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Volumn 75, Issue 9, 2008, Pages 1743-1750

A facile method to screen inhibitors of protein-protein interactions including MDM2-p53 displayed on T7 phage

Author keywords

Dehydroaltenusin; MDM2; Nutlin 3; p53; Phage display; Protein protein interaction

Indexed keywords

NUTLIN 3; PROTEIN MDM2; PROTEIN P53;

EID: 41949120825     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.01.020     Document Type: Article
Times cited : (14)

References (23)
  • 1
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • Rual J.F., Venkatesan K., Hao T., Hirozane-Kishikawa T., Dricot A., Li N., et al. Towards a proteome-scale map of the human protein-protein interaction network. Nature 437 (2005) 1173-1178
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Rual, J.F.1    Venkatesan, K.2    Hao, T.3    Hirozane-Kishikawa, T.4    Dricot, A.5    Li, N.6
  • 2
    • 0035369531 scopus 로고    scopus 로고
    • Protein-protein interaction maps: a lead towards cellular functions
    • Legrain P., Wojcik J., and Gauthier J.M. Protein-protein interaction maps: a lead towards cellular functions. Trends Genet 17 (2001) 346-352
    • (2001) Trends Genet , vol.17 , pp. 346-352
    • Legrain, P.1    Wojcik, J.2    Gauthier, J.M.3
  • 3
    • 25144498379 scopus 로고    scopus 로고
    • A human protein-protein interaction network, a resource for annotating the proteome
    • Stelzl U., Worm U., Lalowski M., Haenig C., Brembeck F.H., Goehler H., et al. A human protein-protein interaction network, a resource for annotating the proteome. Cell 122 (2005) 957-968
    • (2005) Cell , vol.122 , pp. 957-968
    • Stelzl, U.1    Worm, U.2    Lalowski, M.3    Haenig, C.4    Brembeck, F.H.5    Goehler, H.6
  • 4
    • 0034714420 scopus 로고    scopus 로고
    • Genome-wide protein interaction maps using two-hybrid systems
    • Legrain P., and Selig L. Genome-wide protein interaction maps using two-hybrid systems. FEBS Lett 480 (2000) 32-36
    • (2000) FEBS Lett , vol.480 , pp. 32-36
    • Legrain, P.1    Selig, L.2
  • 5
    • 33744974524 scopus 로고    scopus 로고
    • p53 and its downstream proteins as molecular targets of cancer
    • Sun Y. p53 and its downstream proteins as molecular targets of cancer. Mol Carcinog 45 (2006) 409-415
    • (2006) Mol Carcinog , vol.45 , pp. 409-415
    • Sun, Y.1
  • 6
    • 22244443786 scopus 로고    scopus 로고
    • p53 activation by small molecules: application in oncology
    • Vassilev L.T. p53 activation by small molecules: application in oncology. J Med Chem 48 (2005) 4491-4499
    • (2005) J Med Chem , vol.48 , pp. 4491-4499
    • Vassilev, L.T.1
  • 7
    • 33745645832 scopus 로고    scopus 로고
    • Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy
    • Lu Y., Coleska Z.N., Fang X., Gao W., Shangary S., Qiu S., et al. Discovery of a nanomolar inhibitor of the human murine double minute 2 (MDM2)-p53 interaction through an integrated, virtual database screening strategy. J Med Chem 49 (2006) 3759-3762
    • (2006) J Med Chem , vol.49 , pp. 3759-3762
    • Lu, Y.1    Coleska, Z.N.2    Fang, X.3    Gao, W.4    Shangary, S.5    Qiu, S.6
  • 9
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev L.T., Vu B.T., Graves B., Carvajal D., Podlaski F., Filipovic Z., et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 303 (2004) 844-848
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3    Carvajal, D.4    Podlaski, F.5    Filipovic, Z.6
  • 10
    • 33846449110 scopus 로고    scopus 로고
    • Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G
    • Moerke N.J., Aktas H., Chen H., Cantel S., Reibarkh M.Y., Fahmy A., et al. Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell 128 (2007) 257-267
    • (2007) Cell , vol.128 , pp. 257-267
    • Moerke, N.J.1    Aktas, H.2    Chen, H.3    Cantel, S.4    Reibarkh, M.Y.5    Fahmy, A.6
  • 13
    • 33747800052 scopus 로고    scopus 로고
    • T7 lytic phage-displayed peptide libraries exhibit less sequence bias than M13 filamentous phage-displayed peptide libraries
    • Krumpe L.R., Atkinson A.J., Smythers G.W., Kandel A., Schumacher K.M., McMahon J.B., et al. T7 lytic phage-displayed peptide libraries exhibit less sequence bias than M13 filamentous phage-displayed peptide libraries. Proteomics 6 (2006) 4210-4222
