JOURNAL ARTICLE

Visualizing Tyrosine Kinase Activity with Bipartite Tetracysteine Display

Sarmistha Ray‐SahaAlanna Schepartz

Year: 2010 Journal:   ChemBioChem Vol: 11 (15)Pages: 2089-2091   Publisher: Wiley

Abstract

BiAs binding: Recently we reported that the linear tetracysteine sequence preferred by FlAsH and ReAsH could be split between two members of a protein partnership or regions of a folded protein, while maintaining high affinity and brightness. Here we show that this tool—bipartite tetracysteine display—facilitates the design of E2, an encodable, site-selective, Src-family kinase sensor. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.

Keywords:
Bipartite graph Computational biology Tyrosine kinase Computer science Information retrieval Chemistry Biology Biochemistry Theoretical computer science Signal transduction

Metrics

19
Cited By
1.98
FWCI (Field Weighted Citation Impact)
29
Refs
0.84
Citation Normalized Percentile
Is in top 1%
Is in top 10%

Citation History

Topics

Click Chemistry and Applications
Physical Sciences →  Chemistry →  Organic Chemistry
Advanced Biosensing Techniques and Applications
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology
Protein Degradation and Inhibitors
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology
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