Critical contribution of VH-VL interaction to reshaping of an antibody: The case of humanization of anti-lysozyme antibody, HyHEL-10 - Wikidata - wikimedia - TriplyDB

Critical contribution of VH-VL interaction to reshaping of an antibody: The case of humanization of anti-lysozyme antibody, HyHEL-10

Critical contribution of VH-VL interaction to reshaping of an antibody: The case of humanization of anti-lysozyme antibody, HyHEL-10

http://www.wikidata.org/entity/Q27649729

about

Specific Fluorine Labeling of the HyHEL10 Antibody Affects Antigen Binding and Dynamics Computational Screening of the Human TF-Glycome Provides a Structural Definition for the Specificity of Anti-Tumor Antibody JAA-F11 Redistribution of flexibility in stabilizing antibody fragment mutants follows Le Châtelier's principle The Structural Basis of Antibody-Antigen Recognition The association of heavy and light chain variable domains in antibodies: implications for antigen specificity Thermodynamics of antibody-antigen interaction revealed by mutation analysis of antibody variable regions.A universal combinatorial design of antibody framework to graft distinct CDR sequences: a bioinformatics approach.Co-transplantation of human hematopoietic stem cells and human breast cancer cells in NSG mice: a novel approach to generate tumor cell specific human antibodies.Humanization and characterization of an anti-ricin neutralization monoclonal antibody Antibody VH and VL recombination using phage and ribosome display technologies reveals distinct structural routes to affinity improvements with VH-VL interface residues providing important structural diversity Cytokinergic IgE Action in Mast Cell Activation.Construction and humanization of a functional bispecific EGFR × CD16 diabody using a refolding system.An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody.Suppression of antibody-mediated arthritis in mice by Fab fragments of the mediating antibodies.A new scoring function for protein-protein docking that identifies native structures with unprecedented accuracy.Determinants of the assembly and function of antibody variable domains.Structural repertoire of immunoglobulin λ light chains.A natively paired antibody library yields drug leads with higher sensitivity and specificity than a randomly paired antibody library.Understanding the Significance and Implications of Antibody Numbering and Antigen-Binding Surface/Residue Definition

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P2860

Critical contribution of VH-VL interaction to reshaping of an antibody: The case of humanization of anti-lysozyme antibody, HyHEL-10

http://www.wikidata.org/entity/Q27649729

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

@ast

Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

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Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

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type

label

Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

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Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

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Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

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prefLabel

Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

@ast

Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

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Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

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Protein Science

P1476

Critical contribution of VH-VL ...... ti-lysozyme antibody, HyHEL-10

@en

P2093

Akiko Yokota

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

Hidemasa Kondo

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

Izumi Kumagai

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

Kouhei Tsumoto

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

Takeshi Nakanishi

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

P2860

Energetics of the HIV gp120-CD4 binding reaction

A humanized antibody that binds to the interleukin 2 receptor

Basic local alignment search tool

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Crystal structure of anti-Hen egg white lysozyme antibody (HyHEL-10) Fv-antigen complex. Local structural changes in the protein antigen and water-mediated interactions of Fv-antigen and light chain-heavy chain interfaces

Structural evidence for entropic contribution of salt bridge formation to a protein antigen-antibody interaction: the case of hen lysozyme-HyHEL-10 Fv complex

The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction

Structural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10

Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complex

P304

261-70

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scholarly article

P356

10.1110/PS.073156708

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2

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17

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2008-02-01T00:00:00Z

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5625289

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18227432

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P932

2222731

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