메뉴 건너뛰기




Volumn 5, Issue 4, 2013, Pages 320-328

Functional protein-organic/inorganic hybrid nanomaterials

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL SCIENCE; BIOLOGICAL FUNCTIONS; ENZYMATIC CATALYSIS; HYBRID NANOMATERIALS; IN-VITRO; PREPARATION METHOD; RATIONAL DESIGN;

EID: 84879227444     PISSN: 19395116     EISSN: 19390041     Source Type: Journal    
DOI: 10.1002/wnan.1210     Document Type: Article
Times cited : (70)

References (68)
  • 1
    • 53949106970 scopus 로고    scopus 로고
    • Nanobiocatalysis and its potential applications
    • Kim J, Grate J, Wang P. Nanobiocatalysis and its potential applications. Trends Biotechnol 2008, 26:639-646.
    • (2008) Trends Biotechnol , vol.26 , pp. 639-646
    • Kim, J.1    Grate, J.2    Wang, P.3
  • 3
    • 78650300465 scopus 로고    scopus 로고
    • Pt-decorated PdCoPd/C core-shell nanoparticles with enhanced stability and electrocatalytic activity for the oxygen reduction reaction
    • Wang D, Xin H, Yu Y, Wang H, Rus E, Muller D, Abruna H. Pt-decorated PdCoPd/C core-shell nanoparticles with enhanced stability and electrocatalytic activity for the oxygen reduction reaction. J Am Chem Soc 2010, 132:17664-17666.
    • (2010) J Am Chem Soc , vol.132 , pp. 17664-17666
    • Wang, D.1    Xin, H.2    Yu, Y.3    Wang, H.4    Rus, E.5    Muller, D.6    Abruna, H.7
  • 4
    • 79151477024 scopus 로고    scopus 로고
    • Just scratching the surface? New techniques show how surface functionality of nanoparticles infl{ligature}uences their environmental fate
    • Jarvie H, King S. Just scratching the surface? New techniques show how surface functionality of nanoparticles infl{ligature}uences their environmental fate. Nano Today 2010, 5:248-250.
    • (2010) Nano Today , vol.5 , pp. 248-250
    • Jarvie, H.1    King, S.2
  • 5
    • 33751233554 scopus 로고    scopus 로고
    • Nanoparticle polymer composites: where two small worlds meet
    • Balazs A, Emrick T, Russell T. Nanoparticle polymer composites: where two small worlds meet. Science 2006, 314:1107-1110.
    • (2006) Science , vol.314 , pp. 1107-1110
    • Balazs, A.1    Emrick, T.2    Russell, T.3
  • 6
    • 13644250281 scopus 로고    scopus 로고
    • Examination of cholesterol oxidase attachment to magnetic nanoparticles
    • Kouassi GK, Irudayaraj J, McCarty G. Examination of cholesterol oxidase attachment to magnetic nanoparticles. J Nanobiotechnol 2005, 3:1-9.
    • (2005) J Nanobiotechnol , vol.3 , pp. 1-9
    • Kouassi, G.K.1    Irudayaraj, J.2    McCarty, G.3
  • 8
    • 34250221611 scopus 로고    scopus 로고
    • Porous silica nano-tube as host for enzyme immobilization
    • Ding H, Wen L, Chen J. Porous silica nano-tube as host for enzyme immobilization. China Particuol 2004, 2:270-273.
    • (2004) China Particuol , vol.2 , pp. 270-273
    • Ding, H.1    Wen, L.2    Chen, J.3
  • 9
    • 84857501798 scopus 로고    scopus 로고
    • Potential applications of enzymes immobilized on/in nano materials: a review
    • Ansari SA, Husain Q. Potential applications of enzymes immobilized on/in nano materials: a review. Biotechnol Adv 2012, 30:512-523.
