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Volumn 2, Issue 4, 2011, Pages 303-308

RNAi-mediated knockdown of α-enolase increases the sensitivity of tumor cells to antitubulin chemotherapeutics

Author keywords

enolase; A549; Antitubulin chemotherapeutics; Cancer; CaOV3; Chemotherapeutic drugs; H460 lung; Knockdown; MCF7 breast; Rnai; Sensitivity

Indexed keywords

ALPHA ENOLASE; ANTINEOPLASTIC AGENT; CISPLATIN; DOCETAXEL; DOXORUBICIN; ETOPOSIDE; MITOXANTRONE; PACLITAXEL; VINBLASTINE; VINCRISTINE;

EID: 84855939630     PISSN: None     EISSN: 21524114     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (22)

References (28)
  • 1
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • Kim JW, Dang CV. Multifaceted roles of glycolytic enzymes. Trends Biochem Sci 2005; 30: 142-150.
    • (2005) Trends Biochem Sci , vol.30 , pp. 142-150
    • Kim, J.W.1    Dang, C.V.2
  • 2
    • 0026757445 scopus 로고
    • Enolases and PGP9.5 as tissue-specific markers
    • IN, D. Enolases and PGP9.5 as tissue-specific markers. Biochem Soc Trans 1992; 20: 637-642.
    • (1992) Biochem Soc Trans , vol.20 , pp. 637-642
    • In, D.1
  • 3
    • 0014896627 scopus 로고
    • Glycogen metabolism and glycolytic enzymes
    • Villar-Palasi C, Larner J. Glycogen metabolism and glycolytic enzymes. Annu Rev Biochem 1970; 39: 639-672.
    • (1970) Annu Rev Biochem , vol.39 , pp. 639-672
    • Villar-Palasi, C.1    Larner, J.2
  • 5
    • 0027949337 scopus 로고
    • Neuron-specific enolase
    • Cooper EH. Neuron-specific enolase. Int J Biol Markers 1994; 9: 205-210.
    • (1994) Int J Biol Markers , vol.9 , pp. 205-210
    • Cooper, E.H.1
  • 6
    • 0020065737 scopus 로고
    • Serum neuron-specific Enolase: A marker for disease extent and response to therapy of small-cell lung cancer
    • Carney DN, Marangos PJ, Ihde DC, Bunn PA, Cohen MH, Minna JD, Gazdar AF. Serum neuron-specific Enolase: a marker for disease extent and response to therapy of small-cell lung cancer. Lancet 1982; 1: 583-585.
    • (1982) Lancet , vol.1 , pp. 583-585
    • Carney, D.N.1    Marangos, P.J.2    Ihde, D.C.3    Bunn, P.A.4    Cohen, M.H.5    Minna, J.D.6    Gazdar, A.F.7
  • 7
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: Its role in diseases
    • Pancholi V. Multifunctional alpha-enolase: its role in diseases. Cell Mol Life Sci 2001; 58: 902-20.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 9
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plas-minogen binding to cells: Identification of alpha -enolase as a candidate plasminogen receptor
    • Miles LA, Dahlberg CM, Plescia J, Felez J, Kato K, Plow EF. Role of cell-surface lysines in plas-minogen binding to cells: identification of alpha -enolase as a candidate plasminogen receptor. Biochemistry 1991; 30: 1682-1691.
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1    Dahlberg, C.M.2    Plescia, J.3    Felez, J.4    Kato, K.5    Plow, E.F.6
  • 10
  • 11
    • 0027403372 scopus 로고
    • Isolation of a novel 45 kDa plasminogen receptor from human endothelial cells
    • Dudani AK, Cummings C, Hashemi S, Ganz PR. Isolation of a novel 45 kDa plasminogen receptor from human endothelial cells. Thromb Res 1993; 69: 185-196.
    • (1993) Thromb Res , vol.69 , pp. 185-196
    • Dudani, A.K.1    Cummings, C.2    Hashemi, S.3    Ganz, P.R.4
  • 12
    • 0024342987 scopus 로고
    • Glycolytic enzyme interactions with tubulin and microtubules
    • Walsh JL, Keith TJ, Knull HR. Glycolytic enzyme interactions with tubulin and microtubules. Biochim Biophys Acta 1989; 999: 64-70.
    • (1989) Biochim Biophys Acta , vol.999 , pp. 64-70
