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Chapter title |
In-Solution SH2 Domain Binding Assay Based on Proximity Ligation
|
---|---|
Chapter number | 18 |
Book title |
SH2 Domains
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6762-9_18 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6760-5, 978-1-4939-6762-9
|
Authors |
Kazuya Machida |
Editors |
Kazuya Machida, Bernard A. Liu |
Abstract |
Protein-protein interactions mediated by SH2 domains confer specificity in tyrosine kinase pathways. Traditional assays for assessing interactions between an SH2 domain and its interacting protein such as far-Western and pull-down are inherently low throughput. We developed SH2-PLA, an in-solution SH2 domain binding assay, that takes advantage of the speed and sensitivity of proximity ligation and real-time PCR. SH2-PLA allows for rapid assessment of SH2 domain binding to a target protein using only a few microliters of cell lysate, thereby making it an attractive new tool to study tyrosine kinase signaling. |
Mendeley readers
The data shown below were compiled from readership statistics for 4 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 4 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Professor > Associate Professor | 1 | 25% |
Student > Bachelor | 1 | 25% |
Other | 1 | 25% |
Student > Master | 1 | 25% |
Readers by discipline | Count | As % |
---|---|---|
Immunology and Microbiology | 1 | 25% |
Chemistry | 1 | 25% |
Medicine and Dentistry | 1 | 25% |
Unknown | 1 | 25% |