Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins.
about
Antibody vs. HIV in a clash of evolutionary titansHyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine designAiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidatesRole of a Putative gp41 Dimerization Domain in Human Immunodeficiency Virus Type 1 Membrane FusionHuman immunodeficiency virus type 1 env clones from acute and early subtype B infections for standardized assessments of vaccine-elicited neutralizing antibodiesAromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions.Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining regionMulti-Parameter Exploration of HIV-1 Virus-Like Particles as Neutralizing Antibody Immunogens in Guinea Pigs, Rabbits and MacaquesIn-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type 1Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.Comparing antigenicity and immunogenicity of engineered gp120.Induction of neutralizing antibodies against human immunodeficiency virus type 1 primary isolates by Gag-Env pseudovirion immunization.Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope.Structure-guided alterations of the gp41-directed HIV-1 broadly neutralizing antibody 2F5 reveal new properties regarding its neutralizing function.Effect of epitope position on neutralization by anti-human immunodeficiency virus monoclonal antibody 2F5The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes.Receptor binding domain based HIV vaccines.HIV type 1 Env precursor cleavage state affects recognition by both neutralizing and nonneutralizing gp41 antibodies.Binding of anti-membrane-proximal gp41 monoclonal antibodies to CD4-liganded and -unliganded human immunodeficiency virus type 1 and simian immunodeficiency virus virionsHIV-1 replication and pathogenesis in the human thymus.Immunogenic Display of Purified Chemically Cross-Linked HIV-1 Spikes.Neutralizing epitopes in the membrane-proximal external region of HIV-1 gp41 are influenced by the transmembrane domain and the plasma membrane.A call for replicating vector prime-protein boost strategies in HIV vaccine design.Antibodies generated in cats by a lipopeptide reproducing the membrane-proximal external region of the feline immunodeficiency virus transmembrane enhance virus infectivity.A comparative immunogenicity study of HIV-1 virus-like particles bearing various forms of envelope proteins, particles bearing no envelope and soluble monomeric gp120.Human immunodeficiency virus type 1 gp41 antibodies that mask membrane proximal region epitopes: antibody binding kinetics, induction, and potential for regulation in acute infectionThe membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine designSuppressor of cytokine signaling 1 inhibition strategy to enhance anti-HIV vaccination.Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates.Inhibition of HIV-1 entry by antibodies: potential viral and cellular targetsRelationship of HIV-1 and SIV envelope glycoprotein trimer occupation and neutralizationHigh-Density Array of Well-Ordered HIV-1 Spikes on Synthetic Liposomal Nanoparticles Efficiently Activate B Cells.Immunogenicity of recombinant human immunodeficiency virus type 1-like particles expressing gp41 derivatives in a pre-fusion stateAnalysis of the human immunodeficiency virus type 1 gp41 membrane proximal external region arrayed on hepatitis B surface antigen particlesRobust neutralizing antibodies elicited by HIV-1 JRFL envelope glycoprotein trimers in nonhuman primates.Characterization of the outer domain of the gp120 glycoprotein from human immunodeficiency virus type 1Surface plasmon resonance for vaccine design and efficacy studies: recent applications and future trends.Conformational HIV-1 envelope on particulate structures: a tool for chemokine coreceptor binding studies.Multimerized HIV-gp41-derived peptides as fusion inhibitors and vaccines.Evolution of B cell analysis and Env trimer redesign.
P2860
Q24536059-948C7B9A-73B5-42BF-9324-2855F4CD62C3Q24679395-59C5DEBA-474C-494D-A997-21E1A9687701Q27489000-4D712296-37DB-4E68-AF3E-832BB280CC78Q27657871-F0C775EA-2E72-47C5-834B-CF19D1BE7888Q29619015-D4748C1B-A4E3-46C9-88E6-123D6A026FCBQ33667654-99CA9660-E45D-4104-8B8C-A6DB3CF09F85Q33676600-83ADFEEA-512E-45ED-8F9F-59B0807D0D38Q33683203-21E6D25F-1448-41FB-A635-9825473252F1Q33725718-3FCDBB60-403D-4480-B388-566673C3DE4FQ33967039-BB3A4517-0C8A-41BD-AE88-81D4D8BA007BQ33984309-64F81C16-5352-4A0C-AF6C-12F9B721C20DQ34142795-4DE03385-8022-41B6-95BA-BAE7508C65DAQ34348303-D709F2DA-9D82-437D-85F7-B90A349BE27DQ34350894-BE8B3661-47EA-428F-8CB3-F43B14964685Q34434753-FD02936D-AAA6-4517-B6FE-2C9D63702F57Q34610233-E1AC9372-C668-4988-89A7-8B7DC11832BEQ35033862-0614BC14-9DC8-4A93-A78B-4CA0698F8479Q35173635-F8429B57-C3B5-4300-A43C-A268A4E5E48BQ35689608-E41E341D-DBB7-496F-8F2E-EC9E28F7953DQ35716711-F3F1A548-5150-4C38-BCEC-1040E7C57565Q35745442-2BA76E8E-A79C-45B2-9FBB-733ACD4105A9Q35826306-46C530B8-1688-4201-BEB4-7E1E97BD5DFBQ35851801-56360FAB-603B-46D4-B16F-1AB906056F09Q36097111-C715BFCD-B83B-4AEE-A700-B7FC0BFDDCEEQ36149102-57003666-CAC3-4008-84DC-8E8B145B8133Q36423897-DC60250A-C3C0-4CB7-8005-D3CE9475309DQ36497712-15475684-2E60-4366-A923-29E4AF7C0334Q36600347-8D49376D-6ACD-4480-A7B8-15714919D610Q36600380-272BFB66-6BA7-4C6B-A197-C7D28B8FC914Q36631937-DDE59740-BFEF-4E2A-9906-314F285921CAQ36837815-BE360DDD-0E2E-474D-8AA2-7186F6468D1AQ36957800-49144A5E-B2E1-41F3-BA88-F1F11D967398Q37250899-64821A1E-DF8A-4AAC-8B51-C94321376F28Q37251390-8A82C6CC-12AF-44C6-A7A7-15907FB6EE2AQ37336704-7C99E5F0-A636-45F3-A911-A2BBD51E639BQ37596552-F106C6C8-93D7-47E4-AAA7-4528ECEC476DQ37762275-E3E149B4-D2B6-4B77-91E8-BEB3B3E42892Q37834097-8377D822-A71C-43B3-8F5B-519CC621D33CQ38638340-5074D08D-7C65-4AE6-A2F0-77AED0356647Q38992740-F803A00C-E8B9-4CBD-965F-D2543DCE9E3D
P2860
Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@ast
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@en
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@nl
type
label
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@ast
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@en
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@nl
prefLabel
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@ast
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@en
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@nl
P2093
P2860
P1433
P1476
Solid-phase proteoliposomes co ...... virus envelope glycoproteins.
@en
P2093
Christoph Grundner
Richard Wyatt
Tajib Mirzabekov
P2860
P304
P356
10.1128/JVI.76.7.3511-3521.2002
P407
P577
2002-04-01T00:00:00Z