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Volumn 5, Issue 1, 2010, Pages 37-49

Overview of the main methods used to combine proteins with nanosystems: Absorption, bioconjugation, and encapsulation

Author keywords

Absorption; Bioconjugation; Drug delivery; Encapsulation; Nanoparticles; Polypeptides; Proteins

Indexed keywords

ALGINIC ACID; ARGINYLGLYCYLASPARTIC ACID; CHITOSAN; HEPATITIS A VACCINE; LIPOSOME; NANOPARTICLE; POLYGLACTIN; POLYLACTIC ACID; SILICON DIOXIDE;

EID: 77951190722     PISSN: 11769114     EISSN: 11782013     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (108)

References (171)
  • 1
    • 34047273353 scopus 로고    scopus 로고
    • Application of nanotechnology in biomedicine
    • Navalakhe RM, Nandedkar TD. Application of nanotechnology in biomedicine. Indian J Exp Biol. 2007;45:160-165.
    • (2007) Indian J Exp Biol , vol.45 , pp. 160-165
    • Navalakhe, R.M.1    Nandedkar, T.D.2
  • 2
    • 37349069277 scopus 로고    scopus 로고
    • Nanotechnology in regenerative medicine: The materials side
    • Engel E, Michiardi A, Navarro M, et al. Nanotechnology in regenerative medicine: the materials side. Trends Biotechnol. 2008;26:39-47.
    • (2008) Trends Biotechnol , vol.26 , pp. 39-47
    • Engel, E.1    Michiardi, A.2    Navarro, M.3
  • 3
    • 39649092973 scopus 로고    scopus 로고
    • Nanotechnology and Cancer
    • Heath JR, Davis ME. Nanotechnology and Cancer. Annu Rev Med. 2008;59:251-265.
    • (2008) Annu Rev Med , vol.59 , pp. 251-265
    • Heath, J.R.1    Davis, M.E.2
  • 4
    • 37249039423 scopus 로고    scopus 로고
    • Nanoparticles as smart treatment-delivery systems in plants: Assessment of different techniques of microscopy for their visualization in plant tissues
    • Melendi PG, Ferna R, Pacheco RF, et al. Nanoparticles as smart treatment-delivery systems in plants: Assessment of different techniques of microscopy for their visualization in plant tissues. Ann Bot. 2008; 101:187-195.
    • (2008) Ann Bot , vol.101 , pp. 187-195
    • Melendi, P.G.1    Ferna, R.2    Pacheco, R.F.3
  • 5
    • 33947508649 scopus 로고    scopus 로고
    • Nanoparticle gasifier fuel cell for sustainable energy future
    • Gidaspow D, Jiradilok V. Nanoparticle gasifier fuel cell for sustainable energy future. J Power Source. 2007;166:400-410.
    • (2007) J Power Source , vol.166 , pp. 400-410
    • Gidaspow, D.1    Jiradilok, V.2
  • 6
    • 59349094447 scopus 로고    scopus 로고
    • Synthesis and electrical properties of uniform silver nanoparticles for electronic applications
    • Chen D, Qiao X, Qiu X, et al. Synthesis and electrical properties of uniform silver nanoparticles for electronic applications. J Mat Sci. 2009;44:1076-1081.
    • (2009) J Mat Sci , vol.44 , pp. 1076-1081
    • Chen, D.1    Qiao, X.2    Qiu, X.3
  • 7
    • 20144379798 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for imaging, labeling and sensing
    • Medintz IL, Uyeda HT, Goldman ER, et al. Quantum dot bioconjugates for imaging, labeling and sensing. Nat Mater. 2005;4:435-446.
    • (2005) Nat Mater , vol.4 , pp. 435-446
    • Medintz, I.L.1    Uyeda, H.T.2    Goldman, E.R.3
  • 8
    • 33751410697 scopus 로고    scopus 로고
    • Recent advances in iron oxide nanocrystal technology for medical imaging
    • Corot C, Robert P, Idée JM, et al. Recent advances in iron oxide nanocrystal technology for medical imaging. Adv Drug Deliv Rev. 2006;58:1471-1504.
    • (2006) Adv Drug Deliv Rev , vol.58 , pp. 1471-1504
    • Corot, C.1    Robert, P.2    Idée, J.M.3
  • 10
    • 0001374672 scopus 로고    scopus 로고
    • Nanoparticulate drug carrier technology
    • In: Cohen S, Bernstein H, editors, New York, NY: Marcel Dekker
    • Alonso MJ. Nanoparticulate drug carrier technology. In: Cohen S, Bernstein H, editors. Microparticulate Systems for the Delivery of Proteins and Vaccines. New York, NY: Marcel Dekker; 1996. p. 203-242.
    • (1996) Microparticulate Systems For the Delivery of Proteins and Vaccines , pp. 203-242
    • Alonso, M.J.1
  • 11
    • 0019774747 scopus 로고
    • Molecular engineering: An approach to the development of general capabilities for molecular manipulation
    • Drexler KE. Molecular engineering: an approach to the development of general capabilities for molecular manipulation. Proc Natl Acad Sci USA. 1981;78:5275-5278.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 5275-5278
    • Drexler, K.E.1
  • 12
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • Rajagopal K, Schneider JP. Self-assembling peptides and proteins for nanotechnological applications. Curr Opin Struct Biol. 2004;14: 480-486.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 13
    • 33748344520 scopus 로고    scopus 로고
    • Nanotechnology in cancer therapeutics: Bioconjugated nanoparticles for drug delivery
    • Sinha R, Kim GJ, Nie S, Shin DM. Nanotechnology in cancer therapeu- tics: bioconjugated nanoparticles for drug delivery. Mol Cancer Ther. 2006;5:1909-1917.
    • (2006) Mol Cancer Ther , vol.5 , pp. 1909-1917
    • Sinha, R.1    Kim, G.J.2    Nie, S.3    Shin, D.M.4
  • 15
    • 5044226734 scopus 로고    scopus 로고
    • Novel method using a temperature- sensitive polymer (methylcellulose) to thermally gel aqueous alginate as a pH-sensitive hydrogel
    • Liang FH, Hong MH, Ho RM, et al. Novel method using a temperature- sensitive polymer (methylcellulose) to thermally gel aqueous alginate as a pH-sensitive hydrogel. Biomacromolecules. 2004;5:1917-1925.
    • (2004) Biomacromolecules , vol.5 , pp. 1917-1925
    • Liang, F.H.1    Hong, M.H.2    Ho, R.M.3
  • 16
    • 72749093756 scopus 로고    scopus 로고
    • Recent developments in liposomes, microparticles and nanoparticles for protein and peptide drug delivery
    • Oct 9. [Epub ahead of print]
    • Tan ML, Choong PFM, Dass CR. Recent developments in liposomes, microparticles and nanoparticles for protein and peptide drug delivery. Peptides. Oct 9. [Epub ahead of print].
    • Peptides
    • Tan, M.L.1    Choong, P.F.M.2    Dass, C.R.3
  • 17
    • 26444539480 scopus 로고    scopus 로고
    • Medical nanotechnology: Shortening clinical trials and regulatory pathways?
    • Ferrari M, Downing G. Medical nanotechnology: shortening clinical trials and regulatory pathways? Biodrugs. 2005;19:203-210.
    • (2005) Biodrugs , vol.19 , pp. 203-210
    • Ferrari, M.1    Downing, G.2
  • 18
    • 34547899919 scopus 로고    scopus 로고
    • Solid lipid nanoparticles as a drug delivery system for peptides and proteins
    • Almeida AJ, Souto E. Solid lipid nanoparticles as a drug delivery system for peptides and proteins. Adv Drug Delivery Rev. 2007;59:478-490.
    • (2007) Adv Drug Delivery Rev , vol.59 , pp. 478-490
    • Almeida, A.J.1    Souto, E.2
  • 19
    • 41849105252 scopus 로고    scopus 로고
    • Lipid-based colloidal carriers for peptide and protein delivery: Liposomes versus lipid nanoparticles
    • Martins Sarmento B, Ferreira DC, Souto EB. Lipid-based colloidal carriers for peptide and protein delivery: liposomes versus lipid nanoparticles. Int J Nanomed. 2007;2:595-607.
    • (2007) Int J Nanomed , vol.2 , pp. 595-607
    • Martins Sarmento, B.1    Ferreira, D.C.2    Souto, E.B.3
  • 20
    • 0032403533 scopus 로고    scopus 로고
    • Oral particulate delivery: Status and future trends
    • Chen H, Langer R. Oral particulate delivery: status and future trends. Adv Drug Del. 1998;34:339-350.
    • (1998) Adv Drug Del , vol.34 , pp. 339-350
    • Chen, H.1    Langer, R.2
  • 21
    • 15544362279 scopus 로고    scopus 로고
    • Polymeric particulates to improve oral bioavailability of peptide drugs
    • Delie F, Blanco-Príeto MJ. Polymeric particulates to improve oral bioavailability of peptide drugs. Molecules. 2005;10:65-80.