    • (2012) Biotechnol Adv , vol.30 , pp. 512-523
    • Ansari, S.A.1    Husain, Q.2
  • 10
    • 79951581558 scopus 로고    scopus 로고
    • Nano-encapsulations liberated from barley protein microparticles for oral delivery of bioactive compounds
    • Wang R, Tian Z, Chen L. Nano-encapsulations liberated from barley protein microparticles for oral delivery of bioactive compounds. Int J Pharm 2011, 406:153-162.
    • (2011) Int J Pharm , vol.406 , pp. 153-162
    • Wang, R.1    Tian, Z.2    Chen, L.3
  • 11
    • 33746253246 scopus 로고    scopus 로고
    • Infl{ligature}uence of microencapsulation method and peptide loading on formulation of poly(lactide-co-glycolide) insulin nanoparticles
    • Kumar P, Ramakrishna S, Saini T, Diwan P. Infl{ligature}uence of microencapsulation method and peptide loading on formulation of poly(lactide-co-glycolide) insulin nanoparticles. Pharmazie 2006, 61:613-617.
    • (2006) Pharmazie , vol.61 , pp. 613-617
    • Kumar, P.1    Ramakrishna, S.2    Saini, T.3    Diwan, P.4
  • 12
    • 84865309834 scopus 로고    scopus 로고
    • Nano-inside-micro: disease-responsive microgels with encapsulated nanoparticles for intracellular drug delivery to the deep lung
    • Wanakule P, Liu G, Fleury A, Roy K. Nano-inside-micro: disease-responsive microgels with encapsulated nanoparticles for intracellular drug delivery to the deep lung. J Control Release 2012, 162:429-437.
    • (2012) J Control Release , vol.162 , pp. 429-437
    • Wanakule, P.1    Liu, G.2    Fleury, A.3    Roy, K.4
  • 13
    • 67249114390 scopus 로고    scopus 로고
    • Self-assembling peptide amphiphile-based nanofi{ligature}ber gel for bioresponsive cisplatin delivery
    • Kim JK, Anderson J, Jun HW, Repka MA, Jo S. Self-assembling peptide amphiphile-based nanofi{ligature}ber gel for bioresponsive cisplatin delivery. Mol Pharm 2009, 6:978-985.
    • (2009) Mol Pharm , vol.6 , pp. 978-985
    • Kim, J.K.1    Anderson, J.2    Jun, H.W.3    Repka, M.A.4    Jo, S.5
  • 14
    • 34548556479 scopus 로고    scopus 로고
    • Stable enzyme biosensors based on chemically synthesized Au-polypyrrole nanocomposites
    • Njagi J, Andreescu S. Stable enzyme biosensors based on chemically synthesized Au-polypyrrole nanocomposites. Biosens Bioelectron 2007, 23:168-175.
    • (2007) Biosens Bioelectron , vol.23 , pp. 168-175
    • Njagi, J.1    Andreescu, S.2
  • 15
    • 33845644146 scopus 로고    scopus 로고
    • Disposable biosensor based on enzyme immobilized on Au-chitosan-modifi{ligature}ed indiumtinoxide electrode with fl{ligature}ow injection amperometric analysis
    • Lin J, Qu W, Zhang S. Disposable biosensor based on enzyme immobilized on Au-chitosan-modifi{ligature}ed indiumtinoxide electrode with fl{ligature}ow injection amperometric analysis. Anal Biochem 2007, 360:288-293.
    • (2007) Anal Biochem , vol.360 , pp. 288-293
    • Lin, J.1    Qu, W.2    Zhang, S.3
  • 16
    • 59849100750 scopus 로고    scopus 로고
    • An enzyme immobilization platform for biosensor designs of direct electrochemistry using fl{ligature}ower-like ZnO crystals and nano-sized gold particles
    • Zhang Y, Zhang Y, Wang H, Yan B, Shen G, Yu R. An enzyme immobilization platform for biosensor designs of direct electrochemistry using fl{ligature}ower-like ZnO crystals and nano-sized gold particles. J Electroanal Chem 2009, 627:9-14.
