ReviewAdvances in pharmacology (San Diego, Calif.)2020
RAMPs as allosteric modulators of the calcitonin and calcitonin-like class B G protein-coupled receptors.
Review in Advances in pharmacology (San Diego, Calif.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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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
32 citing papers in PubMed, 50 citations in OpenAlex.
- Integration of Multi-Omics Data To Understand the Multifaceted Role of RAMP1 across Different Cancer Types.Cell biochemistry and biophysics · 2026Review
- Intrathecal amylin reverses morphine tolerance through site-specific DNA methylation of Pdyn and Bdnf promoters in rats.Scientific reports · 2026Article
- Expression ofbioRxiv : the preprint server for biology · 2026Article
- The calcitonin receptor controls osteophyte formation, but not cartilage degeneration and subchondral bone loss in experimental osteoarthritis.Bone & joint research · 2026Article
- Temporal regulation of macrophage polarization by abnormally innervated CGRP + Sensory nerves following spinal cord injury.Cellular and molecular life sciences : CMLS · 2026Review
- Structural and mechanistic insights into dual activation of cagrilintide in amylin and calcitonin receptors.Acta pharmacologica Sinica · 2026Article
- CGRP: the immune system's double agent - context-dependent roles in inflammation, resolution and cancer.Frontiers in immunology · 2026Review
- Biased Allosteric Modulation in GPCR Drug Discovery.Handbook of experimental pharmacology · 2026Review
- Modeling cryo-EM structures in alternative states with AlphaFold2-based models and density-guided simulations.Communications chemistry · 2025Article
- In Vitro and In Vivo Characterization of 40 kDa PEGylated Adrenomedullin in a DSS-Induced Colitis Model.International journal of molecular sciences · 2025Article
- Distinctive biochemical properties of the μ-opioid receptor-corticotropin- releasing factor CRFPharmacological research · 2025Article
- Amylin receptor subunit interactions are modulated by agonists and determine signaling.Science signaling · 2025Article
- Characterization of the Two-Domain Peptide Binding Mechanism of the Human CGRP Receptor for CGRP and the Ultrahigh Affinity ssCGRP Variant.Biochemistry · 2025Article
- Intracellular GPCR modulators enable precision pharmacology.npj drug discovery · 2025Review
- Article
- Variable CGRP family peptide signaling durations and the structural determinants thereof.Biochemical pharmacology · 2024Article
- Article
- Receptor activity-modifying protein modulation of parathyroid hormone-1 receptor function and signaling.Frontiers in pharmacology · 2024Article
- Flexible Topology: A Dynamic Model of a Continuous Chemical Space.Journal of chemical theory and computation · 2023Article
- Characterization of serotonin-5-HTR1E signaling pathways and its role in cell survival.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Receptor activity-modifying proteins (RAMPs) are a family of three single span transmembrane proteins in humans that interact with many GPCRs and can modulate their function. RAMPs were discovered as key components of the calcitonin gene-related peptide and adrenomedullin receptors. They are required for transport of this class B GPCR, calcitonin receptor-like receptor (CLR), to the cell surface and determine its peptide ligand binding preferences. Soon thereafter RAMPs were shown to modulate the binding of calcitonin and amylin peptides to the related calcitonin receptor (CTR) and in the years since an ever-growing number of RAMP-interacting receptors have been identified including most if not all of the 15 class B GPCRs and several GPCRs from other families. Studies of CLR, CTR, and a handful of other GPCRs revealed that RAMPs are able to modulate various aspects of receptor function including trafficking, ligand binding, and signaling. Here, we review RAMP interactions and functions with an emphasis on class B receptors for which our understanding is most advanced. A key focus is to discuss recent evidence that RAMPs serve as endogenous allosteric modulators of CLR and CTR. We discuss structural studies of RAMP-CLR complexes and CTR and biochemical and pharmacological studies that collectively have significantly expanded our understanding of the mechanistic basis for RAMP modulation of these class B GPCRs. Last, we consider the implications of these findings for drug development targeting RAMP-CLR/CTR complexes.
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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.