    • (2005) Molecules , vol.10 , pp. 65-80
    • Delie, F.1    Blanco-Príeto, M.J.2
  • 22
    • 0343150936 scopus 로고    scopus 로고
    • The potential of mucoadhesive polymers in enhancing intestinal peptide drug absorption. III: Effects of chitosan-glutamate and carbomer on epithelial tight junctions in vitro
    • Borchard G, Luegen HL, de Boer AG, et al. The potential of mucoadhesive polymers in enhancing intestinal peptide drug absorption. III: Effects of chitosan-glutamate and carbomer on epithelial tight junctions in vitro. J Control Release. 1996;39:131-138.
    • (1996) J Control Release , vol.39 , pp. 131-138
    • Borchard, G.1    Luegen, H.L.2    de Boer, A.G.3
  • 23
    • 34147126384 scopus 로고    scopus 로고
    • Recent advances in protein and peptide drug delivery systems
    • Malik DK, Baboota S, Ahuja A, et al. Recent advances in protein and peptide drug delivery systems. Curr Drug Deliv. 2007;4:141-151.
    • (2007) Curr Drug Deliv , vol.4 , pp. 141-151
    • Malik, D.K.1    Baboota, S.2    Ahuja, A.3
  • 24
    • 33751253462 scopus 로고    scopus 로고
    • Nanoparticles as potential oral delivery systems of proteins and vaccines: A mechanistic approach
    • des Rieux A, Fievez V, Garinot M, et al. Nanoparticles as potential oral delivery systems of proteins and vaccines: A mechanistic approach. J Control Release. 2006;116:1-27.
    • (2006) J Control Release , vol.116 , pp. 1-27
    • des Rieux, A.1    Fievez, V.2    Garinot, M.3
  • 25
    • 62849083225 scopus 로고    scopus 로고
    • Synthesis and evaluation of lauryl succinyl chitosan particles towards oral insulin delivery and absorption
    • Rekha MR, Sharma CP. Synthesis and evaluation of lauryl succinyl chitosan particles towards oral insulin delivery and absorption. J Control Release. 2009;135:144-151.
    • (2009) J Control Release , vol.135 , pp. 144-151
    • Rekha, M.R.1    Sharma, C.P.2
  • 26
    • 0001664347 scopus 로고
    • Oral and parenteral administration of insulin associated to hydrolysable nanoparticles
    • Couvreur P, Lenaerts V, Kante B, et al. Oral and parenteral administration of insulin associated to hydrolysable nanoparticles. Acta Pharm Technol. 1980;26:220-222.
    • (1980) Acta Pharm Technol , vol.26 , pp. 220-222
    • Couvreur, P.1    Lenaerts, V.2    Kante, B.3
  • 27
    • 0033911983 scopus 로고    scopus 로고
    • Insulin-loaded nanocapsules for oral administration: In vitro and in vivo investigation
    • Aboubakar M, Couvreur P, Pinto-Alphandary H, et al. Insulin-loaded nanocapsules for oral administration: in vitro and in vivo investigation. Drug Develop Res. 2000;49:109-117.
    • (2000) Drug Develop Res , vol.49 , pp. 109-117
    • Aboubakar, M.1    Couvreur, P.2    Pinto-Alphandary, H.3
  • 29
    • 39749105878 scopus 로고    scopus 로고
    • Self-assembled glycol chitosan nanoparticles for the sustained and prolonged delivery of antiangiogenic small peptide drugs in cancer therapy
    • Kim JH, Kim YS, Park K, et al. Self-assembled glycol chitosan nanoparticles for the sustained and prolonged delivery of antiangiogenic small peptide drugs in cancer therapy. Biomaterials. 2008;29:1920-1930.
    • (2008) Biomaterials , vol.29 , pp. 1920-1930
    • Kim, J.H.1    Kim, Y.S.2    Park, K.3
  • 30
    • 67849118615 scopus 로고    scopus 로고
    • Pharmacokinetics and bone formation by BMP-2 entrapped in polyethylenimine-coated albumin nanoparticles
    • Zhang S, Doschak MR, Uluda H. Pharmacokinetics and bone formation by BMP-2 entrapped in polyethylenimine-coated albumin nanoparticles. Biomaterials. 2009;30:5143-5155.
    • (2009) Biomaterials , vol.30 , pp. 5143-5155
    • Zhang, S.1    Doschak, M.R.2    Uluda, H.3
  • 31
    • 0038445582 scopus 로고    scopus 로고
    • Biodegradable microspheres for protein delivery
    • Sinha VR, Trehan A. Biodegradable microspheres for protein delivery. J Control Release. 2003;90:261-280.
    • (2003) J Control Release , vol.90 , pp. 261-280
    • Sinha, V.R.1    Trehan, A.2
  • 33
    • 27744508956 scopus 로고    scopus 로고
    • Paclitaxel-loaded PLGA nanoparticles: Potentiation of anticancer activity by surface conjugation with wheat germ agglutinin
    • Mo Y, Lim LY. Paclitaxel-loaded PLGA nanoparticles: potentiation of anticancer activity by surface conjugation with wheat germ agglutinin. J Control Release. 2005;108:244-262.
    • (2005) J Control Release , vol.108 , pp. 244-262
    • Mo, Y.1    Lim, L.Y.2
  • 34
    • 68749092564 scopus 로고    scopus 로고
    • Targeted epidermal growth factor receptor nanoparticle bioconjugates for breast cancer therapy
    • Acharya S, Dilnawaz F, Sahoo SK. Targeted epidermal growth fac- tor receptor nanoparticle bioconjugates for breast cancer therapy. Biomaterials. 2009;30:5737-5750.
    • (2009) Biomaterials , vol.30 , pp. 5737-5750
    • Acharya, S.1    Dilnawaz, F.2    Sahoo, S.K.3
  • 36
    • 24644434876 scopus 로고    scopus 로고
    • In vivo magnetic resonance detection of cancer by using multifunctional magnetic nanocrystals
    • Huh YM. In vivo magnetic resonance detection of cancer by using multifunctional magnetic nanocrystals. J Am Chem Soc. 2005;127:12387-12391.
    • (2005) J Am Chem Soc , vol.127 , pp. 12387-12391
    • Huh, Y.M.1
  • 37
    • 26444620215 scopus 로고    scopus 로고
    • Development of tumor targeting bioprobes (In-chimeric L6 mAb nanoparticles) for alternating magnetic field cancer therapy
    • DeNardo SJ, De Nardo GL, Miers LA, et al. Development of tumor targeting bioprobes (In-chimeric L6 mAb nanoparticles) for alternating magnetic field cancer therapy. Clin Cancer Res. 2005;11:7087-7092.
    • (2005) Clin Cancer Res , vol.11 , pp. 7087-7092
    • Denardo, S.J.1    de Nardo, G.L.2    Miers, L.A.3
  • 38
    • 27944494819 scopus 로고    scopus 로고
    • Development and brain delivery of chitosan-PEG nanoparticles functionalized with the monoclonal antibody OX26
    • Aktaş Y, Yemisci M, Andrieux K, et al. Development and brain delivery of chitosan-PEG nanoparticles functionalized with the monoclonal antibody OX26. Bioconjug Chem. 2005;16:1503-1511.
    • (2005) Bioconjug Chem , vol.16 , pp. 1503-1511
    • Aktaş, Y.1    Yemisci, M.2    Andrieux, K.3
  • 39
    • 6344291059 scopus 로고    scopus 로고
    • A rapid bioassay for single bacterial cell quantitation using bioconjugated nanoparticle
    • Zhao X, Hilliard LR, Merchery SJ, et al. A rapid bioassay for single bacterial cell quantitation using bioconjugated nanoparticle. Proc Natl Acad Sci USA. 2004;101:5027-5032.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5027-5032
    • Zhao, X.1    Hilliard, L.R.2    Merchery, S.J.3
  • 40
    • 39749145048 scopus 로고    scopus 로고
    • Development of multivalent radioimmunonanoparticles for cancer imaging and therapy
    • Natarajan A, Xiong CY, Gruattner C, et al. Development of multivalent radioimmunonanoparticles for cancer imaging and therapy. Cancer Biol Ther. 2008;23:82-90.
    • (2008) Cancer Biol Ther , vol.23 , pp. 82-90
    • Natarajan, A.1    Xiong, C.Y.2    Gruattner, C.3
  • 41
    • 0032721936 scopus 로고    scopus 로고
    • Effect of cell-cell interactions in preservation of cellullar phenotype: Cocultivation of hepatocytes and nonparenchymal cells
    • Bhatia SN, Balis UJ, Yarmush ML, et al. Effect of cell-cell interactions in preservation of cellullar phenotype: cocultivation of hepatocytes and nonparenchymal cells. FASEB J. 1999;13:1883-1900.
    • (1999) FASEB J , vol.13 , pp. 1883-1900
    • Bhatia, S.N.1    Balis, U.J.2    Yarmush, M.L.3
  • 42
    • 0035168305 scopus 로고    scopus 로고
    • Biological responses to materials
    • Anderson JM. Biological responses to materials. Annu Rev Mater Res. 2001;31:81-110.
