Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
about
Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and ImmunityAntiviral Therapy by HIV-1 Broadly Neutralizing and Inhibitory AntibodiesWhat Are the Most Powerful Immunogen Design Vaccine Strategies?Survivors Remorse: antibody-mediated protection against HIV-1.Stabilized HIV-1 envelope glycoprotein trimers for vaccine use.Neutralizing Monoclonal Antibodies to Fight HIV-1: On the Threshold of Success.Mapping Polyclonal HIV-1 Antibody Responses via Next-Generation Neutralization Fingerprinting.Structure and Recognition of a Novel HIV-1 gp120-gp41 Interface Antibody that Caused MPER Exposure through Viral Escape.Antibodyomics: bioinformatics technologies for understanding B-cell immunity to HIV-1.HIV Vaccine Design to Target Germline Precursors of Glycan-Dependent Broadly Neutralizing Antibodies.Progress toward active or passive HIV-1 vaccination.Proteoliposomal formulations of an HIV-1 gp41-based miniprotein elicit a lipid-dependent immunodominant response overlapping the 2F5 binding motif.Promise and problems associated with the use of recombinant AAV for the delivery of anti-HIV antibodiesNative-like Env trimers as a platform for HIV-1 vaccine design.Ontogeny-based immunogens for the induction of V2-directed HIV broadly neutralizing antibodies.Driving HIV-1 into a Vulnerable Corner by Taking Advantage of Viral Adaptation and Evolution.An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability.Use of broadly neutralizing antibodies for HIV-1 prevention.Recognition of HIV-inactivating peptide triazoles by the recombinant soluble Env trimer, BG505 SOSIP.664.Antigenic landscape of the HIV-1 envelope and new immunological concepts defined by HIV-1 broadly neutralizing antibodies.Approaches to the induction of HIV broadly neutralizing antibodies.Evolution of B cell analysis and Env trimer redesign.Antibody-virus co-evolution in HIV infection: paths for HIV vaccine development.The HIV-1 envelope glycoprotein structure: nailing down a moving target.Identification and specificity of broadly neutralizing antibodies against HIVHow HIV-1 entry mechanism and broadly neutralizing antibodies guide structure-based vaccine design.HIV-1 Escape from a Peptidic Anchor Inhibitor through Stabilization of the Envelope Glycoprotein SpikeImmunization-Elicited Broadly Protective Antibody Reveals Ebolavirus Fusion Loop as a Site of Vulnerability.Hidden Lineage Complexity of Glycan-Dependent HIV-1 Broadly Neutralizing Antibodies Uncovered by Digital Panning and Native-Like gp140 Trimer.Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.Comprehensive Mapping of HIV-1 Escape from a Broadly Neutralizing Antibody.Virus-like Particles Identify an HIV V1V2 Apex-Binding Neutralizing Antibody that Lacks a Protruding Loop.Quaternary contact in the initial interaction of CD4 with the HIV-1 envelope trimer.HIV-1 Envelope Mimicry of Host Enzyme Kynureninase Does Not Disrupt Tryptophan Metabolism.A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans.Conformational Heterogeneity of the HIV Envelope Glycan Shield.Env-Specific Antibodies in Chronic Infection versus in Vaccination.Identification of a novel HIV-1-neutralizing antibody from a CRF07_BC-infected Chinese donor.HIV Envelope Glycoform Heterogeneity and Localized Diversity Govern the Initiation and Maturation of a V2 Apex Broadly Neutralizing Antibody Lineage.Increasing the Clinical Potential and Applications of Anti-HIV Antibodies.
P2860
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P2860
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
description
2016 nî lūn-bûn
@nan
2016 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@ast
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@en
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@nl
type
label
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@ast
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@en
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@nl
prefLabel
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@ast
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@en
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@nl
P2093
P2860
P50
P356
P1433
P1476
Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
@en
P2093
Aliaksandr Druz
Andrew B Ward
Chang W Choi
Dennis R Burton
Evan M Cale
Gabriel Ozorowski
Gwo-Yu Chuang
Ivelin S Georgiev
Jinghe Huang
Justin D Taft
P2860
P304
P356
10.1126/SCIENCE.AAE0474
P407
P577
2016-05-01T00:00:00Z