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Chapter title |
LOV2-Controlled Photoactivation of Protein Trans -Splicing
|
---|---|
Chapter number | 15 |
Book title |
Split Inteins
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6451-2_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6449-9, 978-1-4939-6451-2
|
Authors |
Anam Qudrat, Abdullah Mosabbir, Kevin Truong, Qudrat, Anam, Mosabbir, Abdullah, Truong, Kevin |
Abstract |
Protein trans-splicing is a posttranslational modification that joins two protein fragments together via a peptide a bond in a process that does not require exogenous cofactors. Towards achieving cellular control, synthetically engineered systems have used a variety of stimuli such as small molecules and light. Recently, split inteins have been engineered to be photoactive by the LOV2 domain (named LOVInC). Herein, we discuss (1) designing of LOV2-activated target proteins (e.g., inteins), (2) selecting feasible splice sites for the extein, and (3) imaging cells that express LOVInC-based target exteins. |
Mendeley readers
The data shown below were compiled from readership statistics for 11 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 11 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 4 | 36% |
Researcher | 1 | 9% |
Lecturer > Senior Lecturer | 1 | 9% |
Student > Master | 1 | 9% |
Unknown | 4 | 36% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 4 | 36% |
Chemistry | 2 | 18% |
Medicine and Dentistry | 1 | 9% |
Unknown | 4 | 36% |