메뉴 건너뛰기




Volumn 10, Issue 8, 2010, Pages 3101-3105

Protein-nanoparticle interaction: Identification of the ubiquitin-gold nanoparticle interaction site

Author keywords

chemical shift mapping; Gold nanoparticles; NMR; protein nanoparticle interactions

Indexed keywords

CHEMICAL SHIFT MAPPING; CHEMICAL SHIFT PERTURBATIONS; EXPERIMENTAL DATA; GOLD NANOPARTICLES; NANOPARTICLE INTERACTION; PHYSIOLOGICAL CONDITION; UBIQUITIN;

EID: 77955562565     PISSN: 15306984     EISSN: 15306992     Source Type: Journal    
DOI: 10.1021/nl101746v     Document Type: Article
Times cited : (231)

References (23)
  • 1
    • 0037462997 scopus 로고    scopus 로고
    • Biodegradable nanoparticles for drug and gene delivery to cells and tissue
    • Panyam, J.; Labhasetwar, V. Biodegradable nanoparticles for drug and gene delivery to cells and tissue Adv. Drug Delivery Rev. 2003, 55, 329-347
    • (2003) Adv. Drug Delivery Rev. , vol.55 , pp. 329-347
    • Panyam, J.1    Labhasetwar, V.2
  • 2
    • 19944433260 scopus 로고    scopus 로고
    • Quantum dots for live cells, in vivo imaging, and diagnostics
    • Michalet, X. Quantum dots for live cells, in vivo imaging, and diagnostics Science 2005, 307, 538-544
    • (2005) Science , vol.307 , pp. 538-544
    • Michalet, X.1
  • 3
    • 55749091647 scopus 로고    scopus 로고
    • Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts
    • Lundqvist, M. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 14265-14270
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14265-14270
    • Lundqvist, M.1
  • 4
    • 33646183969 scopus 로고    scopus 로고
    • Detecting cryptic epitopes created by nanoparticles
    • Lynch, I.; Dawson, K. A.; Linse, S. Detecting cryptic epitopes created by nanoparticles Sci. STKE 2006, pe14
    • (2006) Sci. STKE , pp. 14
    • Lynch, I.1    Dawson, K.A.2    Linse, S.3
  • 5
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • Gray, J. J. The interaction of proteins 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
  • 6
    • 29544446689 scopus 로고    scopus 로고
    • Weak protein-protein interactions as probed by NMR spectroscopy
    • Vaynberg, J.; Qin, J. Weak protein-protein interactions as probed by NMR spectroscopy Trends Biotechnol. 2006, 24, 22-27
    • (2006) Trends Biotechnol. , vol.24 , pp. 22-27
    • Vaynberg, J.1    Qin, J.2
  • 7
    • 3843093727 scopus 로고    scopus 로고
    • Conformation and orientation of a protein folding intermediate trapped by adsorption
    • Engel, M. F.; Visser, A. J.; van Mierlo, C. P. Conformation and orientation of a protein folding intermediate trapped by adsorption Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 11316-11321
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11316-11321
    • Engel, M.F.1    Visser, A.J.2    Van Mierlo, C.P.3
  • 9
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. Mapping protein-protein interactions in solution by NMR spectroscopy Biochemistry 2002, 41, 1-7
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 10
    • 77649272620 scopus 로고    scopus 로고
    • Rapid structural characterization of human antibody-antigen complexes through experimentally validated computational docking
    • Simonelli, L. Rapid structural characterization of human antibody-antigen complexes through experimentally validated computational docking J. Mol. Biol. 2010, 396, 1491-1507
    • (2010) J. Mol. Biol. , vol.396 , pp. 1491-1507
    • Simonelli, L.1
  • 11
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • Vijay-Kumar, S.; Bugg, C. E.; Cook, W. J. Structure of ubiquitin refined at 1.8 A resolution J. Mol. Biol. 1987, 194, 531-544
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 12
    • 0742321804 scopus 로고    scopus 로고
