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Mendeley readers
| Chapter title |
The Structure and Function of the PRMT5:MEP50 Complex
|
|---|---|
| Chapter number | 7 |
| Book title |
Macromolecular Protein Complexes
|
| Published in |
Sub cellular biochemistry, March 2017
|
| DOI | 10.1007/978-3-319-46503-6_7 |
| Pubmed ID | |
| Book ISBNs |
978-3-31-946501-2, 978-3-31-946503-6
|
| Authors |
Stephen Antonysamy |
| Editors |
J. Robin Harris, Jon Marles-Wright |
| Abstract |
Protein arginine methyltransferase 5 (PRMT5) plays multiple roles in cellular processes at different stages of the cell cycle in a tissue specific manner. PRMT5 in complex with MEP50/p44/WDR77 associates with a plethora of partner proteins to symmetrically dimethylate arginine residues on target proteins in both the nucleus and the cytoplasm. Overexpression of PRMT5 has been observed in several cancers, making it an attractive drug target. The structure of the 453 kDa heterooctameric PRMT5:MEP50 complex bound to an S-adenosylmethionine analog and a substrate peptide provides valuable insights into this intriguing target. |
Mendeley readers
The data shown below were compiled from readership statistics for 22 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 22 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 7 | 32% |
| Student > Master | 4 | 18% |
| Student > Doctoral Student | 3 | 14% |
| Researcher | 3 | 14% |
| Other | 1 | 5% |
| Other | 0 | 0% |
| Unknown | 4 | 18% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 10 | 45% |
| Agricultural and Biological Sciences | 2 | 9% |
| Medicine and Dentistry | 2 | 9% |
| Social Sciences | 1 | 5% |
| Chemistry | 1 | 5% |
| Other | 0 | 0% |
| Unknown | 6 | 27% |