about
Structural Definition of an Antibody-Dependent Cellular Cytotoxicity Response Implicated in Reduced Risk for HIV-1 InfectionCrystal Structure of PG16 and Chimeric Dissection with Somatically Related PG9: Structure-Function Analysis of Two Quaternary-Specific Antibodies That Effectively Neutralize HIV-1Structure of a Major Antigenic Site on the Respiratory Syncytial Virus Fusion Glycoprotein in Complex with Neutralizing Antibody 101FStructure of Respiratory Syncytial Virus Fusion Glycoprotein in the Postfusion Conformation Reveals Preservation of Neutralizing EpitopesStructure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial VirusStructural and molecular basis for Ebola virus neutralization by protective human antibodiesIncreased HIV-1 vaccine efficacy against viruses with genetic signatures in Env V2Structure and function of respiratory syncytial virus surface glycoproteins.A highly stable prefusion RSV F vaccine derived from structural analysis of the fusion mechanismCharacterization of a Prefusion-Specific Antibody That Recognizes a Quaternary, Cleavage-Dependent Epitope on the RSV Fusion GlycoproteinEnhanced Neutralizing Antibody Response Induced by Respiratory Syncytial Virus Prefusion F Protein Expressed by a Vaccine Candidate.Engineering, Structure and Immunogenicity of the Human Metapneumovirus F Protein in the Postfusion Conformation.Molecular mechanism of respiratory syncytial virus fusion inhibitors.Synthetic glycopeptides reveal the glycan specificity of HIV-neutralizing antibodies.Packaging and Prefusion Stabilization Separately and Additively Increase the Quantity and Quality of Respiratory Syncytial Virus (RSV)-Neutralizing Antibodies Induced by an RSV Fusion Protein Expressed by a Parainfluenza Virus Vector.Structural, antigenic and immunogenic features of respiratory syncytial virus glycoproteins relevant for vaccine development.Rapid profiling of RSV antibody repertoires from the memory B cells of naturally infected adult donorsPotent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state.Neutralization of Diverse Human Cytomegalovirus Strains Conferred by Antibodies Targeting Viral gH/gL/pUL128-131 Pentameric Complex.Neutralizing epitopes on the respiratory syncytial virus fusion glycoprotein.Therapeutic efficacy of a respiratory syncytial virus fusion inhibitorImmunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.Improved Prefusion Stability, Optimized Codon Usage, and Augmented Virion Packaging Enhance the Immunogenicity of Respiratory Syncytial Virus Fusion Protein in a Vectored-Vaccine Candidate.A highly potent extended half-life antibody as a potential RSV vaccine surrogate for all infants.RSV N-nanorings fused to palivizumab-targeted neutralizing epitope as a nanoparticle RSV vaccine.Crystal Structures of Two Immune Complexes Identify Determinants for Viral Infectivity and Type-Specific Neutralization of Human PapillomavirusStructural basis of respiratory syncytial virus subtype-dependent neutralization by an antibody targeting the fusion glycoprotein.Structure and immunogenicity of pre-fusion-stabilized human metapneumovirus F glycoprotein.Chimeric Pneumoviridae fusion