    • Gold nanoparticles: Assembly, supramolecular chemistry, quantum-size-related properties, and applications toward biology, catalysis, and nanotechnology
    • Daniel, M. C.; Astruc, D. Gold nanoparticles: assembly, supramolecular chemistry, quantum-size-related properties, and applications toward biology, catalysis, and nanotechnology Chem. Rev. 2004, 104, 293-346
    • (2004) Chem. Rev. , vol.104 , pp. 293-346
    • Daniel, M.C.1    Astruc, D.2
  • 13
    • 56449085388 scopus 로고    scopus 로고
    • Optical investigation of the electron transfer protein azurin-gold nanoparticle system
    • Delfino, I.; Cannistraro, S. Optical investigation of the electron transfer protein azurin-gold nanoparticle system Biophys. Chem. 2009, 139, 1-7
    • (2009) Biophys. Chem. , vol.139 , pp. 1-7
    • Delfino, I.1    Cannistraro, S.2
  • 14
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky, V. N. Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule Biochemistry 1993, 32, 13288-13298
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 15
    • 70249141572 scopus 로고    scopus 로고
    • A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles
    • Rocker, C.; Potzl, M.; Zhang, F.; Parak, W. J.; Nienhaus, G. U. A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles Nat. Nanotechnol. 2009, 4, 577-580
    • (2009) Nat. Nanotechnol. , vol.4 , pp. 577-580
    • Rocker, C.1    Potzl, M.2    Zhang, F.3    Parak, W.J.4    Nienhaus, G.U.5
  • 16
    • 0034645622 scopus 로고    scopus 로고
    • Self-Assembly of CdSe; ZnS Quantum Dot Bioconjugates Using an Engineered Recombinant Protein
    • Mattoussi, H. Self-Assembly of CdSe; ZnS Quantum Dot Bioconjugates Using an Engineered Recombinant Protein J. Am. Chem. Soc. 2000, 122, 12142-12150
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12142-12150
    • Mattoussi, H.1
  • 19
    • 35948969909 scopus 로고    scopus 로고
    • Structure prediction of protein-solid surface interactions reveals a molecular recognition motif of statherin for hydroxyapatite
    • Makrodimitris, K.; Masica, D. L.; Kim, E. T.; Gray, J. J. Structure prediction of protein-solid surface interactions reveals a molecular recognition motif of statherin for hydroxyapatite J. Am. Chem. Soc. 2007, 129, 13713-13722
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 13713-13722
    • Makrodimitris, K.1    Masica, D.L.2    Kim, E.T.3    Gray, J.J.4
  • 20
    • 77950830266 scopus 로고    scopus 로고
    • Hydroxyl-rich beta-sheet adhesion to the gold surface in water by first-principle simulations
    • Calzolari, A. Hydroxyl-rich beta-sheet adhesion to the gold surface in water by first-principle simulations J. Am. Chem. Soc. 2010, 132, 4790-4795
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4790-4795
    • Calzolari, A.1
  • 21
    • 36749006579 scopus 로고    scopus 로고
    • Docking and scoring protein complexes: CAPRI 3rd Edition
    • Lensink, M. F.; Mendez, R.; Wodak, S. J. Docking and scoring protein complexes: CAPRI 3rd Edition Proteins 2007, 69, 704-718
    • (2007) Proteins , vol.69 , pp. 704-718
    • Lensink, M.F.1    Mendez, R.2    Wodak, S.J.3
  • 22
    • 24644501099 scopus 로고    scopus 로고
    • Direct NMR observation of a substrate protein bound to the chaperonin GroEL
    • Horst, R. Direct NMR observation of a substrate protein bound to the chaperonin GroEL Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 12748-12753
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12748-12753
    • Horst, R.1
  • 23
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin, K.; Riek, R.; Wider, G.; Wuthrich, K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 12366-12371
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.