The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Optimized Codon Usage and Chromophore Mutations Provide Enhanced Sensitivity with the Green Fluorescent Protein
Open accessAbstract
The green fluorescent protein (GFP) from Aequorea victoria is a versatile reporter protein for monitoring gene expression and protein localization in a variety of cells and organisms. Despite many early successes using this reporter, wild type GFP is suboptimal for most applications due to low fluorescence intensity when excited by blue light (488 nm), a significant lag in the development of fluorescence after protein synthesis, complex photoisomerization of the GFP chromophore and poor expression in many higher eukaryotes. To improve upon these qualities, we have combined a mutant of GFP with a significantly larger extinction coefficient for excitation at 488 nm with a re-engineered GFP gene sequence containing codons preferentially found in highly expressed human proteins. The combination of improved fluorescence intensity and higher expression levels yield an enhanced GFP which provides greater sensitivity in most systems.
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Cites
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Cited by
Fluorescent Proteins and Their Applications in Imaging Living Cells and Tissues
Chudakov, D. M., Matz, M. V., Lukyanov, S., & Lukyanov, K. A. (2010) · Physiological Reviews · doi:10.1152/physrev.00038.2009 · Cited by 1,375
Rab7: A Key to Lysosome Biogenesis
Bucci, C., Thomsen, P., Nicoziani, P., McCarthy, J., & van Deurs, B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.2.467 · Cited by 1,085
Generation of Destabilized Green Fluorescent Protein as a Transcription Reporter
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Self-citationTachibana, M., Sugimoto, K., Fukushima, T., & Shinkai, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101914200 · Cited by 784
CpG islands influence chromatin structure via the CpG-binding protein Cfp1
Thomson, J. P., Skene, P. J., Selfridge, J., Clouaire, T., Guy, J., Webb, S., Kerr, A. R. W., Deaton, A., Andrews, R., James, K. D., et al. (2010) · Nature · doi:10.1038/nature08924 · Cited by 625
Metadata
- Authors
- Yang, T.-T., Cheng, L., & Kain, S. R.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 1996-11-01
- Volume
- 24
- Issue
- 22
- Pages
- 4592-4593
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2163191416
- Cited by
- 441
- References
- 16
- FWCI
- 15.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Yang, T.-T., Cheng, L., & Kain, S. R. (1996). Optimized Codon Usage and Chromophore Mutations Provide Enhanced Sensitivity with the Green Fluorescent Protein. Nucleic Acids Research. https://doi.org/10.1093/nar/24.22.4592
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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).
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