The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Understanding enzymatic acceleration at nanoparticle interfaces: Approaches and challenges
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Citations
Cites
Chemistry and Properties of Nanocrystals of Different Shapes
Burda, C., Chen, X., Narayanan, R., & El-Sayed, M. A. (2005) · Chemical Reviews · doi:10.1021/cr030063a · Cited by 7,230
Stochastic Gene Expression in a Single Cell
Elowitz, M. B., Levine, A. J., Siggia, E. D., & Swain, P. S. (2002) · Science · doi:10.1126/science.1070919 · Cited by 5,441
Colloidal nanocrystal synthesis and the organic–inorganic interface
Yin, Y., & Alivisatos, A. P. (2005) · Nature · doi:10.1038/nature04165 · Cited by 3,273
Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality
Sletten, E. M., & Bertozzi, C. R. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200900942 · Cited by 3,165
Multifunctional Magnetic Nanoparticles: Design, Synthesis, and Biomedical Applications
Gao, J., Gu, H., & Xu, B. (2009) · Accounts of Chemical Research · doi:10.1021/ar9000026 · Cited by 1,907
Fluorescence-based glucose sensors
Pickup, J. C., Hussain, F., Evans, N. D., Rolinski, O. J., & Birch, D. J. S. (2005) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2004.10.002 · Cited by 616
Engineered nanoparticles for biomolecular imaging
Mahmoudi, M., Serpooshan, V., & Laurent, S. (2011) · Nanoscale · doi:10.1039/c1nr10326a · Cited by 262
Cited by
Quantum dots: bright and versatile in vitro and in vivo fluorescence imaging biosensors
Wegner, K. D., & Hildebrandt, N. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00532e · Cited by 984
Enzymatic reactions in confined environments
Küchler, A., Yoshimoto, M., Luginbühl, S., Mavelli, F., & Walde, P. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.54 · Cited by 733
Hildebrandt, N., Spillmann, C. M., Algar, W. R., Pons, T., Stewart, M. H., Oh, E., Susumu, K., Díaz, S. A., Delehanty, J. B., & Medintz, I. L. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00030 · Cited by 730
Self-citationIncreasing the activity of immobilized enzymes with nanoparticle conjugation
Ding, S., Cargill, A. A., Medintz, I. L., & Claussen, J. C. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.04.005 · Cited by 293
Self-citationStrategies of enzyme immobilization on nanomatrix supports and their intracellular delivery
Sharifi, M., Karim, A. Y., Mustafa Qadir Nanakali, N., Salihi, A., Aziz, F. M., Hong, J., Khan, R. H., Saboury, A. A., Hasan, A., Abou-Zied, O. K., et al. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1643787 · Cited by 29
Metadata
- Authors
- Johnson, B. J., Russ Algar, W., Malanoski, A. P., Ancona, M. G., & Medintz, I. L.
- Venue
- Nano Today
- Publisher
- Elsevier BV
- Published
- 2014-02
- Volume
- 9
- Issue
- 1
- Pages
- 102-131
- ISSN
- 1748-0132 (ISSN-L)
- OpenAlex
- W2039061776
- Cited by
- 215
- References
- 7
- FWCI
- 9.37
- Type
- journal article
- Language
- en
- Open access
- closed
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- The paper
- Johnson, B. J., Russ Algar, W., Malanoski, A. P., Ancona, M. G., & Medintz, I. L. (2014). Understanding enzymatic acceleration at nanoparticle interfaces: Approaches and challenges. Nano Today. https://doi.org/10.1016/j.nantod.2014.02.005
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.