ArticleMolecular and cellular biology1994
Activation and inhibition of erythropoietin receptor function: role of receptor dimerization.
Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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
53 citing papers in PubMed, 200 citations in OpenAlex.
- Erythropoietin promotes cell proliferation in Neuro-2A mouse neuroblastoma cells.Biochemistry and biophysics reports · 2025Article
- NGF, EPO, and IGF-1 in the Male Reproductive System.Journal of clinical medicine · 2024Review
- Structural Modeling of Cytokine-Receptor-JAK2 Signaling Complexes Using AlphaFold Multimer.Journal of chemical information and modeling · 2023Article
- Molecular and cellular factors determining the functional pleiotropy of cytokines.The FEBS journal · 2023Review
- Emerging principles of cytokine pharmacology and therapeutics.Nature reviews. Drug discovery · 2023Review
- Erythropoietin in Optic Neuropathies: Current Future Strategies for Optic Nerve Protection and Repair.International journal of molecular sciences · 2022Review
- A strategy for the selection of monovalent antibodies that span protein dimer interfaces.The Journal of biological chemistry · 2019Article
- Erythropoietin and Its Angiogenic Activity.International journal of molecular sciences · 2017Review
- The Janus Kinase (JAK) FERM and SH2 Domains: Bringing Specificity to JAK-Receptor Interactions.Frontiers in endocrinology · 2017Review
- Exploration of early-life candidate biomarkers for childhood asthma using antibody arrays.Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology · 2016Article
- Low Oxygen Tension Primes Aortic Endothelial Cells to the Reparative Effect of Tissue-Protective Cytokines.Molecular medicine (Cambridge, Mass.) · 2015Article
- PRMT1-mediated methylation of the EGF receptor regulates signaling and cetuximab response.The Journal of clinical investigation · 2015Article
- Insights into cytokine-receptor interactions from cytokine engineering.Annual review of immunology · 2015Review
- Multifarious determinants of cytokine receptor signaling specificity.Advances in immunology · 2014Review
- The erythropoietin receptor: molecular structure and hematopoietic signaling pathways.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2011Review
- Jak/STAT pathways in cytokine signaling and myeloproliferative disorders: approaches for targeted therapies.Genes & cancer · 2010Article
- Interaction between the glucocorticoid and erythropoietin receptors in human erythroid cells.Experimental hematology · 2009Article
- Erythropoietin: elucidating new cellular targets that broaden therapeutic strategies.Progress in neurobiology · 2008Review
- The serine protease TMPRSS6 is required to sense iron deficiency.Science (New York, N.Y.) · 2008Article
- Erythropoietin and oxidative stress.Current neurovascular research · 2008Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Members of the cytokine receptor superfamily have structurally similar extracellular ligand-binding domains yet diverse cytoplasmic regions lacking any obvious catalytic domains. Many of these receptors form ligand-induced oligomers which are likely to participate in transmembrane signaling. A constitutively active (factor-independent) mutant of the erythropoietin receptor (EPO-R), R129C in the exoplasmic domain, forms disulfide-linked homodimers, suggesting that the wild-type EPO-R is activated by ligand-induced homodimerization. Here, we have taken two approaches to probe the role EPO-R dimerization plays in signal transduction. First, on the basis of the crystal structure of the ligand-bound, homodimeric growth hormone receptor (GH-R) and sequence alignment between the GH-R and EPO-R, we identified residues of the EPO-R which may be involved in intersubunit contacts in an EPO-R homodimer. Residue 129 of the EPO-R corresponds to a residue localized to the GH-R dimer interface region. Alanine or cysteine substitutions were introduced at four other residues of the EPO-R predicted to be in the dimer interface region. Substitution of residue E-132 or E-133 with cysteine renders the EPO-R constitutively active. Like the arginine-to-cysteine mutation at position 129 in the exoplasmic domain (R129C), E132C and E133C form disulfide-linked homodimers, suggesting that constitutive activity is due to covalent dimerization. In the second approach, we have coexpressed the wild-type EPO-R with inactive mutants of the receptor missing all or part of the cytosolic domain. These truncated receptors have a dominant inhibitory effect on the proliferative action of the wild-type receptor. Taken together, these results strengthen the hypothesis that an initial step in EPO- and EPO-R-mediated signal transduction is ligand-induced receptor dimerization.
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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.