메뉴 건너뛰기




Volumn 23, Issue 4, 2012, Pages 714-724

Site-specific immobilization of enzymes on magnetic nanoparticles and their use in organic synthesis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COENZYMES; DECOMPOSITION; ENZYME IMMOBILIZATION; ENZYME KINETICS; NANOMAGNETICS; SYNTHESIS (CHEMICAL);

EID: 84859998434     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc200396r     Document Type: Article
Times cited : (86)

References (64)
  • 2
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • DOI 10.1038/35051706
    • Koeller, K. M., and Wong, C.-H. (2001) Enzymes for chemical synthesis. Nature 409, 232-240. (Pubitemid 32146169)
    • (2001) Nature , vol.409 , Issue.6817 , pp. 232-240
    • Koeller, K.M.1    Wong, C.-H.2
  • 3
    • 0035843170 scopus 로고    scopus 로고
    • Industrial biocatalysis today and tomorrow
    • DOI 10.1038/35051736
    • Schmid, A., Dordick, J. S., Hauer, B., Kiener, A., Wubbolt, M., and Witholt, B. (2001) Industrial biocatalysis today and tomorrow. Nature 409, 258-268. (Pubitemid 32144296)
    • (2001) Nature , vol.409 , Issue.6817 , pp. 258-268
    • Schmid, A.1    Dordick, J.S.2    Hauer, B.3    Kiener, A.4    Wubbolts, M.5    Witholt, B.6
  • 4
  • 5
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: The quest for optimum performance
    • Sheldon, R. A. (2007) Enzyme immobilization: the quest for optimum performance. Adv. Synth. Catal. 349, 1289-1307.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 7
    • 33947602594 scopus 로고    scopus 로고
    • Improvement of enzyme activity, stability and selectivity via immobilization techniques
    • DOI 10.1016/j.enzmictec.2007.01.018, PII S0141022907000506
    • Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., and Fernandez-Lafuente, R. (2007) Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb. Technol. 40, 1451-1463. (Pubitemid 46482654)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.6 , pp. 1451-1463
    • Mateo, C.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 8
    • 16244405562 scopus 로고    scopus 로고
    • Immobilised enzymes: Science or art?
    • Cao, L. (2005) Immobilised enzymes: science or art? Curr. Opin. Chem. Biol. 9, 217-226.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 217-226
    • Cao, L.1
  • 10
    • 70349089061 scopus 로고    scopus 로고
    • Recyclable nanobiocatalyst for enantioselective sulfoxidation: Facile fabrication and high performance of chloroperoxidase-coated magnetic nanoparticles with iron oxide core and polymer shell
    • Wang, W., Xu, Y., Wang, D. I. C., and Li, Z. (2009) Recyclable nanobiocatalyst for enantioselective sulfoxidation: facile fabrication and high performance of chloroperoxidase-coated magnetic nanoparticles with iron oxide core and polymer shell. J. Am. Chem. Soc. 131, 12892-12893.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12892-12893
    • Wang, W.1    Xu, Y.2    Wang, D.I.C.3    Li, Z.4
  • 13
    • 4043089079 scopus 로고    scopus 로고
    • Dopamine as a robust anchor to immobilize functional molecules on the iron oxide shell of magnetic nanoparticles
    • DOI 10.1021/ja0464802
    • Xu, C., Xu, K., Gu, H., Zheng, R., Liu, H., Zhang, X., Guo, Z., and Xu, B. (2004) Dopamine as a robust anchor to immobilize functional molecules on the iron oxide shell of magnetic nanoparticles. J. Am. Chem. Soc. 126, 9938-9939. (Pubitemid 39079411)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.32 , pp. 9938-9939
    • Xu, C.1    Xu, K.2    Gu, H.3    Zheng, R.4    Liu, H.5    Zhang, X.6    Guo, Z.7    Xu, B.8
  • 14
    • 0035819944 scopus 로고    scopus 로고
    • Sugar nucleotide regeneration beads (superbeads): A versatile tool for the practical synthesis of oligosaccharides [12]
