An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability.
about
Stabilized HIV-1 envelope glycoprotein trimers for vaccine use.Progress toward active or passive HIV-1 vaccination.Native-like Env trimers as a platform for HIV-1 vaccine design.Driving HIV-1 into a Vulnerable Corner by Taking Advantage of Viral Adaptation and Evolution.Identification and specificity of broadly neutralizing antibodies against HIVHow HIV-1 entry mechanism and broadly neutralizing antibodies guide structure-based vaccine design.Immunization-Elicited Broadly Protective Antibody Reveals Ebolavirus Fusion Loop as a Site of Vulnerability.Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.HIV-1-neutralizing antibody induced by simian adenovirus- and poxvirus MVA-vectored BG505 native-like envelope trimers.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.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.Fine epitope signature of antibody neutralization breadth at the HIV-1 envelope CD4-binding site.Glycoengineering HIV-1 Env creates 'supercharged' and 'hybrid' glycans to increase neutralizing antibody potency, breadth and saturation.Molecular basis of unusually high neutralization resistance in tier 3 HIV-1 strain 253-11.Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer.HIV-1 cell-to-cell transmission and broadly neutralizing antibodiesStructural basis for broad neutralization of ebolaviruses by an antibody targeting the glycoprotein fusion loopComplete functional mapping of infection- and vaccine-elicited antibodies against the fusion peptide of HIVDevelopment of broadly neutralizing antibodies in HIV-1 infected elite neutralizers
P2860
Q30490942-F69ED945-D22B-4812-8618-F57AC8E38154Q37549777-8846B336-80A1-4365-8739-C039905F4466Q37633417-3B4761B9-70E7-40CB-AF67-CD030C3BC974Q37703084-F4929B66-E277-452E-9B97-9747567BA4D5Q39108796-81B2E150-8F09-41A8-B136-2A3C03CE3586Q39250593-ED3030D0-EC97-43B6-9C74-9C288C755332Q40056179-5C962949-4891-4FC3-A446-13B3606C8C48Q40058876-5A805A03-C2E3-4C66-B009-7D9DAA2A85FEQ40089181-62E8F061-1A30-41AE-8EE5-1A87F7E12DDDQ40173474-9976F583-3C1A-415A-9B1B-D8B6139CFAD2Q40198060-A18FB1BE-4057-4BB5-8B68-AF0ED298C337Q47551930-49372CC1-BD71-48D0-9249-8232EEA307EBQ50420466-032F7D45-129D-406E-85B8-2A85C0522536Q53689028-424C73B3-A33F-4786-9F22-98558213C11BQ53695792-BFF0E521-6EEF-470F-90FC-DBB416C5130AQ54209542-781FAD12-8FC7-4222-8D5A-16195ED00259Q57030223-8F449E67-B2C9-40F5-9BD4-791169D32610Q57091851-3CAC4BAF-9B2E-4D31-97D3-98EB6686F479Q57177123-4007BC58-5CB6-424E-A710-BC487804B497Q58763247-5F3A2943-330B-4DE0-A9D5-09772B31B720
P2860
An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年学术文章
@wuu
2016年学术文章
@zh-cn
2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
@yue
2016年學術文章
@zh
2016年學術文章
@zh-hant
name
An HIV-1 antibody from an elit ...... de as a site of vulnerability.
@en
An HIV-1 antibody from an elit ...... de as a site of vulnerability.
@nl
type
label
An HIV-1 antibody from an elit ...... de as a site of vulnerability.
@en
An HIV-1 antibody from an elit ...... de as a site of vulnerability.
@nl
prefLabel
An HIV-1 antibody from an elit ...... de as a site of vulnerability.
@en
An HIV-1 antibody from an elit ...... de as a site of vulnerability.
@nl
P2093
P2860
P50
P1433
P1476
An HIV-1 antibody from an elit ...... de as a site of vulnerability.
@en
P2093
Andrew B Ward
Anila Yasmeen
Anna Schorcht
Chi-Hui Liang
Dennis R Burton
Gabriel Ozorowski
Hanneke Schuitemaker
Inez Johanna
John P Moore
P2860
P2888
P356
10.1038/NMICROBIOL.2016.199
P50
P577
2016-11-14T00:00:00Z