proteins as immunogens to induce cross-neutralizing antibody responses.Clinical Potential of Prefusion RSV F-specific Antibodies.Infants Infected with Respiratory Syncytial Virus Generate Potent Neutralizing Antibodies that Lack Somatic Hypermutation.Structural basis for recognition of the central conserved region of RSV G by neutralizing human antibodies.Global site-specific analysis of glycoprotein N-glycan processing.Five Residues in the Apical Loop of the Respiratory Syncytial Virus Fusion Protein F2 Subunit are Critical for its Fusion Activity.Iterative screen optimization maximizes the efficiency of macromolecular crystallizationTransient opening of trimeric prefusion RSV F proteinsStructural Basis for Potent Neutralization of Betacoronaviruses by Single-domain Camelid AntibodiesCryo-EM structure of the 2019-nCoV spike in the prefusion conformationHCMV glycoprotein B nucleoside-modified mRNA vaccine elicits antibody responses with greater durability and breadth than MF59-adjuvanted gB protein immunizationThe 3.1-Angstrom Cryo-electron Microscopy Structure of the Porcine Epidemic Diarrhea Virus Spike Protein in the Prefusion Conformation
P50
Q27640572-4A25F2B1-F743-4C70-AF84-90B1085F709CQ27662167-C076A803-A550-457D-B34E-EA42BB5F4CE1Q27664797-30DC17C8-5A97-4CC3-A775-AD6DEE88F899Q27668015-129A45E5-C4DC-47E9-B63D-4C64CBD0BC27Q27680499-2D35907F-482A-4FFC-8E67-792DC27FC096Q27704188-D3F72386-C1B7-4DA3-8BBA-2C6D6E0FAC14Q34298408-BF557F17-8F39-43DA-AA89-461C71DCA11FQ34414405-BA3414A2-6938-4A85-8A97-8181BA1EE2D0Q34492100-52D7B4DF-4BD6-48FA-A277-CE22F93D3765Q35687662-0A6ED443-DA1B-41F2-B9F7-2366E80C08B6Q35973617-74DC7CB3-4B22-4B75-8EA6-790C84C88DB3Q36128048-40C3360D-01BE-42EF-90B5-56C49F8BF68FQ36517337-4D281CD7-9183-4584-A931-3E0C471659D6Q37063013-A2F2D87F-1046-4F24-A01B-8EA8AA07F2E1Q37347267-8ED543C3-56E3-4D43-82EA-0BF4F07D011DQ37536191-E4143E9A-6983-4471-81D2-434B5F093F2BQ37593886-BA46AEE4-6848-4A5B-801B-0191B98CFC08Q37651813-18676FC5-291A-45A4-B3AA-2D10572218B3Q37707461-98E90598-4834-4374-ACDA-F46931CFBB87Q38394731-F67F052E-E2CF-46B5-998B-60BFCCFBDDC0Q38650711-BC7883F6-081D-4E94-93A2-79FBB885E7F3Q40083207-6B3698D2-2EB9-4DD0-8479-EDF38C75EC2BQ40187606-93973094-00F9-4E66-AD52-90B2F1858DF1Q40216493-76E2A294-3FCE-4355-8CAD-86108A393DDEQ40565908-25D93CB7-C758-409A-92C2-B2155FDF1AA2Q41676237-4BBD6C8F-ECD6-4478-AEB2-40696479A5CBQ45324052-30C6B000-2D01-4459-B668-A91FE542FD20Q47115678-A3965553-102C-4FA1-991F-6815A019A166Q47317758-10E98BB3-0BF6-4846-9B29-DA55A06C0C70Q47605570-1AEC08E5-430A-43D5-BC3E-1902142C13B4Q49361412-50AE4895-4B20-42EA-B71F-46ECBDDB061BQ52365721-A27B861F-CE7D-4C17-AA39-9AF2485B19F0Q53068939-B0C0EAAD-EA9E-40A0-8C7C-111CD7CDDCD1Q54216743-E9297B16-84AC-4A74-97C6-5A3F0249D2FBQ61809970-5CCF143B-C81C-4ECC-A35E-985FC9F0B8E0Q64062464-5193CFA1-D31C-43E8-A1AE-B86CE6CDDE3BQ88979272-AE8ED1C1-5C33-4E31-8FDB-D004A40CC9F4Q89108866-6CF9FDB4-31AB-4B50-B018-1CCE2A24536DQ89685617-E609FD99-3500-4B41-A5A5-3D791619CBA9Q90167797-AAB58883-9515-445F-BB2E-876D8EC22C03
P50
description
investigador
@es
researcher
@en
name
Jason S McLellan
@en
type
label
Jason S McLellan
@en
prefLabel
Jason S McLellan
@en
P21
P31
P496
0000-0003-3991-542X