    • DOI 10.1021/ja005738v
    • Chen, X., Fang, J., Zhang, J., Liu, Z., Shao, J., Kowal, P., Andreana, P., and Wang, G. P. (2001) Sugar nucleotide regeneration seads (Superbeads): a versatile tool for the practical synthesis of oligosaccharides. J. Am. Chem. Soc. 123, 2081-2082. (Pubitemid 32200039)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.9 , pp. 2081-2082
    • Chen, X.1    Fang, J.2    Zhang, J.3    Liu, Z.4    Shao, J.5    Kowal, P.6    Andreana, P.7    Wang, P.G.8
  • 15
    • 0242466425 scopus 로고    scopus 로고
    • An engineered biocatalyst for the synthesis of glycoconjugates: Utilization of β-1,3-N-acetyl-D-glucosaminyltransferase from Streptococcus agalactiae type Ia expressed in Escherichia coli as a fusion with maltosebinding protein
    • Toda, A., Yamada, K., and Nishimura, S.-I. (2002) An engineered biocatalyst for the synthesis of glycoconjugates: utilization of β-1,3-N-acetyl-D-glucosaminyltransferase from Streptococcus agalactiae type Ia expressed in Escherichia coli as a fusion with maltosebinding protein. Adv. Synth. Catal. 344, 61-69.
    • (2002) Adv. Synth. Catal. , vol.344 , pp. 61-69
    • Toda, A.1    Yamada, K.2    Nishimura, S.-I.3
  • 17
    • 34547535401 scopus 로고    scopus 로고
    • Specifically immobilised Aldo/Keto reductase AKR1A1 shows a dramatic increase in activity relative to the randomly immobilised enzyme
    • DOI 10.1002/cbic.200700056
    • Holland-Nell, K., and Beck-Sickinger, A. G. (2007) Specifically immobilised aldo/keto reductase AKR1A1 shows a dramatic increase in activity relative to the randomly immobilised enzyme. Chem- BioChem 8, 1071-1076. (Pubitemid 47183624)
    • (2007) ChemBioChem , vol.8 , Issue.9 , pp. 1071-1076
    • Holland-Nell, K.1    Beck-Sickinger, A.G.2
  • 19
    • 70349084150 scopus 로고    scopus 로고
    • Selective covalent protein immobilization: Strategies and applications
    • Wong, L. S., Khan, F., and Micklefield, J. (2009) Selective covalent protein immobilization: strategies and applications. Chem. Rev. 109, 4025-4053.
    • (2009) Chem. Rev. , vol.109 , pp. 4025-4053
    • Wong, L.S.1    Khan, F.2    Micklefield, J.3
  • 20
    • 3042546498 scopus 로고    scopus 로고
    • Labeling proteins with small molecules by site-specific posttranslational modification
    • DOI 10.1021/ja047749k
    • Yin, J., Liu, F., Li, X., and Walsh, C. T. (2004) Labeling proteins with small molecules by site-specific posttranslational modification. J. Am. Chem. Soc. 126, 7754-7755. (Pubitemid 38812749)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.25 , pp. 7754-7755
    • Yin, J.1    Liu, F.2    Li, X.3    Walsh, C.T.4
  • 22
    • 33746329936 scopus 로고    scopus 로고
    • Regio- and chemoselective covalent immobilization of proteins through unnatural amino acids
    • DOI 10.1021/ja061131o
    • Gauchet, C., Labadie, G. R., and Poulter, C. D. (2006) Regioand chemoselective covalent immobilization of proteins through unnatural amino acids. J. Am. Chem. Soc. 128, 9274-9275. (Pubitemid 44117054)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.29 , pp. 9274-9275
    • Gauchet, C.1    Labadie, G.R.2    Poulter, C.D.3
  • 23
    • 77949533713 scopus 로고    scopus 로고
    • Highly oriented recombinant glycosyltransferases: Site-specific immobilization of unstable membrane proteins by using Staphylococcus aureus sortase A
    • Ito, T., Sadamoto, R., Naruchi, K., Togame, H., Takemoto, H., Kondo, H., and Nishimura, S.-I. (2010) Highly oriented recombinant glycosyltransferases: site-specific immobilization of unstable membrane proteins by using Staphylococcus aureus sortase A. Biochemistry 49, 2604-2614.
