Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site
about
HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchHIV-Host Interactions: Implications for Vaccine DesignCurrent Advances in Virus-Like Particles as a Vaccination Approach against HIV InfectionThe HIV glycan shield as a target for broadly neutralizing antibodiesTrimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and GNatively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding siteSurvivors Remorse: antibody-mediated protection against HIV-1.Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in Nonhuman PrimatesGlycine Substitution at Helix-to-Coil Transitions Facilitates the Structural Determination of a Stabilized Subtype C HIV Envelope GlycoproteinHIV-1 Envelope Trimer Design and Immunization Strategies To Induce Broadly Neutralizing Antibodies.Reducing V3 Antigenicity and Immunogenicity on Soluble, Native-Like HIV-1 Env SOSIP TrimersMurine Antibody Responses to Cleaved Soluble HIV-1 Envelope Trimers Are Highly Restricted in Specificity.Discrete partitioning of HIV-1 Env forms revealed by viral capture.Minimally Mutated HIV-1 Broadly Neutralizing Antibodies to Guide Reductionist Vaccine Design.Sequential and Simultaneous Immunization of Rabbits with HIV-1 Envelope Glycoprotein SOSIP.664 Trimers from Clades A, B and C.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 BreadthMapping Polyclonal HIV-1 Antibody Responses via Next-Generation Neutralization Fingerprinting.Antibodyomics: bioinformatics technologies for understanding B-cell immunity to HIV-1.Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction.Chemical Cross-Linking Stabilizes Native-Like HIV-1 Envelope Glycoprotein Trimer AntigensRange of CD4-Bound Conformations of HIV-1 gp120, as Defined Using Conditional CD4-Induced Antibodies.Presenting native-like trimeric HIV-1 antigens with self-assembling nanoparticlesInduction of Heterologous Tier 2 HIV-1-Neutralizing and Cross-Reactive V1/V2-Specific Antibodies in Rabbits by Prime-Boost Immunization.Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site.Native-like Env trimers as a platform for HIV-1 vaccine design.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.Changes in Structure and Antigenicity of HIV-1 Env Trimers Resulting from Removal of a Conserved CD4 Binding Site-Proximal Glycan.Approaches to the induction of HIV broadly neutralizing antibodies.Evolution of B cell analysis and Env trimer redesign.Polyvalent vaccine approaches to combat HIV-1 diversityIdentification and specificity of broadly neutralizing antibodies against HIVHow HIV-1 entry mechanism and broadly neutralizing antibodies guide structure-based vaccine design.Targeted N-glycan deletion at the receptor-binding site retains HIV Env NFL trimer integrity and accelerates the elicited antibody response.HIV-1 Cross-reactive Primary Virus Neutralizing Antibody Response Elicited by Immunization in Non-human Primate.Virus-like Particles Identify an HIV V1V2 Apex-Binding Neutralizing Antibody that Lacks a Protruding Loop.A heterologous prime-boosting strategy with replicating Vaccinia virus vectors and plant-produced HIV-1 Gag/dgp41 virus-like particles.Quantification of the Impact of the HIV-1-Glycan Shield on Antibody Elicitation.Global N-Glycan Site Occupancy of HIV-1 gp120 by Metabolic Engineering and High-Resolution Intact Mass Spectrometry.Membrane bound modified form of clade B Env, JRCSF is suitable for immunogen design as it is efficiently cleaved and displays all the broadly neutralizing epitopes including V2 and C2 domain-dependent conformational epitopes.
