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Volumn 71, Issue 5, 2005, Pages 2548-2557

Uptake of CdSe and CdSe/ZnS quantum dots into bacteria via purine-dependent mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CADMIUM COMPOUNDS; CELLS; ELECTRON MICROSCOPY; ENZYMES; SIGNAL PROCESSING;

EID: 18444406877     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.5.2548-2557.2005     Document Type: Article
Times cited : (225)

References (34)
  • 2
    • 0022539786 scopus 로고
    • Growth kinetics of individual Bacillus subtilis cells and correlation with nucleoid extension
    • Burdett, I. D., T. B. Kirkwood, and J. B. Whalley. 1986. Growth kinetics of individual Bacillus subtilis cells and correlation with nucleoid extension. J. Bacteriol. 167:219-230.
    • (1986) J. Bacteriol. , vol.167 , pp. 219-230
    • Burdett, I.D.1    Kirkwood, T.B.2    Whalley, J.B.3
  • 3
    • 0030772416 scopus 로고    scopus 로고
    • Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides
    • Chen, S., D. R. Tomchick, D. Wolle, P. Hu, J. L. Smith, R. L. Switzer, and H. Zalkin. 1997. Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides. Biochemistry 36:10718-10726.
    • (1997) Biochemistry , vol.36 , pp. 10718-10726
    • Chen, S.1    Tomchick, D.R.2    Wolle, D.3    Hu, P.4    Smith, J.L.5    Switzer, R.L.6    Zalkin, H.7
  • 6
    • 0030047151 scopus 로고    scopus 로고
    • The permeability of the wall fabric of Escherichia coli and Bacillus subtilis
    • Demchick, P., and A. L. Koch. 1996. The permeability of the wall fabric of Escherichia coli and Bacillus subtilis. J. Bacteriol. 178:768-773.
    • (1996) J. Bacteriol. , vol.178 , pp. 768-773
    • Demchick, P.1    Koch, A.L.2
  • 7
    • 0035882572 scopus 로고    scopus 로고
    • Adenine recognition: A motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins
    • Denessiouk, K. A., V. V. Rantanen, and M. S. Johnson. 2001. Adenine recognition: a motif present in ATP-, CoA-, NAD-, NADP-, and FAD-dependent proteins. Proteins 44:282-291.
    • (2001) Proteins , vol.44 , pp. 282-291
    • Denessiouk, K.A.1    Rantanen, V.V.2    Johnson, M.S.3
  • 8
    • 0842287342 scopus 로고    scopus 로고
    • Probing the cytotoxicity of semiconductor quantum dots
    • Derfus, A. M., W. C. W. Chan, and S. N. Bhatia. 2004. Probing the cytotoxicity of semiconductor quantum dots. Nano Lett. 4:11-18.
    • (2004) Nano Lett. , vol.4 , pp. 11-18
    • Derfus, A.M.1    Chan, W.C.W.2    Bhatia, S.N.3
  • 10
    • 0034941396 scopus 로고    scopus 로고
    • Quantum-dot-tagged microbeads for multiplexed optical coding of biomolecules
    • Han, M., X. Gao, J. Z. Su, and S. Nie. 2001. Quantum-dot-tagged microbeads for multiplexed optical coding of biomolecules. Nat. Biotechnol. 19:631-635.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 631-635
    • Han, M.1    Gao, X.2    Su, J.Z.3    Nie, S.4
  • 11
    • 0035007851 scopus 로고    scopus 로고
    • Assessment of GFP fluorescence in cells of Streptococcus gordonii under conditions of low pH and low oxygen concentration
    • Hansen, M. C., R. J. Palmer, Jr., C. Udsen, D. C. White, and S. Molin. 2001. Assessment of GFP fluorescence in cells of Streptococcus gordonii under conditions of low pH and low oxygen concentration. Microbiology 147:1383-1391.