    • (2010) Biochemistry , vol.49 , pp. 2604-2614
    • Ito, T.1    Sadamoto, R.2    Naruchi, K.3    Togame, H.4    Takemoto, H.5    Kondo, H.6    Nishimura, S.-I.7
  • 24
    • 34249073784 scopus 로고    scopus 로고
    • Exploring enzymatic catalysis at a solid surface: A case study with transglutaminase-mediated protein immobilization
    • DOI 10.1039/b701595j
    • Tanaka, Y., Tsuruda, Y., Nishi, M., Kamiya, N., and Goto, M. (2007) Exploring enzymatic catalysis at a solid surface: a case study with transglutaminase-mediated protein immobilization. Org. Biomol. Chem. 5, 1764-1770. (Pubitemid 46794167)
    • (2007) Organic and Biomolecular Chemistry , vol.5 , Issue.11 , pp. 1764-1770
    • Tanaka, Y.1    Tsuruda, Y.2    Nishi, M.3    Kamiya, N.4    Goto, M.5
  • 25
    • 33746311225 scopus 로고    scopus 로고
    • Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing
    • DOI 10.1002/anie.200503475
    • Kwon, Y., Coleman, M. A., and Camarero, J. A. (2006) Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing. Angew. Chem., Int. Ed. 45, 1726-1729. (Pubitemid 44105240)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.11 , pp. 1726-1729
    • Kwon, Y.1    Coleman, M.A.2    Camarero, J.A.3
  • 30
    • 8844258757 scopus 로고    scopus 로고
    • Chemoselective attachment of biologically active proteins to surfaces by expressed protein ligation and its application for "protein chip" fabrication
    • DOI 10.1021/ja0456611
    • Camarero, J. A., Kwon, Y., and Coleman, M. A. (2004) Chemoselective attachment of biologically active proteins to surfaces by expressed protein ligation and its application for "protein chip" fabrication. J. Am. Chem. Soc. 126, 14730-14731. (Pubitemid 39532148)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.45 , pp. 14730-14731
    • Camarero, J.A.1    Kwon, Y.2    Coleman, M.A.3
  • 31
    • 35348985488 scopus 로고    scopus 로고
    • Site-specific protein and peptide immobilization on a biosensor surface by pulsed native chemical ligation
    • DOI 10.1002/cbic.200700355
    • Helms, B., van Baal, I., Merkx, M., and Meijer, E. W. (2007) Site-specific protein and peptide immobilization on a biosensor surface by pulsed native chemical ligation. ChemBioChem 8, 1790-1794. (Pubitemid 47612867)
    • (2007) ChemBioChem , vol.8 , Issue.15 , pp. 1790-1794
    • Helms, B.1    Van Baal, I.2    Merkx, M.3    Meijer, E.W.4
  • 32
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality
    • Sletten, E. M., and Bertozzi, C. R. (2009) Bioorthogonal chemistry: fishing for selectivity in a sea of functionality. Angew. Chem., Int. Ed. 48, 6974-6998.
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 33
    • 47249140441 scopus 로고    scopus 로고
    • Magnetic iron oxide nanoparticles: Synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications
    • Laurent, S., Forge, D., Port, M., Roch, A., Robic, C., Vander Elst, L., and Muller, R. (2008) Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem. Rev. 108, 2064-2110.
