ReviewBiochimica et biophysica acta. Molecular cell research2019
Discoidin domain receptors: Micro insights into macro assemblies.
Review in Biochimica et biophysica acta. Molecular cell research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 33 citations in OpenAlex.
- Trial
- Review
- Autoregulation of the MET receptor tyrosine kinase by its intracellular juxtamembrane domain.The Biochemical journal · 2025Article
- Discoidin domain receptor tyrosine kinase 2: A new perspective on microenvironment remodeling and targeted therapy of solid tumors (Review).Oncology letters · 2025Review
- Transmembrane association of DDR1 and DDR2 mediated by Leucine zipper motifs.Magnetic resonance letters · 2025Article
- The NamBio · 2025Article
- Discoidin Domain Receptor 1 impacts bone microarchitecture with aging in female mice.JBMR plus · 2025Article
- Investigation of Cell Mechanics and Migration on DDR2-Expressing Neuroblastoma Cell Line.Life (Basel, Switzerland) · 2024Article
- Integrins in cancer stem cells.Frontiers in cell and developmental biology · 2024Review
- A highly selective humanized DDR1 mAb reverses immune exclusion by disrupting collagen fiber alignment in breast cancer.Journal for immunotherapy of cancer · 2023Article
- Discoidin domain receptor-2 enhances secondary alveolar septation in mice by activating integrins and modifying focal adhesions.American journal of physiology. Lung cellular and molecular physiology · 2023Article
- Discoidin domain receptors; an ancient family of collagen receptors has major roles in bone development, regeneration and metabolism.Frontiers in dental medicine · 2023Article
- Discoidin Domain Receptor-Driven Gene Signatures as Markers of Patient Response to Anti-PD-L1 Immune Checkpoint Therapy.Journal of the National Cancer Institute · 2022Article
- Discoidin Domain Receptor 2 Mediates Lysophosphatidic Acid-Induced Ovarian Cancer Aggressiveness.International journal of molecular sciences · 2021Article
- The Yin and Yang of Discoidin Domain Receptors (DDRs): Implications in Tumor Growth and Metastasis Development.Cancers · 2021Review
- Recent Advances in the Role of Discoidin Domain Receptor Tyrosine Kinase 1 and Discoidin Domain Receptor Tyrosine Kinase 2 in Breast and Ovarian Cancer.Frontiers in cell and developmental biology · 2021Review
- Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?Frontiers in oncology · 2020Review
- Receptor Tyrosine Kinases in Development: Insights fromInternational journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Assembly of cell-surface receptors into specific oligomeric states and/or clusters before and after ligand binding is an important feature governing their biological function. Receptor oligomerization can be mediated by specific domains of the receptor, ligand binding, configurational changes or other interacting molecules. In this review we summarize our understanding of the oligomeric state of discoidin domain receptors (DDR1 and DDR2), which belong to the receptor tyrosine kinase family (RTK). DDRs form an interesting system from an oligomerization perspective as their ligand collagen(s) can also undergo supramolecular assembly to form fibrils. Even though DDR1 and DDR2 differ in the domains responsible to form ligand-free dimers they share similarities in binding to soluble, monomeric collagen. However, only DDR1b forms globular clusters in response to monomeric collagen and not DDR2. Interestingly, both DDR1 and DDR2 are assembled into linear clusters by the collagen fibril. Formation of these clusters is important for receptor phosphorylation and is mediated in part by other membrane components. We summarize how the oligomeric status of DDRs shares similarities with other members of the RTK family and with collagen receptors. Unraveling the multiple macro-molecular configurations adopted by this receptor-ligand pair can provide novel insights into the intricacies of cell-matrix interactions.
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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.