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Mendeley readers
Chapter title |
Detection of ADP-Ribosylating Bacterial Toxins
|
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Chapter number | 20 |
Book title |
ADP-ribosylation and NAD+ Utilizing Enzymes
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Published in |
Methods in molecular biology, August 2018
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DOI | 10.1007/978-1-4939-8588-3_20 |
Pubmed ID | |
Book ISBNs |
978-1-4939-8587-6, 978-1-4939-8588-3
|
Authors |
Chen Chen, Joseph T. Barbieri, Chen, Chen, Barbieri, Joseph T. |
Abstract |
Many bacterial toxins catalyze the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD) to a host protein. Greater than 35 bacterial ADP-ribosyltransferase toxins (bARTTs) have been identified. ADP-ribosylation of host proteins may be specific or promiscuous. Despite this diversity, bARTTs share a common reaction mechanism, three-dimensional active site structure, and a conserved active site glutamic acid. Here, we describe how to measure the ADP-ribosylation of host proteins as purified proteins or within a cell lysate. |
Mendeley readers
The data shown below were compiled from readership statistics for 7 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 7 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Professor | 2 | 29% |
Student > Master | 2 | 29% |
Student > Ph. D. Student | 1 | 14% |
Unknown | 2 | 29% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 2 | 29% |
Immunology and Microbiology | 2 | 29% |
Agricultural and Biological Sciences | 1 | 14% |
Unknown | 2 | 29% |