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Cited by 489

The DOI matches its Crossref record; 134 of the 134 references it cites were found in a registry or an index.

Selective Covalent Protein Immobilization: Strategies and Applications

Wong, Lu Shin, Khan, Farid, Micklefield, Jason·2009·Chemical Reviews

Abstract

A wide range of biologically mediated methods and important applications of site-specific protein immobilization are discussed, through the culmination of a major multidisciplinary research effort spanning molecular biology. The study focused the attention on oriented protein immobilization methodology that allow defined attachment of proteins with uniform orientation at the bioactive site. The study include enzyme-mediated attachment to a small-molecule immobilizing ligand and the development of genetically encoded protein tags for immobilization. The advent of high-density array printing technology and improved methods for high-throughput production and purification of large number of proteins that allowed the preparation of protein microarrays. The development of proteome chip technology is used to probe an entire collection of proteins for specific function of biochemistry.

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Crossref · 10.1021/cr8004668

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Metadata

Authors
Wong, L. S., Khan, F., & Micklefield, J.
Venue
Chemical Reviews
Published
2009-07-02
Volume
109
Issue
9
Pages
4025-4053
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W2125309913
Cited by
489
References
134
FWCI
2.16
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Selective Covalent Protein Immobilization: Strategies and Applications. https://app.cochat.ai/papers/10.1021/cr8004668
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Wong, L. S., Khan, F., & Micklefield, J. (2009). Selective Covalent Protein Immobilization: Strategies and Applications. Chemical Reviews. https://doi.org/10.1021/cr8004668

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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.