Results 91 to 100 of about 1,420 (126)
Some of the next articles are maybe not open access.
IgNAR antibody: Structural features, diversity and applications
Fish and Shellfish Immunology, 2022In response to the invasion of exogenous microorganisms, one of the defence strategies of the immune system is to produce antibodies. Cartilaginous fish is among those who evolved the earliest humoral immune system that utilizes immunoglobulin-type antibodies. The cartilaginous fish antibodies fall into three categories: IgW, IgM, and IgNAR.
Ma Huan +2 more
exaly +5 more sources
Fish and 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.
Bo Zhong +2 more
exaly +3 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.
Bo Zhong +2 more
exaly +3 more sources
Sequence structure character of IgNAR Sec in whitespotted bamboo shark (Chiloscyllium plagiosum)
Fish and 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 ...
Yixin Wu, Guiqian Chen, Zhengbing Lv
exaly +3 more sources
Structural insights and biomedical potential of IgNAR scaffolds from sharks [PDF]
MAbs, 2015 In addition to antibodies with the classical composition of heavy and light chains, the adaptive immune repertoire of sharks also includes a heavy-chain only isotype, where antigen binding is mediated exclusively by a small and highly stable domain, referred to as vNAR.
Stefan Zielonka +2 more
exaly +4 more sources
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 ...
VÍCTOR A Streltsov, Stewart D Nuttall
exaly +3 more sources
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).
VÍCTOR A Streltsov +2 more
exaly +3 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
Jinny L Liu +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
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