Structure-based engineering of a monoclonal antibody for improved solubility. - Wikidata - awgldk - TriplyDB

Structure-based engineering of a monoclonal antibody for improved solubility.

Structure-based engineering of a monoclonal antibody for improved solubility.

http://www.wikidata.org/entity/Q44381771

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Separation of mAbs molecular variants by analytical hydrophobic interaction chromatography HPLC: overview and applications Early implementation of QbD in biopharmaceutical development: a practical example Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions Drugs derived from phage display: from candidate identification to clinical practice Boosting antibody developability through rational sequence optimization.Recent Progress toward Engineering HIV-1-Specific Neutralizing Monoclonal Antibodies Advances in Antibody Design High-throughput analysis of concentration-dependent antibody self-association.High-throughput biophysical analysis and data visualization of conformational stability of an IgG1 monoclonal antibody after deglycosylation.Conditional internalization of PEGylated nanomedicines by PEG engagers for triple negative breast cancer therapy Engineered single human CD4 domains as potent HIV-1 inhibitors and components of vaccine immunogens Frontier of therapeutic antibody discovery: The challenges and how to face them.Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.Strategies to stabilize compact folding and minimize aggregation of antibody-based fragments Development of scoring functions for antibody sequence assessment and optimization.Characterization of N-Linked Glycosylation in a Monoclonal Antibody Produced in NS0 Cells Using Capillary Electrophoresis with Laser-Induced Fluorescence Detection Isolation and optimization for affinity and biophysical characteristics of anti-CCL17 antibodies from the VH1-69 germline gene.Sialic acid methylation refines capillary electrophoresis laser-induced fluorescence analyses of immunoglobulin G N-glycans of ovarian cancer patients.Eliminating antibody polyreactivity through addition of N-linked glycosylation.Signature biochemical properties of broadly cross-reactive HIV-1 neutralizing antibodies in human plasma.Nanoyeast and Other Cell Envelope Compositions for Protein Studies and Biosensor Applications.Strategic addition of an N-linked glycan to a monoclonal antibody improves its HIV-1-neutralizing activity.Engineering the variable region of therapeutic IgG antibodies.Unexpected hematologic effects of biotherapeutics in nonclinical species and in humans.High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy.Rational design of therapeutic mAbs against aggregation through protein engineering and incorporation of glycosylation motifs applied to bevacizumab Biological Insights into Therapeutic Protein Modifications throughout Trafficking and Their Biopharmaceutical Applications.Mechanisms of self-association of a human monoclonal antibody CNTO607.Glycosylation engineering of therapeutic IgG antibodies: challenges for the safety, functionality and efficacy.Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo.Identification of human IgG1 variant with enhanced FcRn binding and without increased binding to rheumatoid factor autoantibody.Facile Affinity Maturation of Antibody Variable Domains Using Natural Diversity Mutagenesis.Resolving self-association of a therapeutic antibody by formulation optimization and molecular approaches.High throughput detection of antibody self-interaction by bio-layer interferometry.Solubility evaluation of murine hybridoma antibodies.Mitigation of reversible self-association and viscosity in a human IgG1 monoclonal antibody by rational, structure-guided Fv engineering Raman spectroscopy characterization of antibody phases in serum.Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody.2nd Charles Richet et Jules Héricourt workshop: therapeutic antibodies and anaphylaxis; May 31-June 1, 2011, Tours, France.Equilibrium and kinetic analysis of human interleukin-13 and IL-13 receptor alpha-2 complex formation.

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Structure-based engineering of a monoclonal antibody for improved solubility.

http://www.wikidata.org/entity/Q44381771

description

2010 nî lūn-bûn

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年學術文章

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2010年學術文章

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name

Structure-based engineering of a monoclonal antibody for improved solubility.

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Structure-based engineering of a monoclonal antibody for improved solubility.

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type

label

Structure-based engineering of a monoclonal antibody for improved solubility.

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Structure-based engineering of a monoclonal antibody for improved solubility.

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prefLabel

Structure-based engineering of a monoclonal antibody for improved solubility.

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Structure-based engineering of a monoclonal antibody for improved solubility.

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Protein Engineering Design and Selection

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Structure-based engineering of a monoclonal antibody for improved solubility.

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Audrey Baker

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Eilyn R Lacy

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Gabriela Canziani

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Gary L Gilliland

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James Kang

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Jinquan Luo

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Karyn T O'Neil

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Maggie Huang

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Qing Mike Tang

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Sheng-Jiun Wu

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P2860

Expression and characterization of a human BMP-7 variant with improved biochemical properties

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Epitope mapping of anti-interleukin-13 neutralizing antibody CNTO607

High-resolution crystal structure of M-protease: phylogeny aided analysis of the high-alkaline adaptation mechanism

Anti-inflammatory actions of intravenous immunoglobulin

Oligosaccharide analysis and molecular modeling of soluble forms of glycoproteins belonging to the Ly-6, scavenger receptor, and immunoglobulin superfamilies expressed in Chinese hamster ovary cells.

The use of recombinant methods and molecular engineering in protein crystallization.

Biophysical properties of human antibody variable domains.

Engineering aggregation-resistant proteins by directed evolution.

Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequentia

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643-651

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10.1093/PROTEIN/GZQ037

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8

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23

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Alexey Teplyakov

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2010-06-11T00:00:00Z

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44668365

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