A putative alpha-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly
about
Potent activity of the HIV-1 maturation inhibitor bevirimat in SCID-hu Thy/Liv miceThe prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particlesPredicting Bevirimat resistance of HIV-1 from genotypeThe host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminusA single polymorphism in HIV-1 subtype C SP1 is sufficient to confer natural resistance to the maturation inhibitor bevirimatHIV type 1 Gag as a target for antiviral therapyVirus maturation as a new HIV-1 therapeutic targetThe sequence of the CA-SP1 junction accounts for the differential sensitivity of HIV-1 and SIV to the small molecule maturation inhibitor 3-O-{3',3'-dimethylsuccinyl}-betulinic acidPharmacological intervention of HIV-1 maturationThe Structure of Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10 Domain in Assembly.Protease cleavage leads to formation of mature trimer interface in HIV-1 capsidEntropic switch regulates myristate exposure in the HIV-1 matrix proteinDomain-swapped dimerization of the HIV-1 capsid C-terminal domainStructure of the Myristylated Human Immunodeficiency Virus Type 2 Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Membrane TargetingCryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly3D visualization of HIV virions by cryoelectron tomographyCharacterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assayStructural and functional insights into the HIV-1 maturation inhibitor binding pocketGag-Pol processing during HIV-1 virion maturation: a systems biology approachMechanistic Studies and Modeling Reveal the Origin of Differential Inhibition of Gag Polymorphic Viruses by HIV-1 Maturation InhibitorsRole of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivityStructure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396Helical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles.Crystal structure of an HIV assembly and maturation switch.Design of in vitro symmetric complexes and analysis by hybrid methods reveal mechanisms of HIV capsid assemblyThe structural biology of HIV assembly.The inhibition of assembly of HIV-1 virus-like particles by 3-O-(3',3'-dimethylsuccinyl) betulinic acid (DSB) is counteracted by Vif and requires its Zinc-binding domain.Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assayElectron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells.Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packagingHow HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Effect of dimerizing domains and basic residues on in vitro and in vivo assembly of Mason-Pfizer monkey virus and human immunodeficiency virus.Novel approaches to inhibiting HIV-1 replication.Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of gag membrane targeting.The capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation.Detection of a trimeric human immunodeficiency virus type 1 Gag intermediate is dependent on sequences in the matrix protein, p17.The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly.Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding.Roles of matrix, p2, and N-terminal myristoylation in human immunodeficiency virus type 1 Gag assembly.Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain.
P2860
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P2860
A putative alpha-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assembly
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
A putative alpha-helical struc ...... al for viral particle assembly
@ast
A putative alpha-helical struc ...... al for viral particle assembly
@en
type
label
A putative alpha-helical struc ...... al for viral particle assembly
@ast
A putative alpha-helical struc ...... al for viral particle assembly
@en
prefLabel
A putative alpha-helical struc ...... al for viral particle assembly
@ast
A putative alpha-helical struc ...... al for viral particle assembly
@en
P2093
P2860
P1433
P1476
A putative alpha-helical struc ...... al for viral particle assembly
@en
P2093
H G Göttlinger
M A Accola
P2860
P304
P577
1998-03-01T00:00:00Z