P2860
Q26746070-3E7F7751-A81C-4E7D-9773-A3053DEAD317Q26765966-807DE137-7E4C-4147-952E-B88130F4FC64Q26775082-DCEEE7AF-3B3F-4DFC-9439-A56BC5834693Q26786540-259C4209-1D22-4B27-ACAC-1FF332DCBD92Q27704710-89FDF713-66F4-4326-80FB-80227A497C66Q27728037-8E33F3BD-4093-45AB-BDB2-E28783A727D4Q30238730-DD6FEF77-C6CD-4F0F-875A-0140C9D6082FQ33612459-F99CFFE1-7E02-4AC4-AFA0-68B7DDE735FFQ33711154-A479C689-2205-4E6B-8D8B-8C66EBB85A16Q33753573-FC772F08-F93B-4D13-BD50-1D9375664718Q33907694-AFE6CF5F-6D46-4000-8A7D-EEC290DE012CQ36086357-A80D6C9E-CF89-42A9-AF54-7A0D5773FE57Q36088254-EFE200FD-91D2-444D-9119-EAD6D05D4299Q36112751-25EBCDFF-0182-4ED1-9AE6-83D3ACB21E33Q36132706-843F7D04-CE1C-4677-B4BC-67A8F744F622Q36194234-3B09D6DC-2434-4ACC-8313-721A572E4E0FQ36239578-23111D64-9A35-420E-9F4B-747129513458Q36263513-38DD5045-41B6-49A6-B467-1ED87A3183DFQ36303368-5B5C1094-97A5-4EA9-A247-7DF325F2B661Q36434196-50B9EF98-BA9E-4576-8348-5213D01B338BQ36811996-6AB3E818-A8A7-4619-BC13-3AF787C2994FQ37060947-09131CF7-9FAB-4729-A3F6-53BEEB4BBF1CQ37252966-BF441021-2696-4F2F-A825-5963FF38AD21Q37409244-05CEEED1-BD1B-48FF-BCB6-AB3B6E7135E4Q37633417-4A483987-E8EB-4DD6-903D-3749D1E053C7Q38665463-B6F04D55-E3D2-4D82-B213-7ADA19A9F773Q38708708-34112418-1FB1-4FB1-8FCD-D7C0E8F72728Q38753943-13CA2235-6C42-401C-AA4B-38984A14F1F4Q38936867-3238DDBB-5108-4C1F-84A7-397A1A05B62DQ38992740-13F750BC-7FBB-4F5F-9D0A-94D149A38840Q39108740-4C643F32-4E33-4055-B457-C73DA1E7AC5EQ39108796-8E86E664-ABA9-46E3-9E49-1575AE4B48D8Q39250593-6C2682A5-444F-4694-A807-6DCDDAD7A30EQ40043429-35498E7E-1B15-485E-B503-434972CB7D34Q40073016-AE3F5A5E-1BD7-4FDB-8577-B9894AE06411Q40198060-49CBBF3D-B48A-4F1C-B26C-07103385E98EQ40220988-6B70AD7A-B52F-4EFE-98C5-3FB49A08A697Q40226810-2F02C580-CB24-445D-BB8D-746F203D2EF2Q40406623-2A4152CA-1EC7-4837-834F-2F3DC3654D0DQ40442031-014FF811-497C-4062-AE16-989821AD7534
P2860
Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site
description
2015 nî lūn-bûn
@nan
2015 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年学术文章
@wuu
2015年学术文章
@zh-cn
2015年学术文章
@zh-hans
2015年学术文章
@zh-my
2015年学术文章
@zh-sg
2015年學術文章
@yue
name
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@ast
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@en
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@nl
type
label
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@ast
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@en
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@nl
prefLabel
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@ast
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@en
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@nl
P2093
P2860
P50
P3181
P1433
P1476
Vaccine-Elicited Tier 2 HIV-1 ...... oximal to the CD4 Binding Site
@en
P2093
Bimal Chakrabarti
Celia LaBranche
Daniel Kulp
Ema T Crooks
Ivelin S Georgiev
James E Robinson
James M Binley
Janelle Muranaka
Joanne Destefano
Keiko Osawa
P2860
P304
P3181
P356
10.1371/JOURNAL.PPAT.1004932
P407
P577
2015-05-01T00:00:00Z