Aggregation-resistant VHs selected by in vitro evolution tend to have disulfide-bonded loops and acidic isoelectric points.
about
Stability engineering of the human antibody repertoireCrystal Structure of a Human Single Domain Antibody Dimer Formed through VH-VH Non-Covalent InteractionsNeutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domainStabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bondsAdvances in Antibody DesignPhysico-chemical determinants of soluble intrabody expression in mammalian cell cytoplasm.Molecular imaging of glioblastoma multiforme using anti-insulin-like growth factor-binding protein-7 single-domain antibodies.Efficient generation of single domain antibodies with high affinities and enhanced thermal stabilities.A V(L) single-domain antibody library shows a high-propensity to yield non-aggregating binders.Disulfide linkage engineering for improving biophysical properties of human VH domains.Engineered antibody variable and constant domains as therapeutic candidates.Single-domain antibodies and their utility.Phage antibody display libraries: a powerful antibody discovery platform for immunotherapy.Increased Fab thermoresistance via VH-targeted directed evolution.Identification of cross-reactive single-domain antibodies against serum albumin using next-generation DNA sequencing.Isolation of TGF-β-neutralizing single-domain antibodies of predetermined epitope specificity using next-generation DNA sequencing.Co-evolution of affinity and stability of grafted amyloid-motif domain antibodies.A Rational Engineering Strategy for Designing Protein A-Binding Camelid Single-Domain AntibodiesEngineered Autonomous Human Variable DomainsLysine and arginine content of proteins: computational analysis suggests a new tool for solubility design.Antibody light chain variable domains and their biophysically improved versions for human immunotherapy.Enhancing Stability of Camelid and Shark Single Domain Antibodies: An Overview.Mutational analysis of domain antibodies reveals aggregation hotspots within and near the complementarity determining regions.Application of Assisted Design of Antibody and Protein Therapeutics (ADAPT) improves efficacy of a Clostridium difficile toxin A single-domain antibody.Stability-Diversity Tradeoffs Impose Fundamental Constraints on Selection of Synthetic Human VH/VL Single-Domain Antibodies from In Vitro Display Libraries.Next-Generation DNA Sequencing of VH/VL Repertoires: A Primer and Guide to Applications in Single-Domain Antibody Discovery.Optimal charged mutations in the complementarity-determining regions that prevent domain antibody aggregation are dependent on the antibody scaffold.
P2860
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P2860
Aggregation-resistant VHs selected by in vitro evolution tend to have disulfide-bonded loops and acidic isoelectric points.
description
2008 nî lūn-bûn
@nan
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Aggregation-resistant VHs sele ...... and acidic isoelectric points.
@ast
Aggregation-resistant VHs sele ...... and acidic isoelectric points.
@en
type
label
Aggregation-resistant VHs sele ...... and acidic isoelectric points.
@ast
Aggregation-resistant VHs sele ...... and acidic isoelectric points.
@en
prefLabel
Aggregation-resistant VHs sele ...... and acidic isoelectric points.
@ast
Aggregation-resistant VHs sele ...... and acidic isoelectric points.
@en
P2093
P2860
P356
P1476
Aggregation-resistant VHs sele ...... and acidic isoelectric points.
@en
P2093
M Arbabi-Ghahroudi
N Gaudette
R MacKenzie
P2860
P356
10.1093/PROTEIN/GZN071
P577
2008-11-24T00:00:00Z