메뉴 건너뛰기




Volumn 8976, Issue , 2014, Pages

Rapid detection of tuberculosis using droplet-based microfluidics

Author keywords

[No Author keywords available]

Indexed keywords

BACILLI; BACTERIOLOGY; BIOMEMS; DROPS; ENZYMES; MICROFLUIDICS; MICROSYSTEMS;

EID: 84900557051     PISSN: 0277786X     EISSN: 1996756X     Source Type: Conference Proceeding    
DOI: 10.1117/12.2038533     Document Type: Conference Paper
Times cited : (3)

References (26)
  • 1
    • 84900541124 scopus 로고    scopus 로고
    • WHO. Global tuberculosis control 2011b
    • WHO. Global tuberculosis control 2011b. http://www. who. int/tb/publications/global-report/ en/2011.
  • 2
    • 79951654084 scopus 로고    scopus 로고
    • Xpert((R)) MTB/RIF for point-of-care diagnosis of TB in high-HIV burden, resource-limited countries: Hype or hope
    • Van Rie, A. Page-Shipp L, Scott L, Sanne I, Stevens W. Xpert((R)) MTB/RIF for point-of-care diagnosis of TB in high-HIV burden, resource-limited countries: hype or hope? Expert Rev. Mol. Diagn. 2010;10:937-46.
    • (2010) Expert Rev. Mol. Diagn. , vol.10 , pp. 937-946
    • Van Rie1    Page-Shipp L, A.2    Scott, L.3    Sanne, I.4    Stevens, W.5
  • 3
    • 84900556322 scopus 로고    scopus 로고
    • WHO/Global Fund. Partners call for increased commitment to tackle MDR-TB.
    • WHO/Global Fund. Partners call for increased commitment to tackle MDR-TB. 2011c. http://www. who. int/mediacentre/news/releases/2011/TBday-20110322/en/ index. html.
    • (2011)
  • 4
    • 77957018729 scopus 로고    scopus 로고
    • Advances in developing HIV-1 viral load assays for resource-limited settings
    • Wang S, Xu F, Demirci U. Advances in developing HIV-1 viral load assays for resource-limited settings. Biotechnol Adv 2010;28:770-81.
    • (2010) Biotechnol Adv , vol.28 , pp. 770-781
    • Wang, S.1    Xu, F.2    Demirci, U.3
  • 5
    • 77954859965 scopus 로고    scopus 로고
    • Uniform amplification of phage with different growth characteristics in individual compartments consisting of monodisperse droplets
    • Derda, R. Tang, S. K. Y. Whitesides G. M., Uniform Amplification of Phage with Different Growth Characteristics in Individual Compartments Consisting of Monodisperse Droplets. Angewandte Chemie-International Edition, 2010, 49(31), 5301-5304.
    • (2010) Angewandte Chemie-International Edition , vol.49 , Issue.31 , pp. 5301-5304
    • Derda, R.1    Tang, G.M.2    Whitesides, S.K.Y.3
  • 7
    • 79851500938 scopus 로고    scopus 로고
    • Continuously tunable microdropletlaser in a microfluidic channel
    • Tang, S. K. Y., Derda, R. Quan, Q. M. Loncar, M. Whitesides G. M., Continuously tunable microdropletlaser in a microfluidic channel. Optics. Express, 2011, 19(3), 2204-2215.
    • (2011) Optics. Express , vol.19 , Issue.3 , pp. 2204-2215
    • Tang, S.K.Y.1    Derda, R.2    Quan, Q.M.3    Loncar, M.4    Whitesides, G.M.5
  • 9
    • 18144420092 scopus 로고    scopus 로고
    • Mechanism for flow-rate controlled breakup in confined geometries: A role to monodisperse emulsions
    • Garstecki, P. Stone H. A. Whitesides G. M., Mechanism for flow-rate controlled breakup in confined geometries: A role to monodisperse emulsions. Phys. Rev. Letters, 2005, 94(16).
    • (2005) Phys. Rev. Letters , vol.94 , Issue.16
    • Garstecki, H.A.1    Stone, P.2    Whitesides, G.M.3
  • 10
    • 64649083723 scopus 로고    scopus 로고
    • Independent control of drop size and velocity in microfluidic flow-focusing generators using variable temperature and flow rate
    • Stan, C. A. Tang, S. K. Y. Whitesides, G. M., Independent control of drop size and velocity in microfluidic flow-focusing generators using variable temperature and flow rate. Anal. Chem., 2009, 81(6), 2399-2402.
    • (2009) Anal. Chem. , vol.81 , Issue.6 , pp. 2399-2402
    • Stan, C.A.1    Tang, S.K.Y.2    Whitesides, G.M.3
  • 12
    • 14044262957 scopus 로고    scopus 로고
    • Genetic analysis of the beta-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to beta-lactam antibiotics
    • Flores, A. R. Parson, L. M. Pavelka, M. S. Jr, Genetic analysis of the beta-lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to beta-lactam antibiotics. Microbiology, 2005, 151, 521-532.
    • (2005) Microbiology , vol.151 , pp. 521-532
    • Flores, A.1    Parson, A.R.2    Pavelka, L.M.3
  • 13
    • 61349183785 scopus 로고    scopus 로고
    • Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis
    • Hugonnet, J. E. Tremblay, L. W. Boshoff, H. I. Barry, C. E. II, Blanchard, J. S., Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis. Science, 2009, 323, 1215-1218.
    • (2009) Science , vol.323 , pp. 1215-1218
    • Hugonnet1    Tremblay, J.E.2    Boshoff, L.W.3    Barry, H.I.4    Ii, C.E.5    Blanchard, J.S.6
  • 14
    • 0018656310 scopus 로고
    • Electronic structures of cephalosporins andpenicillins. 9. Departure of a leaving group in cephalosporins
