  • 220
    • 0025971035 scopus 로고
    • Synthesis and characterization of inhibitors of myristoyl-CoA:protein N-myristoyltransferase
    • Glover C.J., Tellez M.R., Guziec Jr. F.S., and Felsted R.L. Synthesis and characterization of inhibitors of myristoyl-CoA:protein N-myristoyltransferase. Biochem Pharmacol 41 (1991) 1067-1074
    • (1991) Biochem Pharmacol , vol.41 , pp. 1067-1074
    • Glover, C.J.1    Tellez, M.R.2    Guziec Jr., F.S.3    Felsted, R.L.4
  • 222
    • 0030950380 scopus 로고    scopus 로고
    • Demonstration and purification of a myristoyl-CoA binding protein from cardiac muscle
    • Raju R.V., and Sharma R.K. Demonstration and purification of a myristoyl-CoA binding protein from cardiac muscle. Life Sci 60 (1997) 2145-2153
    • (1997) Life Sci , vol.60 , pp. 2145-2153
    • Raju, R.V.1    Sharma, R.K.2
  • 223
    • 0025681492 scopus 로고
    • 2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors
    • 2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. Science 250 (1990) 979-982
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1    Koch, C.A.2    Grey, L.3    Ellis, C.4    Moran, M.F.5
  • 225
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H., Ishiura S., and Suzuki K. Structure and physiological function of calpains. Biochem J 328 (1997) 721-732
    • (1997) Biochem J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 226
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis
    • Rogers S., Wells R., and Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234 (1986) 364-368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 227
    • 0028088153 scopus 로고
    • Calpain: new perspectives in molecular diversity and physiological-pathological involvement
    • Saido T.C., Sorimachi H., and Suzuki K. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J 8 (1994) 814-822
    • (1994) FASEB J , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 228
    • 0029119628 scopus 로고
    • Differential activation of bovine brain N-myristoyltransferase(s) by a novel cytosolic activator
    • King M.J., and Sharma R.K. Differential activation of bovine brain N-myristoyltransferase(s) by a novel cytosolic activator. Biochem Biophys Res Commun 212 (1995) 580-588
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 580-588
    • King, M.J.1    Sharma, R.K.2
  • 229
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80 (1995) 225-236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 230
    • 0035914149 scopus 로고    scopus 로고
    • Phosphorylation of human N-myristoyltransferase by N-myristoylated SRC family tyrosine kinase members
    • Rajala R.V., Datla R.S., Carlsen S.A., Anderson D.H., Qi Z., Wang J.H., et al. Phosphorylation of human N-myristoyltransferase by N-myristoylated SRC family tyrosine kinase members. Biochem Biophys Res Commun 288 (2001) 233-239
    • (2001) Biochem Biophys Res Commun , vol.288 , pp. 233-239
    • Rajala, R.V.1    Datla, R.S.2    Carlsen, S.A.3    Anderson, D.H.4    Qi, Z.5    Wang, J.H.6
  • 231
    • 33751282335 scopus 로고    scopus 로고
    • Selvakumar P, Sharma RK. Phosphorylation of human N-myristoyltransferase type 1. Can J Phy Pharm [in press].
  • 233
    • 0024297795 scopus 로고
    • Structure of the beta subunit of translational initiation factor eIF-2
    • Pathak V.K., Nielsen P.J., Trachsel H., and Hershey J.W. Structure of the beta subunit of translational initiation factor eIF-2. Cell 54 (1988) 633-639
    • (1988) Cell , vol.54 , pp. 633-639
    • Pathak, V.K.1    Nielsen, P.J.2    Trachsel, H.3    Hershey, J.W.4
  • 234
    • 0024297814 scopus 로고
    • Mutations at a Zn(II) finger motif in the yeast elF-2 beta gene alter ribosomal start-site selection during the scanning process
    • Donahue T.F., Cigan A.M., Pabich E.K., and Valavicius B.C. Mutations at a Zn(II) finger motif in the yeast elF-2 beta gene alter ribosomal start-site selection during the scanning process. Cell 54 (1988) 621-632