    • (2009) J Electroanal Chem , vol.627 , pp. 9-14
    • Zhang, Y.1    Zhang, Y.2    Wang, H.3    Yan, B.4    Shen, G.5    Yu, R.6
  • 17
    • 1842790784 scopus 로고    scopus 로고
    • Electrochemical synthesis and impedance characterization of nano-patterned biosensor substrate
    • Takhistov P. Electrochemical synthesis and impedance characterization of nano-patterned biosensor substrate. Biosens Bioelectron 2004, 19:1445-1456.
    • (2004) Biosens Bioelectron , vol.19 , pp. 1445-1456
    • Takhistov, P.1
  • 18
    • 33751256536 scopus 로고    scopus 로고
    • Nanoscale biocatalyst systems
    • Wang P. Nanoscale biocatalyst systems. Curr Opin Biotechnol 2006, 17:574-579.
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 574-579
    • Wang, P.1
  • 19
    • 27844518415 scopus 로고    scopus 로고
    • Nanostructures for enzyme stabilization
    • Kim J, Grate JW, Wang P. Nanostructures for enzyme stabilization. Chem Eng Sci 2006, 61:1017-1026.
    • (2006) Chem Eng Sci , vol.61 , pp. 1017-1026
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 20
    • 60649086344 scopus 로고    scopus 로고
    • Recent advances in nanostructured biocatalysts
    • Ge J, Lu D, Liu Z, Liu Z. Recent advances in nanostructured biocatalysts. Biochem Eng J 2009, 44:53-59.
    • (2009) Biochem Eng J , vol.44 , pp. 53-59
    • Ge, J.1    Lu, D.2    Liu, Z.3    Liu, Z.4
  • 21
    • 84872012694 scopus 로고    scopus 로고
    • Immobilization in biotechnology and biorecognition: from macro-to nanoscale systems
    • Marek B, Danica M, Jozef N. Immobilization in biotechnology and biorecognition: from macro-to nanoscale systems. Chem Pap 2012, 66:983-998.
    • (2012) Chem Pap , vol.66 , pp. 983-998
    • Marek, B.1    Danica, M.2    Jozef, N.3
  • 22
    • 84865347259 scopus 로고    scopus 로고
    • Peptide and protein-based nanotubes for nanobiotechnology
    • Petrov A, Audette G. Peptide and protein-based nanotubes for nanobiotechnology. WIREs Nanomed Nanobiotechnol 2012, 4:575-585.
    • (2012) WIREs Nanomed Nanobiotechnol , vol.4 , pp. 575-585
    • Petrov, A.1    Audette, G.2
  • 24
    • 84861459402 scopus 로고    scopus 로고
    • Immobilization of biocatalysts for enzymatic polymerizations: possibilities, advantages, applications
    • Miletic N, Nastasovic A, Loos K. Immobilization of biocatalysts for enzymatic polymerizations: possibilities, advantages, applications. Bioresour Technol 2012, 115:126-135
    • (2012) Bioresour Technol , vol.115 , pp. 126-135
    • Miletic, N.1    Nastasovic, A.2    Loos, K.3
  • 26
    • 0141684517 scopus 로고    scopus 로고
    • Single-enzyme nanoparticles armored by a nanometer-scale organic/inorganic network
    • Kim J, Grate JW. Single-enzyme nanoparticles armored by a nanometer-scale organic/inorganic network. Nano Lett 2003, 3:1219-1222.
    • (2003) Nano Lett , vol.3 , pp. 1219-1222
    • Kim, J.1    Grate, J.W.2
  • 27
    • 14844322204 scopus 로고    scopus 로고
    • Mesoporous silica spheres as supports for enzyme immobilization and encapsulation
    • Wang YJ, Caruso F. Mesoporous silica spheres as supports for enzyme immobilization and encapsulation. Chem Mater 2005, 17:953-961.
    • (2005) Chem Mater , vol.17 , pp. 953-961
    • Wang, Y.J.1    Caruso, F.2
  • 29
    • 0038137900 scopus 로고    scopus 로고
    • Alumina-pepsin hybrid nanoparticles with orientation-specifi{ligature}c enzyme coupling
    • Li J, Wang JQ, Gavalas VG, Atwood DA, Bachas LG. Alumina-pepsin hybrid nanoparticles with orientation-specifi{ligature}c enzyme coupling. Nano Lett 2003, 3:55-58.
