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Chapter title |
Approaches to Determine Protein Ubiquitination Residue Types
|
---|---|
Chapter number | 1 |
Book title |
Plant Proteostasis
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3759-2_1 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3757-8, 978-1-4939-3759-2
|
Authors |
Qian Chen, Xiaoyuan Yang, Qi Xie |
Editors |
L. Maria Lois, Rune Matthiesen |
Abstract |
Ubiquitination is an important posttranslational modification in eukaryotic organisms and plays a central role in many signaling pathways in plants. Most ubiquitination typically occurs on substrate lysine residues, forming a covalent isopeptide bond. Some recent reports suggested ubiquitin can be attached to non-lysine sites such as serine/threonine, cysteine or the N-terminal methionine, via oxyester or thioester linkages, respectively. In the present protocol, we developed a convenient in vitro assay for investigating ubiquitination on Ser/Thr and Cys residues. |
Mendeley readers
The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 3 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Bachelor | 1 | 33% |
Other | 1 | 33% |
Unknown | 1 | 33% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 1 | 33% |
Agricultural and Biological Sciences | 1 | 33% |
Unknown | 1 | 33% |