    • (1988) Cell , vol.54 , pp. 621-632
    • Donahue, T.F.1    Cigan, A.M.2    Pabich, E.K.3    Valavicius, B.C.4
  • 235
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown M.T., and Cooper J.A. Regulation, substrates and functions of src. Biochim Biophys Acta 1287 (1996) 121-149
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 237
    • 0028972680 scopus 로고
    • Increased N-myristoyltransferase activity observed in rat and human colonic tumors
    • Magnuson B.A., Raju R.V., Moyana T.N., and Sharma R.K. Increased N-myristoyltransferase activity observed in rat and human colonic tumors. J Natl Cancer Inst 87 (1995) 1630-1635
    • (1995) J Natl Cancer Inst , vol.87 , pp. 1630-1635
    • Magnuson, B.A.1    Raju, R.V.2    Moyana, T.N.3    Sharma, R.K.4
  • 238
    • 0025223330 scopus 로고
    • Expression of cellular-yes protein in mammalian tissues
    • Zhao Y.H., Krueger J.G., and Sudol M. Expression of cellular-yes protein in mammalian tissues. Oncogene 5 (1990) 1629-1635
    • (1990) Oncogene , vol.5 , pp. 1629-1635
    • Zhao, Y.H.1    Krueger, J.G.2    Sudol, M.3
  • 240
    • 0025569424 scopus 로고
    • c-src and blockage of its myristoyl acylation with N-fatty acyl compounds resulted in the suppression of colony formation
    • c-src and blockage of its myristoyl acylation with N-fatty acyl compounds resulted in the suppression of colony formation. Biochem Biophys Res Commun 173 (1990) 894-901
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 894-901
    • Shoji, S.1    Kurosawa, T.2    Inoue, H.3    Funakoshi, T.4    Kubota, Y.5
  • 242
    • 0027454032 scopus 로고
    • Subcellular localization specified by protein acylation and phosphorylation
    • Blenis J., and Resh M.D. Subcellular localization specified by protein acylation and phosphorylation. Curr Opin Cell Biol 5 (1993) 984-989
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 984-989
    • Blenis, J.1    Resh, M.D.2
  • 245
    • 0027170840 scopus 로고
    • c-Yes tyrosine kinase activity in human colon carcinoma
    • Park J., Meisler A.I., and Cartwright C.A. c-Yes tyrosine kinase activity in human colon carcinoma. Oncogene 8 (1993) 2627-2635
    • (1993) Oncogene , vol.8 , pp. 2627-2635
    • Park, J.1    Meisler, A.I.2    Cartwright, C.A.3
  • 247
    • 0023317189 scopus 로고
    • src with Triton X-100-resistant cellular structure correlates with morphological transformation
    • src with Triton X-100-resistant cellular structure correlates with morphological transformation. Proc Natl Acad Sci USA 84 (1987) 2312-2316
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2312-2316
    • Hamaguchi, M.1    Hanafusa, H.2
  • 248
    • 0008612674 scopus 로고
    • Biochemical changes in colorectal carcinogenesis
    • Seitz H.K., Simanowski U.A., and Wright N.A. (Eds), Springer, Berlin
    • Toribara N.W., Ho S.B., Bresalier R.S., and Kim Y.S. Biochemical changes in colorectal carcinogenesis. In: Seitz H.K., Simanowski U.A., and Wright N.A. (Eds). Colorectal cancer: from pathogenesis to prevention? (1989), Springer, Berlin 256-288
    • (1989) Colorectal cancer: from pathogenesis to prevention? , pp. 256-288
    • Toribara, N.W.1    Ho, S.B.2    Bresalier, R.S.3    Kim, Y.S.4
  • 249
    • 0021777030 scopus 로고
    • Comparative histogenesis and pathology of naturally occurring and experimentally induced large bowel cancer in the rat
    • Ingall J.R.F., and Mastromarino A.J. (Eds), Alan R. Liss, New York
    • Ward J.M., and Ohshima M. Comparative histogenesis and pathology of naturally occurring and experimentally induced large bowel cancer in the rat. In: Ingall J.R.F., and Mastromarino A.J. (Eds). Carcinoma of the large bowel and its precursors (1985), Alan R. Liss, New York 203-225
    • (1985) Carcinoma of the large bowel and its precursors , pp. 203-225
    • Ward, J.M.1    Ohshima, M.2
  • 250
    • 0021810993 scopus 로고