    • (2008) Chem. Rev. , vol.108 , pp. 2064-2110
    • Laurent, S.1    Forge, D.2    Port, M.3    Roch, A.4    Robic, C.5    Vander Elst, L.6    Muller, R.7
  • 34
    • 11044222650 scopus 로고    scopus 로고
    • Synthesis and surface engineering of iron oxide nanoparticles for biomedical applications
    • DOI 10.1016/j.biomaterials.2004.10.012, PII S0142961204009317
    • Gupta, A. K., and Gupta, M. (2005) Synthesis and surface engineering of iron oxide nanoparticles for biomedical applications. Biomaterials 26, 3995-4021. (Pubitemid 40044762)
    • (2005) Biomaterials , vol.26 , Issue.18 , pp. 3995-4021
    • Gupta, A.K.1    Gupta, M.2
  • 35
    • 35548999721 scopus 로고    scopus 로고
    • Thermally cross-linked superparamagnetic iron oxide nanoparticles: Synthesis and application as a dual imaging probe for cancer in vivo
    • DOI 10.1021/ja072210i
    • Lee, H., Yu, M. K., Park, S., Moon, S., Min, J. J., Jeong, Y. Y., Kang, H.-W., and Jon, S. (2007) Thermally cross-linked superparamagnetic iron oxide nanoparticles: synthesis and application as a dual imaging probe for cancer in vivo. J. Am. Chem. Soc. 129, 12739-12745. (Pubitemid 350004485)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.42 , pp. 12739-12745
    • Lee, H.1    Mi, K.Y.2    Park, S.3    Moon, S.4    Jung, J.M.5    Yong, Y.J.6    Kang, H.-W.7    Jon, S.8
  • 36
    • 0346995010 scopus 로고    scopus 로고
    • Using Biofunctional Magnetic Nanoparticles to Capture Vancomycin-Resistant Enterococci and Other Gram-Positive Bacteria at Ultralow Concentration
    • DOI 10.1021/ja0359310
    • Gu, H., Ho, P.-L., Tsang, K. W. T., Wang, L., and Xu, B. (2003) Using biofunctional magnetic nanoparticles to capture vancomycin-resistant enterococci and other Gram-positive bacteria at ultralow concentration. J. Am. Chem. Soc. 125, 15702-15703. (Pubitemid 37553661)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.51 , pp. 15702-15703
    • Gu, H.1    Ho, P.-L.2    Tsang, K.W.T.3    Wang, L.4    Xu, B.5
  • 37
    • 35948933369 scopus 로고    scopus 로고
    • Magnetic glyco-nanoparticles: A unique tool for rapid pathogen detection, decontamination, and strain differentiation
    • DOI 10.1021/ja076086e
    • El-Boubbou, K., Gruden, C., and Huang, X. (2007) Magnetic glyco-nanoparticles: a unique tool for rapid pathogen detection, decontamination, and strain differentiation. J. Am. Chem. Soc. 129, 13392-13393. (Pubitemid 350071759)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.44 , pp. 13392-13393
    • El-Boubbou, K.1    Gruden, C.2    Huang, X.3
  • 39
    • 33644880505 scopus 로고    scopus 로고
    • Ethylene glycol-protected magnetic nanoparticles for a multiplexed immunoassay in human plasma
    • Lin, P.-C., Chou, P.-H., Chen, S.-H., Liao, H.-K., Wang, K.-Y., Chen, Y.-J., and Lin, C.-C. (2006) Ethylene glycol-protected magnetic nanoparticles for a multiplexed immunoassay in human plasma. Small 2, 485-489.
    • (2006) Small , vol.2 , pp. 485-489
    • Lin, P.-C.1    Chou, P.-H.2    Chen, S.-H.3    Liao, H.-K.4    Wang, K.-Y.5    Chen, Y.-J.6    Lin, C.-C.7
  • 41
    • 70350680894 scopus 로고    scopus 로고
    • Fabrication of oriented antibody-conjugated magnetic nanoprobes and their immunoaffinity application
    • Lin, P.-C., Chen, S.-H., Wang, K.-Y., Chen, M.-L., Adak, A. K., Hwu, J.-R. R., Chen, Y.-J., and Lin, C.-C. (2009) Fabrication of oriented antibody-conjugated magnetic nanoprobes and their immunoaffinity application. Anal. Chem. 81, 8774-8782.
