Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process
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The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3GThe tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif proteinRing finger protein ZIN interacts with human immunodeficiency virus type 1 VifThe cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNAHuman APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replicationHIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factorsThe HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradationIdentification of APOBEC3DE as another antiretroviral factor from the human APOBEC familyComprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virionsInhibitors of human immunodeficiency virus type 1 reverse transcriptase target distinct phases of early reverse transcriptionNewly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase HCharacterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase componentsStructural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloBImplication of the lymphocyte-specific nuclear body protein Sp140 in an innate response to human immunodeficiency virus type 1.The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity.Leveraging APOBEC3 proteins to alter the HIV mutation rate and combat AIDS.Vif is largely absent from human immunodeficiency virus type 1 mature virions and associates mainly with viral particles containing unprocessed gag.Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA.Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein. Importance of the C-terminal unstructured tail.Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins.Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function.Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infection.The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrestMechanistic aspects of HIV-1 reverse transcription initiation.HIV-1 RNA dimerization: It takes two to tangoFeatures, processing states, and heterologous protein interactions in the modulation of the retroviral nucleocapsid protein function.On the solution conformation and dynamics of the HIV-1 viral infectivity factorRole of HIV-1 RNA and protein determinants for the selective packaging of spliced and unspliced viral RNA and host U6 and 7SL RNA in virus particlesCoevolutionary analyses require phylogenetically deep alignments and better null models to accurately detect inter-protein contacts within and between species.The Vif accessory protein alters the cell cycle of human immunodeficiency virus type 1 infected cells.Constructing an integrated genetic and epigenetic cellular network for whole cellular mechanism using high-throughput next-generation sequencing data.Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription.Genetic and functional characterization of HIV-1 Vif on APOBEC3G degradation: First report of emergence of B/C recombinants from North India.APOBEC3G impairs the multimerization of the HIV-1 Vif protein in living cells.Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G.Identification of Vimentin as a Potential Therapeutic Target against HIV InfectionAdvances in the structural understanding of Vif proteinsHuman immunodeficiency virus type 1 (HIV-1) induces the cytoplasmic retention of heterogeneous nuclear ribonucleoprotein A1 by disrupting nuclear import: implications for HIV-1 gene expression.Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.
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Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process
description
2000 nî lūn-bûn
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2000年の論文
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2000年論文
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2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
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name
Human immunodeficiency virus t ...... folding and packaging process
@en
Human immunodeficiency virus t ...... folding and packaging process.
@nl
type
label
Human immunodeficiency virus t ...... folding and packaging process
@en
Human immunodeficiency virus t ...... folding and packaging process.
@nl
prefLabel
Human immunodeficiency virus t ...... folding and packaging process
@en
Human immunodeficiency virus t ...... folding and packaging process.
@nl
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P2860
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Human immunodeficiency virus t ...... folding and packaging process
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P2860
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10.1128/JVI.74.18.8252-8261.2000
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2000-09-01T00:00:00Z