    • Prognostic factors in colorectal carcinomas arising in adenomas: implications for lesions removed by endoscopic polypectomy
    • Haggitt R.C., Glotzbach R.E., Soffer E.E., and Wruble L.D. Prognostic factors in colorectal carcinomas arising in adenomas: implications for lesions removed by endoscopic polypectomy. Gastroenterology 89 (1985) 328-336
    • (1985) Gastroenterology , vol.89 , pp. 328-336
    • Haggitt, R.C.1    Glotzbach, R.E.2    Soffer, E.E.3    Wruble, L.D.4
  • 251
    • 0023132813 scopus 로고
    • Villous and tubulovillous adenomas of the colon and rectum. A retrospective review, 1964-1985
    • Galandiuk S., Fazio V.W., Jagelman D.G., Lavery I.C., Weakley F.A., Petras R.E., et al. Villous and tubulovillous adenomas of the colon and rectum. A retrospective review, 1964-1985. Am J Surg 153 (1987) 41-47
    • (1987) Am J Surg , vol.153 , pp. 41-47
    • Galandiuk, S.1    Fazio, V.W.2    Jagelman, D.G.3    Lavery, I.C.4    Weakley, F.A.5    Petras, R.E.6
  • 252
    • 0025832446 scopus 로고
    • Prognostic implications of proliferative activity and DNA aneuploidy in Astler-Coller Dukes stage C colonic adenocarcinomas
    • Harlow S.P., Eriksen B.L., Poggensee L., Chmiel J.S., Scarpelli D.G., Murad T., et al. Prognostic implications of proliferative activity and DNA aneuploidy in Astler-Coller Dukes stage C colonic adenocarcinomas. Cancer Res 51 (1991) 2403-2409
    • (1991) Cancer Res , vol.51 , pp. 2403-2409
    • Harlow, S.P.1    Eriksen, B.L.2    Poggensee, L.3    Chmiel, J.S.4    Scarpelli, D.G.5    Murad, T.6
  • 253
    • 0022570096 scopus 로고
    • Prognostic indicators of colon tumors. The Gastrointestinal Tumor Study Group experience
    • Steinberg S.M., Barkin J.S., Kaplan R.S., and Stablein D.M. Prognostic indicators of colon tumors. The Gastrointestinal Tumor Study Group experience. Cancer 57 (1986) 1866-1870
    • (1986) Cancer , vol.57 , pp. 1866-1870
    • Steinberg, S.M.1    Barkin, J.S.2    Kaplan, R.S.3    Stablein, D.M.4
  • 254
    • 0025128519 scopus 로고
    • Characterisation of a myristoyl CoA:glycylpeptide N-myristoyltransferase activity in rat brain: subcellular and regional distribution
    • McIlhinney R.A., and McGlone K. Characterisation of a myristoyl CoA:glycylpeptide N-myristoyltransferase activity in rat brain: subcellular and regional distribution. J Neurochem 54 (1990) 110-117
    • (1990) J Neurochem , vol.54 , pp. 110-117
    • McIlhinney, R.A.1    McGlone, K.2
  • 259
    • 0028981123 scopus 로고
    • Elevated c-yes tyrosine kinase activity in premalignant lesions of the colon
    • Pena S.V., Melhem M.F., Meisler A.I., and Cartwright C.A. Elevated c-yes tyrosine kinase activity in premalignant lesions of the colon. Gastroenterology 108 (1995) 117-124
    • (1995) Gastroenterology , vol.108 , pp. 117-124
    • Pena, S.V.1    Melhem, M.F.2    Meisler, A.I.3    Cartwright, C.A.4
  • 261
    • 0018082359 scopus 로고
    • Natural history study of gallbladder cancer: a review of 36 years experience at M D Anderson Hospital and Tumor Institute
    • Perpetuo M.D., Valdivieso M., Heilbrun L.K., Nelson R.S., Connor T., and Bodey G.P. Natural history study of gallbladder cancer: a review of 36 years experience at M D Anderson Hospital and Tumor Institute. Cancer 42 (1978) 330-335
    • (1978) Cancer , vol.42 , pp. 330-335
    • Perpetuo, M.D.1    Valdivieso, M.2    Heilbrun, L.K.3    Nelson, R.S.4    Connor, T.5    Bodey, G.P.6
  • 262
    • 0031586342 scopus 로고    scopus 로고
    • N-myristoyltransferase overexpression in human colorectal adenocarcinomas
    • Raju R.V., Moyana T.N., and Sharma R.K. N-myristoyltransferase overexpression in human colorectal adenocarcinomas. Exp Cell Res 235 (1997) 145-154
    • (1997) Exp Cell Res , vol.235 , pp. 145-154
    • Raju, R.V.1    Moyana, T.N.2    Sharma, R.K.3
  • 263
    • 33645230781 scopus 로고    scopus 로고
    • N-myristoyltransferase 2 expression in human colon cancer: cross-talk between the calpain and caspase system