    • (2009) Anal. Chem. , vol.81 , pp. 8774-8782
    • Lin, P.-C.1    Chen, S.-H.2    Wang, K.-Y.3    Chen, M.-L.4    Adak, A.K.5    Hwu, J.-R.R.6    Chen, Y.-J.7    Lin, C.-C.8
  • 42
    • 76249121175 scopus 로고    scopus 로고
    • A practical heterogeneous catalyst for the Suzuki, Sonogashira, and Stille coupling reactions of unreactive aryl chlorides
    • Jin, M.-J., and Lee, D.-H. (2010) A practical heterogeneous catalyst for the Suzuki, Sonogashira, and Stille coupling reactions of unreactive aryl chlorides. Angew. Chem., Int. Ed. 49, 1119-1122.
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 1119-1122
    • Jin, M.-J.1    Lee, D.-H.2
  • 43
    • 24744435555 scopus 로고    scopus 로고
    • Magnetically recoverable chiral catalysts immobilized on magnetite nanoparticles for asymmetric hydrogenation of aromatic ketones
    • DOI 10.1021/ja053881o
    • Hu, A., Yee, G. T., and Lin, W. (2005) Magnetically recoverable chiral catalysts immobilized on magnetite nanoparticles for asymmetric hydrogenation of aromatic ketones. J. Am. Chem. Soc. 127, 12486-12487. (Pubitemid 41292156)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.36 , pp. 12486-12487
    • Hu, A.1    Yee, G.T.2    Lin, W.3
  • 44
    • 0346112004 scopus 로고    scopus 로고
    • Thiol-Functionalized Gold Surfaces as a Strategy to Induce Order in Membrane-Bound Enzyme Immobilization
    • DOI 10.1021/nl0255505
    • Casero, E., Darder, M., Pariente, F., and Lorenzo, E. (2002) Thiol-functionalized gold surfaces as a strategy to induce order in membrane-bound enzyme immobilization. Nano Lett. 2, 577-582. (Pubitemid 135706392)
    • (2002) Nano Letters , vol.2 , Issue.6 , pp. 577-582
    • Casero, E.1    Darder, M.2    Pariente, F.3    Lorenzo, E.4    Martin-Benito, J.5    Vazquez, L.6
  • 45
    • 70349494352 scopus 로고    scopus 로고
    • Electrodes for integral membrane enzymes
    • Jeuken, L. J. C. (2009) Electrodes for integral membrane enzymes. Nat. Prod. Rep. 26, 1234-1240.
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 1234-1240
    • Jeuken, L.J.C.1
  • 46
    • 79551654430 scopus 로고    scopus 로고
    • Membrane-bound stable glycosyltransferases: Highly oriented protein immobilization by a C-terminal cationic amphipathic peptide
    • Naruchi, K., and Nishimura, S.-I. (2011) Membrane-bound stable glycosyltransferases: highly oriented protein immobilization by a C-terminal cationic amphipathic peptide. Angew. Chem., Int. Ed. 50, 1328-1331.
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 1328-1331
    • Naruchi, K.1    Nishimura, S.-I.2
  • 47
    • 33746302579 scopus 로고    scopus 로고
    • Highly efficient chemoenzymatic synthesis of naturally occurring and non-natural α-2,6-linked sialosides: A P. damsela α-2,6- sialyltransferase with extremely flexible donor-substrate specificity
    • DOI 10.1002/anie.200600572
    • Yu, H., Huang, S., Chokhawala, H., Sun, M., Zheng, H., and Chen, X. (2006) Highly efficient chemoenzymatic synthesis of naturally occurring and non-natural α-2,6-linked sialosides: a P. damsela α-2,6- sialyltransferase with extremely flexible donor-substrate specificity. Angew. Chem., Int. Ed. 45, 3938-3944. (Pubitemid 44105691)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.24 , pp. 3938-3944
