Mutational analysis of domain antibodies reveals aggregation hotspots within and near the complementarity determining regions.
about
Stability engineering of the human antibody repertoireImproving monoclonal antibody selection and engineering using measurements of colloidal protein interactionsGeneral strategy for the generation of human antibody variable domains with increased aggregation resistanceStructure of a low-melting-temperature anti-cholera toxin: llama VHH domainAdvances in Antibody DesignFully Human VH Single Domains That Rival the Stability and Cleft Recognition of Camelid AntibodiesStructural hot spots for the solubility of globular proteins.High-throughput analysis of concentration-dependent antibody self-association.Therapeutic protein aggregation: mechanisms, design, and control.Frontier of therapeutic antibody discovery: The challenges and how to face them.A novel heavy domain antibody library with functionally optimized complementarity determining regions.Strategies to stabilize compact folding and minimize aggregation of antibody-based fragmentsEngineered antibody variable and constant domains as therapeutic candidates.Increased Fab thermoresistance via VH-targeted directed evolution.Engineered Autonomous Human Variable DomainsNanoyeast and Other Cell Envelope Compositions for Protein Studies and Biosensor Applications.Computer-aided antibody design.Design and Optimization of Anti-amyloid Domain Antibodies Specific for β-Amyloid and Islet Amyloid PolypeptideFunctional consequences of complementarity-determining region deactivation in a multifunctional anti-nucleic acid antibody.Lysine and arginine content of proteins: computational analysis suggests a new tool for solubility design.Efficient affinity maturation of antibody variable domains requires co-selection of compensatory mutations to maintain thermodynamic stability.Engineered antibody therapies to counteract mutant huntingtin and related toxic intracellular proteinsMolecular engineering of antibodies for therapeutic and diagnostic purposes.Molecular dynamics simulations and docking enable to explore the biophysical factors controlling the yields of engineered nanobodies.Determinants of the assembly and function of antibody variable domains.Improving the biophysical properties of anti-ricin single-domain antibodies.Sequence composition predicts immunoglobulin superfamily members that could share the intrinsically disordered properties of antibody CH1 domainsDiscovery of highly soluble antibodies prior to purification using affinity-capture self-interaction nanoparticle spectroscopy.Optimal charged mutations in the complementarity-determining regions that prevent domain antibody aggregation are dependent on the antibody scaffold.Modification of the kinetic stability of immunoglobulin G by solvent additives
P2860
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P2860
Mutational analysis of domain antibodies reveals aggregation hotspots within and near the complementarity determining regions.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Mutational analysis of domain ...... mentarity determining regions.
@en
Mutational analysis of domain ...... mentarity determining regions.
@nl
type
label
Mutational analysis of domain ...... mentarity determining regions.
@en
Mutational analysis of domain ...... mentarity determining regions.
@nl
prefLabel
Mutational analysis of domain ...... mentarity determining regions.
@en
Mutational analysis of domain ...... mentarity determining regions.
@nl
P2860
P356
P1433
P1476
Mutational analysis of domain ...... mentarity determining regions.
@en
P2093
Joseph M Perchiacca
Moumita Bhattacharya
P2860
P304
P356
10.1002/PROT.23085
P407
P577
2011-07-05T00:00:00Z