Matches in UGent Biblio for { <https://biblio.ugent.be/publication/5869757#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B937410.
- aggregation creator B937411.
- aggregation creator B937412.
- aggregation creator B937413.
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- aggregation date "2014".
- aggregation format "application/pdf".
- aggregation hasFormat 5869757.bibtex.
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- aggregation isPartOf urn:issn:2041-1723.
- aggregation language "eng".
- aggregation rights "I have retained and own the full copyright for this publication".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Structural basis of IL-23 antagonism by an Alphabody protein scaffold".
- aggregation abstract "Protein scaffolds can provide a promising alternative to antibodies for various biomedical and biotechnological applications, including therapeutics. Here we describe the design and development of the Alphabody, a protein scaffold featuring a single-chain antiparallel triple-helix coiled-coil fold. We report affinity-matured Alphabodies with favourable physicochemical properties that can specifically neutralize human interleukin (IL)-23, a pivotal therapeutic target in autoimmune inflammatory diseases such as psoriasis and multiple sclerosis. The crystal structure of human IL-23 in complex with an affinity-matured Alphabody reveals how the variable interhelical groove of the scaffold uniquely targets a large epitope on the p19 subunit of IL-23 to harness fully the hydrophobic and hydrogen-bonding potential of tryptophan and tyrosine residues contributed by p19 and the Alphabody, respectively. Thus, Alphabodies are suitable for targeting protein-protein interfaces of therapeutic importance and can be tailored to interrogate desired design and binding-mode principles via efficient selection and affinity-maturation strategies.".
- aggregation authorList BK1324755.
- aggregation volume "5".
- aggregation aggregates 5869987.
- aggregation isDescribedBy 5869757.
- aggregation similarTo ncomms6237.
- aggregation similarTo LU-5869757.