    • (2001) Annu Rev Mater Res , vol.31 , pp. 81-110
    • Anderson, J.M.1
  • 43
    • 0037039862 scopus 로고    scopus 로고
    • Third-generation biomedical materials
    • Hench LL, Polak JM. Third-generation biomedical materials. Sci. 2002;295:1014-1017.
    • (2002) Sci , vol.295 , pp. 1014-1017
    • Hench, L.L.1    Polak, J.M.2
  • 44
    • 0037637656 scopus 로고    scopus 로고
    • Interaction of soft condensed Interaction of soft condensed materials with living cells: Phenotype/transcriptome correlations for the hydrophobic effect
    • Allen LT, Fox EJP, Blute I, et al. Interaction of soft condensed Interaction of soft condensed materials with living cells: phenotype/transcriptome correlations for the hydrophobic effect. Proc Natl Acad Sci USA. 2003;100:6331-6336.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6331-6336
    • Allen, L.T.1    Fox, E.J.P.2    Blute, I.3
  • 45
    • 0042562089 scopus 로고    scopus 로고
    • Biomimetic materials for tissue engineering
    • Heungsoo S, Seongbong J, Mikos AG. Biomimetic materials for tissue engineering. Biomaterials. 2003;24:4353-4364.
    • (2003) Biomaterials , vol.24 , pp. 4353-4364
    • Heungsoo, S.1    Seongbong, J.2    Mikos, A.G.3
  • 46
    • 1642303297 scopus 로고    scopus 로고
    • Control of cell adhesion and detachment using temperature and thermoresponsive copolymer grafted culture surfaces
    • Tsuda Y, Kikuchi A, Yamato M, et al. Control of cell adhesion and detachment using temperature and thermoresponsive copolymer grafted culture surfaces. J Biomed Mater Res. 2004;69A:70-78.
    • (2004) J Biomed Mater Res , vol.69 A , pp. 70-78
    • Tsuda, Y.1    Kikuchi, A.2    Yamato, M.3
  • 47
    • 33847789142 scopus 로고    scopus 로고
    • Understanding the nanoparticle- protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles
    • Cedervall T, Lynch I, Lindman S, et al. Understanding the nanoparticle- protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci USA. 2007;104: 2050-2055.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2050-2055
    • Cedervall, T.1    Lynch, I.2    Lindman, S.3
  • 48
    • 31944451232 scopus 로고    scopus 로고
    • Toxic potential of materials at the nanolevel
    • Nel A, Xia T, Madler L, Li N. Toxic potential of materials at the nanolevel. Science. 2006;311:622-627.
    • (2006) Science , vol.311 , pp. 622-627
    • Nel, A.1    Xia, T.2    Madler, L.3    Li, N.4
  • 49
    • 33646183969 scopus 로고    scopus 로고
    • Detecting cryptic epitopes created by nanoparticles
    • Lynch I, Dawson KA, Linse S. Detecting cryptic epitopes created by nanoparticles. Sci STKE. 2006; 327: pe14.
    • (2006) Sci STKE , vol.327
    • Lynch, I.1    Dawson, K.A.2    Linse, S.3
  • 50
    • 35349010059 scopus 로고    scopus 로고
    • The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century
    • Lynch I, Cedervall T, Lundqvist M, et al. The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. Adv Colloid Interface Sci. 2007;134-135:167-174.
    • (2007) Adv Colloid Interface Sci , vol.134-135 , pp. 167-174
    • Lynch, I.1    Cedervall, T.2    Lundqvist, M.3
  • 51
    • 12244291636 scopus 로고    scopus 로고
    • New multivalent cationic lipids reveal bell curve for transfection efficiency versus membrane charge density: Lipid-DNA complexes for gene delivery
    • Ahmad A, Evans HM, Ewert K, et al. New multivalent cationic lipids reveal bell curve for transfection efficiency versus membrane charge density: lipid-DNA complexes for gene delivery. J Gene Med. 2005;7:739-748.
    • (2005) J Gene Med , vol.7 , pp. 739-748
    • Ahmad, A.1    Evans, H.M.2    Ewert, K.3
  • 53
    • 34249894977 scopus 로고    scopus 로고
    • Targeting cancer cells using PLGA nanoparticles surface modified with monoclonal antibody
    • Kocbek P, Obermajer N, Cegnar M, et al. Targeting cancer cells using PLGA nanoparticles surface modified with monoclonal antibody. J Control Release. 2007;120:18-26.
    • (2007) J Control Release , vol.120 , pp. 18-26
    • Kocbek, P.1    Obermajer, N.2    Cegnar, M.3
  • 54
    • 0037051027 scopus 로고    scopus 로고
    • The role of surface science in bioengineered materials
    • Tirrel M, Kokkoli E, Biesalski M. The role of surface science in bioengineered materials. Surf Sci. 2002;500:61-83.
    • (2002) Surf Sci , vol.500 , pp. 61-83
    • Tirrel, M.1    Kokkoli, E.2    Biesalski, M.3
  • 55
    • 0014489983 scopus 로고
    • Identification of rapid changes at plasma-solid interfaces
    • Vroman L, Adams AL. Identification of rapid changes at plasma-solid interfaces. J Biomed Mater Res. 1969;3:43-67.
    • (1969) J Biomed Mater Res , vol.3 , pp. 43-67
    • Vroman, L.1    Adams, A.L.2
  • 56
    • 0000879597 scopus 로고
    • Plasma proteins: Their role in initiating platelet and fibrin deposition on biomaterials
    • Cooper SL, Peppas NA, editors, Washington, DC: American Chemical Society
    • Young BR, Lambrecht LK, Mosher DF, et al. Plasma proteins: Their role in initiating platelet and fibrin deposition on biomaterials. In: Cooper SL, Peppas NA, editors. Biomaterials: Interfacial phenomena and applications. Washington, DC: American Chemical Society: 1982;199:317-349.
    • (1982) Biomaterials: Interfacial Phenomena and Applications , vol.199 , pp. 317-349
    • Young, B.R.1    Lambrecht, L.K.2    Mosher, D.F.3
  • 57
    • 23444444512 scopus 로고
    • Biodegradable long- circulating polymeric nanospheres
    • Gref R, Minamitake Y, Peracchia MT, et al. Biodegradable long- circulating polymeric nanospheres. Science. 1994;263:1600-1603.
    • (1994) Science , vol.263 , pp. 1600-1603
    • Gref, R.1    Minamitake, Y.2    Peracchia, M.T.3
  • 58
    • 28844488494 scopus 로고    scopus 로고
    • Opsonization, biodistribution, and pharmacokinetics of polymeric nanoparticles
    • Owens DE, Peppas NA. Opsonization, biodistribution, and phar- macokinetics of polymeric nanoparticles. Int J Pharm. 2006;307: 93-102.
    • (2006) Int J Pharm , vol.307 , pp. 93-102
    • Owens, D.E.1    Peppas, N.A.2
  • 59
    • 0025781819 scopus 로고
    • The role of complement in inflammation and phagocytosis
    • Frank M, Fries L. The role of complement in inflammation and phagocytosis. Immunol Today. 1991;12:322-326.
    • (1991) Immunol Today , vol.12 , pp. 322-326
    • Frank, M.1    Fries, L.2
  • 60
    • 39749107963 scopus 로고    scopus 로고
    • Protein-nanoparticle interactions
    • Lynch I, Dawson K A. Protein-nanoparticle interactions. Nano Today. 2008;3:40-47.
    • (2008) Nano Today , vol.3 , pp. 40-47
    • Lynch, I.1    Dawson, K.A.2
  • 61
    • 35448990226 scopus 로고    scopus 로고
    • Adsorbed proteins influence the biological activity and molecular targeting of nanomaterials
    • Dutta D, Sundaram SK, Teeguarden JG, et al. Adsorbed proteins influence the biological activity and molecular targeting of nanomaterials. Toxicol Sci. 2007;100:303-315.
    • (2007) Toxicol Sci , vol.100 , pp. 303-315
    • Dutta, D.1    Sundaram, S.K.2    Teeguarden, J.G.3
  • 62
    • 0022575970 scopus 로고
    • The effect of hydrophilic coatings on the uptake of colloidal particles by the liver and by peritonealmacrophages
    • Illum L, Hunneybal IM, Davis SS. The effect of hydrophilic coatings on the uptake of colloidal particles by the liver and by peritonealmacrophages. Int J Pharm. 1986;29:53-65.
    • (1986) Int J Pharm , vol.29 , pp. 53-65
    • Illum, L.1    Hunneybal, I.M.2    Davis, S.S.3
  • 63
    • 0035997341 scopus 로고    scopus 로고
    • Long-circulating poly(ethylene glycol)-modified gelatin nanoparticles for intracellular delivery
    • Kaul G, Amiji M. Long-circulating poly(ethylene glycol)-modified gelatin nanoparticles for intracellular delivery. Pharm Res. 2002;19: 1061-1067.
    • (2002) Pharm Res , vol.19 , pp. 1061-1067
    • Kaul, G.1    Amiji, M.2
  • 64
    • 65749117793 scopus 로고    scopus 로고
    • Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy
    • Aggarwal P, Hall JB, McLeland CB, et al. Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv Drug Del Rev. 2009;61:428-437.
