Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env - Wikidata - awgldk - TriplyDB

Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env

Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env

http://www.wikidata.org/entity/Q28256508

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Harnessing the protective potential of HIV-1 neutralizing antibodies Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Conformational Masking and Receptor-Dependent Unmasking of Highly Conserved Env Epitopes Recognized by Non-Neutralizing Antibodies That Mediate Potent ADCC against HIV-1 Structure and Dynamics of the Native HIV-1 Env Trimer Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and Immunity Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing Epitopes A single mutation in the envelope protein modulates flavivirus antigenicity, stability, and pathogenesis Survivors Remorse: antibody-mediated protection against HIV-1.Isotope Labeling of Biomolecules: Structural Analysis of Viruses by HDX-MS.Induction of a Tier-1-like Phenotype in Diverse Tier-2 Isolates by Agents that Guide HIV-1 Env to Perturbation-sensitive, Non-native States.Stabilized HIV-1 envelope glycoprotein trimers for vaccine use.HIV-1 Envelope Trimer Design and Immunization Strategies To Induce Broadly Neutralizing Antibodies.Probing the Impact of Local Structural Dynamics of Conformational Epitopes on Antibody Recognition.Structure/Function Studies Involving the V3 Region of the HIV-1 Envelope Delineate Multiple Factors That Affect Neutralization Sensitivity.Inhibition of HIV Entry by Targeting the Envelope Transmembrane Subunit gp41.A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene.Comprehensive antigenic map of a cleaved soluble HIV-1 envelope trimer.Strategies to guide the antibody affinity maturation process Murine Antibody Responses to Cleaved Soluble HIV-1 Envelope Trimers Are Highly Restricted in Specificity.Design and structure of two HIV-1 clade C SOSIP.664 trimers that increase the arsenal of native-like Env immunogens.Broadly Neutralizing Antibody 8ANC195 Recognizes Closed and Open States of HIV-1 Env.Experimental Estimation of the Effects of All Amino-Acid Mutations to HIV's Envelope Protein on Viral Replication in Cell Culture Antigenic characterization of the human immunodeficiency virus (HIV-1) envelope glycoprotein precursor incorporated into nanodiscs.Conformational Epitope-Specific Broadly Neutralizing Plasma Antibodies Obtained from an HIV-1 Clade C-Infected Elite Neutralizer Mediate Autologous Virus Escape through Mutations in the V1 Loop.Immunogenicity of a Prefusion HIV-1 Envelope Trimer in Complex with a Quaternary-Structure-Specific Antibody.Antibodies Elicited by Multiple Envelope Glycoprotein Immunogens in Primates Neutralize Primary Human Immunodeficiency Viruses (HIV-1) Sensitized by CD4-Mimetic Compounds.Epitope-Independent Purification of Native-Like Envelope Trimers from Diverse HIV-1 Isolates.Release of gp120 Restraints Leads to an Entry-Competent Intermediate State of the HIV-1 Envelope Glycoproteins.Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site.Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop.Native-like Env trimers as a platform for HIV-1 vaccine design.Structural Analysis of the Glycosylated Intact HIV-1 gp120-b12 Antibody Complex Using Hydroxyl Radical Protein Footprinting.HIV-1 envelope glycoprotein immunogens to induce broadly neutralizing antibodies.Plasticity and Epitope Exposure of the HIV-1 Envelope Trimer.Changes in Structure and Antigenicity of HIV-1 Env Trimers Resulting from Removal of a Conserved CD4 Binding Site-Proximal Glycan.Lack of ADCC Breadth of Human Nonneutralizing Anti-HIV-1 Antibodies.Natural Killer (NK) Cell Education Differentially Influences HIV Antibody-Dependent NK Cell Activation and Antibody-Dependent Cellular Cytotoxicity.HIV-1 Cross-reactive Primary Virus Neutralizing Antibody Response Elicited by Immunization in Non-human Primate.Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design.

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Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env

http://www.wikidata.org/entity/Q28256508

description

2015 nî lūn-bûn

@nan

2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2015年の論文

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2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Antibody potency relates to th ...... ed, pre-fusion form of HIV Env

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Antibody potency relates to th ...... ed, pre-fusion form of HIV Env

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Antibody potency relates to th ...... ed, pre-fusion form of HIV Env

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Antibody potency relates to th ...... ed, pre-fusion form of HIV Env

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Antibody potency relates to th ...... ed, pre-fusion form of HIV Env

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Nature Communications

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Antibody potency relates to th ...... ed, pre-fusion form of HIV Env

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Albert Cupo

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John P Moore

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Kelly K Lee

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Miklos Guttman

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Rogier W Sanders

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P2860

Structural mechanism of trimeric HIV-1 envelope glycoprotein activation

A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals

Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro

bNAber: database of broadly neutralizing HIV antibodies

Structural definition of a conserved neutralization epitope on HIV-1 gp120

HIV-1 neutralizing antibodies: understanding nature's pathways

Molecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structure

Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates

Antibody domain exchange is an immunological solution to carbohydrate cluster recognition

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

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10.1038/NCOMMS7144

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6

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Jean-Philippe Julien

Ian Andrew Wilson

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2015-02-05T00:00:00Z

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1004806672

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4338595

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