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Mendeley readers
Chapter title |
Detecting Posttranslational Modifications of Hsp90
|
---|---|
Chapter number | 16 |
Book title |
Chaperones
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7477-1_16 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7476-4, 978-1-4939-7477-1
|
Authors |
Rebecca A. Sager, Mark R. Woodford, Len Neckers, Mehdi Mollapour |
Abstract |
The molecular chaperone Heat Shock Protein 90 (Hsp90) is essential in eukaryotes. Hsp90 chaperones proteins that are important determinants of multistep carcinogenesis. The chaperone function of Hsp90 is linked to its ability to bind and hydrolyze ATP. Co-chaperones as well as posttranslational modifications (phosphorylation, SUMOylation, and ubiquitination) are important for its stability and regulation of the ATPase activity. Both mammalian and yeast cells can be used to express and purify Hsp90 and also detect its posttranslational modifications by immunoblotting. |
Mendeley readers
The data shown below were compiled from readership statistics for 10 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 10 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 5 | 50% |
Student > Bachelor | 2 | 20% |
Unspecified | 1 | 10% |
Student > Master | 1 | 10% |
Unknown | 1 | 10% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 6 | 60% |
Unspecified | 1 | 10% |
Pharmacology, Toxicology and Pharmaceutical Science | 1 | 10% |
Agricultural and Biological Sciences | 1 | 10% |
Unknown | 1 | 10% |