    • (2009) Adv Drug Del Rev , vol.61 , pp. 428-437
    • Aggarwal, P.1    Hall, J.B.2    McLeland, C.B.3
  • 65
    • 0025509594 scopus 로고
    • The behavior of some model proteins at solid-liquid interfaces. II. Sequential and competitive absorption
    • Arai T, Norde W. The behavior of some model proteins at solid-liquid interfaces. II. Sequential and competitive absorption. Colloid Surf. 1990;51:17-28.
    • (1990) Colloid Surf , vol.51 , pp. 17-28
    • Arai, T.1    Norde, W.2
  • 66
    • 34547454920 scopus 로고    scopus 로고
    • Nucleation of protein fibrillation by nanoparticles
    • Linse S, Cabaleiro-Lago C, Xue WF, et al. Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci USA. 2007;104: 8691-8696.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8691-8696
    • Linse, S.1    Cabaleiro-Lago, C.2    Xue, W.F.3
  • 67
    • 38049172612 scopus 로고    scopus 로고
    • Structure, stability, and activity of myoglobin adsorbed onto phosphate-grafted zirconia nanoparticles
    • Bellezza F, Cipiciani A, Quotadamo MA, et al. Structure, stability, and activity of myoglobin adsorbed onto phosphate-grafted zirconia nanoparticles. Langmuir. 2007;23:13007-13012.
    • (2007) Langmuir , vol.23 , pp. 13007-13012
    • Bellezza, F.1    Cipiciani, A.2    Quotadamo, M.A.3
  • 68
    • 34447517643 scopus 로고    scopus 로고
    • Effects of hydrated forms of C60 fullerene on amyloid b-peptide fibrillization in vitro and performance of the cognitive task
    • Podolski IY, Podlubnaya ZA, Kosenko EA, et al. Effects of hydrated forms of C60 fullerene on amyloid b-peptide fibrillization in vitro and performance of the cognitive task. J Nanosci Nanotechnol. 2007;7:1479-1485.
    • (2007) J Nanosci Nanotechnol , vol.7 , pp. 1479-1485
    • Podolski, I.Y.1    Podlubnaya, Z.A.2    Kosenko, E.A.3
  • 69
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation- based prion inheritance
    • Chien P, Weissman JS, DePace AH. Emerging principles of conformation- based prion inheritance. Annu Rev Biochem. 2004;73:617-656.
    • (2004) Annu Rev Biochem , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    Depace, A.H.3
  • 70
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Ann Rev Biochem. 2006;75:333-366.
    • (2006) Ann Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 71
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its link with human disease
    • Dobson CM. The structural basis of protein folding and its link with human disease. Philos Trans R Soc Lond B Biol Sci. 2001;356:133-145.
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 72
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo EH, Lansbury PT Jr, Kelly JW. Amyloid diseases: abnormal protein aggregation in neurodegeneration. Proc Natl Acad Sci USA. 1999;96:9989-9990.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury Jr., P.T.2    Kelly, J.W.3
  • 73
    • 0030050003 scopus 로고    scopus 로고
    • Beta-2-microglobulin associated amyloidosis
    • Floege J, Ehlerding G. Beta-2-microglobulin associated amyloidosis. Nephron. 1996;72:9-26.
    • (1996) Nephron , vol.72 , pp. 9-26
    • Floege, J.1    Ehlerding, G.2
  • 74
    • 67650376724 scopus 로고    scopus 로고
    • SCENIHR (Scientific Committee on Emerging and Newly Identified Health Risks), Brussels, Belgium: European Commission
    • SCENIHR (Scientific Committee on Emerging and Newly Identified Health Risks). Risk Assessment of Products of Nanotechnologies. Brussels, Belgium: European Commission; 2009. p. 1-71.
    • (2009) Risk Assessment of Products of Nanotechnologies , pp. 1-71
  • 75
    • 77951177107 scopus 로고    scopus 로고
    • Nanoparticles: Coat of proteins
    • Chun AL. Nanoparticles: Coat of proteins. Nat Nanotechnology. 2008.
    • (2008) Nat Nanotechnology
    • Chun, A.L.1
  • 76
    • 33847781099 scopus 로고    scopus 로고
    • Probing the interactions of proteins and nanoparticles
    • Klein J. Probing the interactions of proteins and nanoparticles. Proc Natl Acad Sci USA. 2007;104:2029-2030.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2029-2030
    • Klein, J.1
  • 77
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • Lundqvist M, Stigler J, Elia G, et al. Nanoparticle size and surface properties determine the protein corona with possible implica- tions for biological impacts. Proc Natl Acad Sci USA. 2008;105: 14265-14270.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14265-14270
    • Lundqvist, M.1    Stigler, J.2    Elia, G.3
  • 78
    • 0344306504 scopus 로고    scopus 로고
    • Protein absorption on mixtures of hydroxyl-and methyl-terminated alkanethiols self-assembleted monolayers
    • Martins MCL, Ratner BD, Barbosa MA. Protein absorption on mixtures of hydroxyl-and methyl-terminated alkanethiols self-assem- bleted monolayers. J Biomed Mater Res Pt A. 2003;67A:158-171.
    • (2003) J Biomed Mater Res Pt A , vol.67 A , pp. 158-171
    • Martins, M.C.L.1    Ratner, B.D.2    Barbosa, M.A.3
  • 79
    • 0001512382 scopus 로고
    • Structure and properties of protein films adsorbed at the air-water interface
    • Phillips MC, Evans MTA, Graham DE, et al. Structure and properties of protein films adsorbed at the air-water interface. Colloid Polym Sci. 1975;253:424-427.
    • (1975) Colloid Polym Sci , vol.253 , pp. 424-427
    • Phillips, M.C.1    Evans, M.T.A.2    Graham, D.E.3
  • 80
    • 0003210994 scopus 로고
    • Proteins at Interfaces: Physicochemical and biochemical studies
    • editors, Washington, DC: American Chemical Society
    • Brash JL, Horbett TA, editors. Proteins at Interfaces: Physicochemical and biochemical studies. Advanced Symposium Series, 343. Washington, DC: American Chemical Society; 1987. http://catalogue.nla.gov.au/Record/36034.
    • (1987) Advanced Symposium Series , vol.343
    • Brash, J.L.1    Horbett, T.A.2
  • 81
    • 0003373776 scopus 로고
    • Proteins at Interfaces II: Fundamentals and application
    • editors, Washington, DC: American Chemical Society
    • Horbett TA, Brash JL, editors. Proteins at Interfaces II: Fundamentals and application. Advanced Symposium Series, 602. Washington, DC: American Chemical Society; 1995. http://searchworks.stanford.edu/view/3082531.
    • (1995) Advanced Symposium Series , vol.602
    • Horbett, T.A.1    Brash, J.L.2
  • 82
    • 0030026989 scopus 로고    scopus 로고
    • Protein absorption on solid surfaces
    • Hlady V, Buijs J. Protein absorption on solid surfaces. Curr Opin Biotechnol. 1996;7:72-77.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 72-77
    • Hlady, V.1    Buijs, J.2
  • 83
    • 0032522286 scopus 로고    scopus 로고
    • Effect of surface wetability on the absorption of proteins and detergents
    • Sigal GB, Mrksich M, Whitesides GM. Effect of surface wetability on the absorption of proteins and detergents. J Am Chem Soc. 1998;120:3464-3473.
    • (1998) J Am Chem Soc , vol.120 , pp. 3464-3473
    • Sigal, G.B.1    Mrksich, M.2    Whitesides, G.M.3
  • 84
    • 0031997948 scopus 로고    scopus 로고
    • Imaging the molecular dimensions and oligomerization of proteins at liquid/solid interfaces
    • Waner MJ, Gilchrist M, Schindler M, et al. Imaging the molecular dimensions and oligomerization of proteins at liquid/solid interfaces. J Phys Chem B. 1998;102:1649-1657.
    • (1998) J Phys Chem B , vol.102 , pp. 1649-1657
    • Waner, M.J.1    Gilchrist, M.2    Schindler, M.3
  • 85
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of protein with solid surfaces
    • Gray JJ. The interaction of protein with solid surfaces. Curr Opin Struct Biol. 2004;14:110-115.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 110-115
    • Gray, J.J.1
  • 86
    • 58149181437 scopus 로고    scopus 로고
    • The absorption of globular protein onto a fluorinated PDMS surface
    • Wang D, Douma M, Swift B, et al. The absorption of globular protein onto a fluorinated PDMS surface. J Colloid Interface Sci. 2009;331: 90-97.
    • (2009) J Colloid Interface Sci , vol.331 , pp. 90-97
    • Wang, D.1    Douma, M.2    Swift, B.3
  • 87
    • 0000189822 scopus 로고
    • Absorption of complex proteins at interfaces
    • Andrade JD, Hlady V, Wei AP. Absorption of complex proteins at interfaces. Pure Appl Chem. 1992;64:1777-1781.
