ArticleProtein science : a publication of the Protein Society1997
Characterization of the receptor binding determinants of granulocyte colony stimulating factor.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 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
15 citing papers in PubMed, 41 citations in OpenAlex.
- Tuning of G-CSFR signaling by de novo-designed agonists.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- A strategy to design protein-based antagonists against type I cytokine receptors.PLoS biology · 2024Article
- A topological refactoring design strategy yields highly stable granulopoietic proteins.Nature communications · 2022Article
- Design of novel granulopoietic proteins by topological rescaffolding.PLoS biology · 2020Article
- Characterization of stress-exposed granulocyte colony stimulating factor using ELISA and hydrogen/deuterium exchange mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
- Article
- Article
- Effect of a structurally modified human granulocyte colony stimulating factor, G-CSFa, on leukopenia in mice and monkeys.Journal of hematology & oncology · 2011Article
- Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Site-Specific Protein PEGylation: Application to Cysteine Analogs of Recombinant Human Granulocyte Colony-Stimulating Factor.BioProcess international · 2005Article
- pH Dependence of structural stability of interleukin-2 and granulocyte colony-stimulating factor.Protein science : a publication of the Protein Society · 2003Article
- Computational stabilization of human growth hormone.Protein science : a publication of the Protein Society · 2002Article
- Development of a cytokine analog with enhanced stability using computational ultrahigh throughput screening.Protein science : a publication of the Protein Society · 2002Article
- Phage display mutagenesis of the chimeric dual cytokine receptor agonist myelopoietin.Leukemia · 2001Article
- Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12.The EMBO journal · 2000Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We performed a series of experiments using alanine-scanning mutagenesis to locate side chains within human granulocyte colony-stimulating factor (G-CSF) that are involved in human G-CSF receptor binding. We constructed a panel of 28 alanine mutants that examined all surface exposed residues on helices A and D, as well as all charged residues on the surface of G-CSF. The G-CSF mutants were expressed in a transiently transfected mammalian cell line and quantitated by a sensitive biosensor method. We measured the activity of mutant proteins using an in vitro proliferation assay and an ELISA binding competition assay. These studies show that there is a region of five charged residues on helices A and C employed by G-CSF in binding its receptor, with the most important residue in this binding patch being Glu 19. Both wild-type G-CSF and the E19A mutant were expressed in E. coli. The re-folded proteins were found to have proliferative activities similar to the analogous proteins from mammalian cells: furthermore, biophysical analysis indicated that the E19A mutation does not cause gross structural perturbations in G-CSF. Although G-CSF is likely to signal through receptor homo-dimerization, we found no compelling evidence for a second receptor binding region. We also found no evidence of self-antagonism at high G-CSF concentrations, suggesting that, in contrast to human growth hormone (hGH) and erythropoietin (EPO), G-CSF probably does not signal via a pure 2:1 receptor ligand complex. Thus, G-CSF, while having a similar tertiary structure to hGH and EPO, uses different areas of the four helix bundle for high-affinity interaction with its receptor.
Indexed as
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.