    • Boyd, D. B. Lunn, W. H., Electronic structures of cephalosporins andpenicillins. 9. Departure of a leaving group in cephalosporins. J. Med. Chem. 1979, 22, 778-784.
    • (1979) J. Med. Chem. , vol.22 , pp. 778-784
    • Boyd1    Lunn W H, D.B.2
  • 15
    • 0021341894 scopus 로고
    • Elimination of a good leaving group from the 3'-position of a cephalosporin need not be concerted with beta-lactam ring-opening-TEM-2 beta-lactamase-catalyzed hydrolysis of pyridine-2-azo-4'-(N',N'-dimethylaniline) cephalosporin (PADAC) and of cephaloridine
    • Faraci, W. S. Pratt, R. F., Elimination of a good leaving group from the 3'-position of a cephalosporin need not be concerted with beta-lactam ring-opening-TEM-2 beta-lactamase-catalyzed hydrolysis of pyridine-2-azo-4'-(N', N'-dimethylaniline) cephalosporin (PADAC) and of cephaloridine. J. Am. Chem. Soc. 1984, 106, 1489-1490.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 1489-1490
    • Faraci1    Pratt R F, W.S.2
  • 16
    • 0021970057 scopus 로고
    • Mechanism of inhibition of the PC1 beta-lactamase of Staphylococcus aureus by cephalosporins: Importance of the 3'-leaving group
    • Faraci,W. S. Pratt, R. F. Mechanism of inhibition of the PC1 beta-lactamase of Staphylococcus aureus by cephalosporins: importance of the 3'-leaving group. Biochemistry, 1985, 24, 903-910.
    • (1985) Biochemistry , vol.24 , pp. 903-910
    • Faraci1    Pratt R F, W.S.2
  • 17
    • 0022481301 scopus 로고
    • Direct observation by proton NMR of cephalosporoate intermediates in aqueous solution during the hydrazinolysis and beta-lactamasecatalyzed hydrolysis of cephalosporins with 3' leaving groups: Kinetics and equilibria of the 3' elimination reaction
    • Pratt, R. F. Faraci,W. S. Direct observation by proton NMR of cephalosporoate intermediates in aqueous solution during the hydrazinolysis and beta-lactamasecatalyzed hydrolysis of cephalosporins with 3' leaving groups: kinetics and equilibria of the 3' elimination reaction. J. Am. Chem. Soc. 1986, 108, 5328-5333.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 5328-5333
    • Pratt1    Faraci W S, R.F.2
  • 18
    • 0032472195 scopus 로고    scopus 로고
    • Quantitation of transcription and clonal selection of single living cells with betalactamase as reporter
    • Zlokarnik, G. et al. Quantitation of transcription and clonal selection of single living cells with betalactamase as reporter. Science, 1998, 279, 84-88.
    • (1998) Science , vol.279 , pp. 84-88
    • Zlokarnik, G.1
  • 19
    • 0043195272 scopus 로고    scopus 로고
    • Novel fluorogenic substrates for imaging beta-lactamase gene expression
    • Gao, W., Xing, B., Tsien, R. Y., Rao, J. Novel fluorogenic substrates for imaging beta-lactamase gene expression. J. Am. Chem. Soc. 2003, 125, 11146-11147.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11146-11147
    • Gao, W.1    Xing, B.2    Tsien, R.Y.3    Rao, J.4
  • 20
    • 16244375539 scopus 로고    scopus 로고
    • Cell-permeable near-infrared fluorogenic substrates for imaging betalactamase activity
    • Xing, B., Khanamiryan, A., Rao, J. Cell-permeable near-infrared fluorogenic substrates for imaging betalactamase activity. J. Am. Chem. Soc. 2005, 127, 4158-4159.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4158-4159
    • Xing, B.1    Khanamiryan, A.2    Rao, J.3
  • 21
    • 34848887128 scopus 로고    scopus 로고
    • A bioluminogenic substrate for in vivo imaging of beta-lactamase activity
    • Yao, H., So, M. K., Rao, J. A bioluminogenic substrate for in vivo imaging of beta-lactamase activity. Angew. Chem. Int. Ed. 2007, 46, 7031-7034.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 7031-7034
    • Yao, H.1    So, M.K.2    Rao, J.3
  • 22
    • 80054987081 scopus 로고    scopus 로고
    • Fluorogenic cephalosporin substrates for betalactamase TEM-1
    • Rukavishnikov, A., Gee, K. R., Johnson, I. Corry, S. Fluorogenic cephalosporin substrates for betalactamase TEM-1. Anal. Biochem. 2011, 419, 9-16.
    • (2011) Anal. Biochem. , vol.419 , pp. 9-16
    • Rukavishnikov, A.1    Gee, K.R.2    Johnson3    Corry S, I.4
  • 23
    • 77955461146 scopus 로고    scopus 로고
    • Imaging tuberculosis with endogenous beta-lactamase reporter enzyme fluorescence in live mice
    • Kong, Y. et al. Imaging tuberculosis with endogenous beta-lactamase reporter enzyme fluorescence in live mice. Proc. Natl Acad. Sci. USA, 2010, 107, 12239-12244.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 12239-12244
    • Kong, Y.1
  • 26
    • 84868546870 scopus 로고    scopus 로고
    • Characterization of sensitivity and specificity in leaky droplet-based assays
    • Chen, Y. Gani, A. W. Tang, S. K. Y., Characterization of sensitivity and specificity in leaky droplet-based assays, Lab on Chip, 2012, 12, 5093-5103.
    • (2012) Lab on Chip , vol.12 , pp. 5093-5103
    • Chen, Y.1    Gani, A.W.2    Tang, S.K.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.