ArticleNature communications2022
Structural basis for assembly and disassembly of the IGF/IGFBP/ALS ternary complex.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 32 citations in OpenAlex.
- Engineering human multi-organ tissue chip niches for drug absorption, distribution, metabolism, excretion and toxicity prediction.Nature biomedical engineering · 2026Review
- Review
- Insulin-like growth factor receptor signaling in physiology and disease.Signal transduction and targeted therapy · 2026Review
- Programmable Paracrine-Mimetic Microneedle System for Temporal Regulation of Cardiac Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Bioactive IGF-I Concentrations in Children on GH Therapy.The Journal of clinical endocrinology and metabolism · 2026Article
- Perinatal liver sympathetic innervation governs body size.Communications biology · 2026Article
- Endocrine Implications of Congenital Disorders of GlycosylationJournal of clinical research in pediatric endocrinology · 2026Review
- Molecular Survival Strategies Against Kidney Filtration: Implications for Therapeutic Protein Engineering.Biophysica · 2026Article
- A Functional Shift of IGFBP3 in Osteoarthritis: From Cartilage Protection to Disease Promotion.Journal of inflammation research · 2026Review
- The Influence of Different Light Spectra on Broiler Chicken Endocrine Systems and Productivity.Animals : an open access journal from MDPI · 2025Review
- Pathologic Signaling and Disease Implications of Insulin-like Growth Factor Binding Proteins in Cancer, Cardiovascular Disease, and Fibrosis.International journal of molecular sciences · 2025Review
- Potential of growth factors and steroid hormones from cell cultures to improveOpen veterinary journal · 2025Review
- Regulation and function of insulin and insulin-like growth factor receptor signalling.Nature reviews. Molecular cell biology · 2025Review
- N-acetylglucosaminyltransferase V attenuates myocardial infarction by mediating the insulin-like growth factor 1 receptor signaling pathway.Journal of translational internal medicine · 2025Article
- Interactions between androgen and IGF1 axes in prostate tumorigenesis.Nature reviews. Urology · 2025Review
- Phyllostachyos Caulis in Taeniam extract stimulates longitudinal bone growth via IGF-1 and JAK2/STAT5 signaling in rats.PloS one · 2025Article
- Paraneoplastic hypoglycemia: An overview for optimal clinical guidance.Metabolism open · 2024Review
- Homozygous 6-bp deletion of IGFALS in a prepubertal boy with short stature.Human genome variation · 2024Article
- Endocrine and cellular physiology and pathology of the insulin-like growth factor acid-labile subunit.Nature reviews. Endocrinology · 2024Review
- The Effects of Natural Product-Derived Extracts for Longitudinal Bone Growth: An Overview of In Vivo Experiments.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insulin-like growth factors (IGFs) have pleiotropic roles in embryonic and postnatal growth and differentiation. Most serum IGFs are bound in a ternary complex with IGF-binding protein 3 (IGFBP3) and acid-labile subunit (ALS), extending the serum half-life of IGFs and regulating their availability. Here, we report cryo-EM structure of the human IGF1/IGFBP3/ALS ternary complex, revealing the detailed architecture of a parachute-like ternary complex and crucial determinants for their sequential and specific assembly. In vitro biochemical studies show that proteolysis at the central linker domain of IGFBP3 induces release of its C-terminal domain rather than IGF1 release from the ternary complex, yielding an intermediate complex that enhances IGF1 bioavailability. Our results provide mechanistic insight into IGF/IGFBP3/ALS ternary complex assembly and its disassembly upon proteolysis for IGF bioavailability, suggesting a structural basis for human diseases associated with IGF1 and IGFALS gene mutations such as complete ALS deficiency (ACLSD) and IGF1 deficiency.
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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.