Title |
Quantitative affinity purification mass spectrometry: a versatile technology to study protein–protein interactions
|
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Published in |
Frontiers in Genetics, July 2015
|
DOI | 10.3389/fgene.2015.00237 |
Pubmed ID | |
Authors |
Katrina Meyer, Matthias Selbach |
Abstract |
While the genomic revolution has dramatically accelerated the discovery of disease-associated genes, the functional characterization of the corresponding proteins lags behind. Most proteins fulfill their tasks in complexes with other proteins, and analysis of protein-protein interactions (PPIs) can therefore provide insights into protein function. Several methods can be used to generate large-scale protein interaction networks. However, most of these approaches are not quantitative and therefore cannot reveal how perturbations affect the network. Here, we illustrate how a clever combination of quantitative mass spectrometry with different biochemical methods provides a rich toolkit to study different aspects of PPIs including topology, subunit stoichiometry, and dynamic behavior. |
X Demographics
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Country | Count | As % |
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Germany | 1 | 33% |
Switzerland | 1 | 33% |
Unknown | 1 | 33% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 3 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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United Kingdom | 1 | <1% |
Turkey | 1 | <1% |
United States | 1 | <1% |
Austria | 1 | <1% |
Unknown | 184 | 98% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 48 | 26% |
Researcher | 34 | 18% |
Student > Master | 34 | 18% |
Student > Bachelor | 16 | 9% |
Student > Doctoral Student | 12 | 6% |
Other | 14 | 7% |
Unknown | 30 | 16% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 67 | 36% |
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Chemistry | 13 | 7% |
Medicine and Dentistry | 8 | 4% |
Engineering | 5 | 3% |
Other | 15 | 8% |
Unknown | 34 | 18% |