Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly. - Wikidata - awgldk - TriplyDB

Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.

Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.

http://www.wikidata.org/entity/Q35377316

about

Cellular and viral determinants of retroviral nuclear entry Impact of Chromatin on HIV Replication HIV-1 capsid: the multifaceted key player in HIV-1 infection Misdelivery at the Nuclear Pore Complex-Stopping a Virus Dead in Its Tracks Time-Resolved Imaging of Single HIV-1 Uncoating In Vitro and in Living Cells KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection STRUCTURAL VIROLOGY. Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography Retroviral integration: Site matters: Mechanisms and consequences of retroviral integration site selection All-Atom Molecular Dynamics of Virus Capsids as Drug Targets Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.STRUCTURAL VIROLOGY. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.Structural basis of HIV-1 capsid recognition by PF74 and CPSF6.The MORPHEUS II protein crystallization screen HIV-1 uses dynamic capsid pores to import nucleotides and fuel encapsidated DNA synthesis Chromatin organization at the nuclear pore favours HIV replication Microplate-based assay for identifying small molecules that bind a specific intersubunit interface within the assembled HIV-1 capsid.Evolutionary and Functional Analysis of Old World Primate TRIM5 Reveals the Ancient Emergence of Primate Lentiviruses and Convergent Evolution Targeting a Conserved Capsid Interface HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Identification of a small molecule HIV-1 inhibitor that targets the capsid hexamer.HIV-1 Capsid Inhibitors as Antiretroviral Agents SUN2 Overexpression Deforms Nuclear Shape and Inhibits HIV.HIV-1 capsid is involved in post-nuclear entry steps The Cleavage and Polyadenylation Specificity Factor 6 (CPSF6) Subunit of the Capsid-recruited Pre-messenger RNA Cleavage Factor I (CFIm) Complex Mediates HIV-1 Integration into Genes.HIV-1 assembly, release and maturation.Comparison of Biochemical Properties of HIV-1 and HIV-2 Capsid Proteins.Reverse Transcription Mechanically Initiates HIV-1 Capsid Disassembly.Inhibition of HIV-1 Maturation via Small-Molecule Targeting of the Amino-Terminal Domain in the Viral Capsid Protein.Efficient Transduction of Human and Rhesus Macaque Primary T Cells by a Modified Human Immunodeficiency Virus Type 1-Based Lentiviral Vector.Labeling of virus components for advanced, quantitative imaging analyses.Mx oligomer: a novel capsid pattern sensor?HIV-1 Resistance to the Capsid-Targeting Inhibitor PF74 Results in Altered Dependence on Host Factors Required for Virus Nuclear Entry.Complementary Assays Reveal a Low Level of CA Associated with Viral Complexes in the Nuclei of HIV-1-Infected Cells.Quantitative microscopy of functional HIV post-entry complexes reveals association of replication with the viral capsid Oligomeric viral proteins: small in size, large in presence.Capsid-Dependent Host Factors in HIV-1 Infection.Analysis of HIV-1 Gag protein interactions via biotin ligase tagging.Effects of Inner Nuclear Membrane Proteins SUN1/UNC-84A and SUN2/UNC-84B on the Early Steps of HIV-1 Infection.Digoxin reveals a functional connection between HIV-1 integration preference and T-cell activation.Capsid-CPSF6 Interaction Is Dispensable for HIV-1 Replication in Primary Cells but Is Selected during Virus Passage In Vivo.Roles of Capsid-Interacting Host Factors in Multimodal Inhibition of HIV-1 by PF74.

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P2860

Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly.

http://www.wikidata.org/entity/Q35377316

description

2014 nî lūn-bûn

@nan

2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Host cofactors and pharmacolog ...... that is lost upon disassembly.

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Host cofactors and pharmacolog ...... that is lost upon disassembly.

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type

label

Host cofactors and pharmacolog ...... that is lost upon disassembly.

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Host cofactors and pharmacolog ...... that is lost upon disassembly.

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prefLabel

Host cofactors and pharmacolog ...... that is lost upon disassembly.

@ast

Host cofactors and pharmacolog ...... that is lost upon disassembly.

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JOURNAL.PPAT.1004459

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Host cofactors and pharmacolog ...... that is lost upon disassembly

@en

P2093

Adam J Fletcher

http://www.w3.org/2001/XMLSchema#string

Amanda J Price

http://www.w3.org/2001/XMLSchema#string

Christopher Aiken

http://www.w3.org/2001/XMLSchema#string

Jason W Chin

http://www.w3.org/2001/XMLSchema#string

Leo C James

http://www.w3.org/2001/XMLSchema#string

Sebastian Essig

http://www.w3.org/2001/XMLSchema#string

P2860

Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells

HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency

Identification of host proteins required for HIV infection through a functional genomic screen

X-ray structures of the hexameric building block of the HIV capsid.

Disulfide bond stabilization of the hexameric capsomer of human immunodeficiency virus

HIV Capsid is a Tractable Target for Small Molecule Therapeutic Intervention

CPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 Replication

Discovery of Novel Small-Molecule HIV-1 Replication Inhibitors That Stabilize Capsid Complexes

HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358

HIV-1 evades innate immune recognition through specific cofactor recruitment

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e1004459

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scholarly article

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10.1371/JOURNAL.PPAT.1004459

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10

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10

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P50

David A. Jacques

William A. McEwan

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2014-10-30T00:00:00Z

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267747435

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25356722

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4214760

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