메뉴 건너뛰기




Volumn 2, Issue 1, 2009, Pages 6-10

Quantitative analysis of the expression of human n-myristoyltransferase 1 (hNMT-1) in cancers

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN N MYRISTOYLTRANSFERASE;

EID: 67650152107     PISSN: None     EISSN: 18753183     Source Type: Journal    
DOI: 10.2174/1875318300902010006     Document Type: Article
Times cited : (6)

References (36)
  • 1
    • 0027317391 scopus 로고
    • Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins
    • Luthra M, Balasubramanian D. Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins. J Biol Chem 1993; 268: 18119-27.
    • (1993) J Biol Chem , vol.268 , pp. 18119-18127
    • Luthra, M.1    Balasubramanian, D.2
  • 3
    • 0033614790 scopus 로고    scopus 로고
    • ATP nucleotidylation of creatine kinase
    • David SSM, Haley BE. ATP nucleotidylation of creatine kinase. Biochemistry 1999; 38: 8492-500.
    • (1999) Biochemistry , vol.38 , pp. 8492-8500
    • David, S.S.M.1    Haley, B.E.2
  • 4
    • 0033782777 scopus 로고    scopus 로고
    • Protein glycosylation and its role in protein folding
    • Parodi AJ. Protein glycosylation and its role in protein folding. Annu Rev Biochem 2000; 69: 69-93.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 5
    • 13744255376 scopus 로고    scopus 로고
    • Cell signaling. Stat acetylation-a key facet of cytokine signaling?
    • O'Shea JJ, Kanno Y, Chen X, Levy DE. Cell signaling. Stat acetylation-a key facet of cytokine signaling? Science 2005; 307: 217-8.
    • (2005) Science , vol.307 , pp. 217-218
    • O'Shea, J.J.1    Kanno, Y.2    Chen, X.3    Levy, D.E.4
  • 6
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh MD. Myristylation and palmitylation of Src family members: the fats of the matter. Cell 1994; 76: 411-3.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 7
    • 0030948184 scopus 로고    scopus 로고
    • Myristoylation
    • Boutin JA. Myristoylation. Cell Signal 1997; 9: 15-35.
    • (1997) Cell Signal , vol.9 , pp. 15-35
    • Boutin, J.A.1
  • 8
    • 0033996017 scopus 로고    scopus 로고
    • Raju RV, Datla RS, Moyana TN, Kakkar R, Carlsen SA, Sharma RK. N-myristoyltransferase. Mol Cell Biochem 2000; 204: 135-55.
    • Raju RV, Datla RS, Moyana TN, Kakkar R, Carlsen SA, Sharma RK. N-myristoyltransferase. Mol Cell Biochem 2000; 204: 135-55.
  • 9
    • 18744434901 scopus 로고
    • Mammalian myristoyl CoA: Protein N-myristoyltransferase
    • Raju RV, Magnuson BA, Sharma RK. Mammalian myristoyl CoA: protein N-myristoyltransferase. Mol Cell Biochem 1995; 149: 191-202.
    • (1995) Mol Cell Biochem , vol.149 , pp. 191-202
    • Raju, R.V.1    Magnuson, B.A.2    Sharma, R.K.3
  • 10
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae
    • Robbins SM, Quintrell NA, Bishop JM. Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol Cell Biol 1995; 15: 3507-15.
    • (1995) Mol Cell Biol , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 11
    • 0031788774 scopus 로고    scopus 로고
    • Structure of N-myristoyltransferase with bound myristoyl-CoA and peptide substrate analogs
    • Bhatnagar RS, Futterer K, Farazi TA, et al. Structure of N-myristoyltransferase with bound myristoyl-CoA and peptide substrate analogs. Nat Struct Biol 1998; 5: 1091-7.
    • (1998) Nat Struct Biol , vol.5 , pp. 1091-1097
    • Bhatnagar, R.S.1    Futterer, K.2    Farazi, T.A.3
  • 12
    • 0036775770 scopus 로고    scopus 로고
    • Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors
    • Sogabe S, Masubuchi M, Sakata K, et al. Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors. Chem Biol 2002; 9: 1119-28.
    • (2002) Chem Biol , vol.9 , pp. 1119-1128
    • Sogabe, S.1    Masubuchi, M.2    Sakata, K.3
  • 13
    • 0031889926 scopus 로고    scopus 로고
    • Crystal structure of the antifungal target N-myristoyl transferase
    • Weston SA, Camble R, Colls J, et al. Crystal structure of the antifungal target N-myristoyl transferase. Nat Struct Biol 1998; 5: 213-21.
    • (1998) Nat Struct Biol , vol.5 , pp. 213-221
    • Weston, S.A.1    Camble, R.2    Colls, J.3
  • 14
    • 0028244655 scopus 로고
    • Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase
    • Bhatnagar RS, Jackson-Machelski E, McWherter CA, Gordon JI. Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. J Biol Chem 1994: 269: 11045-53.
