Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers - Test2 - elhamkhani - TriplyDB

Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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The HIV glycan shield as a target for broadly neutralizing antibodies Cell- and Protein-Directed Glycosylation of Native Cleaved HIV-1 Envelope Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing Epitopes HIV-1 VACCINES. HIV-1 neutralizing antibodies induced by native-like envelope trimers Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein Survivors Remorse: antibody-mediated protection against HIV-1.HIV-1 Glycan Density Drives the Persistence of the Mannose Patch within an Infected Individual.Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion.HIV-1 Envelope Trimer Design and Immunization Strategies To Induce Broadly Neutralizing Antibodies.Diversification in the HIV-1 Envelope Hyper-variable Domains V2, V4, and V5 and Higher Probability of Transmitted/Founder Envelope Glycosylation Favor the Development of Heterologous Neutralization Breadth Engineering and Characterization of a Fluorescent Native-Like HIV-1 Envelope Glycoprotein Trimer.Roles of glycans in interactions between gp120 and HIV broadly neutralizing antibodies Modular synthesis of N-glycans and arrays for the hetero-ligand binding analysis of HIV antibodies Native Conformation and Canonical Disulfide Bond Formation Are Interlinked Properties of HIV-1 Env Glycoproteins.Travelling-wave ion mobility and negative ion fragmentation of high-mannose N-glycans.Native-like Env trimers as a platform for HIV-1 vaccine design.An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability.Molecular Architecture of the Cleavage-Dependent Mannose Patch on a Soluble HIV-1 Envelope Glycoprotein Trimer.Structure and Glycan Binding of a New Cyanovirin-N Homolog.Antibody recognition of HIV and dengue glycoproteins.HIV-1 envelope glycoprotein immunogens to induce broadly neutralizing antibodies.Improving the Expression and Purification of Soluble, Recombinant Native-Like HIV-1 Envelope Glycoprotein Trimers by Targeted Sequence Changes.Glycosylation Benchmark Profile for HIV-1 Envelope Glycoprotein Production Based on Eleven Env Trimers.Exclusive Decoration of Simian Immunodeficiency Virus Env with High-Mannose Type N-Glycans Is Not Compatible with Mucosal Transmission in Rhesus Macaques Approaches to the induction of HIV broadly neutralizing antibodies.The HIV-1 envelope glycoprotein structure: nailing down a moving target.Structural principles controlling HIV envelope glycosylation.Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.Improving the Immunogenicity of Native-like HIV-1 Envelope Trimers by Hyperstabilization.The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.Global site-specific N-glycosylation analysis of HIV envelope glycoprotein.Binding of inferred germline precursors of broadly neutralizing HIV-1 antibodies to native-like envelope trimers.Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design.Complete epitopes for vaccine design derived from a crystal structure of the broadly neutralizing antibodies PGT128 and 8ANC195 in complex with an HIV-1 Env trimer.Influences on the Design and Purification of Soluble, Recombinant Native-Like HIV-1 Envelope Glycoprotein Trimers.Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo.cGMP production and analysis of BG505 SOSIP.664, an extensively glycosylated, trimeric HIV-1 envelope glycoprotein vaccine candidate.Epitope-focused immunogens against the CD4-binding site of HIV-1 envelope protein induce neutralizing antibodies against auto- and heterologous viruses.Integrity of Glycosylation Processing of a Glycan-Depleted Trimeric HIV-1 Immunogen Targeting Key B-Cell Lineages.Exploiting glycan topography for computational design of Env glycoprotein antigenicity.

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

http://www.wikidata.org/entity/Q28263063

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Structural Constraints Determine the Glycosylation of HIV-1 Envelope Trimers

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Albert Cupo

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Andrew B Ward

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Ian A Wilson

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John P Moore

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Laura K Pritchard

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Rajesh Ringe

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

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A Blueprint for HIV Vaccine Discovery

Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR

Antibody domain exchange is an immunological solution to carbohydrate cluster recognition

Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9

Molecular architecture of native HIV-1 gp120 trimers

Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies

A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield

Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120

Structural basis for diverse N-glycan recognition by HIV-1–neutralizing V1–V2–directed antibody PG16

Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer

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