    • Selvakumar P., Smith-Windsor E., Bonham K., and Sharma R.K. N-myristoyltransferase 2 expression in human colon cancer: cross-talk between the calpain and caspase system. FEBS Lett 580 (2006) 2021-2026
    • (2006) FEBS Lett , vol.580 , pp. 2021-2026
    • Selvakumar, P.1    Smith-Windsor, E.2    Bonham, K.3    Sharma, R.K.4
  • 264
    • 0034193203 scopus 로고    scopus 로고
    • Increased expression of N-myristoyltransferase in gallbladder carcinomas
    • Rajala R.V., Radhi J.M., Kakkar R., Datla R.S., and Sharma R.K. Increased expression of N-myristoyltransferase in gallbladder carcinomas. Cancer 88 (2000) 1992-1999
    • (2000) Cancer , vol.88 , pp. 1992-1999
    • Rajala, R.V.1    Radhi, J.M.2    Kakkar, R.3    Datla, R.S.4    Sharma, R.K.5
  • 265
    • 0026667397 scopus 로고
    • Carcinoma of the gallbladder. Histologic types, stage of disease, grade, and survival rates
    • Henson D.E., Albores-Saavedra J., and Corle D. Carcinoma of the gallbladder. Histologic types, stage of disease, grade, and survival rates. Cancer 70 (1992) 1493-1497
    • (1992) Cancer , vol.70 , pp. 1493-1497
    • Henson, D.E.1    Albores-Saavedra, J.2    Corle, D.3
  • 266
    • 0032903831 scopus 로고    scopus 로고
    • Gallbladder adenomas have molecular abnormalities different from those present in gallbladder carcinomas
    • Wistuba I.I., Miquel J.F., Gazdar A.F., and AlboresSaavedra J. Gallbladder adenomas have molecular abnormalities different from those present in gallbladder carcinomas. Hum Pathol 30 (1999) 21-25
    • (1999) Hum Pathol , vol.30 , pp. 21-25
    • Wistuba, I.I.1    Miquel, J.F.2    Gazdar, A.F.3    AlboresSaavedra, J.4
  • 267
    • 0028981089 scopus 로고
    • Mutations of p16Ink4/CDKN2 and p15Ink4B/MTS2 genes in biliary tract cancers
    • Yoshida S., Todoroki T., Ichikawa Y., Hanai S., Suzuki H., Hori M., et al. Mutations of p16Ink4/CDKN2 and p15Ink4B/MTS2 genes in biliary tract cancers. Cancer Res 55 (1995) 2756-2760
    • (1995) Cancer Res , vol.55 , pp. 2756-2760
    • Yoshida, S.1    Todoroki, T.2    Ichikawa, Y.3    Hanai, S.4    Suzuki, H.5    Hori, M.6
  • 268
    • 18544407444 scopus 로고    scopus 로고
    • TP53 mutations in stage I gallbladder carcinoma with special attention to growth patterns
    • Hanada K., Itoh M., Fujii K., Tsuchida A., Hirata M., Iwao T., et al. TP53 mutations in stage I gallbladder carcinoma with special attention to growth patterns. Eur J Cancer 33 (1997) 1136-1140
    • (1997) Eur J Cancer , vol.33 , pp. 1136-1140
    • Hanada, K.1    Itoh, M.2    Fujii, K.3    Tsuchida, A.4    Hirata, M.5    Iwao, T.6
  • 269
    • 0029008121 scopus 로고
    • Allele-specific mutations involved in the pathogenesis of endemic gallbladder carcinoma in Chile
    • Wistuba I.I., Sugio K., Hung J., Kishimoto Y., Virmani A.K., Roa I., et al. Allele-specific mutations involved in the pathogenesis of endemic gallbladder carcinoma in Chile. Cancer Res 55 (1995) 2511-2515
    • (1995) Cancer Res , vol.55 , pp. 2511-2515
    • Wistuba, I.I.1    Sugio, K.2    Hung, J.3    Kishimoto, Y.4    Virmani, A.K.5    Roa, I.6
  • 271
    • 33751262352 scopus 로고    scopus 로고
    • Canadian Cancer Statistics, National Cancer Institute of Canada Publication; 2002.
  • 272
    • 0027314975 scopus 로고
    • Postoperative chemotherapy and delayed radiation in children less than three years of age with malignant brain tumors
    • Duffner P.K., Horowitz M.E., Krischer J.P., Friedman H.S., Burger P.C., Cohen M.E., et al. Postoperative chemotherapy and delayed radiation in children less than three years of age with malignant brain tumors. N Engl J Med 328 (1993) 1725-1731
    • (1993) N Engl J Med , vol.328 , pp. 1725-1731
    • Duffner, P.K.1    Horowitz, M.E.2    Krischer, J.P.3    Friedman, H.S.4    Burger, P.C.5    Cohen, M.E.6
  • 273
    • 33751281608 scopus 로고    scopus 로고
    • Canadian Cancer Statistics, Canada; 2003.