    • Yu, H.1    Huang, S.2    Chokhawala, H.3    Sun, M.4    Zheng, H.5    Chen, X.6
  • 50
    • 29344431622 scopus 로고    scopus 로고
    • A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries
    • DOI 10.1021/ja0561690
    • Yu, H., Chokhawala, H., Karpel, R., Yu, H., Wu, B., Zhang, J., Zhang, Y., Jia, Q., and Chen, X. (2005) A multifunctional Pasteurella multocida sialyltransferase: a powerful tool for the synthesis of sialoside libraries. J. Am. Chem. Soc. 127, 17618-17619. (Pubitemid 43003372)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.50 , pp. 17618-17619
    • Yu, H.1    Chokhawala, H.2    Karpel, R.3    Yu, H.4    Wu, B.5    Zhang, J.6    Zhang, Y.7    Jia, Q.8    Chen, X.9
  • 51
    • 73249144598 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of GD3 oligosaccharides and other disialyl glycans containing natural and non-natural sialic acids
    • Yu, H., Cheng, J., Ding, L., Khedri, Z., Chen, Y., Chin, S., Lau, K., Tiwari, V. K., and Chen, X. (2009) Chemoenzymatic synthesis of GD3 oligosaccharides and other disialyl glycans containing natural and non-natural sialic acids. J. Am. Chem. Soc. 131, 18467-18477.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18467-18477
    • Yu, H.1    Cheng, J.2    Ding, L.3    Khedri, Z.4    Chen, Y.5    Chin, S.6    Lau, K.7    Tiwari, V.K.8    Chen, X.9
  • 52
    • 41749101505 scopus 로고    scopus 로고
    • Site-specific immobilization of CMP-sialic acid synthetase on magnetic nanoparticles and its use in the synthesis of CMP-sialic acid
    • DOI 10.1039/b716330d
    • Yu, C.-C., Lin, P.-C., and Lin, C.-C. (2008) Site-specific immobilization of CMP-sialic acid synthetase on magnetic nanoparticles and its use in the synthesis of CMP-sialic acid. Chem. Commun., 1308-1310. (Pubitemid 351490499)
    • (2008) Chemical Communications , Issue.11 , pp. 1308-1310
    • Yu, C.-C.1    Lin, P.-C.2    Lin, C.-C.3
  • 53
    • 0029961489 scopus 로고    scopus 로고
    • Cloning of the lipooligosaccharide α-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae
    • DOI 10.1074/jbc.271.45.28271
    • Gilbert, M., Watson, D. C., Cunningham, A.-M., Jennings, M. P., Young, N. M., and Wakarchuk, W. W. (1996) Cloning of the lipooligosaccharide α-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. J. Biol. Chem. 271, 28271-28276. (Pubitemid 26374640)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28271-28276
    • Gilbert, M.1    Watson, D.C.2    Cunningham, A.-M.3    Jennings, M.P.4    Young, N.M.5    Wakarchuk, W.W.6
  • 55
    • 34250681375 scopus 로고    scopus 로고
    • Surface modification of magnetic nanoparticle via Cu(I)-catalyzed alkyne-azide [2 + 3] cycloaddition
    • Lin, P.-C., Ueng, S.-H., Yu, S.-C., Jan, M.-D., Adak, A. K., Yu, C.- C., and Lin, C.-C. (2007) Surface modification of magnetic nanoparticle via Cu(I)-catalyzed alkyne-azide [2 + 3] cycloaddition. Org. Lett. 9, 2131-2134.
