The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Protein−Nanoparticle Interaction: Identification of the Ubiquitin−Gold Nanoparticle Interaction Site
Abstract
We demonstrate that it is possible to identify the protein--nanoparticle interaction site at amino acid scale in solution. Using NMR, chemical shift perturbation analysis, and dynamic light scattering we have identified a specific domain of human ubiquitin that interacts with gold nanoparticles. This method allows a detailed structural analysis of proteins absorbed onto surfaces of nanoparticles in physiological conditions and it will provide much needed experimental data for better modeling and prediction of protein--nanoparticle interactions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Daniel, M.-C., & Astruc, D. (2004) · Chemical Reviews · doi:10.1021/cr030698+ · Cited by 12,446
NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics News · doi:10.1051/epn/19861701011 · Cited by 7,989
Quantum Dots for Live Cells, in Vivo Imaging, and Diagnostics
Michalet, X., Pinaud, F. F., Bentolila, L. A., Tsay, J. M., Doose, S., Li, J. J., Sundaresan, G., Wu, A. M., Gambhir, S. S., & Weiss, S. (2005) · Science · doi:10.1126/science.1104274 · Cited by 7,790
NMR of Proteins and Nucleic Acids
(2006) · Nuclear Magnetic Resonance · doi:10.1039/9781847555236-00336 · Cited by 5,863
Principles of Nuclear Magnetic Resonance in One and Two Dimensions
Ernst, R. R., Bodenhausen, G., Wokaun, A., & Redfield, A. G. (1989) · Physics Today · doi:10.1063/1.2811094 · Cited by 4,201
Biodegradable nanoparticles for drug and gene delivery to cells and tissue
Panyam, J., & Labhasetwar, V. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00228-4 · Cited by 3,361
Lundqvist, M., Stigler, J., Elia, G., Lynch, I., Cedervall, T., & Dawson, K. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805135105 · Cited by 2,823
Pervushin, K., Riek, R., Wider, G., & Wüthrich, K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12366 · Cited by 2,445
Structure of ubiquitin refined at 1.8 Å resolution
Vijay-kumar, S., Bugg, C. E., & Cook, W. J. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,742
Self-Assembly of CdSe−ZnS Quantum Dot Bioconjugates Using an Engineered Recombinant Protein
Mattoussi, H., Mauro, J. M., Goldman, E. R., Anderson, G. P., Sundar, V. C., Mikulec, F. V., & Bawendi, M. G. (2000) · Journal of the American Chemical Society · doi:10.1021/ja002535y · Cited by 1,681
Principles of nuclear magnetic resonance in one and two dimensions
Redpath, T. W. (1988) · Magnetic Resonance Imaging · doi:10.1016/0730-725x(88)90413-4 · Cited by 1,207
The interaction of proteins with solid surfaces
Gray, J. J. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.12.001 · Cited by 797
A quantitative fluorescence study of protein monolayer formation on colloidal nanoparticles
Röcker, C., Pötzl, M., Zhang, F., Parak, W. J., & Nienhaus, G. U. (2009) · Nature Nanotechnology · doi:10.1038/nnano.2009.195 · Cited by 730
Mapping Protein−Protein Interactions in Solution by NMR Spectroscopy
Zuiderweg, E. R. P. (2002) · Biochemistry · doi:10.1021/bi011870b · Cited by 534
Uversky, V. N. (1993) · Biochemistry · doi:10.1021/bi00211a042 · Cited by 437
Pellecchia, M., Sem, D. S., & Wüthrich, K. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd748 · Cited by 420
Docking and scoring protein complexes: CAPRI 3rd Edition
Lensink, M. F., Méndez, R., & Wodak, S. J. (2007) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21804 · Cited by 340
Detecting Cryptic Epitopes Created by Nanoparticles
Lynch, I., Dawson, K. A., & Linse, S. (2006) · Science's STKE · doi:10.1126/stke.3272006pe14 · Cited by 268
Weak protein–protein interactions as probed by NMR spectroscopy
Vaynberg, J., & Qin, J. (2006) · Trends in Biotechnology · doi:10.1016/j.tibtech.2005.09.006 · Cited by 161
Makrodimitris, K., Masica, D. L., Kim, E. T., & Gray, J. J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja074602v · Cited by 130
Direct NMR observation of a substrate protein bound to the chaperonin GroEL
Horst, R., Bertelsen, E. B., Fiaux, J., Wider, G., Horwich, A. L., & Wüthrich, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505642102 · Cited by 113
Conformation and orientation of a protein folding intermediate trapped by adsorption
Engel, M. F. M., Visser, A. J. W. G., & van Mierlo, C. P. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401603101 · Cited by 95
Simonelli, L., Beltramello, M., Yudina, Z., Macagno, A., Calzolai, L., & Varani, L. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.12.053 · Cited by 36
Self-citation
Cited by
Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology
Tenzer, S., Docter, D., Kuharev, J., Musyanovych, A., Fetz, V., Hecht, R., Schlenk, F., Fischer, D., Kiouptsi, K., Reinhardt, C., et al. (2013) · Nature Nanotechnology · doi:10.1038/nnano.2013.181 · Cited by 2,283
Interaction of nanoparticles with proteins: relation to bio-reactivity of the nanoparticle
Saptarshi, S. R., Duschl, A., & Lopata, A. L. (2013) · Journal of Nanobiotechnology · doi:10.1186/1477-3155-11-26 · Cited by 1,079
Autophagy and lysosomal dysfunction as emerging mechanisms of nanomaterial toxicity
Stern, S. T., Adiseshaiah, P. P., & Crist, R. M. (2012) · Particle and Fibre Toxicology · doi:10.1186/1743-8977-9-20 · Cited by 836
Mechanisms of genotoxicity. A review of in vitro and in vivo studies with engineered nanoparticles
Magdolenova, Z., Collins, A., Kumar, A., Dhawan, A., Stone, V., & Dusinska, M. (2014) · Nanotoxicology · doi:10.3109/17435390.2013.773464 · Cited by 616
Multiple aspects of the interaction of biomacromolecules with inorganic surfaces
Fenoglio, I., Fubini, B., Ghibaudi, E. M., & Turci, F. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.08.001 · Cited by 176
Metadata
- Authors
- Calzolai, L., Franchini, F., Gilliland, D., & Rossi, F.
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-07-19
- Volume
- 10
- Issue
- 8
- Pages
- 3101-3105
- ISSN
- 1530-6984 (ISSN-L)
- 1530-6992
- OpenAlex
- W2075409966
- Cited by
- 254
- References
- 23
- FWCI
- 8.38
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.