N-Terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles.
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Virus maturation as a new HIV-1 therapeutic targetMutations affecting cleavage at the p10-capsid protease cleavage site block Rous sarcoma virus replication.Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cellsSelf-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core proteinFlexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid ProteinDisulfide bond stabilization of the hexameric capsomer of human immunodeficiency virusCryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assemblyDesign of in vitro symmetric complexes and analysis by hybrid methods reveal mechanisms of HIV capsid assemblyThe structural biology of HIV assembly.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 assayEffect of dimerizing domains and basic residues on in vitro and in vivo assembly of Mason-Pfizer monkey virus and human immunodeficiency virus.In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain.The capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation.In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature.Structural analysis of HIV-1 maturation using cryo-electron tomography.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.Assembly of retrovirus capsid-nucleocapsid proteins in the presence of membranes or RNA.Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation.Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells.Characterization of Rous sarcoma virus Gag particles assembled in vitro.Analysis of Mason-Pfizer monkey virus Gag domains required for capsid assembly in bacteria: role of the N-terminal proline residue of CA in directing particle shape.Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin ATripeptide interference with human immunodeficiency virus type 1 morphogenesis.Atomic force microscopy and electron microscopy analysis of retrovirus Gag proteins assembled in vitro on lipid bilayers.The cysteine residues of HIV-1 capsid regulate oligomerization and cyclophilin A-induced changes.In vitro selection of highly darunavir-resistant and replication-competent HIV-1 variants by using a mixture of clinical HIV-1 isolates resistant to multiple conventional protease inhibitors.The Mason-Pfizer monkey virus internal scaffold domain enables in vitro assembly of human immunodeficiency virus type 1 Gag.Reversible binding of recombinant human immunodeficiency virus type 1 gag protein to nucleic acids in virus-like particle assembly in vitro.Analysis of the N-terminal region of the murine leukemia virus nucleocapsid proteinBiophysical characterization of the feline immunodeficiency virus p24 capsid protein conformation and in vitro capsid assembly.Distinct roles for nucleic acid in in vitro assembly of purified Mason-Pfizer monkey virus CANC proteins.Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding.Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant.Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding.Molecular organization of Mason-Pfizer monkey virus capsids assembled from Gag polyprotein in Escherichia coli.Mutation of dileucine-like motifs in the human immunodeficiency virus type 1 capsid disrupts virus assembly, gag-gag interactions, gag-membrane binding, and virion maturationCompensatory substitutions restore normal core assembly in simian immunodeficiency virus isolates with Gag epitope cytotoxic T-lymphocyte escape mutations.Second-site compensatory mutations of HIV-1 capsid mutations.
P2860
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P2860
N-Terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles.
description
1998 nî lūn-bûn
@nan
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
1998年论文
@zh
1998年论文
@zh-cn
name
N-Terminal extension of human ...... ubular to spherical particles.
@en
N-Terminal extension of human ...... ubular to spherical particles.
@nl
type
label
N-Terminal extension of human ...... ubular to spherical particles.
@en
N-Terminal extension of human ...... ubular to spherical particles.
@nl
prefLabel
N-Terminal extension of human ...... ubular to spherical particles.
@en
N-Terminal extension of human ...... ubular to spherical particles.
@nl
P2093
P2860
P1433
P1476
N-Terminal extension of human ...... ubular to spherical particles.
@en
P2093
C Huckhagel
H G Kräusslich
H Hohenberg
P2860
P304
P407
P577
1998-06-01T00:00:00Z