    • (2007) Org. Lett. , vol.9 , pp. 2131-2134
    • Lin, P.-C.1    Ueng, S.-H.2    Yu, S.-C.3    Jan, M.-D.4    Adak, A.K.5    Yu, C.-.C.6    Lin, C.-C.7
  • 56
    • 2442517595 scopus 로고    scopus 로고
    • Synthesis of orthogonal end functionalized oligoethylene glycols of defined lengths
    • DOI 10.1016/j.tetlet.2004.04.004, PII S0040403904007609
    • Iyer, S. S., Anderson, A. S., Reed, S., Swanson, B., and Schmidt, J. G. (2004) Synthesis of orthogonal end functionalized oligoethylene glycols of defined lengths. Tetrahedron Lett. 45, 4285-4288. (Pubitemid 38612860)
    • (2004) Tetrahedron Letters , vol.45 , Issue.22 , pp. 4285-4288
    • Iyer, S.S.1    Anderson, A.S.2    Reed, S.3    Swanson, B.4    Schmidt, J.G.5
  • 57
    • 34547143840 scopus 로고    scopus 로고
    • In silico analysis of enzyme surface and glycosylation effect as a tool for efficient covalent immobilisat ion of CalB and PGA on Sepabeads®
    • Basso, A., Braiuca, P., Cantone, S., Ebert, C., Linda, P., Spizzo, P., Caimi, P., Hanefeld, U., Degrassi, G., and Gardossia, L. (2007) In silico analysis of enzyme surface and glycosylation effect as a tool for efficient covalent immobilisat ion of CalB and PGA on Sepabeads®. Adv. Synth. Catal. 349, 877-886.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 877-886
    • Basso, A.1    Braiuca, P.2    Cantone, S.3    Ebert, C.4    Linda, P.5    Spizzo, P.6    Caimi, P.7    Hanefeld, U.8    Degrassi, G.9    Gardossia, L.10
  • 58
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P. E., Muir, T. W., Clark-Lewis, I., and Kent, S. B. H. (1994) Synthesis of proteins by native chemical ligation. Science 266, 776-779. (Pubitemid 24359280)
    • (1994) Science , vol.266 , Issue.5186 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.H.4
  • 60
    • 23144458654 scopus 로고    scopus 로고
    • Surface modification of magnetic nanoparticles with alkoxysilanes and their application in magnetic bioseparations
    • DOI 10.1021/la050553t
    • Bruce, I. J., and Sen, T. (2005) Surface modification of magnetic nanoparticles with alkoxysilanes and their application in magnetic bioseparations. Langmuir 21, 7029-7035. (Pubitemid 41084494)
    • (2005) Langmuir , vol.21 , Issue.15 , pp. 7029-7035
    • Bruce, I.J.1    Sen, T.2
  • 62
    • 0036081336 scopus 로고    scopus 로고
    • The Neisseria lipooligosaccharide-specific α-2,3-sialyltransferase is a surface-exposed outer membrane protein
    • DOI 10.1128/IAI.70.7.3744-3751.2002
    • Shell, D. M., Chiles, L., Judd, R. C., Seal, S., and Rest, R. F. (2002) The Neisseria lipooligosaccharide-specific α-2,3-sialyltransferase is a surface-exposed outer membrane protein. Infect. Immun. 70, 3744-3751. (Pubitemid 34666014)
    • (2002) Infection and Immunity , vol.70 , Issue.7 , pp. 3744-3751
    • Shell, D.M.1    Chiles, L.2    Judd, R.C.3    Seal, S.4    Rest, R.F.5
  • 63
    • 0031879563 scopus 로고    scopus 로고
    • The synthesis of sialylated oligosaccharides using a CMP-Neu5Ac synthetase/sialyltransferase fusion
    • DOI 10.1038/nbt0898-769
    • Gilbert, M., Bayer, R., Cunningham, A.-M., DeFrees, S., Gao, Y., Watson, D. C., Young, N. M., and Wakarchuk, W. W. (1998) The synthesis of sialylated oligosaccharides using a CMP-Neu5Ac synthetase/sialyltransferase fusion. Nat. Biotechnol. 16, 769-772. (Pubitemid 28363760)
    • (1998) Nature Biotechnology , vol.16 , Issue.8 , pp. 769-772
    • Gilbert, M.1    Bayer, R.2    Cunningham, A.-M.3    DeFrees, S.4    Gao, Y.5    Watson, D.C.6    Young, N.M.7    Wakarchuk, W.W.8
  • 64
    • 72149096051 scopus 로고    scopus 로고
    • Bioluminescent nanosensors for protease detection based upon gold nanoparticle-luciferase conjugates
    • Kim, Y.-P., Daniel, W. L., Xia, Z., Xie, H., Mirkin, C. A., and Rao, J. (2010) Bioluminescent nanosensors for protease detection based upon gold nanoparticle-luciferase conjugates. Chem. Commun. 46, 76-78.
    • (2010) Chem. Commun. , vol.46 , pp. 76-78
    • Kim, Y.-P.1    Daniel, W.L.2    Xia, Z.3    Xie, H.4    Mirkin, C.A.5    Rao, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.