    • (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
  • 15
    • 0026544934 scopus 로고
    • Mutations of human myristoyl-CoA: Protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae
    • Duronio RJ, Reed SI, Gordon JI. Mutations of human myristoyl-CoA: protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 1992; 89: 4129-33.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4129-4133
    • Duronio, R.J.1    Reed, S.I.2    Gordon, J.I.3
  • 16
    • 0028072831 scopus 로고
    • Fatty acyl transfer by human N-myristyl transferase is dependent upon conserved cysteine and histidine residues
    • Peseckis SM, Resh MD. Fatty acyl transfer by human N-myristyl transferase is dependent upon conserved cysteine and histidine residues. J Biol Chem 1994; 269: 30888-92.
    • (1994) J Biol Chem , vol.269 , pp. 30888-30892
    • Peseckis, S.M.1    Resh, M.D.2
  • 17
    • 0020201569 scopus 로고
    • n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle
    • Carr SA, Biemann K, Shoji S, Parmelee DC, Titani K. n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle. Proc Natl Acad Sci USA 1982; 79: 6128-31.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6128-6131
    • Carr, S.A.1    Biemann, K.2    Shoji, S.3    Parmelee, D.C.4    Titani, K.5
  • 18
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • Zha J, Weiler S, Oh KJ, Wei MC, Korsmeyer SJ. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science 2000; 290: 1761-5.
    • (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
  • 19
    • 0021988983 scopus 로고
    • Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein
    • Schultz AM, Henderson LE, Oroszlan S, Garber EA, Hanafusa H. Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein. Science 1985; 227: 427-9.
    • (1985) Science , vol.227 , pp. 427-429
    • Schultz, A.M.1    Henderson, L.E.2    Oroszlan, S.3    Garber, E.A.4    Hanafusa, H.5
  • 21
    • 0027819338 scopus 로고
    • Treatment of T cells with 2-hydroxymyristic acid inhibits the myristoylation and alters the stability of p56lck
    • Nadler MJ, Harrison ML, Ashendel CL, Cassady JM, Geahlen RL. Treatment of T cells with 2-hydroxymyristic acid inhibits the myristoylation and alters the stability of p56lck. Biochemistry 1993; 32: 9250-5.
    • (1993) Biochemistry , vol.32 , pp. 9250-9255
    • Nadler, M.J.1    Harrison, M.L.2    Ashendel, C.L.3    Cassady, J.M.4    Geahlen, R.L.5
  • 22
    • 84866476582 scopus 로고    scopus 로고
    • 2-terminal myristoylation and palmitoylation at cysteine-3
    • 2-terminal myristoylation and palmitoylation at cysteine-3. J Cell Biol 1997; 136: 1023-35.
    • (1997) J Cell Biol , vol.136 , pp. 1023-1035
    • van't Hof, W.1    Resh, M.D.2
  • 23
    • 0020492523 scopus 로고
    • Identification of the NH2-terminal blocking group of calcineurin B as myristic acid
    • Aitken A, Cohen P, Santikarn S, et al. Identification of the NH2-terminal blocking group of calcineurin B as myristic acid. FEBS Lett 1982; 150: 314-8.
    • (1982) FEBS Lett , vol.150 , pp. 314-318
    • Aitken, A.1    Cohen, P.2    Santikarn, S.3
  • 24
    • 0023653310 scopus 로고
    • Hydroxylamine-stable covalent linkage of myristic acid in G0 alpha, a guanine nucleotide-binding protein of bovine brain
    • Schultz AM, Tsai SC, Kung HF, Oroszlan S, Moss J, Vaughan M. Hydroxylamine-stable covalent linkage of myristic acid in G0 alpha, a guanine nucleotide-binding protein of bovine brain. Biochem Biophys Res Commun 1987; 146: 1234-9.
    • (1987) Biochem Biophys Res Commun , vol.146 , pp. 1234-1239
    • Schultz, A.M.1    Tsai, S.C.2    Kung, H.F.3    Oroszlan, S.4    Moss, J.5    Vaughan, M.6
  • 25
    • 0024357985 scopus 로고
    • Replication of human immunodeficiency virus 1 and Moloney murine leukemia virus is inhibited by different heteroatom-containing analogs of myristic acid
    • Bryant ML, Heuckeroth RO, Kimata JT, Ratner L, Gordon JI. Replication of human immunodeficiency virus 1 and Moloney murine leukemia virus is inhibited by different heteroatom-containing analogs of myristic acid. Proc Natl Acad Sci USA 1989; 86: 8655-9.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8655-8659