    • (1992) Pure Appl Chem , vol.64 , pp. 1777-1781
    • Andrade, J.D.1    Hlady, V.2    Wei, A.P.3
  • 89
    • 0031428603 scopus 로고    scopus 로고
    • Protein absorption on chemically modified surfaces
    • Collier TO, Jenney CR, Defife KM, et al. Protein absorption on chemi- cally modified surfaces. Biomed Sci Instrum. 1997;33:178-183.
    • (1997) Biomed Sci Instrum , vol.33 , pp. 178-183
    • Collier, T.O.1    Jenney, C.R.2    Defife, K.M.3
  • 90
    • 0343789033 scopus 로고    scopus 로고
    • Measuring surface- induced conformational changes in proteins
    • Moulin AM, O'Shea SJ, Badley RA, et al. Measuring surface- induced conformational changes in proteins. Langmuir. 1999;15: 8776-8779.
    • (1999) Langmuir , vol.15 , pp. 8776-8779
    • Moulin, A.M.1    O'Shea, S.J.2    Badley, R.A.3
  • 91
    • 0034247564 scopus 로고    scopus 로고
    • Protein deformation and surfactancy at an interface
    • Holt SA, McGillivray DJ, Poon S, et al. Protein deformation and surfactancy at an interface. J Phys Chem B. 2000;104:7431-7438.
    • (2000) J Phys Chem B , vol.104 , pp. 7431-7438
    • Holt, S.A.1    McGillivray, D.J.2    Poon, S.3
  • 92
    • 28144436331 scopus 로고    scopus 로고
    • Protein- poly(silicic)acid interactions at the air/solution interface
    • Henderson MJ, Perriman AW, Robson-Marsden H, et al. Protein- poly(silicic)acid interactions at the air/solution interface. J Phys Chem B. 2005;109:20878-20886.
    • (2005) J Phys Chem B , vol.109 , pp. 20878-20886
    • Henderson, M.J.1    Perriman, A.W.2    Robson-Marsden, H.3
  • 93
    • 37249070892 scopus 로고    scopus 로고
    • Effect of the air-water interface on the stability of ß-Lactoglobulin
    • Perriman AW, Henderson MJ, Holt SA, et al. Effect of the air-water interface on the stability of ß-Lactoglobulin. J Phys Chem B. 2007;111: 13527-13537.
    • (2007) J Phys Chem B , vol.111 , pp. 13527-13537
    • Perriman, A.W.1    Henderson, M.J.2    Holt, S.A.3
  • 94
    • 0022767908 scopus 로고
    • Protein absorption at solid liquid interfaces: Reversibility and conformation aspects
    • Norde W, MacRitchie F, Nowicka G, et al. Protein absorption at solid liquid interfaces: Reversibility and conformation aspects. J Colloid Interface Sci. 1986;112:447-456.
    • (1986) J Colloid Interface Sci , vol.112 , pp. 447-456
    • Norde, W.1    Macritchie, F.2    Nowicka, G.3
  • 95
    • 0029251458 scopus 로고
    • Structures and stabilities of adsorbed proteins
    • Hayens CA, Norde W. Structures and stabilities of adsorbed proteins. J Colloid Interface Sci. 1995;169:313-328.
    • (1995) J Colloid Interface Sci , vol.169 , pp. 313-328
    • Hayens, C.A.1    Norde, W.2
  • 96
    • 0035060814 scopus 로고    scopus 로고
    • On the absorption of proteins on solid surfaces, a common but very complicated phenomenon
    • Nakanishi K, Sakiyama T, Imaura K. On the absorption of proteins on solid surfaces, a common but very complicated phenomenon. J Biosc Bioeng. 2001;91:233-244.
    • (2001) J Biosc Bioeng , vol.91 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imaura, K.3
  • 97
    • 20444421544 scopus 로고    scopus 로고
    • Interpretation of protein absorption: Surface-induced conformational changes
    • Roach P, Farrar D, Perry CC. Interpretation of protein absorption: surface-induced conformational changes. J Am Chem Soc. 2005;127: 8168-8173.
    • (2005) J Am Chem Soc , vol.127 , pp. 8168-8173
    • Roach, P.1    Farrar, D.2    Perry, C.C.3
  • 98
    • 1442358527 scopus 로고    scopus 로고
    • Semi-synthetic DNA-protein conjugates: Novel tools in analytics and nanobiotechnology. Nucleic acids chemistry and biology
    • Niemeyer CM. Semi-synthetic DNA-protein conjugates: Novel tools in analytics and nanobiotechnology. Nucleic acids chemistry and biology. Biochem Soc Trans. 2004;32:51-53.
    • (2004) Biochem Soc Trans , vol.32 , pp. 51-53
    • Niemeyer, C.M.1
  • 99
    • 0036971119 scopus 로고    scopus 로고
    • Functional magnetic particles for medical application
    • Shinkai M. Functional magnetic particles for medical application. J Biosci Bioeng. 2002;94:606-613.
    • (2002) J Biosci Bioeng , vol.94 , pp. 606-613
    • Shinkai, M.1
  • 100
    • 53849138958 scopus 로고    scopus 로고
    • Bioconjugated silica nanoparticles: Development and applications
    • Wang L, Zhao W, Tan W. Bioconjugated silica nanoparticles: Development and applications. Nano Res. 2008;1:99-115.
    • (2008) Nano Res , vol.1 , pp. 99-115
    • Wang, L.1    Zhao, W.2    Tan, W.3
  • 101
    • 23844467409 scopus 로고    scopus 로고
    • Organically modified silica nanoparticles: A nonviral vector for in vivo gene delivery and expression in the brain
    • Bharali DJ, Ilona K, Ewa KS, et al. Organically modified silica nanopar- ticles: A nonviral vector for in vivo gene delivery and expression in the brain. Proc Natl Acad Sci USA. 2005;102:11539-11544.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11539-11544
    • Bharali, D.J.1    Ilona, K.2    Ewa, K.S.3
  • 102
    • 34250793248 scopus 로고    scopus 로고
    • Antibody-functionalized hybrid superparamagnetic nanoparticles
    • Arruebo M, Fernandez-Pacheco R, Velasco B, et al. Antibody-functionalized hybrid superparamagnetic nanoparticles. Adv Funct Mater. 2007;17: 1473-1479.
    • (2007) Adv Funct Mater , vol.17 , pp. 1473-1479
    • Arruebo, M.1    Fernandez-Pacheco, R.2    Velasco, B.3
  • 103
    • 33746889824 scopus 로고    scopus 로고
    • A novel magnetic bead bioassay platform using a microchip-based sensor for infectious disease diagnosis
    • Aytur T, Foley J, Anwar M, et al. A novel magnetic bead bioassay plat- form using a microchip-based sensor for infectious disease diagnosis. J Immunol Methods. 2006;314:21-29.
    • (2006) J Immunol Methods , vol.314 , pp. 21-29
    • Aytur, T.1    Foley, J.2    Anwar, M.3
  • 104
    • 0242586125 scopus 로고    scopus 로고
    • Collection of trace amounts of DNA/mRNA molecules using genomagnetic nanocapturers
    • Zhao X, Tapec-Dytioco R, Wang K, et al. Collection of trace amounts of DNA/mRNA molecules using genomagnetic nanocapturers. Anal Chem. 2003;75:3476-3483.
    • (2003) Anal Chem , vol.75 , pp. 3476-3483
    • Zhao, X.1    Tapec-Dytioco, R.2    Wang, K.3
  • 105
    • 33749003117 scopus 로고    scopus 로고
    • Receptor- targeted liposomal delivery of boron-containing cholesterol mimics for boron neutron capture therapy (BNCT)
    • Thirumamagal BTS, Zhao XB, Bandyopadhyaya AK, et al. Receptor- targeted liposomal delivery of boron-containing cholesterol mimics for boron neutron capture therapy (BNCT). Bioconjug Chem. 2006;17:1141-1150.
    • (2006) Bioconjug Chem , vol.17 , pp. 1141-1150
    • Thirumamagal, B.T.S.1    Zhao, X.B.2    Bandyopadhyaya, A.K.3
  • 107
    • 0037567245 scopus 로고    scopus 로고
    • Reductive dehalogenation of monobromobimane by tris(2-carboxyethyl)phosphine
    • Graham DE, Harich KC, White RH. Reductive dehalogenation of monobromobimane by tris(2-carboxyethyl)phosphine. Anal Biochem. 2003;318:325-328.
    • (2003) Anal Biochem , vol.318 , pp. 325-328
    • Graham, D.E.1    Harich, K.C.2    White, R.H.3
  • 108
    • 15744365262 scopus 로고    scopus 로고
    • Nanoparticle-based optical biosensors for the direct detection of organophosphate chemical warfare agents and pesticides
    • Simonian AL, Good TA, Wang SS, et al. Nanoparticle-based optical biosensors for the direct detection of organophosphate chemical warfare agents and pesticides. Anal Chim Acta. 2005;534: 69-77.
    • (2005) Anal Chim Acta , vol.534 , pp. 69-77
    • Simonian, A.L.1    Good, T.A.2    Wang, S.S.3
  • 109
    • 31544455023 scopus 로고    scopus 로고
    • Development of nanoparticle libraries for biosensing
    • Sun EY, Josephson L, Kelly KA, et al. Development of nanoparticle libraries for biosensing. Bioconjug Chem. 2006;17:109-113.
