Results 121 to 130 of about 1,618 (161)
Structure of a shark IgNAR antibody variable domain and modeling of an early-developmental isotype [PDF]
Protein Science, 2005 AbstractThe new antigen receptor (IgNAR) antibodies from sharks are disulphide bonded dimers of two protein chains, each containing one variable and five constant domains. Three types of IgNAR variable domains have been discovered, with Type 3 appearing early in shark development and being overtaken by the antigen‐driven affinity‐matured Type 1 and 2 ...
Victor A Streltsov, Stewart D Nuttall
exaly +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Dimerisation strategies for shark IgNAR single domain antibody fragments
Journal of Immunological Methods, 2006Immunoglobulin new antigen receptors (IgNARs) are unique single domain antibodies found in the serum of sharks. The individual variable (VNAR) domains bind antigen independently and are candidates for the smallest antibody-based immune recognition units (approximately 13 kDa).
Victor A Streltsov +2 more
exaly +3 more sources
Fish & Shellfish Immunology, 2023
Single domain antibodies (sdAb) are promising candidates in cancer and anti-virus biotherapies for their unique structure characters. Though VHH and IgNAR have been discovered in camelidae and nurse shark (Ginlymostoma cirratum) respectively serval decades ago, expense of these large animals still limits the studies and applications of sdAb.
Lei Jia +9 more
openaire +2 more sources
Single domain antibodies (sdAb) are promising candidates in cancer and anti-virus biotherapies for their unique structure characters. Though VHH and IgNAR have been discovered in camelidae and nurse shark (Ginlymostoma cirratum) respectively serval decades ago, expense of these large animals still limits the studies and applications of sdAb.
Lei Jia +9 more
openaire +2 more sources
Journal of Molecular Biology, 2010
The shark antigen-binding V(NAR) domain has the potential to provide an attractive alternative to traditional biotherapeutics based on its small size, advantageous physiochemical properties, and unusual ability to target clefts in enzymes or cell surface molecules. The V(NAR) shares many of the properties of the well-characterised single-domain camelid
B J, Fennell +9 more
openaire +2 more sources
The shark antigen-binding V(NAR) domain has the potential to provide an attractive alternative to traditional biotherapeutics based on its small size, advantageous physiochemical properties, and unusual ability to target clefts in enzymes or cell surface molecules. The V(NAR) shares many of the properties of the well-characterised single-domain camelid
B J, Fennell +9 more
openaire +2 more sources
Selection of cholera toxin specific IgNAR single-domain antibodies from a naïve shark library
Molecular Immunology, 2007Shark immunoglobulin new antigen receptor (IgNAR, also referred to as NAR) variable domains (Vs) are single-domain antibody (sdAb) fragments containing only two hypervariable loop structures forming 3D topologies for a wide range of antigen recognition and binding. Their small size ( approximately 12kDa) and high solubility, thermostability and binding
George P. Anderson +2 more
exaly +3 more sources
Shark IgNAR-derived binding domains as potential diagnostic and therapeutic agents
Developmental and Comparative Immunology, 2019Many of the most successful drugs generated in recent years are based upon monoclonal antibodies (mAbs). However, for some therapeutic and diagnostic applications mAbs are far from ideal; for example, while their relatively large size and inherent receptor binding aids their longevity in vivo it can also limit their tissue penetration.
Helen Dooley
exaly +3 more sources
Sequence structure character of IgNAR Sec in whitespotted bamboo shark (Chiloscyllium plagiosum)
Fish & Shellfish Immunology, 2020Whitespotted bamboo shark (Chiloscyllium plagiosum) is a demersal cartilaginous fish with an adaptive immune system founded upon immunoglobulins. In this manuscript, we characterize the IgNAR of the whitespotted bamboo shark. A newly discovered alternative splicing form of IgNAR Sec (IgNARshort (ΔC2-C3) Sec) was identified, in which the C1 domain was ...
Wenjie, Zhang +11 more
openaire +2 more sources
Cas9-Based Local Enrichment and Genomics Sequence Revision of Megabase-Sized Shark IgNAR Loci
The Journal of Immunology, 2022Abstract The 0.8-Mb Ig new Ag receptor (IgNAR) region of the whitespotted bamboo shark (Chiloscyllium plagiosum) is incompletely assembled in Chr_44 of the reference genome. Here we used Cas9-assisted targeting of chromosome segments (CATCH) to enrich the 2 Mb region of the Chr_44 IgNAR loci and sequenced it by PacBio and next-generation
Hongming Dong +14 more
openaire +2 more sources
Phage Display Derived IgNAR V Region Binding Domains for Therapeutic Development
Current Pharmaceutical Design, 2017Phage display technology has revolutionized the science of drug discovery by transforming the generation and manipulation of ligands, such as antibody fragments, enzymes, and peptides. The basis of this technology is the expression of recombinant proteins or peptides fused to a phage coat protein, and subsequent isolation of ligands based on a variety ...
Obinna C, Ubah +3 more
openaire +2 more sources
Maturation of Shark Single-domain (IgNAR) Antibodies: Evidence for Induced-fit Binding
Journal of Molecular Biology, 2007Sharks express an unusual heavy-chain isotype called IgNAR, whose variable regions bind antigen as independent soluble domains. To further probe affinity maturation of the IgNAR response, we structurally characterized the germline and somatically matured versions of a type II variable (V) region, both in the presence and absence of its antigen, hen egg-
Robyn L, Stanfield +4 more
openaire +2 more sources