메뉴 건너뛰기




Volumn 4, Issue 4, 2008, Pages 463-468

Alternative modes of binding of recombinant human histone deacetylase 8 to colloidal gold nanoparticles

Author keywords

Binding; Cancer; Gold nanoparticles; Histone deacetylase

Indexed keywords

BINDING ENERGY; COLLOIDS; DRUG THERAPY; ENZYMES; FLOCCULATION; FLOW INTERACTIONS; GOLD; NANOPARTICLES; PYROLYSIS;

EID: 58149289831     PISSN: 15507033     EISSN: 15507041     Source Type: Journal    
DOI: 10.1166/jbn.2008.011     Document Type: Article
Times cited : (17)

References (29)
  • 1
    • 0034387004 scopus 로고    scopus 로고
    • 25 years after the nucleosome model: Chromatin modifications
    • J. Wu and M. GrunStein, 25 years after the nucleosome model: Chromatin modifications. Trends Biochem. Sci. 25, 619 (2000).
    • (2000) Trends Biochem. Sci , vol.25 , pp. 619
    • Wu, J.1    GrunStein, M.2
  • 2
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • B. D. Strahl and C. D. Allis, The language of covalent histone modifications. Nature 403, 41 (2000).
    • (2000) Nature , vol.403 , pp. 41
    • Strahl, B.D.1    Allis, C.D.2
  • 3
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatment for cancer
    • S. Minucci and P. G. Pelicci, Histone deacetylase inhibitors and the promise of epigenetic (and more) treatment for cancer. Nature Rev. Cancer 6, 38 (2006).
    • (2006) Nature Rev. Cancer , vol.6 , pp. 38
    • Minucci, S.1    Pelicci, P.G.2
  • 5
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylase and cancer
    • M. A. Glozak and E. Seto, Histone deacetylase and cancer. Oncogene 26, 5420 (2007).
    • (2007) Oncogene , vol.26 , pp. 5420
    • Glozak, M.A.1    Seto, E.2
  • 6
    • 33947313218 scopus 로고    scopus 로고
    • HDACs, histone deacetylation and gene transcription: From molecular biology to cancer therapeutics
    • P. Gallinari, S. Di Marco, P. Jones, M. Pallaoro, and C. Steinkuhler, HDACs, histone deacetylation and gene transcription: From molecular biology to cancer therapeutics. Cell Res. 17, 195 (2007).
    • (2007) Cell Res , vol.17 , pp. 195
    • Gallinari, P.1    Di Marco, S.2    Jones, P.3    Pallaoro, M.4    Steinkuhler, C.5
  • 7
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • R. W. Johnstone, Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer. Nature Rev. Drug Discov. 1, 287 (2002).
    • (2002) Nature Rev. Drug Discov , vol.1 , pp. 287
    • Johnstone, R.W.1
  • 8
    • 33846142183 scopus 로고    scopus 로고
    • HDAC inhibitors overcome first hurdle, News feature
    • G. Ken, HDAC inhibitors overcome first hurdle, News feature. Nature Biotechnol. 25, 17 (2007).
    • (2007) Nature Biotechnol , vol.25 , pp. 17
    • Ken, G.1
  • 9
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • I. V. Gregoretti, Y. Lee, and H. V. Goodson, Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis. J. Mol. Bio. 338, 31 (2004).
    • (2004) J. Mol. Bio , vol.338 , pp. 31
    • Gregoretti, I.V.1    Lee, Y.2    Goodson, H.V.3
  • 10
    • 13844252820 scopus 로고    scopus 로고
    • Regulation of histone deacetylase activities
    • N. Sengupta and E. Seto, Regulation of histone deacetylase activities. J. Cell Biochem. 93, 57 (2004).
    • (2004) J. Cell Biochem , vol.93 , pp. 57
    • Sengupta, N.1    Seto, E.2
  • 11
    • 0037382681 scopus 로고    scopus 로고
    • Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression
    • X. J. Yang and E. Seto, Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression. Curr. Opin. Genet. Dev. 13, 143 (2003).
    • (2003) Curr. Opin. Genet. Dev , vol.13 , pp. 143
    • Yang, X.J.1    Seto, E.2
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248 (1976).
    • (1976) Anal. Biochem , vol.72 , pp. 248
    • Bradford, M.M.1
  • 15
    • 0017717846 scopus 로고
    • Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of Concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: A new method, theory and application
    • W. D. Geoghegan and G. A. Ackerman, Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of Concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: A new method, theory and application. J. Hist. Cyt. 25, 1187 (1977).
    • (1977) J. Hist. Cyt , vol.25 , pp. 1187
    • Geoghegan, W.D.1    Ackerman, G.A.2
  • 16
    • 0032502269 scopus 로고    scopus 로고
    • Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-coa, to medium-chain acyl-coenzyme-a dehydrogenase
    • L. Qin and D. K. Srivastava, Energetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-coa, to medium-chain acyl-coenzyme-a dehydrogenase. Biochemistry 37, 3499 (1998).
    • (1998) Biochemistry , vol.37 , pp. 3499
    • Qin, L.1    Srivastava, D.K.2
  • 17
    • 0016760197 scopus 로고
    • Colloidal gold granules as markers for cell surface receptors in the scanning electron microscope
    • M. Horisberger, J. Rosset, and H. Bauer, Colloidal gold granules as markers for cell surface receptors in the scanning electron microscope. Experientia 31, 1147 (1975).
    • (1975) Experientia , vol.31 , pp. 1147
    • Horisberger, M.1    Rosset, J.2    Bauer, H.3
  • 18
    • 4444278825 scopus 로고    scopus 로고
    • Protein surface-assisted enhancement in the binding affinity of an inhibitor for recombinant human carbonic anhydrase-II
    • A. L. Banerjee, M. Swanson, B. C. Roy, X. Jia, M. K. Haldar, S. Mallik, and D. K. Srivastava, Protein surface-assisted enhancement in the binding affinity of an inhibitor for recombinant human carbonic anhydrase-II. J. Am. Chem. Soc. 126, 10875 (2004).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 10875
    • Banerjee, A.L.1    Swanson, M.2    Roy, B.C.3    Jia, X.4    Haldar, M.K.5    Mallik, S.6    Srivastava, D.K.7
  • 19
    • 4644295841 scopus 로고    scopus 로고
    • Kinetics and comparative reactivity of human class I and class IIb histone deacetylases
    • B. E. Schultz, S. Misialek, J. Wu, J. Tang, M. T. Conn, R. Tahilramani, and L. Wong, Kinetics and comparative reactivity of human class I and class IIb histone deacetylases. Biochemistry 43, 11083 (2004).
    • (2004) Biochemistry , vol.43 , pp. 11083
    • Schultz, B.E.1    Misialek, S.2    Wu, J.3    Tang, J.4    Conn, M.T.5    Tahilramani, R.6    Wong, L.7
  • 20
    • 0030939055 scopus 로고    scopus 로고
    • Two dimensional arrangement of a functional protein by cysteine-gold interaction: Enzyme activity and characterization of a protein monolayer on a gold substrate
    • Y. C. Sasaki, K. Yasuda, Y. Suzuki, T. Ishibashi, I. Satoh, Y. Fujiki, and S. Ishiwata, Two dimensional arrangement of a functional protein by cysteine-gold interaction: Enzyme activity and characterization of a protein monolayer on a gold substrate. Biophys. J. 72, 1842 (1997).
    • (1997) Biophys. J , vol.72 , pp. 1842
    • Sasaki, Y.C.1    Yasuda, K.2    Suzuki, Y.3    Ishibashi, T.4    Satoh, I.5    Fujiki, Y.6    Ishiwata, S.7
  • 22
    • 34047259227 scopus 로고    scopus 로고
