메뉴 건너뛰기




Volumn 4, Issue , 2006, Pages

A nanoparticle-based immobilization assay for prion-kinetics study

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PRECIPITATION (CHEMICAL); REACTION KINETICS; SYNTHESIS (CHEMICAL); TRANSMISSION ELECTRON MICROSCOPY;

EID: 33749422892     PISSN: 14773155     EISSN: 14773155     Source Type: Journal    
DOI: 10.1186/1477-3155-4-8     Document Type: Article
Times cited : (25)

References (26)
  • 1
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein misfolding diseases
    • Cohen FE, Kelly JW: Therapeutic approaches to protein misfolding diseases. Nature 2003, 426:905-909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 3
    • 0036606794 scopus 로고    scopus 로고
    • Conformational polymorphism of wildtype and mutant rion proteins: Energy landscape analysis
    • Levy Y, Becker OM: Conformational polymorphism of wildtype and mutant rion proteins: Energy landscape analysis. Proteins, structure, function and genetics 2002, 47:458-468.
    • (2002) Proteins, Structure, Function and Genetics , vol.47 , pp. 458-468
    • Levy, Y.1    Becker, O.M.2
  • 4
    • 0038266598 scopus 로고    scopus 로고
    • Atypical effect of salts on the thermodynamics stability of human prion protein
    • Apetri AC, Surewicz WK: Atypical effect of salts on the thermodynamics stability of human prion protein. J Biol Chem 2003, 278:22187-22191.
    • (2003) J Biol Chem , vol.278 , pp. 22187-22191
    • Apetri, A.C.1    Surewicz, W.K.2
  • 8
    • 0035794531 scopus 로고    scopus 로고
    • Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form
    • Leclerc E, Peretz D, Ball H, Sakurai H, Legname G, Serban A, Prusiner SB, Burton D, Williamson RA: Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form. EMBO J 2001, 20:1547-1554.
    • (2001) EMBO J , vol.20 , pp. 1547-1554
    • Leclerc, E.1    Peretz, D.2    Ball, H.3    Sakurai, H.4    Legname, G.5    Serban, A.6    Prusiner, S.B.7    Burton, D.8    Williamson, R.A.9
  • 9
    • 0037069065 scopus 로고    scopus 로고
    • Preliminary epidemiological analyses of the first 16 cases of the BSE born after July 1996
    • Welesmith JW: Preliminary epidemiological analyses of the first 16 cases of the BSE born after July 1996. Vet Rec 2002, 151:451-452.
    • (2002) Vet Rec , vol.151 , pp. 451-452
    • Welesmith, J.W.1
  • 10
    • 33749409437 scopus 로고    scopus 로고
    • Canada wraps up BSE investigation
    • Kuehn BM: Canada wraps up BSE investigation. J Am Vet Assoc 2003, 223:919-921.
    • (2003) J Am Vet Assoc , vol.223 , pp. 919-921
    • Kuehn, B.M.1
  • 11
    • 24044438861 scopus 로고    scopus 로고
    • Protein Nanotechnology- a powerful futuristic diagnostic technique
    • Gupta PD, Dave M, Vasavada AR: Protein Nanotechnology- a powerful futuristic diagnostic technique. Ind J Clin Biochem 2005, 20:48-53.
    • (2005) Ind J Clin Biochem , vol.20 , pp. 48-53
    • Gupta, P.D.1    Dave, M.2    Vasavada, A.R.3
  • 12
    • 0033970146 scopus 로고    scopus 로고
    • Elucidation of protein-protein interaction using chemical cross-linking or label transfer techniques
    • Fancy DA: Elucidation of protein-protein interaction using chemical cross-linking or label transfer techniques. Curr Opin Chem Biol 2000, 4:28-33.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 28-33
    • Fancy, D.A.1
  • 13
    • 0031888694 scopus 로고    scopus 로고
    • Quantitative structure-function and structure-stability relationship of purposely modified proteins
    • Damborský J: Quantitative structure-function and structure-stability relationship of purposely modified proteins. Protein Eng 1998, 11:21-30.
    • (1998) Protein Eng , vol.11 , pp. 21-30
    • Damborský, J.1
  • 14
    • 33745627647 scopus 로고    scopus 로고
