The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
A highly photostable and bright green fluorescent protein
Open accessAbstract
The low photostability of fluorescent proteins is a limiting factor in many applications of fluorescence microscopy. Here we present StayGold, a green fluorescent protein (GFP) derived from the jellyfish Cytaeis uchidae. StayGold is over one order of magnitude more photostable than any currently available fluorescent protein and has a cellular brightness similar to mNeonGreen. We used StayGold to image the dynamics of the endoplasmic reticulum (ER) with high spatiotemporal resolution over several minutes using structured illumination microscopy (SIM) and observed substantially less photobleaching than with a GFP variant optimized for stability in the ER. Using StayGold fusions and SIM, we also imaged the dynamics of mitochondrial fusion and fission and mapped the viral spike proteins in fixed cells infected with severe acute respiratory syndrome coronavirus 2. As StayGold is a dimer, we created a tandem dimer version that allowed us to observe the dynamics of microtubules and the excitatory post-synaptic density in neurons. StayGold will substantially reduce the limitations imposed by photobleaching, especially in live cell or volumetric imaging.
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Self-citationVisualizing Spatiotemporal Dynamics of Multicellular Cell-Cycle Progression
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Self-citationFluorescent proteins from nonbioluminescent Anthozoa species
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PDZ domain proteins of synapses
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A bright monomeric green fluorescent protein derived from Branchiostoma lanceolatum
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mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells
Hatano, T., Lim, T. C., Billault-Chaumartin, I., Dhar, A., Gu, Y., Massam-Wu, T., Scott, W., Adishesha, S., Chapa-y-Lazo, B., Springall, L., et al. (2022) · Journal of Cell Science · doi:10.1242/jcs.260288 · Cited by 19
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Ohno, H., Nishimura, T., Kainoh, K., Ohashi, Y., Onodera, N., Kano, M., Sari, L. N., Masuda, M., Tamura, Y., Nishino, T., et al. (2026) · The FEBS Journal · doi:10.1111/febs.70286 · Cited by 2
Barrel Shape and Chromophore Rigidity Predict Fluorescent-Protein Photophysics
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Metadata
- Authors
- Hirano, M., Ando, R., Shimozono, S., Sugiyama, M., Takeda, N., Kurokawa, H., Deguchi, R., Endo, K., Haga, K., Takai-Todaka, R., Inaura, S., Matsumura, Y., Hama, H., Okada, Y., Fujiwara, T., Morimoto, T., Katayama, K., & Miyawaki, A.
- Venue
- Nature Biotechnology
- Published
- 2022-04-25
- Volume
- 40
- Issue
- 7
- Pages
- 1132-1142
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- OpenAlex
- W4224837766
- Cited by
- 293
- References
- 57
- FWCI
- 24.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Hirano, M., Ando, R., Shimozono, S., Sugiyama, M., Takeda, N., Kurokawa, H., Deguchi, R., Endo, K., Haga, K., Takai-Todaka, R., Inaura, S., Matsumura, Y., Hama, H., Okada, Y., Fujiwara, T., Morimoto, T., Katayama, K., & Miyawaki, A. (2022). A highly photostable and bright green fluorescent protein. Nature Biotechnology. https://doi.org/10.1038/s41587-022-01278-2
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