ArticleNature communications2014
Structural basis of IL-23 antagonism by an Alphabody protein scaffold.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 70 citations in OpenAlex.
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- The IL-23R and Its Genetic Variants: A Hitherto Unforeseen Bridge Between the Immune System and Cancer Development.Cancers · 2024Review
- Structures of complete extracellular receptor assemblies mediated by IL-12 and IL-23.Nature structural & molecular biology · 2024Article
- The Role of IL-23 Inhibitors in Crohn's Disease.Journal of clinical medicine · 2023Review
- Structural basis of activation and antagonism of receptor signaling mediated by interleukin-27.Cell reports · 2022Article
- Triazolinedione protein modification: from an overlooked off-target effect to a tryptophan-based bioconjugation strategy.Chemical science · 2022Article
- Design and Synthesis of Crosslinked Helix Dimers as Protein Tertiary Structure Mimics.Current protocols · 2022Article
- Amelioration of systemic inflammation via the display of two different decoy protein receptors on extracellular vesicles.Nature biomedical engineering · 2021Article
- 5-Hydroxy-pyrrolone based building blocks as maleimide alternatives for protein bioconjugation and single-site multi-functionalization.Chemical science · 2021Article
- Cell-penetrating Alphabody protein scaffolds for intracellular drug targeting.Science advances · 2021Article
- Homogeneously N-glycosylated proteins derived from the GlycoDelete HEK293 cell line enable diffraction-quality crystallogenesis.Acta crystallographica. Section D, Structural biology · 2020Article
- IL-12 and IL-23-Close Relatives with Structural Homologies but Distinct Immunological Functions.Cells · 2020Review
- Review
- Modulation of virus-induced NF-κB signaling by NEMO coiled coil mimics.Nature communications · 2020Article
- Integration of phage and yeast display platforms: A reliable and cost effective approach for binning of peptides as displayed on-phage.PloS one · 2020Article
- The molecular basis of chaperone-mediated interleukin 23 assembly control.Nature communications · 2019Article
- Pathophysiology and inhibition of IL-23 signaling in psoriatic arthritis: A molecular insight.Clinical immunology (Orlando, Fla.) · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.