Analysis of modified human papillomavirus type 16 L1 capsomeres: the ability to assemble into larger particles correlates with higher immunogenicity. - Wikidata - awgldk - TriplyDB

Analysis of modified human papillomavirus type 16 L1 capsomeres: the ability to assemble into larger particles correlates with higher immunogenicity.

Analysis of modified human papillomavirus type 16 L1 capsomeres: the ability to assemble into larger particles correlates with higher immunogenicity.

http://www.wikidata.org/entity/Q43096878

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Structural Basis of Oligosaccharide Receptor Recognition by Human Papillomavirus Capsomer vaccines protect mice from vaginal challenge with human papillomavirus Expression of HPV-16 L1 capsomeres with glutathione-S-transferase as a fusion protein in tobacco plastids: an approach for a capsomere-based HPV vaccine.Vaccination with multimeric L2 fusion protein and L1 VLP or capsomeres to broaden protection against HPV infection.Multivalent human papillomavirus l1 DNA vaccination utilizing electroporation.Immunoprevention of human papillomavirus-associated malignancies Non-carrier nanoparticles adjuvant modular protein vaccine in a particle-dependent manner.Multiscale simulation of microbe structure and dynamics.Plastid genetic engineering in Solanaceae A Cell-Free Assembly System for Generating Infectious Human Papillomavirus 16 Capsids Implicates a Size Discrimination Mechanism for Preferential Viral Genome Packaging Influence of oxidation and multimerization on the immunogenicity of a thioredoxin-l2 prophylactic papillomavirus vaccine Chloroplast-derived vaccines against human diseases: achievements, challenges and scopes.Bioengineering virus-like particles as vaccines.HPV vaccines: Global perspectives.Crystal Structures of Two Immune Complexes Identify Determinants for Viral Infectivity and Type-Specific Neutralization of Human Papillomavirus Immunogenic assessment of plant-produced human papillomavirus type 16 L1/L2 chimaeras.Development of human papillomavirus chimaeric L1/L2 candidate vaccines.Explanations for the high potency of HPV prophylactic vaccines.Transplastomic expression of a modified human papillomavirus L1 protein leading to the assembly of capsomeres in tobacco: a step towards cost-effective second-generation vaccines.Emerging human papillomavirus vaccines Plastid expression of a double-pentameric vaccine candidate containing human papillomavirus-16 L1 antigen fused with LTB as adjuvant: transplastomic plants show pleiotropic phenotypes N-terminal truncations on L1 proteins of human papillomaviruses promote their soluble expression in Escherichia coli and self-assembly in vitro

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P2860

Analysis of modified human papillomavirus type 16 L1 capsomeres: the ability to assemble into larger particles correlates with higher immunogenicity.

http://www.wikidata.org/entity/Q43096878

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

@zh-cn

2009年学术文章

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2009年学术文章

@zh-my

2009年学术文章

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2009年學術文章

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2009年學術文章

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name

Analysis of modified human pap ...... es with higher immunogenicity.

@en

Analysis of modified human pap ...... es with higher immunogenicity.

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type

label

Analysis of modified human pap ...... es with higher immunogenicity.

@en

Analysis of modified human pap ...... es with higher immunogenicity.

@nl

prefLabel

Analysis of modified human pap ...... es with higher immunogenicity.

@en

Analysis of modified human pap ...... es with higher immunogenicity.

@nl

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Journal of Virology

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Analysis of modified human pap ...... es with higher immunogenicity.

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P2093

Britta Gerlach

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Corinna Klein

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Ignacio G Bravo

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Lutz Gissmann

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Lysann Schädlich

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Martin Müller

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Norbert Mücke

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Tilo Senger

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P2860

Antigen presentation and T cell stimulation by dendritic cells

Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16

Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product

Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction.

Mutational analysis of human papillomavirus type 16 major capsid protein L1: the cysteines affecting the intermolecular bonding and structure of L1-capsids.

Papillomavirus capsid protein expression in Escherichia coli: purification and assembly of HPV11 and HPV16 L1.

Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly.

Human papillomavirus type 11 recombinant L1 capsomeres induce virus-neutralizing antibodies.

Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines.

Characterization of a major neutralizing epitope on human papillomavirus type 16 L1

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7690-7705

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scholarly article

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10.1128/JVI.02588-08

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15

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83

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2009-05-20T00:00:00Z

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24442208

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19457985

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