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Cited by 188

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The Incorporation of a Photoisomerizable Amino Acid into Proteins in E. c oli

Bose, Mohua, Groff, Dan, Xie, Jianming, Brustad, Eric, Schultz, Peter G.·2006·Journal of the American Chemical Society

Abstract

An orthogonal aminoacyl tRNA synthetase/tRNA pair has been evolved that allows the incorporation of the photoisomerizable amino acid phenylalanine-4'-azobenzene (AzoPhe) into proteins in E. coli in response to the amber nonsense codon. Further, we show that AzoPhe can be used to photoregulate the binding affinity of catabolite activator protein to its promoter. The ability to selectively incorporate AzoPhe into proteins at defined sites should make it possible to regulate a variety of biological processes with light, including enzyme, receptor, and ion channel activity.

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Metadata

Authors
Bose, M., Groff, D., Xie, J., Brustad, E., & Schultz, P. G.
Venue
Journal of the American Chemical Society
Published
2005-12-17
Volume
128
Issue
2
Pages
388-389
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W2012537676
Cited by
188
References
0
FWCI
3.92
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: The Incorporation of a Photoisomerizable Amino Acid into Proteins in E. c oli. https://app.cochat.ai/papers/10.1021/ja055467u
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Bose, M., Groff, D., Xie, J., Brustad, E., & Schultz, P. G. (2006). The Incorporation of a Photoisomerizable Amino Acid into Proteins in E. c oli. Journal of the American Chemical Society. https://doi.org/10.1021/ja055467u

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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.