Results 21 to 30 of about 478,505 (298)

Allosteric inhibition of Aurora-A kinase by a synthetic vNAR domain [PDF]

open access: yesOpen Biology, 2016
The vast majority of clinically approved protein kinase inhibitors target the ATP-binding pocket directly. Consequently, many inhibitors have broad selectivity profiles and most have significant off-target effects.
Selena G. Burgess   +6 more
doaj   +1 more source

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

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

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

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

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

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

The effects of affinity and valency of an albumin-binding domain (ABD) on the half-life of a single-chain diabody-ABD fusion protein [PDF]

open access: yesProtein Engineering Design and Selection, 2010
Fusion of small recombinant antibody fragments to an albumin-binding domain (ABD) from streptococcal protein G strongly extends their plasma half-life. This ABD binds with nanomolar affinity to human (HSA) and mouse serum albumin (MSA). It was speculated that an increase in albumin-binding affinity should lead to a further increase in half-life. In the
Jonas, Hopp   +6 more
openaire   +2 more sources

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