    • (2001) Microbiology , vol.147 , pp. 1383-1391
    • Hansen, M.C.1    Palmer Jr., R.J.2    Udsen, C.3    White, D.C.4    Molin, S.5
  • 12
    • 0035850513 scopus 로고    scopus 로고
    • Electrochemistry of CdS nanoparticles: A correlation between optical and electrochemical band gaps
    • Haram, S. K., B. M. Quinn, and A. J. Bard. 2001. Electrochemistry of CdS nanoparticles: a correlation between optical and electrochemical band gaps. J. Am. Chem. Soc. 123:8860-8861.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8860-8861
    • Haram, S.K.1    Quinn, B.M.2    Bard, A.J.3
  • 13
    • 0027413114 scopus 로고
    • Characterization of mutations in divIB of Bacillus subtilis and cellular localization of the DivIB protein
    • Harry, E. J., B. J. Stewart, and R. G. Wake. 1993. Characterization of mutations in divIB of Bacillus subtilis and cellular localization of the DivIB protein. Mol. Microbiol. 7:611-621.
    • (1993) Mol. Microbiol. , vol.7 , pp. 611-621
    • Harry, E.J.1    Stewart, B.J.2    Wake, R.G.3
  • 15
    • 4243721522 scopus 로고
    • Size-dependent redox potentials of quantized zinc-oxide measured with an optically transparent thin-layer electrode
    • Hoyer, P., and H. Weller. 1994. Size-dependent redox potentials of quantized zinc-oxide measured with an optically transparent thin-layer electrode. Chem. Phys. Lett. 221:379-384.
    • (1994) Chem. Phys. Lett. , vol.221 , pp. 379-384
    • Hoyer, P.1    Weller, H.2
  • 16
    • 0348087040 scopus 로고    scopus 로고
    • Long-term multiple color imaging of live cells using quantum dot bioconjugates
    • Jaiswal, J. K., H. Mattoussi, J. M. Mauro, and S. M. Simon. 2003. Long-term multiple color imaging of live cells using quantum dot bioconjugates. Nat. Biotechnol. 21:47-51.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 47-51
    • Jaiswal, J.K.1    Mattoussi, H.2    Mauro, J.M.3    Simon, S.M.4
  • 18
    • 0346096860 scopus 로고    scopus 로고
    • Using nanoparticle optics assay for direct observation of the function of antimicrobial agents in single live bacterial cells
    • Kyriacou, S. V., W. J. Brownlow, and X. H. Xu. 2004. Using nanoparticle optics assay for direct observation of the function of antimicrobial agents in single live bacterial cells. Biochemistry 43:140-147.
    • (2004) Biochemistry , vol.43 , pp. 140-147
    • Kyriacou, S.V.1    Brownlow, W.J.2    Xu, X.H.3
  • 20
    • 0018397704 scopus 로고
    • Regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase activity by end products
    • Meyer, E., and R. L. Switzer. 1979. Regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase activity by end products. J. Biol. Chem. 254:5397-5402.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5397-5402
    • Meyer, E.1    Switzer, R.L.2
  • 21
    • 0030297640 scopus 로고    scopus 로고
    • Protein recognition of adenylate: An example of a fuzzy recognition template
    • Moodie, S. L., J. B. Mitchell, and J. M. Thornton. 1996. Protein recognition of adenylate: an example of a fuzzy recognition template. J. Mol. Biol. 263:486-500.
    • (1996) J. Mol. Biol. , vol.263 , pp. 486-500
    • Moodie, S.L.1    Mitchell, J.B.2    Thornton, J.M.3
  • 22
    • 0030029377 scopus 로고    scopus 로고
    • Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis
    • Nygaard, P., P. Duckert, and H. H. Saxild. 1996. Role of adenine deaminase in purine salvage and nitrogen metabolism and characterization of the ade gene in Bacillus subtilis. J. Bacteriol. 178:846-853.
    • (1996) J. Bacteriol. , vol.178 , pp. 846-853
    • Nygaard, P.1    Duckert, P.2    Saxild, H.H.3
  • 23
    • 0038149452 scopus 로고    scopus 로고
    • Comparative study of the growth curves of B. subtilis, K. pneumoniae, C. xerosis and E. coli bacteria in medium containing nanometric silicon particles
    • Péreza, L., M. Floresa, J. Avalosa, L. San Miguel, O. Resto, and L. Fonseca. 2003. Comparative study of the growth curves of B. subtilis, K. pneumoniae, C. xerosis and E. coli bacteria in medium containing nanometric silicon particles. Mat. Res. Soc. Symp. Proc. 737:F3.6.1-F3.6.6.
