Human interleukin-23 receptor antagonists derived from an albumin-binding domain scaffold inhibit IL-23-dependent ex vivo expansion of IL-17-producing T-cells
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00064203%3A_____%2F14%3A10293045" target="_blank" >RIV/00064203:_____/14:10293045 - isvavai.cz</a>
Alternative codes found
RIV/86652036:_____/14:00431238 RIV/61388971:_____/14:00431238 RIV/67985882:_____/14:00431238 RIV/00216208:11130/14:10293045
Result on the web
<a href="http://dx.doi.org/10.1002/prot.24472" target="_blank" >http://dx.doi.org/10.1002/prot.24472</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/prot.24472" target="_blank" >10.1002/prot.24472</a>
Alternative languages
Result language
angličtina
Original language name
Human interleukin-23 receptor antagonists derived from an albumin-binding domain scaffold inhibit IL-23-dependent ex vivo expansion of IL-17-producing T-cells
Original language description
Engineered combinatorial libraries derived from small protein scaffolds represent a powerful tool for generating novel binders with high affinity, required specificity and designed inhibitory function. This work was aimed to generate a collection of recombinant binders of human interleukin-23 receptor (IL-23R), which is a key element of proinflammatory IL-23-mediated signaling. A library of variants derived from the three-helix bundle scaffold of the albumin-binding domain (ABD) of streptococcal proteinG and ribosome display were used to select for high-affinity binders of recombinant extracellular IL-23R. A collection of 34 IL-23R-binding proteins (called REX binders), corresponding to 18 different sequence variants, was used to identify a group of ligands that inhibited binding of the recombinant p19 subunit of IL-23, or the biologically active human IL-23 cytokine, to the recombinant IL-23R or soluble IL-23R-IgG chimera. The strongest competitors for IL-23R binding in ELISA were co
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FD - Oncology and haematology
OECD FORD branch
—
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proteins: Structure, Function and Genetics
ISSN
0887-3585
e-ISSN
—
Volume of the periodical
82
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
15
Pages from-to
975-989
UT code for WoS article
000335955300009
EID of the result in the Scopus database
—