Results 1 to 10 of about 852,815 (296)

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   +2 more sources

Selection of single chain antibody fragments binding to the extracellular domain of 4-1BB receptor by phage display technology [PDF]

open access: yesTumor Biology, 2017
The 4-1BB is a surface glycoprotein that pertains to the tumor necrosis factor–receptor family. There is compelling evidence suggesting important roles for 4-1BB in the immune response, including cell activation and proliferation and also cytokine ...
Salman Bagheri   +8 more
doaj   +3 more sources

Kinetic Characterisation of a Single Chain Antibody against the Hormone Abscisic Acid: Comparison with Its Parental Monoclonal [PDF]

open access: yes, 2016
A single-chain Fv fragment antibody (scFv) specific for the plant hormone abscisic acid (ABA) has been expressed in the bacterium Escherichia coli as a fusion protein.
A Hayhurst   +38 more
core   +17 more sources

The eIg technology to generate Ig-like bispecific antibodies

open access: yesmAbs, 2022
Bispecific antibodies have emerged as therapeutic molecules with a multitude of modes of action and applications. Here, we present a novel approach to solve the light-chain problem for the generation of bispecific Ig-like antibodies using the second ...
Lennart Kühl   +3 more
doaj   +1 more source

Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56

open access: yesNature Communications, 2023
Bacterial AB toxins are secreted key virulence factors that are internalized by target cells through receptor-mediated endocytosis, translocating their enzymatic domain to the cytosol from endosomes (short-trip) or the endoplasmic reticulum (long-trip ...
Johnny Lisboa   +12 more
doaj   +1 more source

Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VHH antibodies

open access: yesScientific Reports, 2021
The high binding affinities and specificities of antibodies have led to their use as drugs and biosensors. Single-domain VHH antibodies exhibit high specificity and affinity but have higher stability and solubility than conventional antibodies as they ...
Emina Ikeuchi   +4 more
doaj   +1 more source

A Fab-Selective Immunoglobulin-Binding Domain from Streptococcal Protein G with Improved Half-Life Extension Properties. [PDF]

open access: yesPLoS ONE, 2015
Half-life extension strategies have gained increasing interest to improve the pharmacokinetic and pharmacodynamic properties of protein therapeutics. Recently, we established an immunoglobulin-binding domain (IgBD) from streptococcal protein G (SpGC3) as
Felix Unverdorben   +3 more
doaj   +1 more source

Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domains [PDF]

open access: yesProceedings of the National Academy of Sciences, 2001
To study the molecular structure and function of gene productsin situ, we developed a molecular immunolabeling technology. Starting with cDNA from hybridomas producing monoclonal antibodies against biotin, catalase, and superoxide dismutase, we bioengineered recombinant single-chain variable fragment antibodies (scFv) and their derivatives containing ...
Marek, Malecki   +3 more
openaire   +2 more sources

Development and evaluation of single domain antibodies for vaccinia and the L1 antigen. [PDF]

open access: yesPLoS ONE, 2014
There is ongoing interest to develop high affinity, thermal stable recognition elements to replace conventional antibodies in biothreat detection assays. As part of this effort, single domain antibodies that target vaccinia virus were developed.
Scott A Walper   +4 more
doaj   +1 more source

Serum albumin binding knob domains engineered within a VH framework III bispecific antibody format and as chimeric peptides

open access: yesFrontiers in Immunology, 2023
BackgroundSerum albumin binding is an established mechanism to extend the serum half-life of antibody fragments and peptides. The cysteine rich knob domains, isolated from bovine antibody ultralong CDRH3, are the smallest single chain antibody fragments ...
Ralph Adams   +18 more
doaj   +1 more source

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