    • (2006) Bioconjug Chem , vol.17 , pp. 109-113
    • Sun, E.Y.1    Josephson, L.2    Kelly, K.A.3
  • 110
    • 33947178862 scopus 로고    scopus 로고
    • Synthesis and antibody conjugation of magnetic nanoparticles with improved specific power absorp- tion rates for alternating magnetic field cancer therapy
    • Grüttner C, Müller K, Teller J, et al. Synthesis and antibody conjuga- tion of magnetic nanoparticles with improved specific power absorp- tion rates for alternating magnetic field cancer therapy. J Magn Magn Mater. 2007;311:181-186.
    • (2007) J Magn Magn Mater , vol.311 , pp. 181-186
    • Grüttner, C.1    Müller, K.2    Teller, J.3
  • 111
    • 52649165549 scopus 로고    scopus 로고
    • Structure and function of nanoparticle- protein conjugates
    • 034001
    • Aubin-Tam ME, Schifferli KA. Structure and function of nanoparticle- protein conjugates. Biomed Mater. 2008;3(3):034001.
    • (2008) Biomed Mater , vol.3 , Issue.3
    • Aubin-Tam, M.E.1    Schifferli, K.A.2
  • 112
    • 0034671908 scopus 로고    scopus 로고
    • Preparation of surface modified protein nanoparticles by introduction of sulfhydryl groups
    • Weber C, Reiss S, Langer K. Preparation of surface modified protein nanoparticles by introduction of sulfhydryl groups. Int J Pharm. 2000;211:67-78.
    • (2000) Int J Pharm , vol.211 , pp. 67-78
    • Weber, C.1    Reiss, S.2    Langer, K.3
  • 113
    • 0013770208 scopus 로고
    • Reactions of N-ethylmaleimide with peptides and amino acids
    • Derek B, Smyth DG. Reactions of N-ethylmaleimide with peptides and amino acids. Biochem J. 1964;91:589-595.
    • (1964) Biochem J , vol.91 , pp. 589-595
    • Derek, B.1    Smyth, D.G.2
  • 115
    • 0021750406 scopus 로고
    • Use of the heterobifunctional cross-linker rn-maleimidobenzoyl N-hydroxysuccinimide ester to affinity label cholecystokinin binding proteins on rat pancreatic plasma membranes
    • Madison LD, Rosenzweig SA, Jamieson JD. Use of the heterobifunc- tional cross-linker rn-maleimidobenzoyl N-hydroxysuccinimide ester to affinity label cholecystokinin binding proteins on rat pancreatic plasma membranes. J Biol Chem. 1984;259:1481-1482.
    • (1984) J Biol Chem , vol.259 , pp. 1481-1482
    • Madison, L.D.1    Rosenzweig, S.A.2    Jamieson, J.D.3
  • 116
  • 117
    • 77951199713 scopus 로고    scopus 로고
    • Protein-Protein Interactions
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Golemis E. Protein-Protein Interactions. A molecular cloning manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 2002.
    • (2002) A Molecular Cloning Manual
    • Golemis, E.1
  • 118
    • 58149375843 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for in vitro diagnostics and in vivo imaging
    • Xing Y, Rao Y. Quantum dot bioconjugates for in vitro diagnostics and in vivo imaging. Cancer Biomark. 2008;4:307-319.
    • (2008) Cancer Biomark , vol.4 , pp. 307-319
    • Xing, Y.1    Rao, Y.2
  • 119
    • 57049104569 scopus 로고    scopus 로고
    • Chemical strategies for generating protein biochips
    • Jonkheijm P, Weinrich D, Schröder H, et al. Chemical strategies for generating protein biochips. Angew Chem Int Ed. 2008;47:9618-9647.
    • (2008) Angew Chem Int Ed , vol.47 , pp. 9618-9647
    • Jonkheijm, P.1    Weinrich, D.2    Schröder, H.3
  • 120
    • 33947482089 scopus 로고
    • Dithiothreitol, a new protective reagent for SH groups
    • Cleland WW. Dithiothreitol, a new protective reagent for SH groups. Biochemistry. 1964;3:480-482.
    • (1964) Biochemistry , vol.3 , pp. 480-482
    • Cleland, W.W.1
  • 121
    • 0015874433 scopus 로고
    • Methyl 4-mercaptobutyrimidate as a cleavable cross-linking reagent and its application to the Escherichia coli 30S ribosome
    • Traut RR, Bollen A, Sun TT, et al. Methyl 4-mercaptobutyrimidate as a cleavable cross-linking reagent and its application to the Escherichia coli 30S ribosome. Biochemistry. 1973;12:3266-3273.
    • (1973) Biochemistry , vol.12 , pp. 3266-3273
    • Traut, R.R.1    Bollen, A.2    Sun, T.T.3
  • 122
    • 0034595291 scopus 로고    scopus 로고
    • Preparation of avidin-labeled protein nanoparticles as carriers for biotinylated peptide nucleic acid
    • Langer K, Coester C, Weber C, et al. Preparation of avidin-labeled protein nanoparticles as carriers for biotinylated peptide nucleic acid. Eur J Pharm Biopharm. 2000;49:303-307.
    • (2000) Eur J Pharm Biopharm , vol.49 , pp. 303-307
    • Langer, K.1    Coester, C.2    Weber, C.3
  • 123
    • 0001654969 scopus 로고    scopus 로고
    • Antigen/antibody immunocomplex from CdTe nanoparticle bioconjugates
    • Wang S, Mamedova N, Kotov NA, et al. Antigen/antibody immunocomplex from CdTe nanoparticle bioconjugates. Nano Lett. 2002;2:817-822.
    • (2002) Nano Lett , vol.2 , pp. 817-822
    • Wang, S.1    Mamedova, N.2    Kotov, N.A.3
  • 124
    • 0039456274 scopus 로고    scopus 로고
    • Interaction of biotin with streptavidin. Thermostability and conformational changes upon binding
    • Gonzalez M, Bagatolli LA, Echabe I, et al. Interaction of biotin with streptavidin. Thermostability and conformational changes upon binding. J Biol Chem. 1997;272:11288-11294.
    • (1997) J Biol Chem , vol.272 , pp. 11288-11294
    • Gonzalez, M.1    Bagatolli, L.A.2    Echabe, I.3
  • 125
    • 0025288944 scopus 로고
    • Avidin and streptavidin
    • Green NM. Avidin and streptavidin. Method Enzymol. 1990;184:51-67.
    • (1990) Method Enzymol , vol.184 , pp. 51-67
    • Green, N.M.1
  • 126
    • 37349007292 scopus 로고    scopus 로고
    • Magnetic and MR relaxation properties of avidin-biotin conjugated superparamagnetic nanoparticles
    • Parka JA, Lee JJ, Kim IS, et al. Magnetic and MR relaxation properties of avidin-biotin conjugated superparamagnetic nanoparticles. Colloid Surf A. 2008;313-314:288-291.
    • (2008) Colloid Surf A , vol.313-314 , pp. 288-291
    • Parka, J.A.1    Lee, J.J.2    Kim, I.S.3
  • 127
    • 0034595291 scopus 로고    scopus 로고
    • Preparation of avidin-labeled protein nanoparticles as carriers for biotinylated peptide nucleic acid
    • Langer K, Coester C, Weber C, et al. Preparation of avidin-labeled protein nanoparticles as carriers for biotinylated peptide nucleic acid. Eu J Pharm Biopharm. 2000;49:303-307.
    • (2000) Eu J Pharm Biopharm , vol.49 , pp. 303-307
    • Langer, K.1    Coester, C.2    Weber, C.3
  • 128
    • 0033976710 scopus 로고    scopus 로고
    • Preparation of avidin- labelled gelatin nanoparticles as carriers for biotinylated peptide nucleic acid (PNA)
    • Coester C, Kreuter J, von Briesen H, et al. Preparation of avidin- labelled gelatin nanoparticles as carriers for biotinylated peptide nucleic acid (PNA). Int J Pharm. 2000;196:147-149.
    • (2000) Int J Pharm , vol.196 , pp. 147-149
    • Coester, C.1    Kreuter, J.2    von Briesen, H.3
  • 129
    • 0034814675 scopus 로고    scopus 로고
    • On the preparation, characterization, and enzymatic activity of fungal proteasegold colloid bioconjugates
    • Gole A, Dash C, Soman C, et al. On the preparation, characterization, and enzymatic activity of fungal proteasegold colloid bioconjugates. Bioconjug Chem. 2001;12:684-690.
    • (2001) Bioconjug Chem , vol.12 , pp. 684-690
    • Gole, A.1    Dash, C.2    Soman, C.3
  • 130
    • 0344444282 scopus 로고    scopus 로고
    • Influence of electrostatically bound proteins on the structure of linkage monolayers: Absorption of bovine serum albumin on silver and gold substrates coated with monolayers of 2-mercaptoethanesulphonate
    • Kudelski A. Influence of electrostatically bound proteins on the structure of linkage monolayers: absorption of bovine serum albumin on silver and gold substrates coated with monolayers of 2-mercaptoethanesulphonate. Vib Spectrosc. 2003;33:197-204.
