The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The Small Heat Shock Protein Cage from Methanococcus jannaschii Is a Versatile Nanoscale Platform for Genetic and Chemical Modification
Abstract
Nature has provided us with a range of reactive nanoscale platforms, in the form of protein cage architectures such as viral capsids and the cages of ferritin-like proteins. Protein cage architectures have clearly demarcated exterior, interior, and interface surfaces consisting of precisely located chemical functionalities. In the present work, we demonstrate that the small heat shock protein (MjHsp) cage from Methanococcus jannaschii is a new and versatile nanoscale platform whose exterior and interior surfaces are amenable to both genetic and chemical modification . Wild type and genetic mutants of the Hsp cage are shown to react with activated fluorescein molecules in a site specific manner. In addition, the 12 nm Hsp cage serves as a size constrained reaction vessel for the oxidative mineralization of iron, resulting in the formation of monodispersed 9 nm iron oxide nanoparticles. These results demonstrate the utility of the Hsp cage to serve as a nanoscale platform for the synthesis of both soft (organic) and hard (inorganic) materials.
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Cites
Mineralization in ferritin: an efficient means of iron storage
Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815
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Jeevanandam, J., Barhoum, A., Chan, Y. S., Dufresne, A., & Danquah, M. K. (2018) · Beilstein Journal of Nanotechnology · doi:10.3762/bjnano.9.98 · Cited by 3,297
Dual-Surface Modification of the Tobacco Mosaic Virus
Schlick, T. L., Ding, Z., Kovacs, E. W., & Francis, M. B. (2005) · Journal of the American Chemical Society · doi:10.1021/ja046239n · Cited by 516
Biomimetic and Bioinspired Synthesis of Nanomaterials/Nanostructures
Zan, G., & Wu, Q. (2016) · Advanced Materials · doi:10.1002/adma.201503215 · Cited by 434
Ferritin: A Versatile Building Block for Bionanotechnology
Jutz, G., van Rijn, P., Santos Miranda, B., & Böker, A. (2015) · Chemical Reviews · doi:10.1021/cr400011b · Cited by 408
Targeting of Cancer Cells with Ferrimagnetic Ferritin Cage Nanoparticles
Uchida, M., Flenniken, M. L., Allen, M., Willits, D. A., Crowley, B. E., Brumfield, S., Willis, A. F., Jackiw, L., Jutila, M., Young, M. J., et al. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0655690 · Cited by 395
Self-citationMass-Selective Soft-Landing of Protein Assemblies with Controlled Landing Energies
Mikhailov, V. A., Mize, T. H., Benesch, J. L. P., & Robinson, C. V. (2014) · Analytical Chemistry · doi:10.1021/ac5018327 · Cited by 71
Metadata
- Authors
- Flenniken, M. L., Willits, D. A., Brumfield, S., Young, M. J., & Douglas, T.
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-10-11
- Volume
- 3
- Issue
- 11
- Pages
- 1573-1576
- ISSN
- 1530-6984 (ISSN-L)
- 1530-6992
- OpenAlex
- W1969501683
- Cited by
- 170
- References
- 1
- FWCI
- 3.54
- Type
- journal article
- Language
- en
- Open access
- closed
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