FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W148977602> ?p ?o ?g. }

• W148977602 abstract "Retroviruses have evolved sophisticated mechanisms to ensure timely export of incompletely spliced viral messenger ribonucleic acids (mRNAs) for gene expression and for viral packaging. For example, the Human Immunodeficiency Virus type 1 (HIV-1) encodes the Rev regulatory protein, a sequence-specific RNA-binding protein that is responsible for the cytoplasmic accumulation of intron-containing viral mRNAs. The HIV-1 Rev protein contains an amino terminal (N-terminal) Arginine-Rich Motif (ARM) RNA-binding domain (RBD) and a carboxy terminal (C-terminal) leucine-rich activation domain which functions as a Nuclear Export Signal (NES). The Rev ARM interacts in a sequence-specific manner with a cis -acting viral RNA stem-loop structure, the Rev Responsive Element (RRE), located in all incompletely spliced viral mRNAs. This initial interaction is followed by the recruitment of additional Rev molecules to form a RiboNucleoProtein (RNP) complex involving the RRE and Rev molecules. The cytoplasmic accumulation of the Rev:RRE RNP complex is dependent on the interaction of Rev with key cellular cofactors. Rev activation domain mutants exhibit a trans -dominant negative phenotype, suggesting that this domain of Rev interacts with cellular proteinsrequired for Rev function. Biochemical and genetic studies have identified several cellular proteins that bind to the activation domain of Rev and are therefore candidate cofactors for Rev function. Amongst these is the human Rev Interacting Protein [hRIP, 79], which is also known as the Rev/Rex activation domain-binding protein [Rab, 18]. hRIP was identified in a yeast two-hybrid assay with the HIV-1 Rev and its functionally equivalent Human T-cell Leukemia Virus type-1 (HTLV-1) Rex protein as baits. The interaction between hRIP and HIV-1 Rev is dependent on a functional Rev NES, as predicted for a bona fide Rev cellular cofactor, and the Nucleoporin-like (Nup-like) repeats in the C-terminus of hRIP (18, 79]. Additional genetic studies indicated that the interaction between hRIP and Rev is indirect and is most likely mediated by the cellular export receptor CRM1 (Chromosomal Region Maintenance 1) [1, 153]. A role for hRIP in Rev function or HIV-1 replication has remained elusive. The goal of this dissertation was to determine whether hRIP is required for Rev function and HIV-1 replication. We used two approaches, a dominant-negative mutant and RNA interference (RNAi), to ablate hRIP activity and analyzed Rev function and HIV-1 replication using standard assays. The results of this dissertation demonstrate that hRIP is required for Rev function and HIV-1 replication. We show that Rev function is inhibited upon ablation of hRIP activity by either a trans -dominant negative mutant or RNAL Furthermore, we find that depletion of endogenoushRIP by RNAi results in the loss of viral replication in human cell lines and primary human macrophages. Unexpectedly, in the absence of functional hRIP, RRE-containing viral RNAs accumulate in the…" @default.
• W148977602 created "2016-06-24" @default.
• W148977602 creator A5081542513 @default.
• W148977602 date "2005-01-01" @default.
• W148977602 modified "2023-09-23" @default.
• W148977602 title "The Human Rev Interacting Protein (hRIP) is Required for Rev Function and HIV-1 Replication: a Dissertation" @default.
• W148977602 hasPublicationYear "2005" @default.
• W148977602 type Work @default.
• W148977602 sameAs 148977602 @default.
• W148977602 citedByCount "0" @default.
• W148977602 crossrefType "journal-article" @default.
• W148977602 hasAuthorship W148977602A5081542513 @default.
• W148977602 hasConcept C104317684 @default.
• W148977602 hasConcept C128943096 @default.
• W148977602 hasConcept C41282012 @default.
• W148977602 hasConcept C54355233 @default.
• W148977602 hasConcept C54757728 @default.
• W148977602 hasConcept C67705224 @default.
• W148977602 hasConcept C75934600 @default.
• W148977602 hasConcept C86803240 @default.
• W148977602 hasConcept C94671646 @default.
• W148977602 hasConcept C95444343 @default.
• W148977602 hasConceptScore W148977602C104317684 @default.
• W148977602 hasConceptScore W148977602C128943096 @default.
• W148977602 hasConceptScore W148977602C41282012 @default.
• W148977602 hasConceptScore W148977602C54355233 @default.
• W148977602 hasConceptScore W148977602C54757728 @default.
• W148977602 hasConceptScore W148977602C67705224 @default.
• W148977602 hasConceptScore W148977602C75934600 @default.
• W148977602 hasConceptScore W148977602C86803240 @default.
• W148977602 hasConceptScore W148977602C94671646 @default.
• W148977602 hasConceptScore W148977602C95444343 @default.
• W148977602 hasLocation W1489776021 @default.
• W148977602 hasOpenAccess W148977602 @default.
• W148977602 hasPrimaryLocation W1489776021 @default.
• W148977602 hasRelatedWork W1502927669 @default.
• W148977602 hasRelatedWork W1559998360 @default.
• W148977602 hasRelatedWork W1972015499 @default.
• W148977602 hasRelatedWork W1993057782 @default.
• W148977602 hasRelatedWork W2003092241 @default.
• W148977602 hasRelatedWork W2045186821 @default.
• W148977602 hasRelatedWork W2050072148 @default.
• W148977602 hasRelatedWork W2094236211 @default.
• W148977602 hasRelatedWork W2111268498 @default.
• W148977602 hasRelatedWork W2119408339 @default.
• W148977602 hasRelatedWork W2119451435 @default.
• W148977602 hasRelatedWork W2133430876 @default.
• W148977602 hasRelatedWork W2142154079 @default.
• W148977602 hasRelatedWork W2155739077 @default.
• W148977602 hasRelatedWork W2158826003 @default.
• W148977602 hasRelatedWork W2330729502 @default.
• W148977602 hasRelatedWork W2392281544 @default.
• W148977602 hasRelatedWork W3000191656 @default.
• W148977602 hasRelatedWork W2551428035 @default.
• W148977602 hasRelatedWork W2845555680 @default.
• W148977602 isParatext "false" @default.
• W148977602 isRetracted "false" @default.
• W148977602 magId "148977602" @default.
• W148977602 workType "article" @default.