  • 274
    • 33751269287 scopus 로고    scopus 로고
    • American Cancer Society. Cancer facts and figures, 2002, Surveillance Research Atlanta, GA 2002. CBTRUS Statistical Report: Primary Brain Tumors in the United States, 1995-1999, 45 Central Brain Tumor Registry of the Unites States, Chicago; 2002.
  • 275
    • 12144290194 scopus 로고    scopus 로고
    • Comparative measurements of hypoxia in human brain tumors using needle electrodes and EF5 binding
    • Evans S.M., Judy K.D., Dunphy I., Jenkins W.T., Nelson P.T., Collins R., et al. Comparative measurements of hypoxia in human brain tumors using needle electrodes and EF5 binding. Cancer Res 64 (2004) 1886-1892
    • (2004) Cancer Res , vol.64 , pp. 1886-1892
    • Evans, S.M.1    Judy, K.D.2    Dunphy, I.3    Jenkins, W.T.4    Nelson, P.T.5    Collins, R.6
  • 276
    • 0023429079 scopus 로고
    • Increased expression of the epidermal growth factor receptor gene in malignant gliomas is invariably associated with gene amplification
    • Wong A.J., Bigner S.H., Bigner D.D., Kinzler K.W., Hamilton S.R., and Vogelstein B. Increased expression of the epidermal growth factor receptor gene in malignant gliomas is invariably associated with gene amplification. Proc Natl Acad Sci USA 84 (1987) 6899-6903
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6899-6903
    • Wong, A.J.1    Bigner, S.H.2    Bigner, D.D.3    Kinzler, K.W.4    Hamilton, S.R.5    Vogelstein, B.6
  • 278
    • 0030778206 scopus 로고    scopus 로고
    • Molecular changes during the genesis of human gliomas
    • Sehgal A. Molecular changes during the genesis of human gliomas. Seminar Surg Oncol 14 (1998) 3-12
    • (1998) Seminar Surg Oncol , vol.14 , pp. 3-12
    • Sehgal, A.1
  • 279
    • 2542463425 scopus 로고    scopus 로고
    • SRC gene expression in human cancer: the role of transcriptional activation
    • Dehm S.M., and Bonham K. SRC gene expression in human cancer: the role of transcriptional activation. Biochem Cell Biol 82 (2004) 263-274
    • (2004) Biochem Cell Biol , vol.82 , pp. 263-274
    • Dehm, S.M.1    Bonham, K.2
  • 280
    • 0141538143 scopus 로고    scopus 로고
    • SRC family kinases: potential targets for the treatment of human cancer and leukemia
    • Warmuth M., Damoiseaux R., Liu Y., Fabbro D., and Gray N. SRC family kinases: potential targets for the treatment of human cancer and leukemia. Curr Pharm Des 9 (2003) 2043-2059
    • (2003) Curr Pharm Des , vol.9 , pp. 2043-2059
    • Warmuth, M.1    Damoiseaux, R.2    Liu, Y.3    Fabbro, D.4    Gray, N.5
  • 281
  • 282
    • 0038386613 scopus 로고    scopus 로고
    • Src family kinases in tumor progression and metastasis
    • Summy J.M., and Gallick G.E. Src family kinases in tumor progression and metastasis. Cancer Metastasis Rev 22 (2003) 337-358
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 337-358
    • Summy, J.M.1    Gallick, G.E.2
  • 284
    • 0036570357 scopus 로고    scopus 로고
    • Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples
    • Hecker T.P., Grammer J.R., Gillespie G.Y., Stewart Jr. J., and Gladson C.L. Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples. Cancer Res 62 (2002) 2699-2707
    • (2002) Cancer Res , vol.62 , pp. 2699-2707
    • Hecker, T.P.1    Grammer, J.R.2    Gillespie, G.Y.3    Stewart Jr., J.4    Gladson, C.L.5
  • 285
    • 0032566002 scopus 로고    scopus 로고
    • Stimulation of the protein tyrosine kinase c-Yes but not c-Src by neurotrophins in human brain-metastatic melanoma cells
    • Marchetti D., Parikh N., Sudol M., and Gallick G.E. Stimulation of the protein tyrosine kinase c-Yes but not c-Src by neurotrophins in human brain-metastatic melanoma cells. Oncogene 16 (1998) 3253-3260
    • (1998) Oncogene , vol.16 , pp. 3253-3260
    • Marchetti, D.1    Parikh, N.2    Sudol, M.3    Gallick, G.E.4


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