    • (2003) Nano Lett , vol.3 , pp. 55-58
    • Li, J.1    Wang, J.Q.2    Gavalas, V.G.3    Atwood, D.A.4    Bachas, L.G.5
  • 30
  • 31
    • 32044474875 scopus 로고    scopus 로고
    • Directed assembly of carbon nanotubes at liquid-liquid interfaces: nanoscale conveyors for interfacial biocatalysis
    • Asuri P, Karajanagi SS, Dordick JS, Kane RS. Directed assembly of carbon nanotubes at liquid-liquid interfaces: nanoscale conveyors for interfacial biocatalysis. J Am Chem Soc 2006, 128:1046-1047.
    • (2006) J Am Chem Soc , vol.128 , pp. 1046-1047
    • Asuri, P.1    Karajanagi, S.S.2    Dordick, J.S.3    Kane, R.S.4
  • 32
    • 78650330875 scopus 로고    scopus 로고
    • Lipase covalently attached to multiwalled carbon nanotubes as an effi{ligature}cient catalyst in organic solvent
    • Ji PJ, Tan HS, Xu X, Feng W. Lipase covalently attached to multiwalled carbon nanotubes as an effi{ligature}cient catalyst in organic solvent. AIChE J 2010, 56:3005-3011.
    • (2010) AIChE J , vol.56 , pp. 3005-3011
    • Ji, P.J.1    Tan, H.S.2    Xu, X.3    Feng, W.4
  • 34
    • 27944432572 scopus 로고    scopus 로고
    • Fabrication and application of enzyme-incorporated peptide nanotubes
    • Yu LT, Banerjee IA, Gao XY, Nuraje N, Matsui H. Fabrication and application of enzyme-incorporated peptide nanotubes. Bioconjug Chem 2005, 16:1484-1487.
    • (2005) Bioconjug Chem , vol.16 , pp. 1484-1487
    • Yu, L.T.1    Banerjee, I.A.2    Gao, X.Y.3    Nuraje, N.4    Matsui, H.5
  • 35
    • 0017388651 scopus 로고
    • Eff{ligature}ect of covalent attachment of polyethylene-glycol on immunogenicity and circulating life of bovine liver catalase
    • Abuchowski A, Mccoy JR, Palczuk NC, Vanes T, Davis FF. Eff{ligature}ect of covalent attachment of polyethylene-glycol on immunogenicity and circulating life of bovine liver catalase. J Biol Chem 1977, 252:3582-3586.
    • (1977) J Biol Chem , vol.252 , pp. 3582-3586
    • Abuchowski, A.1    Mccoy, J.R.2    Palczuk, N.C.3    Vanes, T.4    Davis, F.F.5
  • 36
    • 0033230001 scopus 로고    scopus 로고
    • Synthesis and biological activity of polyethylene glycol-mouse nerve growth factor conjugate
    • Belcheva N, Woodrow-Mumford K, Mahoney MJ, Saltzman WM. Synthesis and biological activity of polyethylene glycol-mouse nerve growth factor conjugate. Bioconjug Chem 1999, 10:932-937.
    • (1999) Bioconjug Chem , vol.10 , pp. 932-937
    • Belcheva, N.1    Woodrow-Mumford, K.2    Mahoney, M.J.3    Saltzman, W.M.4
  • 37
    • 0020630987 scopus 로고
    • Synthesis and spectroscopic characterization of insulin derivatives containing one or 2 poly(ethylene oxide) chains at specifi{ligature}c positions
    • Ehrat M, Luisi PL. Synthesis and spectroscopic characterization of insulin derivatives containing one or 2 poly(ethylene oxide) chains at specifi{ligature}c positions. Biopolymers 1983, 22:569-573.
