A cryo-electron microscopy study identifies the complete H16.V5 epitope and reveals global conformational changes initiated by binding of the neutralizing antibody fragment
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Self-assembling protein nanoparticles in the design of vaccinesStructural and Computational Biology in the Design of Immunogenic Vaccine AntigensLessons learned from successful human vaccines: Delineating key epitopes by dissecting the capsid proteinsThe C-Terminal Arm of the Human Papillomavirus Major Capsid Protein Is Immunogenic and Involved in Virus-Host InteractionChimeric L2-Based Virus-Like Particle (VLP) Vaccines Targeting Cutaneous Human Papillomaviruses (HPV)The U4 Antibody Epitope on Human Papillomavirus 16 Identified by Cryo-electron MicroscopyA human monoclonal antibody against HPV16 recognizes an immunodominant and neutralizing epitope partially overlapping with that of H16.V5Naturally Occurring Major and Minor Capsid Protein Variants of Human Papillomavirus 45 (HPV45): Differential Recognition by Cross-Neutralizing Antibodies Generated by HPV Vaccines.Furin Cleavage of L2 during Papillomavirus Infection: Minimal Dependence on CyclophilinsNear-Atomic Resolution Structure of a Highly Neutralizing Fab Bound to Canine Parvovirus.The DE and FG loops of the HPV major capsid protein contribute to the epitopes of vaccine-induced cross-neutralising antibodies.Functional assessment and structural basis of antibody binding to human papillomavirus capsid.Human papillomavirus major capsid protein L1 remains associated with the incoming viral genome throughout the entry process.An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-type protein.Modeling the Role of Epitope Arrangement on Antibody Binding Stoichiometry in Flaviviruses.Structural comparison of four different antibodies interacting with human papillomavirus 16 and mechanisms of neutralization.Crystal Structures of Two Immune Complexes Identify Determinants for Viral Infectivity and Type-Specific Neutralization of Human PapillomavirusNaturally Occurring Single Amino Acid Substitution in the L1 Major Capsid Protein of Human Papillomavirus Type 16: Alteration of Susceptibility to Antibody-Mediated Neutralization.High-Resolution Structure Analysis of Antibody V5 and U4 Conformational Epitopes on Human Papillomavirus 16.Antibody Competition Reveals Surface Location of HPV L2 Minor Capsid Protein Residues 17-36.Complex and dynamic interactions between parvovirus capsids, transferrin receptors and antibodies control cell infection and host range.
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P2860
A cryo-electron microscopy study identifies the complete H16.V5 epitope and reveals global conformational changes initiated by binding of the neutralizing antibody fragment
description
2014 nî lūn-bûn
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2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
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2014年论文
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name
A cryo-electron microscopy stu ...... neutralizing antibody fragment
@en
type
label
A cryo-electron microscopy stu ...... neutralizing antibody fragment
@en
prefLabel
A cryo-electron microscopy stu ...... neutralizing antibody fragment
@en
P2093
P2860
P50
P356
P1433
P1476
A cryo-electron microscopy stu ...... neutralizing antibody fragment
@en
P2093
Alexander M Makhov
Hyunwook Lee
Joshua D Yoder
Neil D Christensen
Robert E Ashley
Sarah A Brendle
P2860
P304
P356
10.1128/JVI.02898-14
P407
P577
2014-11-12T00:00:00Z