Results 11 to 20 of about 7,630,796 (295)

Bglbrick strategy for the construction of single domain antibody fusions

open access: yesHeliyon, 2017
Single domain antibodies, recombinantly expressed variable domains derived from camelid heavy chain antibodies, are often expressed as multimers for detection and therapeutic applications.
Ellen R. Goldman   +3 more
doaj   +2 more sources

Single domain antibody multimers confer protection against rabies infection. [PDF]

open access: yesPLoS ONE, 2013
Post-exposure prophylactic (PEP) neutralizing antibodies against Rabies are the most effective way to prevent infection-related fatality. The outer envelope glycoprotein of the Rabies virus (RABV) is the most significant surface antigen for generating ...
Bhargavi M Boruah   +10 more
doaj   +2 more sources

Conjugation of biotin-coated luminescent quantum dots with single domain antibody-rhizavidin fusions [PDF]

open access: yesBiotechnology Reports, 2016
Straightforward and effective methods are required for the bioconjugation of proteins to surfaces and particles. Previously we demonstrated that the fusion of a single domain antibody with the biotin binding molecule rhizavidin provided a facile method ...
Jinny L. Liu   +9 more
doaj   +2 more sources

mRNA Encoding a Bispecific Single Domain Antibody Construct Protects against Influenza A Virus Infection in Mice [PDF]

open access: yesMolecular Therapy: Nucleic Acids, 2020
To date, mRNA-based biologics have mainly been developed for prophylactic and therapeutic vaccination to combat infectious diseases or cancer. In the past years, optimization of the characteristics of in vitro transcribed mRNA has led to significant ...
Lien Van Hoecke   +10 more
doaj   +2 more sources

Biotechnological applications of recombinant single-domain antibody fragments [PDF]

open access: yesMicrobial Cell Factories, 2011
Background Single-domain antibody fragments possess structural features, such as a small dimension, an elevated stability, and the singularity of recognizing epitopes non-accessible for conventional antibodies that make them interesting for several ...
de Marco Ario
doaj   +2 more sources

Intracellular Antibody Capture (IAC) Methods for Single Domain Antibodies

open access: yes, 2012
Intracellular single domain antibodies are recombinant proteins, comprising one variable region domain fragment, that bind specifically to intracellular molecules and can interfere with their particular functions within various cellular compartments.
Tanaka, T, Rabbitts, T
openaire   +4 more sources

Immunogenicity and humanization of single‐domain antibodies [PDF]

open access: yesThe FEBS Journal, 2021
Single‐domain antibodies (sdAbs), the autonomous variable domains of camelid and shark heavy‐chain antibodies, have many desirable properties as components of biologic drugs. However, their sequences may increase the risk of immunogenicity and antidrug antibody (ADA) development in humans, and thus, sdAbs are routinely humanized during development ...
Rossotti, Martin A.   +3 more
openaire   +2 more sources

Single-domain antibodies make a difference [PDF]

open access: yesScience, 2021
A double hit with one antibody construct may avoid viral ...
Xavier, Saelens, Bert, Schepens
openaire   +2 more sources

Single‐Domain Antibodies and Their Utility

open access: yesCurrent Protocols in Immunology, 2013
AbstractEngineered monoclonal antibody fragments have gained market attention due to their versatility and tailor‐made potential and are now considered to be an important part of future immunobiotherapeutics. Single‐domain antibodies (sdAbs), also known as nanobodies, are derived from VHHs [variable domains (V) of heavy‐chain‐only antibodies (HCAb)] of
Baral, Toya Nath   +2 more
openaire   +4 more sources

Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation [PDF]

open access: yes, 2009
Single-domain antibody fragments (VHHs) have several beneficial properties as compared to conventional antibody fragments. However, their small size complicates their toxin- and virus-neutralizing capacity.
Fijten, H.P.D.   +5 more
core   +1 more source

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