    • Theoretical study on gold-coated iron oxide nanostructure: Magnetism and bioselectivity for amino acids
    • Q. Sun, B. V. Reddy, M. Marquez, P. Jena, C. Gonzales, and Q. Wang, Theoretical study on gold-coated iron oxide nanostructure: Magnetism and bioselectivity for amino acids. J. Phys. Chem. C 111, 4159 (2007).
    • (2007) J. Phys. Chem. C , vol.111 , pp. 4159
    • Sun, Q.1    Reddy, B.V.2    Marquez, M.3    Jena, P.4    Gonzales, C.5    Wang, Q.6
  • 23
    • 33847216926 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability
    • D. Li, Q. He, Y. Cui, L. Duan, and J. Li, Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability. Biochem. Biophys. Res. Comm. 355, 488 (2007).
    • (2007) Biochem. Biophys. Res. Comm , vol.355 , pp. 488
    • Li, D.1    He, Q.2    Cui, Y.3    Duan, L.4    Li, J.5
  • 24
    • 28844476150 scopus 로고    scopus 로고
    • Cytochrome c superstructure biocomposite nucleated by gold nanoparticle: Thermal stability and voltammetric behaviour
    • X. Jiang, L. Shang, Y. Wang, and S. Dong, Cytochrome c superstructure biocomposite nucleated by gold nanoparticle: Thermal stability and voltammetric behaviour. Biomacromolecules 6, 3030 (2005).
    • (2005) Biomacromolecules , vol.6 , pp. 3030
    • Jiang, X.1    Shang, L.2    Wang, Y.3    Dong, S.4
  • 25
    • 0000400687 scopus 로고
    • Protein adsorption and inactivation on surfaces: Influence of heterogeneities
    • A. Sadana, Protein adsorption and inactivation on surfaces: Influence of heterogeneities. Chem. Rev. 92, 1799 (1992).
    • (1992) Chem. Rev , vol.92 , pp. 1799
    • Sadana, A.1
  • 26
    • 34249048873 scopus 로고    scopus 로고
    • Effect of the surface curvature on the secondary structure of peptide adsorbed on nanoparticles
    • H. S. Mandal and H.-B. Kraatz, Effect of the surface curvature on the secondary structure of peptide adsorbed on nanoparticles. J. Am. Chem. Soc. 129, 6356 (2007).
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 6356
    • Mandal, H.S.1    Kraatz, H.-B.2
  • 27
    • 15744387165 scopus 로고    scopus 로고
    • Gold nanoparticles as a colorimetric sensor for protein conformational changes
    • S. Chah, M. R. Hammond, and R. N. Zare, Gold nanoparticles as a colorimetric sensor for protein conformational changes. Chem. and Biol. 12, 323 (2005).
    • (2005) Chem. and Biol , vol.12 , pp. 323
    • Chah, S.1    Hammond, M.R.2    Zare, R.N.3
  • 28
    • 26444569477 scopus 로고    scopus 로고
    • Probing BSA binding to citrate-coated gold nanoparticles and surfaces
    • S. H. Brewer, W. R. Glomm, M. C. Johnson, M. K. Knag, and S. Franzen, Probing BSA binding to citrate-coated gold nanoparticles and surfaces. Langmuir 21, 9303 (2005).
    • (2005) Langmuir , vol.21 , pp. 9303
    • Brewer, S.H.1    Glomm, W.R.2    Johnson, M.C.3    Knag, M.K.4    Franzen, S.5
  • 29
    • 0037051601 scopus 로고    scopus 로고
    • Selective binding of mannose-encapsulated gold nanoparticles to type 1 pili in Escherichia coli
    • C. Lin, Y.-C. Yeh, C.-Y. Yang, C.-L. Chen, G.-F. Chen, C. Chen, and Y. Wu, Selective binding of mannose-encapsulated gold nanoparticles to type 1 pili in Escherichia coli. J. Am. Chem. Soc. 124, 3508 (2002).
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 3508
    • Lin, C.1    Yeh, Y.-C.2    Yang, C.-Y.3    Chen, C.-L.4    Chen, G.-F.5    Chen, C.6    Wu, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.