    • (1983) Biopolymers , vol.22 , pp. 569-573
    • Ehrat, M.1    Luisi, P.L.2
  • 40
    • 28844444181 scopus 로고    scopus 로고
    • In situ preparation of protein- "smart" polymer conjugates with retention of bioactivity
    • Heredia KL, Bontempo D, Ly T, Byers JT, Halstenberg S, Maynard HD. In situ preparation of protein- "smart" polymer conjugates with retention of bioactivity. J Am Chem Soc 2005, 127:16955-16960.
    • (2005) J Am Chem Soc , vol.127 , pp. 16955-16960
    • Heredia, K.L.1    Bontempo, D.2    Ly, T.3    Byers, J.T.4    Halstenberg, S.5    Maynard, H.D.6
  • 41
    • 34547959155 scopus 로고    scopus 로고
    • Hyperbranched polymer conjugated lipase with enhanced activity and stability
    • Ge J, Yan M, Lu DN, Zhang ML, Liu Z. Hyperbranched polymer conjugated lipase with enhanced activity and stability. Biochem Eng J 2007, 36:93-99.
    • (2007) Biochem Eng J , vol.36 , pp. 93-99
    • Ge, J.1    Yan, M.2    Lu, D.N.3    Zhang, M.L.4    Liu, Z.5
  • 42
    • 84863926409 scopus 로고    scopus 로고
    • A fl{ligature}uorescently labeled dendronized polymer-enzyme conjugate carrying multiple copies of two diff{ligature}erent types of active enzymes
    • Grotzky A, Nauser T, Erdogan H, Schluter AD, Walde P. A fl{ligature}uorescently labeled dendronized polymer-enzyme conjugate carrying multiple copies of two diff{ligature}erent types of active enzymes. J Am Chem Soc 2012, 134:11392-11395.
    • (2012) J Am Chem Soc , vol.134 , pp. 11392-11395
    • Grotzky, A.1    Nauser, T.2    Erdogan, H.3    Schluter, A.D.4    Walde, P.5
  • 43
    • 33748082007 scopus 로고    scopus 로고
    • Encapsulation of single enzyme in nanogel with enhanced biocatalytic activity and stability
    • Yan M, Ge J, Liu Z, Ouyang P. Encapsulation of single enzyme in nanogel with enhanced biocatalytic activity and stability. J Am Chem Soc 2006, 128:11008-11009.
    • (2006) J Am Chem Soc , vol.128 , pp. 11008-11009
    • Yan, M.1    Ge, J.2    Liu, Z.3    Ouyang, P.4
  • 45
    • 67049119394 scopus 로고    scopus 로고
    • Lipase nanogel catalyzed transesterifi{ligature}cation in anhydrous dimethyl sulfoxide
    • Ge J, Lu DN, Wang J, Liu Z. Lipase nanogel catalyzed transesterifi{ligature}cation in anhydrous dimethyl sulfoxide. Biomacromolecules 2009, 10:1612-1618.
    • (2009) Biomacromolecules , vol.10 , pp. 1612-1618
    • Ge, J.1    Lu, D.N.2    Wang, J.3    Liu, Z.4
  • 46
    • 33847245460 scopus 로고    scopus 로고
    • Fabrication of single carbonic anhydrase nanogel against denaturation and aggregation at high temperature
    • Yan M, Liu ZX, Lu DN, Liu Z. Fabrication of single carbonic anhydrase nanogel against denaturation and aggregation at high temperature. Biomacromolecules 2007, 8:560-565.
    • (2007) Biomacromolecules , vol.8 , pp. 560-565
    • Yan, M.1    Liu, Z.X.2    Lu, D.N.3    Liu, Z.4
  • 47
    • 79960342212 scopus 로고    scopus 로고
    • Strengthening the stability of a tunnel-shaped homotetramer protein with nanogels
    • Liu ZX, Lu DN, Yin L, Li JM, Cui YC, Chen W, Liu Z. Strengthening the stability of a tunnel-shaped homotetramer protein with nanogels. J Phys Chem B 2011, 115:8875-8882.
