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Mendeley readers
Chapter title |
NMR Spectroscopy to Study MAP Kinase Binding to MAP Kinase Phosphatases
|
---|---|
Chapter number | 11 |
Book title |
Protein Tyrosine Phosphatases
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Published in |
Methods in molecular biology, January 2016
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DOI | 10.1007/978-1-4939-3746-2_11 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3744-8, 978-1-4939-3746-2
|
Authors |
Wolfgang Peti, Rebecca Page, Peti, Wolfgang, Page, Rebecca |
Abstract |
NMR spectroscopy and other solution methods are increasingly being used to obtain novel insights into the mechanisms by which MAPK regulatory proteins bind and direct the activity of MAPKs. Here, we describe how interactions between the MAPK p38α and its regulatory proteins are studied using NMR spectroscopy, isothermal titration calorimetry, and small angle X-ray scattering (SAXS). |
Mendeley readers
The data shown below were compiled from readership statistics for 9 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 9 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 2 | 22% |
Researcher | 2 | 22% |
Student > Bachelor | 1 | 11% |
Professor | 1 | 11% |
Unknown | 3 | 33% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 3 | 33% |
Chemistry | 2 | 22% |
Physics and Astronomy | 1 | 11% |
Unknown | 3 | 33% |