about
Virological and cellular roles of the transcriptional coactivator LEDGF/p75Therapeutic protein transduction of mammalian cells and mice by nucleic acid-free lentiviral nanoparticles.Structural basis for functional tetramerization of lentiviral integraseA symmetric region of the HIV-1 integrase dimerization interface is essential for viral replicationDriving DNA transposition by lentiviral protein transductionUnselected mutations in the human immunodeficiency virus type 1 genome are mostly nonsynonymous and often deleteriousInhibition of HIV-1 integrase by modified oligonucleotides derived from U5' LTR.The lentiviral integrase binding protein LEDGF/p75 and HIV-1 replication.Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.Pathogenesis of HIV-1 infection within bone marrow cells.Human immunodeficiency virus type 1 integrase protein promotes reverse transcription through specific interactions with the nucleoprotein reverse transcription complex.Genetic analyses of DNA-binding mutants in the catalytic core domain of human immunodeficiency virus type 1 integrase.Production of uninfectious human immunodeficiency virus type 1 containing viral protein R fused to a single-chain antibody against viral integrase.Virion-targeted viral inactivation of human immunodeficiency virus type 1 by using Vpr fusion proteins.Retroviral DNA integration.Integrase-lexA fusion proteins incorporated into human immunodeficiency virus type 1 that contains a catalytically inactive integrase gene are functional to mediate integrationTargeting human immunodeficiency virus (HIV) type 2 integrase protein into HIV type 1.Structure-based HIV-1 integrase inhibitor design: a future perspective.Division of labor within human immunodeficiency virus integrase complexes: determinants of catalysis and target DNA captureTy3 integrase is required for initiation of reverse transcriptionCoding sequences upstream of the human immunodeficiency virus type 1 reverse transcriptase domain in Gag-Pol are not essential for incorporation of the Pr160(gag-pol) into virus particles.Subcellular localization and integration activities of rous sarcoma virus reverse transcriptase.Human immunodeficiency virus type 1 incorporated with fusion proteins consisting of integrase and the designed polydactyl zinc finger protein E2C can bias integration of viral DNA into a predetermined chromosomal region in human cellsDisulfide-linked integrase oligomers involving C280 residues are formed in vitro and in vivo but are not essential for human immunodeficiency virus replication.Retroviral DNA Transposition: Themes and VariationsInhibition of HIV-1 Viral Infection by an Engineered CRISPR Csy4 RNA EndoribonucleaseThe Continuing Evolution of HIV-1 Therapy: Identification and Development of Novel Antiretroviral Agents Targeting Viral and Cellular Targets.Characterization of HIV-1 integrase N-terminal mutant viruses.The role of lysine 186 in HIV-1 integrase multimerizationIntegrase, LEDGF/p75 and HIV replication.Site-specific integration of retroviral DNA in human cells using fusion proteins consisting of human immunodeficiency virus type 1 integrase and the designed polydactyl zinc-finger protein E2C.Integrase and integration: biochemical activities of HIV-1 integrase.Targeted genome editing by lentiviral protein transduction of zinc-finger and TAL-effector nucleasesHIV-1 integrase multimerization as a therapeutic target.Sequential deletion of the integrase (Gag-Pol) carboxyl terminus reveals distinct phenotypic classes of defective HIV-1.The karyophilic properties of human immunodeficiency virus type 1 integrase are not required for nuclear import of proviral DNA.Oligomerization within virions and subcellular localization of human immunodeficiency virus type 1 integrase.Association of murine leukemia virus pol with virions, independent of Gag-Pol expressionBiochemical analyses of the interactions between human immunodeficiency virus type 1 Vpr and p6(Gag).Contribution of the C-terminal region within the catalytic core domain of HIV-1 integrase to yeast lethality, chromatin binding and viral replication.
P2860
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P2860
description
1997 nî lūn-bûn
@nan
1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Complementation of integrase function in HIV-1 virions.
@ast
Complementation of integrase function in HIV-1 virions.
@en
type
label
Complementation of integrase function in HIV-1 virions.
@ast
Complementation of integrase function in HIV-1 virions.
@en
prefLabel
Complementation of integrase function in HIV-1 virions.
@ast
Complementation of integrase function in HIV-1 virions.
@en
P2093
P2860
P356
P1433
P1476
Complementation of integrase function in HIV-1 virions
@en
P2093
A D Leavitt
M A Muesing
M A Soares
M Wiskerchen
S McPhearson
T M Fletcher
P2860
P304
P356
10.1093/EMBOJ/16.16.5123
P407
P577
1997-08-01T00:00:00Z