Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
about
Shake, rattle, and roll: Impact of the dynamics of flavivirus particles on their interactions with the hostHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchDynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane FusionConformational Masking and Receptor-Dependent Unmasking of Highly Conserved Env Epitopes Recognized by Non-Neutralizing Antibodies That Mediate Potent ADCC against HIV-1Structure and Dynamics of the Native HIV-1 Env TrimerCrystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 EnvStructures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine designDeconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and ImmunityStructure-Based Reverse Vaccinology Failed in the Case of HIV Because it Disregarded Accepted Immunological TheoryFusion of Enveloped Viruses in Endosomes.HIV-1 gp120 as a therapeutic target: navigating a moving labyrinthAntibody potency relates to the ability to recognize the closed, pre-fusion form of HIV EnvImmunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing EpitopesHow to Distinguish Conformational Selection and Induced Fit Based on Chemical Relaxation RatesHIV-1 VACCINES. HIV-1 neutralizing antibodies induced by native-like envelope trimersWhat Are the Most Powerful Immunogen Design Vaccine Strategies?A single mutation in the envelope protein modulates flavivirus antigenicity, stability, and pathogenesisSurvivors Remorse: antibody-mediated protection against HIV-1.Stabilized HIV-1 envelope glycoprotein trimers for vaccine use.SERINC5 protein inhibits HIV-1 fusion pore formation by promoting functional inactivation of envelope glycoproteins.Exposing HIV's weaknessesAntigenicity-defined conformations of an extremely neutralization-resistant HIV-1 envelope spike.Flow virometry analysis of envelope glycoprotein conformations on individual HIV virions.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.Reducing V3 Antigenicity and Immunogenicity on Soluble, Native-Like HIV-1 Env SOSIP TrimersStructure/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.Recent advances in human viruses imaging studies.Fusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.Different infectivity of HIV-1 strains is linked to number of envelope trimers required for entryA 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.Intra-spike crosslinking overcomes antibody evasion by HIV-1Kinetically coupled folding of a single HIV-1 glycoprotein 41 complex in viral membrane fusion and inhibition.Rationally Targeted Mutations at the V1V2 Domain of the HIV-1 Envelope to Augment Virus Neutralization by Anti-V1V2 Monoclonal Antibodies.Peptide Triazole Inactivators of HIV-1 Utilize a Conserved Two-Cavity Binding Site at the Junction of the Inner and Outer Domains of Env gp120.Coevolution Analysis of HIV-1 Envelope Glycoprotein Complex.Arenavirus Glycan Shield Promotes Neutralizing Antibody Evasion and Protracted Infection.Strain-Specific V3 and CD4 Binding Site Autologous HIV-1 Neutralizing Antibodies Select Neutralization-Resistant Viruses.
P2860
Q23925011-DF38DC40-DF43-408B-BC6A-99CF0965428FQ26746070-4D3B4FAE-97AB-4ACD-BB40-C765D2964BD7Q26772129-8B1E1231-0C89-492C-B85C-99A4C7A1CC92Q26782237-48C29CB7-A7D0-41ED-AF15-74208BEA5448Q27027570-31A05374-2522-4DCA-A2CD-BFC3A84BE09EQ27644383-A8AF105A-85BD-4A7D-A6FF-DCADB8DA7209Q27644634-E21BF81E-D421-45CA-98BE-2C805C6701B3Q27654848-102B975F-1741-457C-982B-112AA384E204Q28071559-899344E7-6BC3-41D6-A0A8-6A892A437C31Q28073406-5CDC51C3-5896-41D0-B3FF-B52D0297D746Q28086826-AFBFC8D2-83B4-44DE-9E2C-DDCA8D1B9E59Q28256508-2FCCB762-52B9-4068-B0C6-313934F4A154Q28271300-7089181A-EB71-40A6-85F4-CC362AADCD2EQ28554216-A1D19AC1-FF54-4893-A159-80B8BA9B540EQ28647225-36F4C84F-005B-412F-9A2F-D06EE1BF82B4Q28729792-148631F6-42D9-4D3C-9BA1-5867AED286BDQ28804076-25367BCA-EC46-4A3A-8AD5-C75739A759F7Q30238730-B8D76A62-235F-42A8-88A6-E8944334B0DDQ30490942-19B8B8BB-8437-48BF-A759-95A37D87C48BQ33567639-F6812104-2914-487B-8651-0CEB53A77668Q33567645-0C492451-85F7-4A21-9FFB-1CC2E9295716Q33620194-C7A26BF6-9656-454C-9361-CEB0353666E3Q33680883-4DBA6376-D6C5-4E84-89C6-8C53B58C774CQ33753573-021ADBE0-95CD-4DEC-8451-F82B37ADBC0EQ33821896-559C86C1-19E4-408E-B5FB-7C49E02B0198Q33907694-677B4654-0BFB-4C3B-B39C-685056D5451DQ34499013-0FD2F4B5-02A1-48CB-AF57-147A25F52683Q34517381-58E136FD-AFD1-4DB0-80B5-D194329D0706Q34521364-83653AA0-699B-4290-945B-EC7B82DC235BQ34526404-1EEA8DF8-FABE-4C7F-9B9A-BC66003B493AQ34875765-B5F57C0E-E36A-408C-BA2D-97AE05AC2FE9Q35110976-40CEA694-A056-4712-A953-CE7ED96B950DQ35217426-3763B87D-A261-46DE-89B0-399F38B6354AQ35462906-3069ECC7-1331-41A5-A53B-14AE3530EEF9Q35699218-31075346-948B-4B8E-BCA1-39E4942D96F3Q35817106-277C51C2-2FCC-4DD3-8B06-02E18306B20AQ35835515-8683F73E-1442-43AD-A895-17F38C8A2574Q35844799-C99671E0-D50A-45F9-9C29-78DE7952B7A4Q35847032-0A9C81D5-91B1-4D9C-A92F-E220CDE9E8CFQ36053810-FDD1F28C-CF56-4A14-966B-AA395E2985DD
P2860
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
name
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
@ast
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
@en
type
label
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
@ast
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
@en
prefLabel
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
@ast
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
@en
P2093
P2860
P50
P356
P1433
P1476
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
@en
P2093
Amos B Smith
Dennis R Burton
James Arthos
James B Munro
Joel R Courter
Peter D Kwong
Wayne C Koff
Xiaochu Ma
P2860
P304
P356
10.1126/SCIENCE.1254426
P407
P577
2014-10-08T00:00:00Z