Anti-HIV B Cell lines as candidate vaccine biosensors. - Wikidata - wikimedia - TriplyDB

Anti-HIV B Cell lines as candidate vaccine biosensors.

Anti-HIV B Cell lines as candidate vaccine biosensors.

http://www.wikidata.org/entity/Q36766704

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Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody Rational HIV Immunogen Design to Target Specific Germline B Cell Receptors Humanized Immunoglobulin Mice: Models for HIV Vaccine Testing and Studying the Broadly Neutralizing Antibody Problem.Multi-Parameter Exploration of HIV-1 Virus-Like Particles as Neutralizing Antibody Immunogens in Guinea Pigs, Rabbits and Macaques Autoreactivity in HIV-1 broadly neutralizing antibodies: implications for their function and induction by vaccination.Elicitation of HIV-1-neutralizing antibodies against the CD4-binding site.HIV antibodies. Antigen modification regulates competition of broad and narrow neutralizing HIV antibodies.Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelope HIV-1 envelope gp41 broadly neutralizing antibodies: hurdles for vaccine development.Immunogenic Display of Purified Chemically Cross-Linked HIV-1 Spikes.Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction.Mouse marginal zone B cells harbor specificities similar to human broadly neutralizing HIV antibodies.2G12-expressing B cell lines may aid in HIV carbohydrate vaccine design strategies.Structural basis for germline antibody recognition of HIV-1 immunogens.Engineering HIV envelope protein to activate germline B cell receptors of broadly neutralizing anti-CD4 binding site antibodies Common tolerance mechanisms, but distinct cross-reactivities associated with gp41 and lipids, limit production of HIV-1 broad neutralizing antibodies 2F5 and 4E10 Presenting native-like trimeric HIV-1 antigens with self-assembling nanoparticles Immune tolerance negatively regulates B cells in knock-in mice expressing broadly neutralizing HIV antibody 4E10 B cells from knock-in mice expressing broadly neutralizing HIV antibody b12 carry an innocuous B cell receptor responsive to HIV vaccine candidates HIV Vaccine Design to Target Germline Precursors of Glycan-Dependent Broadly Neutralizing Antibodies.Native-like Env trimers as a platform for HIV-1 vaccine design.Diverse recombinant HIV-1 Envs fail to activate B cells expressing the germline B cell receptors of the broadly neutralizing anti-HIV-1 antibodies PG9 and 447-52D.Antibody-based candidate therapeutics against HIV-1: implications for virus eradication and vaccine design.Covalent Linkage of HIV-1 Trimers to Synthetic Liposomes Elicits Improved B Cell and Antibody Responses.In vitro reconstitution of B cell receptor-antigen interactions to evaluate potential vaccine candidates.Dense Array of Spikes on HIV-1 Virion Particles.Immunological tolerance as a barrier to protective HIV humoral immunity.Glycosylation profiling to evaluate glycoprotein immunogens against HIV-1.Nanoparticles decorated with viral antigens are more immunogenic at low surface density.Priming HIV-1 broadly neutralizing antibody precursors in human Ig loci transgenic mice Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design.Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo.Targeting B-cell germlines and focusing affinity maturation: the next hurdles in HIV-1-vaccine development?Topological analysis of HIV-1 glycoproteins expressed in situ on virus surfaces reveals tighter packing but greater conformational flexibility than for soluble gp120.Increased surface expression of HIV-1 envelope is associated with improved antibody response in vaccinia prime/protein boost immunization.Integrity of Glycosylation Processing of a Glycan-Depleted Trimeric HIV-1 Immunogen Targeting Key B-Cell Lineages.Co-delivery of a CD4 T cell helper epitope via covalent liposome attachment with a surface-arrayed B cell target antigen fosters higher affinity antibody responses

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Anti-HIV B Cell lines as candidate vaccine biosensors.

http://www.wikidata.org/entity/Q36766704

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2012 nî lūn-bûn

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Anti-HIV B Cell lines as candidate vaccine biosensors.

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Anti-HIV B Cell lines as candidate vaccine biosensors.

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Anti-HIV B Cell lines as candidate vaccine biosensors.

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Anti-HIV B Cell lines as candidate vaccine biosensors.

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JIMMUNOL.1202165

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Journal of Immunology

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Anti-HIV B Cell lines as candidate vaccine biosensors.

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Anthony B Cooper

http://www.w3.org/2001/XMLSchema#string

Bimal K Chakrabarti

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Colleen Doyle-Cooper

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David Nemazee

http://www.w3.org/2001/XMLSchema#string

Dennis R Burton

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Devin Sok

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Emilia Falkowska

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James M Binley

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Jeffrey Lifson

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Joseph Jardine

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P2860

Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design

Antibody domain exchange is an immunological solution to carbohydrate cluster recognition

Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9

Structure and function of broadly reactive antibody PG16 reveal an H3 subdomain that mediates potent neutralization of HIV-1

Crystal Structure of PG16 and Chimeric Dissection with Somatically Related PG9: Structure-Function Analysis of Two Quaternary-Specific Antibodies That Effectively Neutralize HIV-1

Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01

Sequence and Structural Convergence of Broad and Potent HIV Antibodies That Mimic CD4 Binding

Focused Evolution of HIV-1 Neutralizing Antibodies Revealed by Structures and Deep Sequencing

Computation-guided backbone grafting of a discontinuous motif onto a protein scaffold

Broadly neutralizing anti-HIV antibody 4E10 recognizes a helical conformation of a highly conserved fusion-associated motif in gp41

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10.4049/JIMMUNOL.1202165

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10

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189

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Pascal Poignard

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2012-10-12T00:00:00Z

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232248346

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23066156

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