    • (2006) Proteomics , vol.6 , pp. 4210-4222
    • Krumpe, L.R.1    Atkinson, A.J.2    Smythers, G.W.3    Kandel, A.4    Schumacher, K.M.5    McMahon, J.B.6
  • 14
    • 28444469838 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging-based protein arrays for high-throughput screening of protein-protein interaction inhibitors
    • Jung S.O., Ro H.S., Kho B.H., Shin Y.B., Kim M.G., and Chung B.H. Surface plasmon resonance imaging-based protein arrays for high-throughput screening of protein-protein interaction inhibitors. Proteomics 5 (2005) 4427-4431
    • (2005) Proteomics , vol.5 , pp. 4427-4431
    • Jung, S.O.1    Ro, H.S.2    Kho, B.H.3    Shin, Y.B.4    Kim, M.G.5    Chung, B.H.6
  • 15
    • 33645742269 scopus 로고    scopus 로고
    • A high-throughput phage display screening method using a combination of real-time PCR and affinity chromatography
    • Morohashi K., Arai T., Saito S., Watanabe M., Sakaguchi K., and Sugawara F. A high-throughput phage display screening method using a combination of real-time PCR and affinity chromatography. Comb Chem High Throughput Screen 9 (2006) 55-61
    • (2006) Comb Chem High Throughput Screen , vol.9 , pp. 55-61
    • Morohashi, K.1    Arai, T.2    Saito, S.3    Watanabe, M.4    Sakaguchi, K.5    Sugawara, F.6
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 33644867888 scopus 로고    scopus 로고
    • Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display
    • Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., et al. Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display. J Biol Chem 281 (2005) 1137-1144
    • (2005) J Biol Chem , vol.281 , pp. 1137-1144
    • Xie, B.1    Tassi, E.2    Swift, M.R.3    McDonnell, K.4    Bowden, E.T.5    Wang, S.6
  • 19
    • 33749378169 scopus 로고    scopus 로고
    • Determinants of specificity of MDM2 for the activation domains of p53 and p65 proline27 disrupts the MDM-binding motif of p53
    • Zondlo S.C., Lee A.E., and Aondlo N.J. Determinants of specificity of MDM2 for the activation domains of p53 and p65 proline27 disrupts the MDM-binding motif of p53. Biochemistry 45 (2006) 11945-11957
    • (2006) Biochemistry , vol.45 , pp. 11945-11957
    • Zondlo, S.C.1    Lee, A.E.2    Aondlo, N.J.3
  • 20
    • 19944431684 scopus 로고    scopus 로고
    • The effects of dehydroaltenusin, a novel mammalian DNA polymerase alpha inhibitor, on cell proliferation and cell cycle progression
    • Murakami-Nakai C., Maeda N., Yonezawa Y., Kuriyama I., Kamisuki S., Takahashi S., et al. The effects of dehydroaltenusin, a novel mammalian DNA polymerase alpha inhibitor, on cell proliferation and cell cycle progression. Biochim Biophys Acta 1674 (2004) 193-199
    • (2004) Biochim Biophys Acta , vol.1674 , pp. 193-199
    • Murakami-Nakai, C.1    Maeda, N.2    Yonezawa, Y.3    Kuriyama, I.4    Kamisuki, S.5    Takahashi, S.6
  • 21
    • 33751558603 scopus 로고    scopus 로고
    • Anti-tumor effects of dehydroaltenusin, a specific inhibitor of mammalian DNA polymerase alpha
    • Maeda N., Kokai Y., Ohtani S., Sahara H., Kuriyama I., Kamisuki S., et al. Anti-tumor effects of dehydroaltenusin, a specific inhibitor of mammalian DNA polymerase alpha. Biochem Biophys Res Commun 352 (2007) 390-396
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 390-396
    • Maeda, N.1    Kokai, Y.2    Ohtani, S.3    Sahara, H.4    Kuriyama, I.5    Kamisuki, S.6
  • 23
    • 0029339184 scopus 로고
    • Isolation of myosin light chain kinase inhibitors from microorganisms: dehydroaltenusin, altenusin, atrovenetinone, and cyclooctasulfur
    • Nakanishi S., Toki S., Saitoh Y., Tsukuda E., Kawahara K., Ando K., et al. Isolation of myosin light chain kinase inhibitors from microorganisms: dehydroaltenusin, altenusin, atrovenetinone, and cyclooctasulfur. Biosci Biotechnol Biochem 59 (1995) 1333-1335
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 1333-1335
    • Nakanishi, S.1    Toki, S.2    Saitoh, Y.3    Tsukuda, E.4    Kawahara, K.5    Ando, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.