Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics - Wikidata - awgldk - TriplyDB

Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics

Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics

http://www.wikidata.org/entity/Q34415921

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HIV-1 induced bystander apoptosis Comprehensive cross-clade neutralization analysis of a panel of anti-human immunodeficiency virus type 1 monoclonal antibodies Establishment of a novel CCR5 and CXCR4 expressing CD4+ cell line which is highly sensitive to HIV and suitable for high-throughput evaluation of CCR5 and CXCR4 antagonists Single-Cell and Single-Cycle Analysis of HIV-1 Replication Viral membrane fusion Design of a Potent D-Peptide HIV-1 Entry Inhibitor with a Strong Barrier to Resistance Solution Structure of the Monovalent Lectin Microvirin in Complex with Man (1-2)Man Provides a Basis for Anti-HIV Activity with Low Toxicity Griffithsin, a potent HIV entry inhibitor, is an excellent candidate for anti-HIV microbicide HIV entry inhibitors: mechanisms of action and resistance pathways Insensitivity of paediatric HIV-1 subtype C viruses to broadly neutralising monoclonal antibodies raised against subtype B V3 loop truncations in HIV-1 envelope impart resistance to coreceptor inhibitors and enhanced sensitivity to neutralizing antibodies Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding Impact of the HIV-1 env genetic context outside HR1-HR2 on resistance to the fusion inhibitor enfuvirtide and viral infectivity in clinical isolates HIV-1 fusion is blocked through binding of GB Virus C E2-derived peptides to the HIV-1 gp41 disulfide loop [corrected]A compensatory mutation provides resistance to disparate HIV fusion inhibitor peptides and enhances membrane fusion A general strategy to endow natural fusion-protein-derived peptides with potent antiviral activity Functional stability of unliganded envelope glycoprotein spikes among isolates of human immunodeficiency virus type 1 (HIV-1)Development of a High-Throughput Functional Screen Using Nanowell-Assisted Cell Patterning Viral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41.Closing the door to human immunodeficiency virus.Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup a infection and identify a fusion intermediate DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4.Flat clathrin lattices: stable features of the plasma membrane.A single-residue change in the HIV-1 V3 loop associated with maraviroc resistance impairs CCR5 binding affinity while increasing replicative capacity.Antibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics.The benzamide derivative N-[1-(7-tert-Butyl-1H-indol-3-ylmethyl)-2-(4-cyclopropanecarbonyl-3-methyl-piperazin-1-yl)-2-oxo-ethyl]-4-nitro-benzamide (SP-10) reduces HIV-1 infectivity in vitro by modifying actin dynamics.A monoclonal Fab derived from a human nonimmune phage library reveals a new epitope on gp41 and neutralizes diverse human immunodeficiency virus type 1 strains.Enhancing exposure of HIV-1 neutralization epitopes through mutations in gp41.Sequestering of the prehairpin intermediate of gp41 by peptide N36Mut(e,g) potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41 Llama antibody fragments with cross-subtype human immunodeficiency virus type 1 (HIV-1)-neutralizing properties and high affinity for HIV-1 gp120 Elite suppressor-derived HIV-1 envelope glycoproteins exhibit reduced entry efficiency and kinetics Affinity maturation by targeted diversification of the CDR-H2 loop of a monoclonal Fab derived from a synthetic naïve human antibody library and directed against the internal trimeric coiled-coil of gp41 yields a set of Fabs with improved HIV-1 neut Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation.Analysis of memory B cell responses and isolation of novel monoclonal antibodies with neutralizing breadth from HIV-1-infected individuals.SERINC5 protein inhibits HIV-1 fusion pore formation by promoting functional inactivation of envelope glycoproteins.Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus Variants of human immunodeficiency virus type 1 that efficiently use CCR5 lacking the tyrosine-sulfated amino terminus have adaptive mutations in gp120, including loss of a functional N-glycan Human immunodeficiency virus (HIV) gp41 escape mutants: cross-resistance to peptide inhibitors of HIV fusion and altered receptor activation of gp120.Inhibition of lysosome and proteasome function enhances human immunodeficiency virus type 1 infection.Differences in the fitness of two diverse wild-type human immunodeficiency virus type 1 isolates are related to the efficiency of cell binding and entry.

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P2860

Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics

http://www.wikidata.org/entity/Q34415921

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2002 nî lūn-bûn

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2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Sensitivity of HIV-1 to entry ...... r density, and fusion kinetics

@en

P2093

Cynthia A Derdeyn

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

Eric Hunter

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

Jacqueline D Reeves

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

Jeffrey N Sfakianos

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John L Miamidian

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Matthew Sharron

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

Navid Ahmad

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

Phoebe E Harvey

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

Robert Blumenthal

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

Robert W Doms

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

P2860

Core structure of gp41 from the HIV envelope glycoprotein

Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor

Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides.

Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion

HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process

The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide

A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding

Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy.

Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes

Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry

P304

16249-16254

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scholarly article

P356

10.1073/PNAS.252469399

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P407

P433

25

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P478

99

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P50

Stefan Pöhlmann

Stephen A. Gallo

P577

2002-11-20T00:00:00Z

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P5875

235609497

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P698

12444251

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P932

138597

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