    • (2003) Vib Spectrosc , vol.33 , pp. 197-204
    • Kudelski, A.1
  • 131
    • 0034660232 scopus 로고    scopus 로고
    • Effects of dithiothreitol on protein activity unrelated to thiol-disulfide exchange: For consideration in the analysis of protein function with Cleland's reagent
    • Alliegro MC. Effects of dithiothreitol on protein activity unrelated to thiol-disulfide exchange: for consideration in the analysis of protein function with Cleland's reagent. Anal Biochem. 2000;282: 102-106.
    • (2000) Anal Biochem , vol.282 , pp. 102-106
    • Alliegro, M.C.1
  • 132
    • 51249173761 scopus 로고
    • Effect of chemical modification on structure and activity of glucoamylase from Aspergillus candidus and Rhizopus species
    • Shenoy BC, Appu Rao AG, Raghavendra Rao MR. Effect of chemical modification on structure and activity of glucoamylase from Aspergillus candidus and Rhizopus species. J Biosci. 1987;11: 339-350.
    • (1987) J Biosci , vol.11 , pp. 339-350
    • Shenoy, B.C.1    Appu Rao, A.G.2    Raghavendra Rao, M.R.3
  • 133
    • 38949102704 scopus 로고    scopus 로고
    • Imaging epidermal growth factor receptor expression in vivo: Pharmacokinetic and biodistribution characterization of a bioconjugated quantum dot nanoprobe
    • Diagaradjane P, Orenstein-Cardona JM, Colon-Casasnovas NE, et al. Imaging epidermal growth factor receptor expression in vivo: pharmacokinetic and biodistribution characterization of a bioconjugated quantum dot nanoprobe. Clin Cancer Res. 2008;14:731-741.
    • (2008) Clin Cancer Res , vol.14 , pp. 731-741
    • Diagaradjane, P.1    Orenstein-Cardona, J.M.2    Colon-Casasnovas, N.E.3
  • 134
    • 0035937527 scopus 로고    scopus 로고
    • Liposomes with phosphatidylethanol as a carrier for oral delivery of insulin: Studies in the rat
    • Kisel MA, Kulik LN, Tsybovsky IS, et al. Liposomes with phospha- tidylethanol as a carrier for oral delivery of insulin: studies in the rat. Int J Pharm. 2001;216:105-115.
    • (2001) Int J Pharm , vol.216 , pp. 105-115
    • Kisel, M.A.1    Kulik, L.N.2    Tsybovsky, I.S.3
  • 135
    • 0029125089 scopus 로고
    • Liposomal hepatitis A vaccine and liposomal multiantigen combination vaccines
    • Gluck R. Liposomal hepatitis A vaccine and liposomal multiantigen combination vaccines. J Lipo Res. 1995;5:467-469.
    • (1995) J Lipo Res , vol.5 , pp. 467-469
    • Gluck, R.1
  • 136
    • 0028842728 scopus 로고
    • Engineering liposomes for drug delivery: Progress and problems
    • Gregoriadis G. Engineering liposomes for drug delivery: progress and problems. Trends Biotechnol. 1995;13:527-537.
    • (1995) Trends Biotechnol , vol.13 , pp. 527-537
    • Gregoriadis, G.1
  • 137
    • 3042611512 scopus 로고    scopus 로고
    • Protein encapsulation in liposomes: Efficiency depends on interactions between protein and phospholipid bilayer
    • Colletier JP, Chaize B, Winterhalter M, et al. Protein encapsulation in liposomes: efficiency depends on interactions between protein and phospholipid bilayer. BMC Biotechnol. 2002;2:1-8.
    • (2002) BMC Biotechnol , vol.2 , pp. 1-8
    • Colletier, J.P.1    Chaize, B.2    Winterhalter, M.3
  • 139
    • 33749323228 scopus 로고    scopus 로고
    • Entrapment of membrane proteins in Sol Gel derived silica
    • Besanger TR, Brennan JD. Entrapment of membrane proteins in Sol Gel derived silica. J Sol Gel Sci Techn. 2006;40:209-225.
    • (2006) J Sol Gel Sci Techn , vol.40 , pp. 209-225
    • Besanger, T.R.1    Brennan, J.D.2
  • 140
    • 3843083869 scopus 로고    scopus 로고
    • Bionanotechnology based on silica nanoparticles
    • Tan W, Wang K, He X, et al. Bionanotechnology based on silica nanoparticles. Med Res Rev. 2004;24:621-638.
    • (2004) Med Res Rev , vol.24 , pp. 621-638
    • Tan, W.1    Wang, K.2    He, X.3
  • 141
    • 60949086135 scopus 로고    scopus 로고
    • Synthesis of spherical mesoporous silica nanoparticles with nanometer-size controllable pores and outer diameters
    • Nandiyanto ABD, Kim SG, Iskandar F, et al. Synthesis of spherical mesoporous silica nanoparticles with nanometer-size controllable pores and outer diameters. Micropor Mesopor Mat. 2009;120: 447-453.
    • (2009) Micropor Mesopor Mat , vol.120 , pp. 447-453
    • Nandiyanto, A.B.D.1    Kim, S.G.2    Iskandar, F.3
  • 142
    • 0030595356 scopus 로고    scopus 로고
    • Immunological activities of IgG antibody on pre-coated Fc receptor surfaces
    • Lu B, Smyth MR, O'Keneddy JR. Immunological activities of IgG antibody on pre-coated Fc receptor surfaces. Anal Chim Acta. 1996;331:97-102.
    • (1996) Anal Chim Acta , vol.331 , pp. 97-102
    • Lu, B.1    Smyth, M.R.2    O'Keneddy, J.R.3
  • 144
    • 34548010536 scopus 로고    scopus 로고
    • Structural and functional characterization of enzyme quantum dots conjugates: Covalent attachment of CdS nanocryrtal to α-chemo trypsin
    • Narayanan SS, Sarkar R, Pal SK. Structural and functional characterization of enzyme quantum dots conjugates: covalent attachment of CdS nanocryrtal to α-chemo trypsin. J Phys Chem C. 2007;111:11539-11543.
    • (2007) J Phys Chem C , vol.111 , pp. 11539-11543
    • Narayanan, S.S.1    Sarkar, R.2    Pal, S.K.3
  • 145
    • 42049092775 scopus 로고    scopus 로고
    • Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses
    • Menaa B, Herrero M, Rives V, Lavrenko M, Eggers DK. Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses. Biomaterials. 2008;29:2710-2718.
    • (2008) Biomaterials , vol.29 , pp. 2710-2718
    • Menaa, B.1    Herrero, M.2    Rives, V.3    Lavrenko, M.4    Eggers, D.K.5
  • 146
    • 0037102139 scopus 로고    scopus 로고
    • Bone morphogenetic protein delivery systems
    • Seeherman H, Wozney J, Li R. Bone morphogenetic protein delivery systems. Spine. 2002;27:16-23.
    • (2002) Spine , vol.27 , pp. 16-23
    • Seeherman, H.1    Wozney, J.2    Li, R.3
  • 147
    • 0035937593 scopus 로고    scopus 로고
    • Polysaccharide colloidal particles as delivery systems for macromolecules
    • Janes KA, Calvo P, Alonso MJ. Polysaccharide colloidal particles as delivery systems for macromolecules. Adv Drug Deliv Rev. 2001;47:83-97.
    • (2001) Adv Drug Deliv Rev , vol.47 , pp. 83-97
    • Janes, K.A.1    Calvo, P.2    Alonso, M.J.3
  • 148
    • 0029335538 scopus 로고
    • Biodegradable polymers for protein and peptide drug delivery
    • Gombotz VR, Pettit DK. Biodegradable polymers for protein and peptide drug delivery. Bioconjug Chem. 1995;6:332-351.
    • (1995) Bioconjug Chem , vol.6 , pp. 332-351
    • Gombotz, V.R.1    Pettit, D.K.2
  • 149
    • 0343247711 scopus 로고    scopus 로고
    • Biodegradation and biocompatibility of PLA and PLGA microspheres
    • Anderson JM, Shive MS. Biodegradation and biocompatibility of PLA and PLGA microspheres. Adv Drug Deliv Rev. 1997;28:5-24.
    • (1997) Adv Drug Deliv Rev , vol.28 , pp. 5-24
    • Anderson, J.M.1    Shive, M.S.2
  • 150
    • 0031752709 scopus 로고    scopus 로고
    • Protein delivery from poly(lactic-coglycolic acid) biodegradable microspheres: Release kinetics and stability issues
    • Crotts G, Park TG. Protein delivery from poly(lactic-coglycolic acid) biodegradable microspheres: release kinetics and stability issues. J Microencapsul. 1998;15:699-713.
