Results 11 to 20 of about 852,815 (296)

Enhancing neutralizing activity against influenza H1N1/PR8 by engineering a single-domain VL-M2 specific into a bivalent form.

open access: yesPLoS ONE, 2022
Flu disease, with high mortality and morbidity, is caused by the influenza virus. Influenza infections are most effectively prevented through vaccination, but it requires annual reformulation due to the antigenic shift or drift of hemagglutinin and ...
Phuong Thi Hoang   +8 more
doaj   +1 more source

Effect of single-chain antibody targeting of the ligand-binding domain in the anaplastic lymphoma kinase receptor [PDF]

open access: yesOncogene, 2009
The tyrosine kinase receptor anaplastic lymphoma kinase (ALK) and its ligand, the growth factor pleiotrophin (PTN), are highly expressed during the development of the nervous system and have been implicated in the malignant progression of different tumor types.
D C, Stylianou   +7 more
openaire   +2 more sources

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

Importance of Hypervariable Region 2 for Stability and Affinity of a Shark Single-Domain Antibody Specific for Ebola Virus Nucleoprotein. [PDF]

open access: yesPLoS ONE, 2016
Single-domain antibodies derived from the unique New Antigen Receptor found in sharks have numerous potential applications, ranging from diagnostic reagents to therapeutics.
George P Anderson   +7 more
doaj   +1 more source

The Application of Nanobody in CAR-T Therapy

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 ...
Chaolemeng Bao   +9 more
doaj   +1 more source

Heavy and Light Chain Variable Single Domains of an Anti-DNA Binding Antibody Hydrolyze Both Double- and Single-stranded DNAs without Sequence Specificity [PDF]

open access: yesJournal of Biological Chemistry, 2006
Anti-DNA antibodies (Abs) are of biomedical interest because they are associated with autoimmune diseases in human and mice. Previously we isolated an anti-DNA monoclonal Ab 3D8 from an autoimmune-prone MRL-lpr/lpr mouse. Here we have characterized DNA binding kinetics and hydrolyzing activities of the recombinant single chain variable fragment (scFv ...
Young-Rim, Kim   +9 more
openaire   +2 more sources

Special Issue: Nanobody

open access: yesAntibodies, 2020
Since their first description in 1993 [1], single-domain antibody fragments derived from heavy-chain-only antibodies of camelids have received increasing attention as highly versatile binding molecules in the fields of biotechnology and medicine [...]
Patrick Chames, Ulrich Rothbauer
doaj   +1 more source

Discrete analysis of camelid variable domains: sequences, structures, and in-silico structure prediction [PDF]

open access: yesPeerJ, 2020
Antigen binding by antibodies requires precise orientation of the complementarity- determining region (CDR) loops in the variable domain to establish the correct contact surface.
Akhila Melarkode Vattekatte   +9 more
doaj   +2 more sources

Grabbing the Bull by Both Horns: Bovine Ultralong CDR-H3 Paratopes Enable Engineering of ‘Almost Natural’ Common Light Chain Bispecific Antibodies Suitable For Effector Cell Redirection

open access: yesFrontiers in Immunology, 2022
A subset of antibodies found in cattle comprises ultralong CDR-H3 regions of up to 70 amino acids. Interestingly, this type of immunoglobulin usually pairs with the single germline VL gene, V30 that is typically very conserved in sequence.
Daniel Klewinghaus   +6 more
doaj   +1 more source

Hormone-induced Conformational Change of the Purified Soluble Hormone Binding Domain of Follitropin Receptor Complexed with Single Chain Follitropin [PDF]

open access: yesJournal of Biological Chemistry, 2001
Human follicle-stimulating hormone receptor (hFSHR) belongs to family I of G protein-coupled receptors. FSHR extracellular domain (ECD) is predicted to have 8-9 alphabeta or leucine-rich repeat motif elements. The objective of this study was to identify elements of the FSHR ECD involved in ligand binding.
A, Schmidt   +4 more
openaire   +2 more sources

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