HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation - Wikidata - awgldk - TriplyDB

HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation

HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation

http://www.wikidata.org/entity/Q34812952

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Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse Viral and developmental cell fusion mechanisms: conservation and divergence HIV entry: a game of hide-and-fuse?Cell entry of enveloped viruses Novel approaches to inhibit HIV entry Imaging single retrovirus entry through alternative receptor isoforms and intermediates of virus-endosome fusion Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme Functional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane Fusion Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation Charge-Surrounded Pockets and Electrostatic Interactions with Small Ions Modulate the Activity of Retroviral Fusion Proteins Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusion Inner/Outer nuclear membrane fusion in nuclear pore assembly: biochemical demonstration and molecular analysis Receptor-induced thiolate couples Env activation to retrovirus fusion and infection Impact of the HIV-1 env genetic context outside HR1-HR2 on resistance to the fusion inhibitor enfuvirtide and viral infectivity in clinical isolates The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH.Induction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a Trigger Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoprotein Liposome reconstitution of a minimal protein-mediated membrane fusion machine.FUS1 regulates the opening and expansion of fusion pores between mating yeast.Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion.Identification of the HIV-1 gp41 core-binding motif in the scaffolding domain of caveolin-1.The mechanism by which molecules containing the HIV gp41 core-binding motif HXXNPF inhibit HIV-1 envelope glycoprotein-mediated syncytium formation.Enhanced fusion pore expansion mediated by the trans-acting Endodomain of the reovirus FAST proteins.Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation.Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus Role of the simian virus 5 fusion protein N-terminal coiled-coil domain in folding and promotion of membrane fusion.Human immunodeficiency virus (HIV) gp41 escape mutants: cross-resistance to peptide inhibitors of HIV fusion and altered receptor activation of gp120.Kinetic analyses of the surface-transmembrane disulfide bond isomerization-controlled fusion activation pathway in Moloney murine leukemia virus Time-resolved imaging of HIV-1 Env-mediated lipid and content mixing between a single virion and cell membrane.A study of low pH-induced refolding of Env of avian sarcoma and leukosis virus into a six-helix bundle.Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation.Class I and class II viral fusion protein structures reveal similar principles in membrane fusion.HIV entry and envelope glycoprotein-mediated fusion Folded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external region Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain.Identification of a human protein-derived HIV-1 fusion inhibitor targeting the gp41 fusion core structure.Sub-inhibitory concentrations of human α-defensin potentiate neutralizing antibodies against HIV-1 gp41 pre-hairpin intermediates in the presence of serum.Increasing hydrophobicity of residues in an anti-HIV-1 Env peptide synergistically improves potency Different infectivity of HIV-1 strains is linked to number of envelope trimers required for entry

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P2860

HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation

http://www.wikidata.org/entity/Q34812952

description

2003 nî lūn-bûn

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2003 թուականի Մարտին հրատարակուած գիտական յօդուած

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2003 թվականի մարտին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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HIV-1 envelope proteins comple ...... ly after fusion pore formation

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HIV-1 envelope proteins comple ...... ly after fusion pore formation

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HIV-1 envelope proteins comple ...... ly after fusion pore formation

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HIV-1 envelope proteins comple ...... ly after fusion pore formation

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MBC.E02-09-0573

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Molecular Biology of the Cell

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HIV-1 envelope proteins comple ...... ly after fusion pore formation

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Fredric S Cohen

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

Grigory B Melikyan

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Ruben M Markosyan

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P2860

Expression cloning of new receptors used by simian and human immunodeficiency viruses

Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusion

Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis.

Atomic structure of the ectodomain from HIV-1 gp41

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

HIV entry and its inhibition

Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion

Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection

Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target

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926-938

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10.1091/MBC.E02-09-0573

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3

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14

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2003-03-01T00:00:00Z

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10860424

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12631714

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protein folding

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151570

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