ArticleThe Journal of biological chemistry2010
The 1.5 Å crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding.
Article in The Journal of biological chemistry, 2010. 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 75 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.
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
75 citing papers in PubMed, 150 citations in OpenAlex.
- RAGE Signalling in Acute Inflammatory Disorders: Therapeutic Potential of Natural Products.Biomolecules · 2026Review
- Coconut Milk-Derived Bioactive Peptides as Multifunctional Agents Against Hyperglycemia, Oxidative Stress, and Glycation: An Integrated Experimental and Computational Study.International journal of molecular sciences · 2025Article
- Article
- Type 1 diabetes mellitus prevention: present and future.Nature reviews. Endocrinology · 2025Review
- Modulation of Aging Diseases via RAGE Targets: A Dietary Intervention Review.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Virtual Probing on the Influence of CaCell biochemistry and biophysics · 2025Article
- Diverse role of S100 calcium-binding protein B in alzheimer's disease: pathological mechanisms and therapeutic implications.Inflammopharmacology · 2025Review
- Investigating the Inhibitory Effects of Paliperidone on RAGEs: Docking, DFT, MD Simulations, MMPBSA, MTT, Apoptosis, and Immunoblotting Studies.International journal of molecular sciences · 2025Article
- Targeting the AGEs-RAGE axis: pathogenic mechanisms and therapeutic interventions in diabetic wound healing.Frontiers in medicine · 2025Review
- Understanding the interactions between repurposed drugs sertindole and temoporfin with receptor for advanced glycation endproducts: Therapeutic implications in cancer and metabolic diseases.Journal of molecular modeling · 2024Article
- Fructose-mediated AGE-RAGE axis: approaches for mild modulation.Frontiers in nutrition · 2024Review
- RAGE engagement by SARS-CoV-2 enables monocyte infection and underlies COVID-19 severity.Cell reports. Medicine · 2023Article
- Effect of β-amyloid on blood-brain barrier properties and function.Biophysical reviews · 2023Review
- Methylglyoxal-Modified Albumin Effects on Endothelial Arginase Enzyme and Vascular Function.Cells · 2023Article
- DNA binding and cleavage, BRCA1 gene interaction, antiglycation and anticancer studies of transition metal complexes of sulfonamides.Molecular diversity · 2022Article
- Docking and Molecular Dynamics-Based Identification of Interaction between Various Beta-Amyloid Isoforms and RAGE Receptor.International journal of molecular sciences · 2022Article
- Receptor for advanced glycation end-products (RAGE) mediates phagocytosis in nonprofessional phagocytes.Communications biology · 2022Article
- Advanced Glycation End Products (AGEs) and Chronic Kidney Disease: Does the Modern Diet AGE the Kidney?Nutrients · 2022Review
- Review
- Macrophage scavenger receptors: Tumor support and tumor inhibition.Frontiers in oncology · 2022Review
15 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issuedAdsit, Floyd G [added]
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Interaction of the pattern recognition receptor, RAGE with key ligands such as advanced glycation end products (AGE), S100 proteins, amyloid β, and HMGB1 has been linked to diabetic complications, inflammatory and neurodegenerative disorders, and cancer. To help answer the question of how a single receptor can recognize and respond to a diverse set of ligands we have investigated the structure and binding properties of the first two extracellular domains of human RAGE, which are implicated in various ligand binding and subsequent signaling events. The 1.5-Å crystal structure reveals an elongated molecule with a large basic patch and a large hydrophobic patch, both highly conserved. Isothermal titration calorimetry (ITC) and deletion experiments indicate S100B recognition by RAGE is an entropically driven process involving hydrophobic interaction that is dependent on Ca(2+) and on residues in the C'D loop (residues 54-67) of domain 1. In contrast, competition experiments using gel shift assays suggest that RAGE interaction with AGE is driven by the recognition of negative charges on AGE-proteins. We also demonstrate that RAGE can bind to dsDNA and dsRNA. These findings reveal versatile structural features of RAGE that help explain its ability to recognize of multiple ligands.
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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.