ArticleScience (New York, N.Y.)2013
Erythropoietin derived by chemical synthesis.
Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 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
83 citing papers in PubMed.
- Modifications of Lysine Residues 294 and 311 Within the Microtubule-Binding Region Alter Tau Aggregation and Tubulin Binding Equilibria.Angewandte Chemie (International ed. in English) · 2026Article
- Silver(I)-mediated amide-to-ester transformation on unprotected peptides for protein chemical synthesis and engineering.Science advances · 2026Article
- Revealing the Biological Effect of theJournal of the American Chemical Society · 2026Article
- Pyridium-π interaction preserves N,S-benzylidene thioacetals in acidolysis enabling efficient protein chemical synthesis.Nature communications · 2026Article
- Article
- Stirring glycopeptides away from the constraints of solid-phase synthesis misconceptions.Frontiers in molecular biosciences · 2026Article
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Backbone Protecting Groups for Enhanced Peptide and Protein Synthesis.Angewandte Chemie (International ed. in English) · 2025Review
- Examining the Role of Threonine Phosphorylation in Ubiquitin's Function Using Chemical Protein Synthesis.JACS Au · 2025Article
- Convergent Assembly of Homo- and Heterotypic Ubiquitin Chains from Functionalized, Expressed Monomers via Thiol-Ene Chemistry.Angewandte Chemie (International ed. in English) · 2025Article
- An Enabling Peptide Ligation Induced by Thiol-Salicylaldehyde Ester for Chemical Protein Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Mammalian cell-based production of glycans, glycopeptides and glycomodules.Nature communications · 2024Article
- A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins.Journal of the American Chemical Society · 2024Article
- Enhanced native chemical ligation by peptide conjugation in trifluoroacetic acid.Science advances · 2024Article
- O-glycosylation in viruses: A sweet tango.mLife · 2024Review
- Semisynthesis of homogeneous spike RBD glycoforms from SARS-CoV-2 for profiling the correlations between glycan composition and function.National science review · 2024Article
- A Hitchhiker's Guide to Problem Selection in Carbohydrate Synthesis.ACS central science · 2023Review
- Total synthesis of interleukin-2Chemical science · 2023Article
- Identification of the effect ofRSC advances · 2022Article
- Synthesis of glycopeptides and glycopeptide conjugates.Organic & biomolecular chemistry · 2022Review
23 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
7 authors.
Funding
Abstract
Erythropoietin is a signaling glycoprotein that controls the fundamental process of erythropoiesis, orchestrating the production and maintenance of red blood cells. As administrated clinically, erythropoietin has a polypeptide backbone with complex dishomogeneity in its carbohydrate domains. Here we describe the total synthesis of homogeneous erythropoietin with consensus carbohydrate domains incorporated at all of the native glycosylation sites. The oligosaccharide sectors were built by total synthesis and attached stereospecifically to peptidyl fragments of the wild-type primary sequence, themselves obtained by solid-phase peptide synthesis. The glycopeptidyl constructs were joined by chemical ligation, followed by metal-free dethiylation, and subsequently folded. This homogeneous erythropoietin glycosylated at the three wild-type aspartates with N-linked high-mannose sialic acid-containing oligosaccharides and O-linked glycophorin exhibits Procrit-level in vivo activity in mice.
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.