ArticleProceedings of the National Academy of Sciences of the United States of America2010
Construction and genetic selection of small transmembrane proteins that activate the human erythropoietin receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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
27 citing papers in PubMed, 37 citations in OpenAlex.
- Traptamer screening: a new functional genomics approach to study virus entry and other cellular processes.The FEBS journal · 2022Review
- Spiers Memorial Lecture: Analysis andFaraday discussions · 2021Article
- Activation of the PDGF β Receptor by a Persistent Artificial Signal Peptide.Journal of molecular biology · 2021Article
- TBC1D5-Catalyzed Cycling of Rab7 Is Required for Retromer-Mediated Human Papillomavirus Trafficking during Virus Entry.Cell reports · 2020Article
- Membrane receptor activation mechanisms and transmembrane peptide tools to elucidate them.The Journal of biological chemistry · 2020Review
- Biologically Active Ultra-Simple Proteins Reveal Principles of Transmembrane Domain Interactions.Journal of molecular biology · 2019Article
- Transmembrane Protein Aptamer Induces Cooperative Signaling by the EPO Receptor and the Cytokine Receptor β-Common Subunit.iScience · 2019Article
- Small size, big impact: how studies of small DNA tumour viruses revolutionized biology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Review
- Regulation of C-C chemokine receptor 5 (CCR5) stability by LysThe Journal of biological chemistry · 2018Article
- De novo designed transmembrane peptides activating the α5β1 integrin.Protein engineering, design & selection : PEDS · 2018Article
- Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions.eLife · 2017Article
- Drugging Membrane Protein Interactions.Annual review of biomedical engineering · 2016Review
- A topological and conformational stability alphabet for multipass membrane proteins.Nature chemical biology · 2016Article
- Targeting EPO and EPO receptor pathways in anemia and dysregulated erythropoiesis.Expert opinion on therapeutic targets · 2016Review
- Biologically active LIL proteins built with minimal chemical diversity.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- JAK2 activation by growth hormone and other cytokines.The Biochemical journal · 2015Review
- Is virology dead?mBio · 2014Article
- De novo selection of oncogenes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mapping the homodimer interface of an optimized, artificial, transmembrane protein activator of the human erythropoietin receptor.PloS one · 2014Article
- Viral miniproteins.Annual review of microbiology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
This work describes a genetic approach to isolate small, artificial transmembrane (TM) proteins with biological activity. The bovine papillomavirus E5 protein is a dimeric, 44-amino acid TM protein that transforms cells by specifically binding and activating the platelet-derived growth factor beta receptor (PDGFbetaR). We used the E5 protein as a scaffold to construct a retrovirus library expressing approximately 500,000 unique 44-amino acid proteins with randomized TM domains. We screened this library to select small, dimeric TM proteins that were structurally unrelated to erythropoietin (EPO), but specifically activated the human EPO receptor (hEPOR). These proteins did not activate the murine EPOR or the PDGFbetaR. Genetic studies with one of these activators suggested that it interacted with the TM domain of the hEPOR. Furthermore, this TM activator supported erythroid differentiation of primary human hematopoietic progenitor cells in vitro in the absence of EPO. Thus, we have changed the specificity of a protein so that it no longer recognizes its natural target but, instead, modulates an entirely different protein. This represents a novel strategy to isolate small artificial proteins that affect diverse membrane proteins. We suggest the word "traptamer" for these transmembrane aptamers.
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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.