Identification of Phosphorylation Sites at the Carboxy Terminus of the 55-K (496R) Adenovirus Type 5 E1B Protein
| dc.contributor.advisor | Branton, P. E. | |
| dc.contributor.advisor | Graham, F. L. | |
| dc.contributor.author | Halliday, Todd | |
| dc.contributor.department | Biology | en_US |
| dc.date.accessioned | 2018-06-21T15:02:29Z | |
| dc.date.available | 2018-06-21T15:02:29Z | |
| dc.date.issued | 1993-09 | |
| dc.description.abstract | The 55K product of early region 1B (E1B) of human adenoviruses is required for viral replication and participates in cell transformation. Both biochemical and genetic approaches have been used to show that this 496-residue (496R) protein of adenovirus (Ad5) is phosphorylated at both serine and threonine residues at sites near the carboxy terminus within sequences characteristic of a casein kinase II. Mutations which converted serines 490 and 491 to alanine residues decreased virus replication and reduced the efficiency of transformation of primary baby rat kidney cells, suggesting that phosphorylation at these sites is of importance in the regulation of 55K biological activity. | en_US |
| dc.description.degree | Master of Science (MS) | en_US |
| dc.description.degreetype | Thesis | en_US |
| dc.identifier.uri | http://hdl.handle.net/11375/23120 | |
| dc.language.iso | en | en_US |
| dc.subject | phosphorylation | en_US |
| dc.subject | carboxy | en_US |
| dc.subject | terminus | en_US |
| dc.subject | adenovirus | en_US |
| dc.subject | protein | en_US |
| dc.title | Identification of Phosphorylation Sites at the Carboxy Terminus of the 55-K (496R) Adenovirus Type 5 E1B Protein | en_US |
| dc.title.alternative | Phosphorylation of the AD5 E1B 55K Protein | en_US |
| dc.type | Thesis | en_US |