    • Walsh, J.L.1    Keith, T.J.2    Knull, H.R.3
  • 13
    • 0026489887 scopus 로고
    • Association of glycolytic enzymes with the cytoskeleton
    • Knull HR, Walsh JL. Association of glycolytic enzymes with the cytoskeleton. Curr Top Cell Regul 1992; 33: 15-30.
    • (1992) Curr Top Cell Regul , vol.33 , pp. 15-30
    • Knull, H.R.1    Walsh, J.L.2
  • 14
    • 0026693656 scopus 로고
    • Enolase is present at the centrosome of HeLa cells
    • Johnstone SA, Waisman DM, Rattner JB. Enolase is present at the centrosome of HeLa cells. Exp Cell Res 1992; 202: 458-63.
    • (1992) Exp Cell Res , vol.202 , pp. 458-463
    • Johnstone, S.A.1    Waisman, D.M.2    Rattner, J.B.3
  • 15
    • 70350302054 scopus 로고    scopus 로고
    • P-glycoprotein (ABCB1) Modulates Collateral Sensitivity of a Multidrug Resistant Cell Line to Vera-pamil
    • Laberge RM, Ambadipudi R, Georges E. P-glycoprotein (ABCB1) modulates collateral sensitivity of a multidrug resistant cell line to vera-pamil Arch Biochem Biophys 2009; 49: 53-60.
    • (2009) Arch Biochem Biophys , vol.49 , pp. 53-60
    • Laberge, R.M.1    Ambadipudi, R.2    Georges, E.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacterio-phage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacterio-phage T4. Nature 1970; 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0009482260 scopus 로고
    • Electropho-retic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electropho-retic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76: 4350-434.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4434
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 20
    • 0032374058 scopus 로고    scopus 로고
    • Endothelial cell hypoxic stress proteins
    • Graven KK, Farber HW. Endothelial cell hypoxic stress proteins. J Lab Clin Med 1998; 132: 456 -463.
    • (1998) J Lab Clin Med , vol.132 , pp. 456-463
    • Graven, K.K.1    Farber, H.W.2
  • 21
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza GL, Roth PH, Fang HM, Wang GL. Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1. J Biol Chem 1994; 269: 23757-23763.
    • (1994) J Biol Chem , vol.269 , pp. 23757-23763
    • Semenza, G.L.1    Roth, P.H.2    Fang, H.M.3    Wang, G.L.4
  • 23
    • 0033636357 scopus 로고    scopus 로고
    • VEGF: An update on biological and therapeutic aspects
    • Ferrara N. VEGF: an update on biological and therapeutic aspects. Curr Opin Biotechnol 2000; 11: 617-24
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 617-624
    • Ferrara, N.1
  • 25
  • 26
    • 0034100185 scopus 로고    scopus 로고
    • The glycolytic enzyme enolase is present in sperm tail and displays nucleotide-dependent association with microtubules
    • Gitlits VM, Toh BH, Loveland KL, Sentry JW. The glycolytic enzyme enolase is present in sperm tail and displays nucleotide-dependent association with microtubules. Eur J Cell Biol 2000; 79: 104-111.
    • (2000) Eur J Cell Biol , vol.79 , pp. 104-111
    • Gitlits, V.M.1    Toh, B.H.2    Loveland, K.L.3    Sentry, J.W.4
  • 27
    • 0040697068 scopus 로고    scopus 로고
    • Characterization of microtubule-phosphofructokinase complex: Specific effects of MgATP and vinblastine
    • Vertessy BG, Kovacs J, Low P, Lehotzky A, Molnar A, Orosz F, Ovadi J. Characterization of microtubule-phosphofructokinase complex: specific effects of MgATP and vinblastine. Biochemistry 1997; 36: 2051-2062.
    • (1997) Biochemistry , vol.36 , pp. 2051-2062
    • Vertessy, B.G.1    Kovacs, J.2    Low, P.3    Lehotzky, A.4    Molnar, A.5    Orosz, F.6    Ovadi, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.