Results 11 to 20 of about 611,465 (258)

An Inside Job: Applications of Intracellular Single Domain Antibodies [PDF]

open access: yesBiomolecules, 2020
Sera of camelid species contain a special kind of antibody that consists only of heavy chains. The variable antigen binding domain of these heavy chain antibodies can be expressed as a separate entity, called a single domain antibody that is ...
Eline Soetens   +2 more
doaj   +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

Application Progress of the Single Domain Antibody in Medicine. [PDF]

open access: yesInt J Mol Sci, 2023
The camelid-derived single chain antibody (sdAb), also termed VHH or nanobody, is a unique, functional heavy (H)-chain antibody (HCAb). In contrast to conventional antibodies, sdAb is a unique antibody fragment consisting of a heavy-chain variable domain. It lacks light chains and a first constant domain (CH1).
Tang H, Gao Y, Han J.
europepmc   +3 more sources

A comparison of the binding sites of antibodies and single-domain antibodies

open access: yesFrontiers in Immunology, 2023
Antibodies are the largest class of biotherapeutics. However, in recent years, single-domain antibodies have gained traction due to their smaller size and comparable binding affinity. Antibodies (Abs) and single-domain antibodies (sdAbs) differ in the structures of their binding sites: most significantly, single-domain antibodies lack a light chain and
Gemma L. Gordon   +5 more
openaire   +3 more sources

Single domain antibody: Development and application in biotechnology and biopharma. [PDF]

open access: yesImmunol Rev
SummaryHeavy‐chain antibodies (HCAbs) are a unique type of antibodies devoid of light chains, and comprised of two heavy chains‐only that recognize their cognate antigen by virtue of a single variable domain also referred to as VHH, single domain antibody (sdAb), or nanobody (Nb). These functional HCAbs, serendipitous discovered about three decades ago,
Yu T   +4 more
europepmc   +4 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

Single-domain antibodies for biomedical applications [PDF]

open access: yesImmunopharmacology and Immunotoxicology, 2015
Single-domain antibodies are the smallest antigen-binding units of antibodies, consisting either only of one variable domain or one engineered constant domain that solely facilitates target binding. This class of antibody derivatives comprises naturally occurring variable domains derived from camelids and sharks as well as engineered human variable or ...
Krah, Simon   +5 more
openaire   +3 more sources

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   +1 more source

NbX: Machine Learning-Guided Re-Ranking of Nanobody–Antigen Binding Poses

open access: yesPharmaceuticals, 2021
Modeling the binding pose of an antibody is a prerequisite to structure-based affinity maturation and design. Without knowing a reliable binding pose, the subsequent structural simulation is largely futile.
Chunlai Tam   +2 more
doaj   +1 more source

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