Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region - Wikidata - thesis-toulmin - TriplyDB

Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region

Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region

http://www.wikidata.org/entity/Q33676600

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Advances in structure-based vaccine design Structural insights on the role of antibodies in HIV-1 vaccine and therapy HIV-1 neutralizing antibodies: understanding nature's pathways Optimization of the Solubility of HIV-1-Neutralizing Antibody 10E8 through Somatic Variation and Structure-Based Design Structural Characterization of HIV gp41 with the Membrane-proximal External Region Crystal Structure of PG16 and Chimeric Dissection with Somatically Related PG9: Structure-Function Analysis of Two Quaternary-Specific Antibodies That Effectively Neutralize HIV-1 Elicitation of structure-specific antibodies by epitope scaffolds Crystal structure of a non-neutralizing antibody to the HIV-1 gp41 membrane-proximal external region Structure-Based Design of a Protein Immunogen that Displays an HIV-1 gp41 Neutralizing Epitope A gp41 MPER-specific Llama VHH Requires a Hydrophobic CDR3 for Neutralization but not for Antigen Recognition Structural Basis for HIV-1 Neutralization by 2F5-Like Antibodies m66 and m66.6 Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer Recognition of membrane-bound fusion-peptide/MPER complexes by the HIV-1 neutralizing 2F5 antibody: implications for anti-2F5 immunogenicity Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies Recent advances on the use of structural biology for the design of novel envelope immunogens of HIV-1 Generation of Long-Lived Bone Marrow Plasma Cells Secreting Antibodies Specific for the HIV-1 gp41 Membrane-Proximal External Region in the Absence of Polyreactivity.Estimating the probability of polyreactive antibodies 4E10 and 2F5 disabling a gp41 trimer after T cell-HIV adhesion.In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type 1 HIV-1 gp41 core with exposed membrane-proximal external region inducing broad HIV-1 neutralizing antibodies Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies.Autoreactivity in HIV-1 broadly neutralizing antibodies: implications for their function and induction by vaccination.Chemically modified peptides based on the membrane-proximal external region of the HIV-1 envelope induce high-titer, epitope-specific nonneutralizing antibodies in rabbits Scaffolding to build a rational vaccine design strategy.Evaluation of the potency of the anti-idiotypic antibody Ab2/3H6 mimicking gp41 as an HIV-1 vaccine in a rabbit prime/boost study Identification of autoantigens recognized by the 2F5 and 4E10 broadly neutralizing HIV-1 antibodies Structure-guided alterations of the gp41-directed HIV-1 broadly neutralizing antibody 2F5 reveal new properties regarding its neutralizing function.A fusion intermediate gp41 immunogen elicits neutralizing antibodies to HIV-1 Designer antigens for elicitation of broadly neutralizing antibodies against HIV.Dramatic potentiation of the antiviral activity of HIV antibodies by cholesterol conjugation.Synergy in monoclonal antibody neutralization of HIV-1 pseudoviruses and infectious molecular clones.Chimeric rhinoviruses displaying MPER epitopes elicit anti-HIV neutralizing responses.HN125: A Novel Immunoadhesin Targeting MUC16 with Potential for Cancer Therapy Is developing an HIV-1 vaccine possible?Role of immune mechanisms in induction of HIV-1 broadly neutralizing antibodies.Co-expression of foreign proteins tethered to HIV-1 envelope glycoprotein on the cell surface by introducing an intervening second membrane-spanning domain.Rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1.Computational design of protein antigens that interact with the CDR H3 loop of HIV broadly neutralizing antibody 2F5.Antibody mechanics on a membrane-bound HIV segment essential for GP41-targeted viral neutralization Enhanced HIV-1 neutralization by antibody heteroligation Neutralizing epitopes in the membrane-proximal external region of HIV-1 gp41 are influenced by the transmembrane domain and the plasma membrane.

P2860

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P2860

Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region

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description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Relationship between antibody ...... lementarity-determining region

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Relationship between antibody ...... lementarity-determining region

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type

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Relationship between antibody ...... lementarity-determining region

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Relationship between antibody ...... lementarity-determining region

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P1433

Journal of Virology

P1476

Relationship between antibody ...... lementarity-determining region

@en

P2093

F Javier Guenaga

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

Gilad Ofek

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

Krisha McKee

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

Michael B Zwick

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

Peter D Kwong

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Richard Wyatt

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

Yongping Yang

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

P2860

Structural definition of a conserved neutralization epitope on HIV-1 gp120

Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion

The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles

A monomeric 3(10)-helix is formed in water by a 13-residue peptide representing the neutralizing determinant of HIV-1 on gp41

Structural analysis of the epitope of the anti-HIV antibody 2F5 sheds light into its mechanism of neutralization and HIV fusion

HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane

Structural details of HIV-1 recognition by the broadly neutralizing monoclonal antibody 2F5: epitope conformation, antigen-recognition loop mobility, and anion-binding site

Structure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation † , ‡

Crystallographic Definition of the Epitope Promiscuity of the Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5: Vaccine Design Implications

Structural constraints imposed by the conserved fusion peptide on the HIV-1 gp41 epitope recognized by the broadly neutralizing antibody 2F5

P304

2955-2962

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scholarly article

P356

10.1128/JVI.02257-09

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6

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84

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20042512

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P932

2826063

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