dc.contributor.advisor | Bowie, Andrew | |
dc.contributor.author | Hurst, Tara | |
dc.date.accessioned | 2019-04-30T09:21:40Z | |
dc.date.available | 2019-04-30T09:21:40Z | |
dc.date.issued | 2008 | |
dc.identifier.citation | Tara Hurst, 'Modulation of TRAF6 function by the vaccinia virus protein A52', [thesis], Trinity College (Dublin, Ireland). School of Biochemistry and Immunology, 2008, pp 309 | |
dc.identifier.other | THESIS 8670 | |
dc.identifier.uri | http://hdl.handle.net/2262/86383 | |
dc.description.abstract | Large DNA viruses, like Vaccinia virus (VACV), encode numerous proteins that are not
essential for viral replication but which modulate the antiviral immune response. A
number of VACV immunomodulatory proteins have been found to target different
components of the innate immune response, including interleukin-1 receptor/ Toll-like
receptor (IL-1R/TLR) signalling pathways. The VACV protein A52 has previously been
shown to interact with two members of the IL-1R/TLR signalling pathways, TRAF6 and
IRAK2. Further, A52 is a potent inhibitor of IL-IR/TLR-induced NF-kB activation, likely
by inhibiting the function of IRAK2. Interestingly, A52 was also found to activate p38
MAP kinase (MARK), enhancing TLR-dependent IL-10 induction. The interaction between
A52 and TRAF6 was found to be crucial for A52-induced MARK activation. | |
dc.format | 1 volume | |
dc.language.iso | en | |
dc.publisher | Trinity College (Dublin, Ireland). School of Biochemistry and Immunology | |
dc.relation.isversionof | http://stella.catalogue.tcd.ie/iii/encore/record/C__Rb13577933 | |
dc.subject | Biochemistry, Ph.D. | |
dc.subject | Ph.D. Trinity College Dublin | |
dc.title | Modulation of TRAF6 function by the vaccinia virus protein A52 | |
dc.type | thesis | |
dc.type.supercollection | thesis_dissertations | |
dc.type.supercollection | refereed_publications | |
dc.type.qualificationlevel | Doctoral | |
dc.type.qualificationname | Doctor of Philosophy (Ph.D.) | |
dc.rights.ecaccessrights | openAccess | |
dc.format.extentpagination | pp 309 | |
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