    • Functional antibody immobilization and 3-dimentional polymeric surface generated by reactive ion etching
    • Rucker VC, Havenstrite KL, Simmons BA, Sickafoose SM, Herr AE, Shediac R: Functional antibody immobilization and 3-dimentional polymeric surface generated by reactive ion etching. Longmuir 2005, 21:7621-7625.
    • (2005) Langmuir , vol.21 , pp. 7621-7625
    • Rucker, V.C.1    Havenstrite, K.L.2    Simmons, B.A.3    Sickafoose, S.M.4    Herr, A.E.5    Shediac, R.6
  • 16
    • 0038039289 scopus 로고    scopus 로고
    • Direct binding and characterization of lipase onto magnetic nanoparticles
    • Huang SH, Liao MH, Chen DH: Direct binding and characterization of lipase onto magnetic nanoparticles. Biotechnol Prog 2003, 19:1095-1100.
    • (2003) Biotechnol Prog , vol.19 , pp. 1095-1100
    • Huang, S.H.1    Liao, M.H.2    Chen, D.H.3
  • 18
    • 0035915124 scopus 로고    scopus 로고
    • Nanoparticles, proteins, and nucleic acid: Biotechnology meets materials science
    • Niemeyer CM: Nanoparticles, proteins, and nucleic acid: Biotechnology meets materials science. Angew Chem In Ed 2001, 4:4128-4148.
    • (2001) Angew Chem In Ed , vol.4 , pp. 4128-4148
    • Niemeyer, C.M.1
  • 19
    • 18144426112 scopus 로고    scopus 로고
    • Gold-nanoparticles-assisted oligonucleotides immobilization for improved DNA detection
    • Minard-Basquin C, Kögler R, Matsuzawa NN, Yasuda A: Gold-nanoparticles-assisted oligonucleotides immobilization for improved DNA detection. IEEE Proc-Nanotechnol 2005, 152:97-103.
    • (2005) IEEE Proc-Nanotechnol , vol.152 , pp. 97-103
    • Minard-Basquin, C.1    Kögler, R.2    Matsuzawa, N.N.3    Yasuda, A.4
  • 20
    • 0034669474 scopus 로고    scopus 로고
    • A fluorescence-based method for determining the surface coverage and hybridization efficiency of thiolcapped oligonucleotides bound to gold thin films and nanoparticles
    • Demers LM, Mirkin CA, Mucic RC, Reynolds RA, Leitsinger RL, Viswanadham G: A fluorescence-based method for determining the surface coverage and hybridization efficiency of thiolcapped oligonucleotides bound to gold thin films and nanoparticles. Anal Chem 2000, 72:5535-5541.
    • (2000) Anal Chem , vol.72 , pp. 5535-5541
    • Demers, L.M.1    Mirkin, C.A.2    Mucic, R.C.3    Reynolds, R.A.4    Leitsinger, R.L.5    Viswanadham, G.6
  • 21
    • 13644250281 scopus 로고    scopus 로고
    • Examination of cholesterol oxidase immobilization onto magnetic nanoparticles
    • Kouassi KG, Irudayaraj J, McCarthy G: Examination of cholesterol oxidase immobilization onto magnetic nanoparticles. Biomagnetic Res Technol 2005, 3:1.
    • (2005) Biomagnetic Res Technol , vol.3 , pp. 1
    • Kouassi, K.G.1    Irudayaraj, J.2    McCarthy, G.3
  • 22
    • 0034809883 scopus 로고    scopus 로고
    • Gold coated iron (FeΑu) nanoparticles. synthesis, characterization, and magnetic field induced self-assembly
    • Jun L, Zhou W, Kumbhar J, Wiemann J, Fang J, Carpentier EE, O'Connor CJ: Gold coated iron (FeΑu) nanoparticles. synthesis, characterization, and magnetic field induced self-assembly. J Solid State Chem 2001, 159:26-31.
    • (2001) J Solid State Chem , vol.159 , pp. 26-31
    • Jun, L.1    Zhou, W.2    Kumbhar, J.3    Wiemann, J.4    Fang, J.5    Carpentier, E.E.6    O'Connor, C.J.7
  • 24
    • 0034498172 scopus 로고    scopus 로고
    • Mixed silver/gold colloids: A study of their formation, morphology, and surface enhanced raman activity
    • Rivas L, Sanchez-Cortes S, Garcia-Ramos JV, Morrcillo G: Mixed silver/ gold colloids: A study of their formation, morphology, and surface enhanced raman activity. Langmuir 2000, 16:9722-9728.
    • (2000) Langmuir , vol.16 , pp. 9722-9728
    • Rivas, L.1    Sanchez-Cortes, S.2    Garcia-Ramos, J.V.3    Morrcillo, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.