    • (2003) Mat. Res. Soc. Symp. Proc. , vol.737
    • Péreza, L.1    Floresa, M.2    Avalosa, J.3    San Miguel, L.4    Resto, O.5    Fonseca, L.6
  • 24
    • 1642453597 scopus 로고    scopus 로고
    • An amphiphilic approach to nanocrystal quantum dot-titania nanocomposites
    • Petruska, M. A., A. P. Bartko, and V. I. Klimov. 2004. An amphiphilic approach to nanocrystal quantum dot-titania nanocomposites. J. Am. Chem. Soc. 126:714-715.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 714-715
    • Petruska, M.A.1    Bartko, A.P.2    Klimov, V.I.3
  • 25
    • 1642542400 scopus 로고    scopus 로고
    • Functional expression and characterization of a purine nucleobase transporter gene from Leishmania major
    • Sanchez, M. A., R. Tryon, S. Pierce, G. Vasudevan, and S. M. Landfear. 2004. Functional expression and characterization of a purine nucleobase transporter gene from Leishmania major. Mol. Membr. Biol. 21:11-18.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 11-18
    • Sanchez, M.A.1    Tryon, R.2    Pierce, S.3    Vasudevan, G.4    Landfear, S.M.5
  • 26
    • 0016529714 scopus 로고
    • Control of cell length in Bacillus subtilis
    • Sargent, M. G. 1975. Control of cell length in Bacillus subtilis. J. Bacteriol. 123:7-19.
    • (1975) J. Bacteriol. , vol.123 , pp. 7-19
    • Sargent, M.G.1
  • 27
    • 0023228531 scopus 로고
    • Genetic and physiological characterization of Bacillus subtilis mutants resistant to purine analogs
    • Saxild, H. H., and P. Nygaard. 1987. Genetic and physiological characterization of Bacillus subtilis mutants resistant to purine analogs. J. Bacteriol. 169:2977-2983.
    • (1987) J. Bacteriol. , vol.169 , pp. 2977-2983
    • Saxild, H.H.1    Nygaard, P.2
  • 28
    • 2442686414 scopus 로고    scopus 로고
    • Silver nanoparticles as antimicrobial agent: A case study on E. coli as a model for Gram-negative bacteria
    • Sondi, I., and B. Salopek-Sondi. 2004. Silver nanoparticles as antimicrobial agent: a case study on E. coli as a model for Gram-negative bacteria. J. Colloid Interface Sci. 275:177-182.
    • (2004) J. Colloid Interface Sci. , vol.275 , pp. 177-182
    • Sondi, I.1    Salopek-Sondi, B.2
  • 29
    • 0001615271 scopus 로고
    • Citation classic - Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate
    • Spizizen, J. 1958. Citation classic - transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc. Natl. Acad. Sci. USA 44:1072-1078.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 1072-1078
    • Spizizen, J.1
  • 32
    • 0037389586 scopus 로고    scopus 로고
    • Ring-like pore structures of SecA: Implication for bacterial protein-conducting channels
    • Wang, H. W., Y. Chen, H. Yang, X. Chen, M. X. Duan, P. C. Tai, and S. F. Sui. 2003. Ring-like pore structures of SecA: implication for bacterial protein-conducting channels. Proc. Natl. Acad. Sci. USA 100:4221-4226.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4221-4226
    • Wang, H.W.1    Chen, Y.2    Yang, H.3    Chen, X.4    Duan, M.X.5    Tai, P.C.6    Sui, S.F.7
  • 33
  • 34
    • 0347634258 scopus 로고    scopus 로고
    • Quantum dots as a novel immunofluorescent detection system for Cryptosporidium parvum and Giardia lamblia
    • Zhu, L., S. Ang, and W. T. Liu. 2004. Quantum dots as a novel immunofluorescent detection system for Cryptosporidium parvum and Giardia lamblia. Appl. Environ. Microbiol. 70:597-598.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 597-598
    • Zhu, L.1    Ang, S.2    Liu, W.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.