ArticleCells2014
Mechanisms of activation of receptor tyrosine kinases: monomers or dimers.
Article in Cells, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
99 citing papers in PubMed, 205 citations in OpenAlex.
- Ligand regulation and function of preformed EGFR dimers.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Advances in the design and discovery of small-molecule tyrosine kinase inhibitors for breast cancer.RSC advances · 2026Review
- Tyrosine Kinase Receptors, Inhibition, and Potential Role in the Pharmacotherapy of Retinal Disorders.Ophthalmology and therapy · 2026Review
- Integrative structural and dynamics studies of epidermal growth factor receptor (EGFR).Experimental & molecular medicine · 2026Review
- Exploring the Potential of Receptor Silencing in the Tumor Microenvironment by RNA Interference.Biomolecules · 2026Review
- Molecular determinants of signal transduction in tropomyosin receptor kinases.FEBS open bio · 2026Review
- A Chemically Inducible Multimerization System for Tunable and Background-Free RTK Activation.Analytical chemistry · 2026Article
- Decreased Kinase Activity of the VEGFR3 Variant c.3175G>C Associated with Primary Lymphedema.Current issues in molecular biology · 2026Article
- Deciphering the enigma: long noncoding RNAs in disease pathogenesis and therapeutic prospects.Molecular and cellular biochemistry · 2025Review
- Advanced cancer therapy: unlocking the potential of small molecule inhibitors.Future medicinal chemistry · 2025Review
- Single-Molecule Protein Profiling Using Nanopores and Dimeric Aptamer-Modified DNA Carriers.Angewandte Chemie (International ed. in English) · 2025Article
- A chemically inducible multimerization system for tunable and background-free RTK activation.bioRxiv : the preprint server for biology · 2025Article
- Characterization of mAb104, a mAb Targeting a Conformationally Exposed, Tumor-Specific Epitope of HER2.Molecular cancer therapeutics · 2025Article
- Novel Function for Endothelial Protease-Activated Receptors in Modulating Insulin Receptor Activity With Implications for Diabetes.Arteriosclerosis, thrombosis, and vascular biology · 2025Article
- The Role of Twisted Gastrulation 1 (TWSG1) Gene in TGF-β Signaling Linked to Cancer: A Comprehensive Review.Asian Pacific journal of cancer prevention : APJCP · 2025Review
- Incorporation of human β-defensin-1 into immunoliposomes to facilitate targeted autophagy therapy of colon carcinoma.World journal of clinical oncology · 2025Article
- Molecular crosstalk between GPCR and receptor tyrosine-protein kinase in neuroblastoma: molecular mechanism and therapeutic implications.Medical oncology (Northwood, London, England) · 2025Review
- Molecular mechanism of genetic, epigenetic, and metabolic alteration in lung cancer.Medical oncology (Northwood, London, England) · 2025Review
- Mechanisms in Thyroid Eye Disease: The TSH Receptor Interacts Directly With the IGF-1 Receptor.Endocrinology · 2025Article
- A Promising Druggable Target for Translational Therapy of Ovarian Cancer: A Molecular Profiling of Therapeutic Innovations, Extracellular Vesicle Acquired Resistance, and Signaling Pathways.Current medicinal chemistry · 2025Review
39 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Receptor tyrosine kinases (RTKs) play essential roles in cellular processes, including metabolism, cell-cycle control, survival, proliferation, motility and differentiation. RTKs are all synthesized as single-pass transmembrane proteins and bind polypeptide ligands, mainly growth factors. It has long been thought that all RTKs, except for the insulin receptor (IR) family, are activated by ligand-induced dimerization of the receptors. An increasing number of diverse studies, however, indicate that RTKs, previously thought to exist as monomers, are present as pre-formed, yet inactive, dimers prior to ligand binding. The non-covalently associated dimeric structures are reminiscent of those of the IR family, which has a disulfide-linked dimeric structure. Furthermore, recent progress in structural studies has provided insight into the underpinnings of conformational changes during the activation of RTKs. In this review, I discuss two mutually exclusive models for the mechanisms of activation of the epidermal growth factor receptor, the neurotrophin receptor and IR families, based on these new insights.
Identifiers
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.