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Mendeley readers
Chapter title |
Affinity purification combined with mass spectrometry to identify herpes simplex virus protein-protein interactions.
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Chapter number | 14 |
Book title |
Herpes Simplex Virus
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Published in |
Methods in molecular biology, March 2014
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DOI | 10.1007/978-1-4939-0428-0_14 |
Pubmed ID | |
Book ISBNs |
978-1-4939-0427-3, 978-1-4939-0428-0
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Authors |
Meckes DG Jr, David G. Meckes, Meckes, David G. |
Abstract |
The identification and characterization of herpes simplex virus protein interaction complexes are fundamental to understanding the molecular mechanisms governing the replication and pathogenesis of the virus. Recent advances in affinity-based methods, mass spectrometry configurations, and bioinformatics tools have greatly increased the quantity and quality of protein-protein interaction datasets. In this chapter, detailed and reliable methods that can easily be implemented are presented for the identification of protein-protein interactions using cryogenic cell lysis, affinity purification, trypsin digestion, and mass spectrometry. |
Mendeley readers
The data shown below were compiled from readership statistics for 8 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 8 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 2 | 25% |
Unspecified | 1 | 13% |
Professor | 1 | 13% |
Student > Doctoral Student | 1 | 13% |
Student > Ph. D. Student | 1 | 13% |
Other | 1 | 13% |
Unknown | 1 | 13% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 3 | 38% |
Unspecified | 1 | 13% |
Agricultural and Biological Sciences | 1 | 13% |
Energy | 1 | 13% |
Unknown | 2 | 25% |