    • (2011) J Phys Chem B , vol.115 , pp. 8875-8882
    • Liu, Z.X.1    Lu, D.N.2    Yin, L.3    Li, J.M.4    Cui, Y.C.5    Chen, W.6    Liu, Z.7
  • 50
    • 84863280762 scopus 로고    scopus 로고
    • Magnetic enzyme nanogel (MENG): a universal synthetic route for biocatalysts
    • Lin M, Lu D, Zhu J, Yang C, Zhang Y, Liu Z. Magnetic enzyme nanogel (MENG): a universal synthetic route for biocatalysts. Chem Commun 2012, 48:3315-3317.
    • (2012) Chem Commun , vol.48 , pp. 3315-3317
    • Lin, M.1    Lu, D.2    Zhu, J.3    Yang, C.4    Zhang, Y.5    Liu, Z.6
  • 51
    • 84863719219 scopus 로고    scopus 로고
    • Protein-inorganic hybrid nanofl{ligature}owers
    • Ge J, Lei JD, Zare RN. Protein-inorganic hybrid nanofl{ligature}owers. Nat Nanotechnol 2012, 7:428-432.
    • (2012) Nat Nanotechnol , vol.7 , pp. 428-432
    • Ge, J.1    Lei, J.D.2    Zare, R.N.3
  • 52
    • 78650124917 scopus 로고    scopus 로고
    • Fabrication of ordered nanostructures of sulfi{ligature}de nanocrystal assemblies over self-assembled genetically engineered P22 coat protein
    • Shen LM, Bao NZ, Prevelige PE, Gupta A. Fabrication of ordered nanostructures of sulfi{ligature}de nanocrystal assemblies over self-assembled genetically engineered P22 coat protein. J Am Chem Soc 2010, 132:17354-17357.
    • (2010) J Am Chem Soc , vol.132 , pp. 17354-17357
    • Shen, L.M.1    Bao, N.Z.2    Prevelige, P.E.3    Gupta, A.4
  • 53
    • 0037174353 scopus 로고    scopus 로고
    • Entrapping enzyme in a functionalized nanoporous support
    • Lei C, Shin Y, Liu J, Ackerman EJ. Entrapping enzyme in a functionalized nanoporous support. J Am Chem Soc 2002, 24:11242-11243.
    • (2002) J Am Chem Soc , vol.24 , pp. 11242-11243
    • Lei, C.1    Shin, Y.2    Liu, J.3    Ackerman, E.J.4
  • 56
    • 0032938527 scopus 로고    scopus 로고
    • Enzyme modifi{ligature}cation by polymers with solubilities that change in response to photoirradiation in organic media
    • Ito Y, Sugimura N, Kwon O, Imanishi Y. Enzyme modifi{ligature}cation by polymers with solubilities that change in response to photoirradiation in organic media. Nat Biotechnol 1999, 17:73-75.
    • (1999) Nat Biotechnol , vol.17 , pp. 73-75
    • Ito, Y.1    Sugimura, N.2    Kwon, O.3    Imanishi, Y.4
  • 57
    • 79958854544 scopus 로고    scopus 로고
    • Bovine serum albumin-poly(methyl methacrylate) nanoparticles: an example of frustrated phase separation
    • Ge J, Lei J, Zare R. Bovine serum albumin-poly(methyl methacrylate) nanoparticles: an example of frustrated phase separation. Nano Lett 2011, 11:2551-2554.
    • (2011) Nano Lett , vol.11 , pp. 2551-2554
    • Ge, J.1    Lei, J.2    Zare, R.3
  • 58
    • 84870578063 scopus 로고    scopus 로고
    • Protein-polymer hybrid nanoparticles for drug delivery
    • Ge J, Neofytou E, Lei JD, Beygui RE, Zare RN. Protein-polymer hybrid nanoparticles for drug delivery. Small 2012, 8:3573-3578.
