Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected. - Wikidata - wikimedia - TriplyDB

Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected.

Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected.

http://www.wikidata.org/entity/Q35076987

about

A Blueprint for HIV Vaccine Discovery Antibody responses to envelope glycoproteins in HIV-1 infection Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site Antigenic properties of the human immunodeficiency virus envelope glycoprotein gp120 on virions bound to target cells Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env A gp41 MPER-specific Llama VHH Requires a Hydrophobic CDR3 for Neutralization but not for Antigen Recognition Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers Cell- and Protein-Directed Glycosylation of Native Cleaved HIV-1 Envelope Allosteric modulation of the HIV-1 gp120-gp41 association site by adjacent gp120 variable region 1 (V1) N-glycans linked to neutralization sensitivity A Novel Two-Tag System for Monitoring Transport and Cleavage through the Classical Secretory Pathway - Adaptation to HIV Envelope Processing Functional stability of unliganded envelope glycoprotein spikes among isolates of human immunodeficiency virus type 1 (HIV-1)HIV Envelope gp120 Alters T Cell Receptor Mobilization in the Immunological Synapse of Uninfected CD4 T Cells and Augments T Cell Activation Autoantibodies induced by chimeric cytokine-HIV envelope glycoprotein immunogens.Multi-Parameter Exploration of HIV-1 Virus-Like Particles as Neutralizing Antibody Immunogens in Guinea Pigs, Rabbits and Macaques Antibody to gp41 MPER alters functional properties of HIV-1 Env without complete neutralization The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection.A novel, live-attenuated vesicular stomatitis virus vector displaying conformationally intact, functional HIV-1 envelope trimers that elicits potent cellular and humoral responses in mice.Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers.Inhibition of HIV Entry by Targeting the Envelope Transmembrane Subunit gp41.Increased functional stability and homogeneity of viral envelope spikes through directed evolution.Chimeric HIV-1 envelope glycoproteins with potent intrinsic granulocyte-macrophage colony-stimulating factor (GM-CSF) activity.Optimized Infectivity of the Cell-Free Single-Cycle Human Immunodeficiency Viruses Type 1 (HIV-1) and Its Restriction by Host Cells.An HIV-1 envelope glycoprotein trimer with an embedded IL-21 domain activates human B cells Mechanism of multivalent nanoparticle encounter with HIV-1 for potency enhancement of peptide triazole virus inactivation.Comparative Immunogenicity of Evolved V1V2-Deleted HIV-1 Envelope Glycoprotein Trimers Binding of anti-membrane-proximal gp41 monoclonal antibodies to CD4-liganded and -unliganded human immunodeficiency virus type 1 and simian immunodeficiency virus virions Targeting HIV-1 envelope glycoprotein trimers to B cells by using APRIL improves antibody responses.Discrete partitioning of HIV-1 Env forms revealed by viral capture.Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction.Significant differences in cell-cell fusion and viral entry between strains revealed by scanning mutagenesis of the C-heptad repeat of HIV gp41 Chemical Cross-Linking Stabilizes Native-Like HIV-1 Envelope Glycoprotein Trimer Antigens Proteolytic processing of the human immunodeficiency virus envelope glycoprotein precursor decreases conformational flexibility Native Conformation and Canonical Disulfide Bond Formation Are Interlinked Properties of HIV-1 Env Glycoproteins.Identification of an HIV-1 clade A envelope that exhibits broad antigenicity and neutralization sensitivity and elicits antibodies targeting three distinct epitopes.Development of prophylactic vaccines against HIV-1.Impact of HIV-1 Membrane Cholesterol on Cell-Independent Lytic Inactivation and Cellular Infectivity.Isolation of HIV-1-reactive antibodies using cell surface-expressed gp160Δc(BaL.).Antigenic properties of the HIV envelope on virions in solution.Native-like Env trimers as a platform for HIV-1 vaccine design.

P2860

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P2860

Enzyme digests eliminate nonfunctional Env from HIV-1 particle surfaces, leaving native Env trimers intact and viral infectivity unaffected.

http://www.wikidata.org/entity/Q35076987

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年学术文章

@wuu

2011年学术文章

@zh-cn

2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

name

Enzyme digests eliminate nonfu ...... viral infectivity unaffected.

@ast

Enzyme digests eliminate nonfu ...... viral infectivity unaffected.

@en

type

label

Enzyme digests eliminate nonfu ...... viral infectivity unaffected.

@ast

Enzyme digests eliminate nonfu ...... viral infectivity unaffected.

@en

prefLabel

Enzyme digests eliminate nonfu ...... viral infectivity unaffected.

@ast

Enzyme digests eliminate nonfu ...... viral infectivity unaffected.

@en

P1433

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P1433

Journal of Virology

P1476

Enzyme digests eliminate nonfu ...... viral infectivity unaffected.

@en

P2093

Ema T Crooks

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

James M Binley

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

Keiko Osawa

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

Tommy Tong

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

P2860

Neutralizing antibody responses drive the evolution of human immunodeficiency virus type 1 envelope during recent HIV infection

Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies

Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport

Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 binding

Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport

Furin at the cutting edge: from protein traffic to embryogenesis and disease

Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates

Antibody domain exchange is an immunological solution to carbohydrate cluster recognition

Assembly of asparagine-linked oligosaccharides

Anti-V3 monoclonal antibodies display broad neutralizing activities against multiple HIV-1 subtypes

P304

5825-5839

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scholarly article

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10.1128/JVI.00154-11

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P433

12

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P478

85

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2011-04-06T00:00:00Z

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21471242

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