    • Bryant, M.L.1    Heuckeroth, R.O.2    Kimata, J.T.3    Ratner, L.4    Gordon, J.I.5
  • 26
    • 0024331985 scopus 로고
    • Nef protein of human immunodeficiency virus type 1: Evidence against its role as a transcriptional inhibitor
    • Hammes SR, Dixon EP, Malim MH, Cullen BR, Greene WC. Nef protein of human immunodeficiency virus type 1: evidence against its role as a transcriptional inhibitor. Proc Natl Acad Sci USA 1989; 86: 9549-53.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9549-9553
    • Hammes, S.R.1    Dixon, E.P.2    Malim, M.H.3    Cullen, B.R.4    Greene, W.C.5
  • 27
    • 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, 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 1990; 64: 4099-107.
    • (1990) J Virol , vol.64 , pp. 4099-4107
    • Marc, D.1    Masson, G.2    Girard, M.3    van der Werf, S.4
  • 28
    • 0342394457 scopus 로고
    • Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1
    • Gottlinger HG, Sodroski JG, Haseltine WA. Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 1989; 86: 5781-5.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5781-5785
    • Gottlinger, H.G.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 29
    • 0025569424 scopus 로고
    • Human cellular src gene product: Identification of the myristoylated pp60c-src and blockage of its myristoyl acylation with N-fatty acyl compounds resulted in the suppression of colony formation
    • Shoji S, Kurosawa T, Inoue H, Funakoshi T, Kubota Y. Human cellular src gene product: identification of the myristoylated pp60c-src and blockage of its myristoyl acylation with N-fatty acyl compounds resulted in the suppression of colony formation. Biochem Biophys Res Commun 1990; 173: 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
  • 30
    • 0028972680 scopus 로고
    • Increased N-myristoyltransferase activity observed in rat and human colonic tumors
    • Magnuson BA, Raju RV, Moyana TN, Sharma RK. Increased N-myristoyltransferase activity observed in rat and human colonic tumors. J Natl Cancer Inst 1995; 87: 1630-5.
    • (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
  • 31
    • 0034193203 scopus 로고    scopus 로고
    • Increased expression of N-myristoyltransferase in gallbladder carcinomas
    • Rajala RV, Radhi JM, Kakkar R, Datla RS, Sharma RK. Increased expression of N-myristoyltransferase in gallbladder carcinomas. Cancer 2000; 88: 1992-9.
    • (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
  • 32
    • 13844250630 scopus 로고    scopus 로고
    • Expression of N-myristoyltransferase in human brain tumors
    • Lu Y, Selvakumar P, Ali K, et al. Expression of N-myristoyltransferase in human brain tumors. Neurochem Res 2005; 30: 9-13.
    • (2005) Neurochem Res , vol.30 , pp. 9-13
    • Lu, Y.1    Selvakumar, P.2    Ali, K.3
  • 34
    • 0032728199 scopus 로고    scopus 로고
    • Blockage of HIV-1 production through inhibition of proviral DNA synthesis by N,O-didecanoyl serinal dimethylacetal
    • Takemune N, Misumi S, Furuishi K, Shoji S. Blockage of HIV-1 production through inhibition of proviral DNA synthesis by N,O-didecanoyl serinal dimethylacetal. IUBMB Life 1999; 48: 311-5.
    • (1999) IUBMB Life , vol.48 , pp. 311-315
    • Takemune, N.1    Misumi, S.2    Furuishi, K.3    Shoji, S.4
  • 35
    • 0037063359 scopus 로고    scopus 로고
    • Novel strategy for anti-HIV-1 action: Selective cytotoxic effect of N-myristoyltransferase inhibitor on HIV-1-infected cells
    • Takamune N, Hamada H, Misumi S, Shoji S. Novel strategy for anti-HIV-1 action: selective cytotoxic effect of N-myristoyltransferase inhibitor on HIV-1-infected cells. FEBS Lett 2002; 527: 138-42.
    • (2002) FEBS Lett , vol.527 , pp. 138-142
    • Takamune, N.1    Hamada, H.2    Misumi, S.3    Shoji, S.4
  • 36
    • 12444334525 scopus 로고    scopus 로고
    • 3,5-bis(phenylmethylene)-1-(N-arylmaleamoyl)-4-piperidones: A novel group of cytotoxic agents
    • Dimmock JR, Jha A, Zello GA, et al. 3,5-bis(phenylmethylene)-1-(N-arylmaleamoyl)-4-piperidones: a novel group of cytotoxic agents. J Enzyme Inhib Med Chem 2003; 18: 325-32.
    • (2003) J Enzyme Inhib Med Chem , vol.18 , pp. 325-332
    • Dimmock, J.R.1    Jha, A.2    Zello, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.