    • (2012) Small , vol.8 , pp. 3573-3578
    • Ge, J.1    Neofytou, E.2    Lei, J.D.3    Beygui, R.E.4    Zare, R.N.5
  • 59
    • 34250158892 scopus 로고    scopus 로고
    • In situ formation of protein-polymer conjugates through reversible addition fragmentation chain transfer polymerization
    • Liu J, Bulmus V, Herlambang D, Barner-Kowollik C, Stenzel M, Davis T. In situ formation of protein-polymer conjugates through reversible addition fragmentation chain transfer polymerization. Angew Chem Int Ed 2007, 46:3099-3103.
    • (2007) Angew Chem Int Ed , vol.46 , pp. 3099-3103
    • Liu, J.1    Bulmus, V.2    Herlambang, D.3    Barner-Kowollik, C.4    Stenzel, M.5    Davis, T.6
  • 60
    • 33751102375 scopus 로고    scopus 로고
    • Fluorescently tagged polymer bioconjugates from protein derived macroinitiators
    • Nicolas J, Miguel V, Mantovania G, Haddleton D. Fluorescently tagged polymer bioconjugates from protein derived macroinitiators. Chem Commun 2006, 45:4697-4699.
    • (2006) Chem Commun , vol.45 , pp. 4697-4699
    • Nicolas, J.1    Miguel, V.2    Mantovania, G.3    Haddleton, D.4
  • 61
    • 79953864734 scopus 로고    scopus 로고
    • Uniform polymer-protein conjugate by aqueous AGET ATRP using protein as a macroinitiator
    • Zhu B, Lu D, Ge J, Liu Z. Uniform polymer-protein conjugate by aqueous AGET ATRP using protein as a macroinitiator. Acta Biomater 2011, 7:2131-2138.
    • (2011) Acta Biomater , vol.7 , pp. 2131-2138
    • Zhu, B.1    Lu, D.2    Ge, J.3    Liu, Z.4
  • 63
    • 8844264559 scopus 로고    scopus 로고
    • Shaping crystals with biomolecules
    • Yoreo J, Dove P. Shaping crystals with biomolecules. Science 2004, 306:1301-1302.
    • (2004) Science , vol.306 , pp. 1301-1302
    • Yoreo, J.1    Dove, P.2
  • 64
    • 79952613808 scopus 로고    scopus 로고
    • A lipase-responsive vehicle using amphipathic polymer synthesized with the lipase as catalyst
    • Ge J, Lu DN, Yang C, Liu Z. A lipase-responsive vehicle using amphipathic polymer synthesized with the lipase as catalyst. Macromol Rapid Commun 2011, 32:546-550.
    • (2011) Macromol Rapid Commun , vol.32 , pp. 546-550
    • Ge, J.1    Lu, D.N.2    Yang, C.3    Liu, Z.4
  • 65
    • 79953186583 scopus 로고    scopus 로고
    • How PEGylation enhances the stability and potency of insulin: a molecular dynamics simulation
    • Yang C, Lu DN, Liu Z. How PEGylation enhances the stability and potency of insulin: a molecular dynamics simulation. Biochemistry 2011, 50:2585-2593.
    • (2011) Biochemistry , vol.50 , pp. 2585-2593
    • Yang, C.1    Lu, D.N.2    Liu, Z.3
  • 66
    • 0031047280 scopus 로고    scopus 로고
    • Structure and function of subtilisin BPN' solubilized in organic solvents
    • Wangikar PP, Michels PC, Clark DS, Dordick JS. Structure and function of subtilisin BPN' solubilized in organic solvents. J Am Chem Soc 1997, 119:70-76.
    • (1997) J Am Chem Soc , vol.119 , pp. 70-76
    • Wangikar, P.P.1    Michels, P.C.2    Clark, D.S.3    Dordick, J.S.4
  • 67
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks A, Klibanov AM. Enzymatic catalysis in nonaqueous solvents. J Biol Chem 1988, 263:3194-3201.
    • (1988) J Biol Chem , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 68
    • 0002823418 scopus 로고    scopus 로고
    • The solubility of proteins in organic solvents
    • Houen G. The solubility of proteins in organic solvents. Acta Chem Scand 1996, 50:68-70.
    • (1996) Acta Chem Scand , vol.50 , pp. 68-70
    • Houen, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.