Single domain antibodies with VH hallmarks are positively selected during panning of llama (Lama glama) naïve libraries

This publication has 44 references indexed in Scilit:

• Biotechnological applications of recombinant single-domain antibody fragments
  Microbial Cell Factories, 2011
• A Novel Promiscuous Class of Camelid Single-Domain Antibody Contributes to the Antigen-Binding Repertoire
  The Journal of Immunology, 2010
• Aggregation-resistant VHs selected by in vitro evolution tend to have disulfide-bonded loops and acidic isoelectric points
  Protein Engineering, Design and Selection, 2008
• Construction of a Large Phage-Displayed Human Antibody Domain Library with a Scaffold Based On a Newly Identified Highly Soluble, Stable Heavy Chain Variable Domain
  Journal of Molecular Biology, 2008
• Comprehensive Analysis of the Factors Contributing to the Stability and Solubility of Autonomous Human VH Domains
  Journal of Biological Chemistry, 2008
• Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli
  Nature Protocols, 2007
• Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
  Proceedings of the National Academy of Sciences, 2006
• Contributions of CDR3 to VHH Domain Stability and the Design of Monobody Scaffolds for Naive Antibody Libraries
  Journal of Molecular Biology, 2003
• Emergence and evolution of functional heavy-chain antibodies in Camelidae
  Developmental & Comparative Immunology, 2003
• A melanoma-specific VH antibody cloned from a fusion phage library of a vaccinated melanoma patient.
  Proceedings of the National Academy of Sciences, 1996