Results 1 to 10 of about 1,385 (169)

VNAR development through antigen immunization of Japanese topeshark (Hemitriakis japanica) [PDF]

open access: yesFrontiers in Bioengineering and Biotechnology, 2023
The VNAR (Variable New Antigen Receptor) is the smallest single-domain antibody derived from the variable domain of IgNAR of cartilaginous fishes. Despite its biomedical and diagnostic potential, research on VNAR has been limited due to the difficulties ...
Hiroyuki Takeda
exaly   +6 more sources

The influence of antibody humanization on shark variable domain (VNAR) binding site ensembles [PDF]

open access: yesFrontiers in Immunology, 2022
Sharks and other cartilaginous fish produce new antigen receptor (IgNAR) antibodies, as key part of their humoral immune response and are the phylogenetically oldest living organisms that possess an immunoglobulin (Ig)-based adaptive immune system. IgNAR
Franz Waibl   +2 more
exaly   +6 more sources

Allosteric inhibition of Aurora-A kinase by a synthetic vNAR domain [PDF]

open access: yesOpen Biology, 2016
The vast majority of clinically approved protein kinase inhibitors target the ATP-binding pocket directly. Consequently, many inhibitors have broad selectivity profiles and most have significant off-target effects.
Selena G. Burgess   +6 more
doaj   +6 more sources

Construction and application of a large capacity VNAR library from the whitespotted bamboo shark (Chiloscyllium playgiosum) [PDF]

open access: yesActa Pharmaceutica Sinica B
Fifty whitespotted bamboo sharks (Chiloscyllium playgiosum) of both sexes were used to establish a large capacity variable domain of the new antigen receptor (VNAR) library with a total capacity of over 109 colony-forming units (CFU).
ChuanWei CHEN, Ming-Wei Wang
exaly   +4 more sources

Isolation and Characterization of Targeting-HBsAg VNAR Single Domain Antibodies from Whitespotted Bamboo Sharks (Chiloscyllium plagiosum) [PDF]

open access: yesMarine Drugs, 2023
Immunoglobulin new antigen receptor (IgNAR) is a naturally occurring antibody that consists of only two heavy chains with two independent variable domains.
Xierui Jiang   +3 more
doaj   +4 more sources

CDR3 Variants of the TXB2 Shuttle with Increased TfR1 Association Rate and Enhanced Brain Penetration [PDF]

open access: yesPharmaceutics, 2023
Since the delivery of biologic drugs to the brain is greatly hampered by the existence of the blood–brain barrier (BBB), brain shuttles are being developed to enhance therapeutic efficacy.
Pawel Stocki   +11 more
doaj   +6 more sources

Expression Analysis of Heavy-Chain-Only Antibodies in Cloudy Catshark and Japanese Bullhead Shark [PDF]

open access: yesMarine Drugs
Heavy chain-only antibodies in sharks are called immunoglobulin new antigen receptors (IgNAR), consisting of one variable region (VNAR) and five constant regions (C1-C5).
Reo Uemura   +8 more
doaj   +5 more sources

Novel Approach for Obtaining Variable Domain of New Antigen Receptor with Different Physicochemical Properties from Japanese Topeshark (Hemitriakis japanica) [PDF]

open access: yesMarine Drugs, 2023
Diverse candidate antibodies are needed to successfully identify therapeutic and diagnostic applications. The variable domain of IgNAR (VNAR), a shark single-domain antibody, has attracted attention owing to its favorable physicochemical properties.
Tomofumi Nakada-Masuta   +2 more
doaj   +2 more sources

First pan-specific vNAR against human TGF-β as a potential therapeutic application: in silico modeling assessment [PDF]

open access: yesScientific Reports, 2023
Immunotherapies based on antibody fragments have been developed and applied to human diseases, describing novel antibody formats. The vNAR domains have a potential therapeutic use related to their unique properties.
Mirna Burciaga-Flores   +5 more
doaj   +2 more sources

Mechanisms of SARS-CoV-2 neutralization by shark variable new antigen receptors elucidated through X-ray crystallography [PDF]

open access: yesNature Communications, 2021
Shark antibodies (Variable New Antigen Receptors, VNARs) are the smallest naturally occurring antibody fragments. Here, the authors screen a VNAR phage display library against the SARS-CoV2 receptor binding domain (RBD) and identify VNARs that neutralize
Obinna C. Ubah   +20 more
doaj   +2 more sources

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