ReviewAmino acids2007
Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification.
Review in Amino acids, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 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
74 citing papers in PubMed, 146 citations in OpenAlex.
- Mutually exclusive pathways for biosynthesis of polyamine homospermidine dependent on putrescine or agmatine.The Journal of biological chemistry · 2026Article
- The arginase-polyamine signaling axis in immune cells: Implications for immune modulation and host-pathogen interactions.iScience · 2026Review
- A noncanonical polyamine from bacteria antagonizes host mitochondrial function.Nature communications · 2025Article
- Spermidine is a key polyamine required by intracellular parasites for survival within host erythrocytes.Science advances · 2025Article
- Optimal Reference Genes for Gene Expression Analysis of Overmating Stress-Induced Aging and Natural Aging in MaleInternational journal of molecular sciences · 2025Article
- Multi-omics analysis reveals the impact of YAP/TEAD4-mediated EIF5A1 expression on mitochondrial apoptosis and bladder cancer progression.BMC cancer · 2025Article
- DHPS-Mediated Hypusination Regulates METTL3 Self-m6A-Methylation Modification to Promote Melanoma Proliferation and the Development of Novel Inhibitors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Top-Down Proteomics of Mouse Islets With Beta Cell CPE Deletion Reveals Molecular Details in Prohormone Processing.Endocrinology · 2023Article
- Arginine metabolism regulates human erythroid differentiation through hypusination of eIF5A.Blood · 2023Article
- A genome-wide CRISPR functional survey of the human phagocytosis molecular machinery.Life science alliance · 2023Article
- Comparison of Human Eukaryotic Translation Initiation Factors 5A1 and 5AL1: Identification of Amino Acid Residues Important for EIF5A1 Lysine 50 Hypusination and Its Protein Stability.International journal of molecular sciences · 2023Article
- Eukaryotic Initiation Factor 5A2 localizes to actively translating ribosomes to promote cancer cell protrusions and invasive capacity.Cell communication and signaling : CCS · 2023Article
- Nutraceutical activation of Sirt1: a review.Open heart · 2022Review
- Article
- Spermidine-mediated hypusination of translation factor EIF5A improves mitochondrial fatty acid oxidation and prevents non-alcoholic steatohepatitis progression.Nature communications · 2022Article
- Bi-allelic variants in DOHH, catalyzing the last step of hypusine biosynthesis, are associated with a neurodevelopmental disorder.American journal of human genetics · 2022Article
- Post-translational formation of hypusine in eIF5A: implications in human neurodevelopment.Amino acids · 2022Review
- Nutraceutical and Dietary Strategies for Up-Regulating Macroautophagy.International journal of molecular sciences · 2022Review
- Role of eIF5A in Mitochondrial Function.International journal of molecular sciences · 2022Review
- Nonheme Diiron Oxygenase Mimic That Generates a Diferric-Peroxo Intermediate Capable of Catalytic Olefin Epoxidation and Alkane Hydroxylation Including Cyclohexane.Inorganic chemistry · 2022Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
A naturally occurring unusual amino acid, hypusine [N (epsilon)-(4-amino-2-hydroxybutyl)-lysine] is a component of a single cellular protein, eukaryotic translation initiation factor 5A (eIF5A). It is a modified lysine with structural contribution from the polyamine spermidine. Hypusine is formed in a novel posttranslational modification that involves two enzymes, deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). eIF5A and deoxyhypusine/hypusine modification are essential for growth of eukaryotic cells. The hypusine synthetic pathway has evolved in eukaryotes and eIF5A, DHS and DOHH are highly conserved, suggesting maintenance of a fundamental cellular function of eIF5A through evolution. The unique feature of the hypusine modification is the strict specificity of the enzymes toward its substrate protein, eIF5A. Moreover, DHS exhibits a narrow specificity toward spermidine. In view of the extraordinary specificity and the requirement for hypusine-containing eIF5A for mammalian cell proliferation, eIF5A and the hypusine biosynthetic enzymes present new potential targets for intervention in aberrant cell proliferation.
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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.