The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Quantitative assessment of fluorescent proteins
Open accessAbstract
The advent of fluorescent proteins (FPs) for genetic labeling of molecules and cells has revolutionized fluorescence microscopy. Genetic manipulations have created a vast array of bright and stable FPs spanning blue to red spectral regions. Common to autofluorescent FPs is their tight β-barrel structure, which provides the rigidity and chemical environment needed for effectual fluorescence. Despite the common structure, each FP has unique properties. Thus, there is no single 'best' FP for every circumstance, and each FP has advantages and disadvantages. To guide decisions about which FP is right for a given application, we have quantitatively characterized the brightness, photostability, pH stability and monomeric properties of more than 40 FPs to enable straightforward and direct comparison between them. We focus on popular and/or top-performing FPs in each spectral region.
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Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N. G., Palmer, A. E., & Tsien, R. Y. (2004) · Nature Biotechnology · doi:10.1038/nbt1037 · Cited by 4,619
Improving FRET dynamic range with bright green and red fluorescent proteins
Lam, A. J., St-Pierre, F., Gong, Y., Marshall, J. D., Cranfill, P. J., Baird, M. A., McKeown, M. R., Wiedenmann, J., Davidson, M. W., Schnitzer, M. J., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2171 · Cited by 732
Self-citation
Cited by
mScarlet: a bright monomeric red fluorescent protein for cellular imaging
Bindels, D. S., Haarbosch, L., van Weeren, L., Postma, M., Wiese, K. E., Mastop, M., Aumonier, S., Gotthard, G., Royant, A., Hink, M. A., et al. (2017) · Nature Methods · doi:10.1038/nmeth.4074 · Cited by 1,156
Phototoxicity in live fluorescence microscopy, and how to avoid it
Icha, J., Weber, M., Waters, J. C., & Norden, C. (2017) · BioEssays · doi:10.1002/bies.201700003 · Cited by 622
Tutorial: guidance for quantitative confocal microscopy
Jonkman, J., Brown, C. M., Wright, G. D., Anderson, K. I., & North, A. J. (2020) · Nature Protocols · doi:10.1038/s41596-020-0313-9 · Cited by 401
Switchable Fluorophores for Single-Molecule Localization Microscopy
Li, H., & Vaughan, J. C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00767 · Cited by 319
Kinase-mediated RAS signaling via membraneless cytoplasmic protein granules
Tulpule, A., Guan, J., Neel, D. S., Allegakoen, H. R., Lin, Y. P., Brown, D., Chou, Y.-T., Heslin, A., Chatterjee, N., Perati, S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.031 · Cited by 189
Metadata
- Authors
- Cranfill, P. J., Sell, B. R., Baird, M. A., Allen, J. R., Lavagnino, Z., de Gruiter, H. M., Kremers, G.-J., Davidson, M. W., Ustione, A., & Piston, D. W.
- Venue
- Nature Methods
- Published
- 2016-05-30
- Volume
- 13
- Issue
- 7
- Pages
- 557-562
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2416471421
- Cited by
- 497
- References
- 2
- FWCI
- 31.20
- Type
- journal article
- Language
- en
- Open access
- green
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- Cranfill, P. J., Sell, B. R., Baird, M. A., Allen, J. R., Lavagnino, Z., de Gruiter, H. M., Kremers, G.-J., Davidson, M. W., Ustione, A., & Piston, D. W. (2016). Quantitative assessment of fluorescent proteins. Nature Methods. https://doi.org/10.1038/nmeth.3891
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