ArticleThe Journal of biological chemistry2016
i-bodies, Human Single Domain Antibodies That Antagonize Chemokine Receptor CXCR4.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 66 citations in OpenAlex.
- An abundant merozoite surface protein ofeLife · 2026Article
- Latest surface plasmon resonance advances for G protein-coupled receptors.Journal of pharmaceutical analysis · 2026Review
- TR-FRET between engineered nanobodies reveals the existence of endogenous CXCR4 oligomers.Communications biology · 2025Article
- Article
- Novel human single-domain antibodies exert potent anti-tumor activity by targeting EGF-like repeat epitope of EpCAM.Frontiers in pharmacology · 2025Article
- Second Generation I-Body AD-214 Attenuates Unilateral Ureteral Obstruction (UUO)-Induced Kidney Fibrosis Through Inhibiting Leukocyte Infiltration and Macrophage Migration.International journal of molecular sciences · 2024Article
- A broadly cross-reactive i-body to AMA1 potently inhibits blood and liver stages of Plasmodium parasites.Nature communications · 2024Article
- PROSCA: an online platform for humanized scaffold mining facilitating rational protein engineering.Nucleic acids research · 2024Article
- Development of N-Terminally Modified Variants of the CXCR4-Antagonistic Peptide EPI-X4 for Enhanced Plasma Stability.Journal of medicinal chemistry · 2023Article
- Improving antibody drug development using bionanotechnology.Current opinion in biotechnology · 2022Review
- A single-domain i-body, AD-114, attenuates renal fibrosis through blockade of CXCR4.JCI insight · 2022Article
- SYNBIP: synthetic binding proteins for research, diagnosis and therapy.Nucleic acids research · 2022Article
- Overview, Generation, and Significance of Variable New Antigen Receptors (VNARs) as a Platform for Drug and Diagnostic Development.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Detection of genome-edited and endogenously expressed G protein-coupled receptors.The FEBS journal · 2021Review
- Development of a Novel SPR Assay to Study CXCR4-Ligand Interactions.Biosensors · 2020Article
- Nanobodies: Next Generation of Cancer Diagnostics and Therapeutics.Frontiers in oncology · 2020Review
- Structure-guided discovery of a single-domain antibody agonist against human apelin receptor.Science advances · 2020Article
- Antibody Structure and Function: The Basis for Engineering Therapeutics.Antibodies (Basel, Switzerland) · 2019Review
- Article
- Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor.Nature communications · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
23 authors at 8 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CXCR4 is a G protein-coupled receptor with excellent potential as a therapeutic target for a range of clinical conditions, including stem cell mobilization, cancer prognosis and treatment, fibrosis therapy, and HIV infection. We report here the development of a fully human single-domain antibody-like scaffold termed an "i-body," the engineering of which produces an i-body library possessing a long complementarity determining region binding loop, and the isolation and characterization of a panel of i-bodies with activity against human CXCR4. The CXCR4-specific i-bodies show antagonistic activity in a range of in vitro and in vivo assays, including inhibition of HIV infection, cell migration, and leukocyte recruitment but, importantly, not the mobilization of hematopoietic stem cells. Epitope mapping of the three CXCR4 i-bodies AM3-114, AM4-272, and AM3-523 revealed binding deep in the binding pocket of the receptor.
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What OpenQuestion holds
Registered trials
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.