about
Activity of and effect of subcutaneous treatment with the broad-spectrum antiviral lectin griffithsin in two laboratory rodent modelsBeyond humanization and de-immunization: tolerization as a method for reducing the immunogenicity of biologicsMapping the Pareto optimal design space for a functionally deimmunized biotherapeutic candidateComputationally driven deletion of broadly distributed T cell epitopes in a biotherapeutic candidate.Protein deimmunization via structure-based design enables efficient epitope deletion at high mutational loadsAntibody humanization by structure-based computational protein design.Insights into Hunter syndrome from the structure of iduronate-2-sulfataseOptMAVEn--a new framework for the de novo design of antibody variable region models targeting specific antigen epitopes.Depletion of T cell epitopes in lysostaphin mitigates anti-drug antibody response and enhances antibacterial efficacy in vivo.Structure-based redesign of lysostaphin yields potent antistaphylococcal enzymes that evade immune cell surveillance.EpiSweep: Computationally Driven Reengineering of Therapeutic Proteins to Reduce Immunogenicity While Maintaining Function.Engineered binding to erythrocytes induces immunological tolerance to E. coli asparaginase.Computationally optimized deimmunization libraries yield highly mutated enzymes with low immunogenicity and enhanced activity.Scratching the Surface: Resurfacing Proteins to Endow New Properties and Function.HIV-1 and its resistance to peptidic carbohydrate-binding agents (CBAs): an overview.OSPREY Predicts Resistance Mutations Using Positive and Negative Computational Protein Design.Design and engineering of deimmunized biotherapeutics.Development of a high affinity, non-covalent biologic to add functionality to Fabs.A high throughput MHC II binding assay for quantitative analysis of peptide epitopes.NICTABA and UDA, two GlcNAc-binding lectins with unique antiviral activity profiles.Computationally driven antibody engineering enables simultaneous humanization and thermostabilization.Computationally-driven identification of antibody epitopes.Application of Assisted Design of Antibody and Protein Therapeutics (ADAPT) improves efficacy of a Clostridium difficile toxin A single-domain antibody.Population-specific design of de-immunized protein biotherapeutics.The burgeoning antibody landscape.Recent advances in automated protein design and its future challenges.DisruPPI: structure-based computational redesign algorithm for protein binding disruption.
P2860
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P2860
description
2013 nî lūn-bûn
@nan
2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Structure-guided deimmunization of therapeutic proteins
@ast
Structure-guided deimmunization of therapeutic proteins
@en
Structure-guided deimmunization of therapeutic proteins
@nl
type
label
Structure-guided deimmunization of therapeutic proteins
@ast
Structure-guided deimmunization of therapeutic proteins
@en
Structure-guided deimmunization of therapeutic proteins
@nl
prefLabel
Structure-guided deimmunization of therapeutic proteins
@ast
Structure-guided deimmunization of therapeutic proteins
@en
Structure-guided deimmunization of therapeutic proteins
@nl
P2860
P356
P1476
Structure-guided deimmunization of therapeutic proteins
@en
P2093
Andrew S Parker
Chris Bailey-Kellogg
P2860
P304
P356
10.1089/CMB.2012.0251
P407
P577
2013-02-01T00:00:00Z