title: Functional Analysis of Potential Phosphorylation Sites in the HIV-1 p6 Gag Domain
creator: Morales, Ivonne
subject: ddc-570
subject: 570 Life sciences
description: The human immunodeficiency virus type 1 (HIV-1) interacts with multiple host components and usurps cellular regulatory mechanisms, such as phosphorylation to help direct different events of its replication cycle. Protein phosphorylation is a posttranslational modification widely used by the cell to convey specific messages in response to specific stimuli and allows the coordination of a myriad of cellular processes in a timely and specific manner. The C-terminal p6 domain of the HIV-1 Gag protein, besides carrying the PTAP L-domain required to mediate virus release is subject to phosphorylation. Although p6 has been identified to exist as the major phosphoprotein in HIV-1 particles, an in-depth study of the functional role of p6 phosphorylation has not been conducted to date. Thus, these observations prompted us to perform a comprehensive analysis of the consequences of potential p6 phosphorylation in the HIV-1 replication cycle. 
date: 2011
type: Dissertation
type: info:eu-repo/semantics/doctoralThesis
type: NonPeerReviewed
format: application/pdf
identifier: https://archiv.ub.uni-heidelberg.de/volltextserverhttps://archiv.ub.uni-heidelberg.de/volltextserver/12052/1/PhD_thesis_IM_r.pdf
identifier: DOI:10.11588/heidok.00012052
identifier: urn:nbn:de:bsz:16-opus-120525
identifier:   Morales, Ivonne  (2011) Functional Analysis of Potential Phosphorylation Sites in the HIV-1 p6 Gag Domain.  [Dissertation]     
relation: https://archiv.ub.uni-heidelberg.de/volltextserver/12052/
rights: info:eu-repo/semantics/openAccess
rights: http://archiv.ub.uni-heidelberg.de/volltextserver/help/license_urhg.html
language: eng