Functional surfaces of the human immunodeficiency virus type 1 capsid protein. - Wikidata - awgldk - TriplyDB

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

http://www.wikidata.org/entity/Q39748566

about

Variable fitness impact of HIV-1 escape mutations to cytotoxic T lymphocyte (CTL) response The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A.HIV type 1 Gag as a target for antiviral therapy Virus maturation as a new HIV-1 therapeutic target Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cells Real-time visualization of HIV-1 GAG trafficking in infected macrophages Ebselen, a Small-Molecule Capsid Inhibitor of HIV-1 Replication.Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid Domain-swapped dimerization of the HIV-1 capsid C-terminal domain Solution Structure of a Hydrocarbon Stapled Peptide Inhibitor in Complex with Monomeric C-terminal Domain of HIV-1 Capsid Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein X-ray structures of the hexameric building block of the HIV capsid.Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function Disulfide bond stabilization of the hexameric capsomer of human immunodeficiency virus Atomic-level modelling of the HIV capsid CPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 Replication Structure of a Monomeric Mutant of the HIV-1 Capsid Protein A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface Distinct Effects of Two HIV-1 Capsid Assembly Inhibitor Families That Bind the Same Site within the N-Terminal Domain of the Viral CA Protein Discovery of Novel Small-Molecule HIV-1 Replication Inhibitors That Stabilize Capsid Complexes Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy Monitoring binding of HIV-1 capsid assembly inhibitors using (19)F ligand-and (15)N protein-based NMR and X-ray crystallography: early hit validation of a benzodiazepine series Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution Structure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular Assemblies Ty3 capsid mutations reveal early and late functions of the amino-terminal domain Rationally designed interfacial peptides are efficient in vitro inhibitors of HIV-1 capsid assembly with antiviral activity Efficient production of HIV-1 virus-like particles from a mammalian expression vector requires the N-terminal capsid domain Structural and functional insights into the HIV-1 maturation inhibitor binding pocket The effect of chemical chaperones on the assembly and stability of HIV-1 capsid protein Fitness costs of mutations at the HIV-1 capsid hexamerization interface Tracking interspecies transmission and long-term evolution of an ancient retrovirus using the genomes of modern mammals Structure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396 eEF2 and Ras-GAP SH3 domain-binding protein (G3BP1) modulate stress granule assembly during HIV-1 infection Crystal structure of an HIV assembly and maturation switch.Coarse-grained simulation reveals key features of HIV-1 capsid self-assembly.STRUCTURAL VIROLOGY. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.Structural and dynamics studies of the D54A mutant of human T cell leukemia virus-1 capsid protein.

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P2860

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

http://www.wikidata.org/entity/Q39748566

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

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2003年學術文章

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name

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

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Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

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type

label

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

@en

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

@nl

prefLabel

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

@en

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

@nl

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JVI.77.9.5439-5450.2003

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Journal of Virology

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Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

@en

P2093

Jennifer E Garrus

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Kirsten M Stray

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Uta K von Schwedler

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Wesley I Sundquist

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P2860

Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release

Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1

The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix

Differential membrane binding of the human immunodeficiency virus type 1 matrix protein

Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution

Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses

Contribution of surface salt bridges to protein stability

Structure and self-association of the Rous sarcoma virus capsid protein

Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein

Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis

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5439-5450

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10.1128/JVI.77.9.5439-5450.2003

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