Six amino acid residues in a 1200 Å2 interface mediate binding of factor VIII to an IgG4κ inhibitory antibody. - Wikidata - awgldk - TriplyDB

Six amino acid residues in a 1200 Å2 interface mediate binding of factor VIII to an IgG4κ inhibitory antibody.

Six amino acid residues in a 1200 Å2 interface mediate binding of factor VIII to an IgG4κ inhibitory antibody.

http://www.wikidata.org/entity/Q35007278

about

High-resolution mapping of epitopes on the C2 domain of factor VIII by analysis of point mutants using surface plasmon resonance.Conservative mutations in the C2 domains of factor VIII and factor V alter phospholipid binding and cofactor activity.High-affinity, noninhibitory pathogenic C1 domain antibodies are present in patients with hemophilia A and inhibitors.Engineering less immunogenic and antigenic FVIII proteins.Design and engineering of deimmunized biotherapeutics.Life in the shadow of a dominant partner: the FVIII-VWF association and its clinical implications for hemophilia A.T cells from hemophilia A subjects recognize the same HLA-restricted FVIII epitope with a narrow TCR repertoire.

P2860

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P2860

Six amino acid residues in a 1200 Å2 interface mediate binding of factor VIII to an IgG4κ inhibitory antibody.

http://www.wikidata.org/entity/Q35007278

description

2015 nî lūn-bûn

@nan

2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Six amino acid residues in a 1 ...... an IgG4κ inhibitory antibody.

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Six amino acid residues in a 1 ...... an IgG4κ inhibitory antibody.

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type

label

Six amino acid residues in a 1 ...... an IgG4κ inhibitory antibody.

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Six amino acid residues in a 1 ...... an IgG4κ inhibitory antibody.

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prefLabel

Six amino acid residues in a 1 ...... an IgG4κ inhibitory antibody.

@ast

Six amino acid residues in a 1 ...... an IgG4κ inhibitory antibody.

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P356

JOURNAL.PONE.0116577

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Six amino acid residues in a 1 ...... an IgG4κ inhibitory antibody.

@en

P2093

Ai-Hong Zhang

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

Arthur R Thompson

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Jason T Schuman

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Jasper C Lin

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Kathleen P Pratt

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Komal Puranik

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Muhammad Wamiq-Adhami

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Phuong-Cac T Nguyen

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Ruth A Ettinger

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Shelley M Nakaya-Fletcher

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P2860

Structure of the C2 domain of human factor VIII at 1.5 A resolution

Convergent solutions to binding at a protein-protein interface

Structure of a factor VIII C2 domain-immunoglobulin G4kappa Fab complex: identification of an inhibitory antibody epitope on the surface of factor VIII

Structure of the factor VIII C2 domain in a ternary complex with 2 inhibitor antibodies reveals classical and nonclassical epitopes

Mechanism and kinetics of factor VIII inactivation: study with an IgG4 monoclonal antibody derived from a hemophilia A patient with inhibitor

A hot spot of binding energy in a hormone-receptor interface

High-resolution mapping of epitopes on the C2 domain of factor VIII by analysis of point mutants using surface plasmon resonance.

Mapping of the minimal domain encoding a conformational epitope by lambda phage surface display: factor VIII inhibitor antibodies from haemophilia A patients.

Phage display technology: a tool to explore the diversity of inhibitors to blood coagulation factor VIII.

Antigenicity of putative phospholipid membrane-binding residues in factor VIII.

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e0116577

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scholarly article

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10.1371/JOURNAL.PONE.0116577

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1

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