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Cited by 577

The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.

Cell Surface Labeling of Escherichia coli via Copper(I)-Catalyzed [3+2] Cycloaddition

Link, A. James, Tirrell, David A.·2003·Journal of the American Chemical Society

Abstract

Labeling of the cell surface of Escherichia coli was accomplished by expression of a recombinant outer membrane protein, OmpC, in the presence of the unnatural amino acid azidohomoalanine, which acts as a methionine surrogate. The surface-exposed azide moieties of whole cells were biotinylated via Cu(1)-catalyzed [3+2] azide-alkyne cycloaddition. The specificity of labeling of both wild-type OmpC and a mutant containing additional methionine sites for azidohomoalanine incorporation was confirmed by Western blotting. Flow cytometry was performed to examine the specificity of the labeling. Cells that express the mutant form of OmpC in the presence of azidohomoalanine, which were biotinylated and stained with fluorescent avidin, exhibit a mean fluorescence 10-fold higher than the background. Incorporation of an unnatural amino acid can thus be determined on a single-cell basis.

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Crossref · 10.1021/ja036765z

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Metadata

Authors
Link, A. J., & Tirrell, D. A.
Venue
Journal of the American Chemical Society
Published
2003-08-23
Volume
125
Issue
37
Pages
11164-11165
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W1993016234
Cited by
577
References
14
FWCI
15.73
Type
journal article
Language
en
Open access
closed

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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).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.