ArticleJournal of cell science2012
Antibodies binding the ADAM10 substrate recognition domain inhibit Eph function.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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.
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
24 citing papers in PubMed, 43 citations in OpenAlex.
- Antibodies targeting ADAM17 reverse neurite outgrowth inhibition by myelin-associated inhibitors.Life science alliance · 2025Article
- ADAM Proteases in Cancer: Biological Roles, Therapeutic Challenges, and Emerging Opportunities.Cancers · 2025Review
- A Valuable Target for Therapy: The Metalloproteinase ADAM10.Current protein & peptide science · 2025Review
- EphA2 in Cancer: Molecular Complexity and Therapeutic Opportunities.International journal of molecular sciences · 2024Review
- Endothelial ADAM10 utilization defines a molecular pathway of vascular injury in mice with bacterial sepsis.The Journal of clinical investigation · 2023Article
- Fully human monoclonal antibody targeting activated ADAM10 on colorectal cancer cells.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023Article
- Mechanism of action and therapeutic targeting of CD30 molecule in lymphomas.Frontiers in oncology · 2023Review
- Preferential Antibody and Drug Conjugate Targeting of the ADAM10 Metalloprotease in Tumours.Cancers · 2022Article
- ADAM10-cleaved ephrin-A5 contributes to prostate cancer metastasis.Cell death & disease · 2022Article
- Key metalloproteinase-mediated pathways in the kidney.Nature reviews. Nephrology · 2021Review
- Interplay of Eph-Ephrin Signalling and Cadherin Function in Cell Segregation and Boundary Formation.Frontiers in cell and developmental biology · 2021Review
- Novel Approaches and Challenges of Discovery of Exosite Modulators of a Disintegrin and Metalloprotease 10.Frontiers in molecular biosciences · 2020Review
- Role of ADAM10 as a CD30 Sheddase in Classical Hodgkin Lymphoma.Frontiers in immunology · 2020Review
- Monoclonal antibodies against metzincin targets.British journal of pharmacology · 2019Review
- Therapeutic potential of targeting the Eph/ephrin signaling complex.The international journal of biochemistry & cell biology · 2018Review
- EphA2 Transmembrane Domain Is Uniquely Required for Keratinocyte Migration by Regulating Ephrin-A1 Levels.The Journal of investigative dermatology · 2018Article
- Tyrosine phosphorylation of the transmembrane protein SIRPα: Sensing synaptic activity and regulating ectodomain cleavage for synapse maturation.The Journal of biological chemistry · 2018Article
- Renal ADAM10 and 17: Their Physiological and Medical Meanings.Frontiers in cell and developmental biology · 2018Article
- Article
- An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth.The Journal of experimental medicine · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The ADAM10 transmembrane metalloprotease cleaves a variety of cell surface proteins that are important in disease, including ligands for receptor tyrosine kinases of the erbB and Eph families. ADAM10-mediated cleavage of ephrins, the ligands for Eph receptors, is suggested to control Eph/ephrin-mediated cell-cell adhesion and segregation, important during normal developmental processes, and implicated in tumour neo-angiogenesis and metastasis. We previously identified a substrate-binding pocket in the ADAM10 C domain that binds the EphA/ephrin-A complex thereby regulating ephrin cleavage. We have now generated monoclonal antibodies specifically recognising this region of ADAM10, which inhibit ephrin cleavage and Eph/ephrin-mediated cell function, including ephrin-induced Eph receptor internalisation, phosphorylation and Eph-mediated cell segregation. Our studies confirm the important role of ADAM10 in cell-cell interactions mediated by both A- and B-type Eph receptors, and suggest antibodies against the ADAM10 substrate-recognition pocket as promising therapeutic agents, acting by inhibiting cleavage of ephrins and potentially other ADAM10 substrates.
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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.