    • (1998) J Microencapsul , vol.15 , pp. 699-713
    • Crotts, G.1    Park, T.G.2
  • 151
    • 4644255691 scopus 로고    scopus 로고
    • A protein delivery system: Biodegradable alginate-chitosan-poly(lactic-co-glycolic acid) composite microspheres
    • Zheng CH, Goa JQ, Zhang YP, Liang WQ. A protein delivery system: biodegradable alginate-chitosan-poly(lactic-co-glycolic acid) composite microspheres. Biochem Biophys Res Commun. 2004;323: 1321-1327.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 1321-1327
    • Zheng, C.H.1    Goa, J.Q.2    Zhang, Y.P.3    Liang, W.Q.4
  • 153
    • 34249043665 scopus 로고    scopus 로고
    • Glycol chitosan as a stabilizer for protein encapsulated into poly(lactide-co-glycolide) microparticle
    • Lee ES, Park KH, Park IS, et al. Glycol chitosan as a stabilizer for protein encapsulated into poly(lactide-co-glycolide) microparticle. Int J Pharm. 2007;338:310-316.
    • (2007) Int J Pharm , vol.338 , pp. 310-316
    • Lee, E.S.1    Park, K.H.2    Park, I.S.3
  • 154
    • 62649106308 scopus 로고    scopus 로고
    • Intracellular drug delivery by poly(lactic-co-glycolic acid) nanoparticles, revisited
    • Xu P, Gullotti E, Tong L, et al. Intracellular drug delivery by poly(lactic-co-glycolic acid) nanoparticles, revisited. Mol Pharm. 2009;6:190-201.
    • (2009) Mol Pharm , vol.6 , pp. 190-201
    • Xu, P.1    Gullotti, E.2    Tong, L.3
  • 155
    • 0033003073 scopus 로고    scopus 로고
    • FTIR characterization of the secondary structure of proteins encapsulated with PLGA microspheres
    • Fu K, Griebenow K, Hsieh L, et al. FTIR characterization of the secondary structure of proteins encapsulated with PLGA microspheres. J Control Release. 1999;58:357-366.
    • (1999) J Control Release , vol.58 , pp. 357-366
    • Fu, K.1    Griebenow, K.2    Hsieh, L.3
  • 156
    • 0035850257 scopus 로고    scopus 로고
    • Pegylation enhances protein stability during encapsulation in PLGA microspheres
    • Diwan M, Park TG. Pegylation enhances protein stability during encapsulation in PLGA microspheres. J Control Release. 2001;73: 233-244.
    • (2001) J Control Release , vol.73 , pp. 233-244
    • Diwan, M.1    Park, T.G.2
  • 157
    • 0036027563 scopus 로고    scopus 로고
    • Comparison of the effects of Mg(OH)2 and sucrose on the stability of bovine serum albumin encapsulated in injectable poly(d,l-lactide-co-glycolide) implants
    • Kang J, Schwendeman SP. Comparison of the effects of Mg(OH)2 and sucrose on the stability of bovine serum albumin encapsulated in injectable poly(d,l-lactide-co-glycolide) implants. Biomaterials. 2002;23:239-245.
    • (2002) Biomaterials , vol.23 , pp. 239-245
    • Kang, J.1    Schwendeman, S.P.2
  • 158
    • 0033635054 scopus 로고    scopus 로고
    • Protein instability in poly(lactic-co-glycolic acid) microparticles
    • Van de Weert M, Hennink WE, Jiskoot W. Protein instability in poly(lactic-co-glycolic acid) microparticles. Pharm Res. 2004;17: 1159-1167.
    • (2004) Pharm Res , vol.17 , pp. 1159-1167
    • van de Weert, M.1    Hennink, W.E.2    Jiskoot, W.3
  • 159
    • 0037122736 scopus 로고    scopus 로고
    • Design of biodegradable particles for protein delivery
    • Vila A, Sanchez A, Tobio M, et al. Design of biodegradable particles for protein delivery. J Control Release. 2002;78:15-24.
    • (2002) J Control Release , vol.78 , pp. 15-24
    • Vila, A.1    Sanchez, A.2    Tobio, M.3
  • 160
    • 0030779190 scopus 로고    scopus 로고
    • Chitosan and chitosan/ ethylene oxide-propylene oxide block copolymer nanoparticles as novel carriers for proteins and vaccines
    • Calvo P, Remuñan-López C, Vila-Jato JL, et al. Chitosan and chitosan/ ethylene oxide-propylene oxide block copolymer nanoparticles as novel carriers for proteins and vaccines. Pharm Res. 1997;14: 1431-1436.
    • (1997) Pharm Res , vol.14 , pp. 1431-1436
    • Calvo, P.1    Remuñan-López, C.2    Vila-Jato, J.L.3
  • 161
    • 0031550212 scopus 로고    scopus 로고
    • Novel hydrophilic chitosan-polyethylene oxide nanoparticles as protein carriers
    • Calvo P, Remunan-Lopez C, Vila-Jato JL, et al. Novel hydrophilic chitosan-polyethylene oxide nanoparticles as protein carriers. J Appl Polymer Sci. 1997;63:125-132.
    • (1997) J Appl Polymer Sci , vol.63 , pp. 125-132
    • Calvo, P.1    Remunan-Lopez, C.2    Vila-Jato, J.L.3
  • 162
    • 0030779190 scopus 로고    scopus 로고
    • Chitosan and chitosan/ ethylene oxide-propylene oxide block copolymer nanoparticles as novel carriers for proteins and vaccines
    • Calvo P, Remunan-Lopez C, Vila-Jato JL, et al. Chitosan and chitosan/ ethylene oxide-propylene oxide block copolymer nanoparticles as novel carriers for proteins and vaccines. Pharm Res. 1997;14: 1431-1436.
    • (1997) Pharm Res , vol.14 , pp. 1431-1436
    • Calvo, P.1    Remunan-Lopez, C.2    Vila-Jato, J.L.3
  • 163
    • 33344467489 scopus 로고    scopus 로고
    • Preparation and characterization of protein-loaded N-trimethyl chitosan nanoparticles as nasal delivery system
    • Amidi M, Romeijn SG, Borchard G, et al. Preparation and character- ization of protein-loaded N-trimethyl chitosan nanoparticles as nasal delivery system. J Control Release. 2006;111:107-116.
    • (2006) J Control Release , vol.111 , pp. 107-116
    • Amidi, M.1    Romeijn, S.G.2    Borchard, G.3
  • 164
    • 34948841373 scopus 로고    scopus 로고
    • Probing insulin's secondary structure after entrapment into alginate/chitosan nanoparticles
    • Sarmento B, Ferreira DC, Jorgensen L, et al. Probing insulin's secondary structure after entrapment into alginate/chitosan nanoparticles. Eur J Pharm Biopharm. 2007;65:10-17.
    • (2007) Eur J Pharm Biopharm , vol.65 , pp. 10-17
    • Sarmento, B.1    Ferreira, D.C.2    Jorgensen, L.3
  • 165
    • 35048879814 scopus 로고    scopus 로고
    • Quaternized chitosan/alginate nanoparticles for protein delivery
    • Li T, Shi XW, Du YM, et al. Quaternized chitosan/alginate nanoparticles for protein delivery. J Biomed Mater Res A. 2007;83:383-390.
    • (2007) J Biomed Mater Res A , vol.83 , pp. 383-390
    • Li, T.1    Shi, X.W.2    Du, Y.M.3
  • 166
    • 58149166741 scopus 로고    scopus 로고
    • Novel composite microparticles for protein stabilization and delivery
    • Schoubben A, Blasi P, Giovagnoli S, et al. Novel composite microparticles for protein stabilization and delivery. Eur J Pharm Sci. 2009;36:226-234.
    • (2009) Eur J Pharm Sci , vol.36 , pp. 226-234
    • Schoubben, A.1    Blasi, P.2    Giovagnoli, S.3
  • 167
    • 0025239633 scopus 로고
    • The gene 1.2 protein of bacteriophage T7 interacts with the E. coli dGTP triphosphohydrolase to form a GTP-binding protein
    • Nakai H, Richardson CC. The gene 1.2 protein of bacteriophage T7 interacts with the E. coli dGTP triphosphohydrolase to form a GTP-binding protein. J Biol Chem. 1990;265:4411-4419.
    • (1990) J Biol Chem , vol.265 , pp. 4411-4419
    • Nakai, H.1    Richardson, C.C.2
  • 169
    • 0016649099 scopus 로고
    • Lactose synthetase
    • Hill RL, Brew K. Lactose synthetase. Adv Enzymol. 1975;43: 411-490.
    • (1975) Adv Enzymol , vol.43 , pp. 411-490
    • Hill, R.L.1    Brew, K.2
  • 170
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzyme
    • Srere PA. Complexes of sequential metabolic enzyme. Ann Rev Biochem. 1987;56:89-124.
    • (1987) Ann Rev Biochem , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 171
    • 0023091938 scopus 로고
    • Functional identity of proliferating cell nuclear antigen and a DNA Polymerase-δ auxiliary protein
    • Prelich G, Tan CK, Kostura M, et al. Functional identity of proliferating cell nuclear antigen and a DNA Polymerase-δ auxiliary protein. Nature. 1989;326:517-520.
    • (1989) Nature , vol.326 , pp. 517-520
    • Prelich, G.1    Tan, C.K.2    Kostura, M.3


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