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An Inside Job: Applications of Intracellular Single Domain Antibodies

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   +1 more source

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

Single-domain antibodies and their formatting to combat viral infections [PDF]

open access: yes, 2018
Since their discovery in the 1990s, single-domain antibodies (VHHs), also known as NanobodiesA (R), have changed the landscape of affinity reagents. The outstanding solubility, stability, and specificity of VHHs, as well as their small size, ease of ...
Ballegeer, Marlies   +4 more
core   +2 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

Photobodies: Light‐Activatable Single‐Domain Antibody Fragments [PDF]

open access: yesAngewandte Chemie, 2019
AbstractPhotocaged antibody fragments, termed photobodies, have been developed that are impaired in their antigen‐binding capacity and can be activated by irradiation with UV light (365 nm). This rational design concept builds on the selective photocaging of a single tyrosine in a nanobody (a single‐domain antibody fragment).
Benedikt Jedlitzke   +3 more
openaire   +3 more sources

Single domain antibodies: promising experimental and therapeutic tools in infection and immunity [PDF]

open access: yes, 2009
Antibodies are important tools for experimental research and medical applications. Most antibodies are composed of two heavy and two light chains. Both chains contribute to the antigen-binding site which is usually flat or concave.
Janusz Wesolowski   +146 more
core   +3 more sources

Seed-produced anti-globulin VHH-Fc antibodies retrieve globulin precursors in the insoluble fraction and modulate the Arabidopsis thaliana seed subcellular morphology [PDF]

open access: yes, 2020
Key message Nanobody-heavy chain (VHH-Fc) antibody formats have the potential to immunomodulate even highly accumulating proteins and provide a valuable tool to experimentally modulate the subcellular distribution of seed storage proteins.
Altmann, Friedrich   +7 more
core   +2 more sources

NANOBODIES: STRUCTURE, MANUFACTURING, APPLICATION (REVIEW)

open access: yesРазработка и регистрация лекарственных средств, 2019
Introduction. Single-domain antibodies (nanobodies) are composed of the heavy-chain variable domain only. Compared to conventional immunoglobulins G (IgG) nanobodies have such qualities as: high bioavailability, ability to bind epitopes that are ...
A. V. Shatalova   +3 more
doaj   +1 more source

Brain Delivery of Single-Domain Antibodies: A Focus on VHH and VNAR

open access: yesPharmaceutics, 2020
Passive immunotherapy, i.e., treatment with therapeutic antibodies, has been increasingly used over the last decade in several diseases such as cancers or inflammation.
Elodie Pothin   +2 more
doaj   +1 more source

Potent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state [PDF]

open access: yes, 2017
Human respiratory syncytial virus (RSV) is the main cause of lower respiratory tract infections in young children. The RSV fusion protein (F) is highly conserved and is the only viral membrane protein that is essential for infection.
Chen, Man   +13 more
core   +2 more sources

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