Results 11 to 20 of about 19,829 (313)

Camelid immunoglobulins and nanobody technology [PDF]

open access: greenVeterinary Immunology and Immunopathology, 2008
It is well established that all camelids have unique antibodies circulating in their blood. Unlike antibodies from other species, these special antibodies are devoid of light chains and are composed of a heavy-chain homodimer. These so-called heavy-chain antibodies (HCAbs) are expressed after a V-D-J rearrangement and require dedicated constant gamma ...
Serge Muyldermans   +16 more
openalex   +7 more sources

Structure of Nanobody Nb23 [PDF]

open access: yesMolecules, 2021
Background: Nanobodies, or VHHs, are derived from heavy chain-only antibodies (hcAbs) found in camelids. They overcome some of the inherent limitations of monoclonal antibodies (mAbs) and derivatives thereof, due to their smaller molecular size and higher stability, and thus present an alternative to mAbs for therapeutic use.
Percipalle M.   +4 more
openaire   +6 more sources

Immunogenicity Risk Profile of Nanobodies [PDF]

open access: yesFrontiers in Immunology, 2021
Nanobodies (Nbs), the variable domains of camelid heavy chain-only antibodies, are a promising class of therapeutics or in vivo imaging reagents entering the clinic. They possess unique characteristics, including a minimal size, providing fast pharmacokinetics, high-target specificity, and an affinity in the (sub-)nanomolar range in conjunction with an
Chloé Ackaert   +17 more
openaire   +5 more sources

Nanobodies in cancer

open access: yesSeminars in Immunology, 2021
For treatment and diagnosis of cancer, antibodies have proven their value and now serve as a first line of therapy for certain cancers. A unique class of antibody fragments called nanobodies, derived from camelid heavy chain-only antibodies, are gaining increasing acceptance as diagnostic tools and are considered also as building blocks for chimeric ...
Andrew W. Woodham   +3 more
openaire   +4 more sources

Nanobodies and Nanobody-Based Human Heavy Chain Antibodies As Antitumor Therapeutics [PDF]

open access: goldFrontiers in Immunology, 2017
Monoclonal antibodies have revolutionized cancer therapy. However, delivery to tumor cells in vivo is hampered by the large size (150 kDa) of conventional antibodies. The minimal target recognition module of a conventional antibody is composed of two non-covalently associated variable domains (VH and VL).
Peter Bannas   +2 more
openalex   +5 more sources

Special Issue: Nanobody [PDF]

open access: yesAntibodies, 2020
Since their first description in 1993 [...]
Patrick Chames, Ulrich Rothbauer
openaire   +5 more sources

Nanobody-based trispecific T cell engager (Nb-TriTE) enhances therapeutic efficacy by overcoming tumor-mediated immunosuppression

open access: yesJournal of Hematology & Oncology, 2023
Background T cell engagers (TCEs) have been established as an emerging modality for hematologic malignancies, but solid tumors remain refractory. However, the upregulation of programmed cell death 1 (PD-1) is correlated with T cell dysfunction that ...
Ziqiang Ding   +12 more
doaj   +1 more source

Recent advances of nanobody applications in diagnosis and detection

open access: yesMedComm – Biomaterials and Applications, 2023
Nanobodies (Nbs) are the variable domain of heavy‐chain antibodies derived from the blood of camelids or sharks. Nanobodies are the smallest antibody fragment with intact antigen‐binding ability.
Qianling Su   +5 more
doaj   +1 more source

The Application of Nanobody in CAR-T Therapy [PDF]

open access: yesBiomolecules, 2021
Chimeric antigen receptor (CAR) T therapy represents a form of immune cellular therapy with clinical efficacy and a specific target. A typical chimeric antigen receptor (CAR) construct consists of an antigen binding domain, a transmembrane domain, and a cytoplasmic domain.
Lin-Lin Li   +10 more
openaire   +3 more sources

Chemogenetic Control of Nanobodies [PDF]

open access: yesNature Methods, 2019
ABSTRACTWe introduce an engineered nanobody whose affinity to green fluorescent protein (GFP) can be switched on and off with small molecules. By controlling the cellular localization of GFP fusion proteins, the engineered nanobody allows to study their role in basic biological processes, an approach that should be applicable to numerous previously ...
Shotaro Otsuka   +12 more
openaire   +6 more sources

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