Receptor Activity-Modifying Protein 2
"Receptor Activity-Modifying Protein 2" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A receptor activity-modifying protein that heterodimerizes with CALCITONIN RECEPTOR-LIKE PROTEIN to form the ADRENOMEDULLIN RECEPTOR. In addition, an isoform of the ISLET AMYLOID POLYPEPTIDE RECEPTOR is formed from this protein dimerizing with the CALCITONIN RECEPTOR.
| Descriptor ID |
D058263
|
| MeSH Number(s) |
D12.776.476.024.414.200 D12.776.543.725.200
|
| Concept/Terms |
Receptor Activity-Modifying Protein 2- Receptor Activity-Modifying Protein 2
- Receptor Activity Modifying Protein 2
- Calcitonin-Receptor-Like Receptor Activity-Modifying Protein 2
- Calcitonin Receptor Like Receptor Activity Modifying Protein 2
|
Below are MeSH descriptors whose meaning is more general than "Receptor Activity-Modifying Protein 2".
Below are MeSH descriptors whose meaning is more specific than "Receptor Activity-Modifying Protein 2".
This graph shows the total number of publications written about "Receptor Activity-Modifying Protein 2" by people in this website by year, and whether "Receptor Activity-Modifying Protein 2" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2012 | 0 | 1 | 1 |
| 2015 | 1 | 0 | 1 |
| 2016 | 1 | 1 | 2 |
| 2017 | 1 | 0 | 1 |
| 2018 | 0 | 2 | 2 |
| 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "Receptor Activity-Modifying Protein 2" by people in Profiles.
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Molecular interaction of an antagonistic amylin analog with the extracellular domain of receptor activity-modifying protein 2 assessed by fluorescence polarization. Biophys Chem. 2020 12; 267:106477.
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Structure-function analyses reveal a triple ß-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design. J Biol Chem. 2018 10 12; 293(41):15840-15854.
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Probing the Mechanism of Receptor Activity-Modifying Protein Modulation of GPCR Ligand Selectivity through Rational Design of Potent Adrenomedullin and Calcitonin Gene-Related Peptide Antagonists. Mol Pharmacol. 2018 04; 93(4):355-367.
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N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity. Biochemistry. 2017 07 05; 56(26):3380-3393.
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Receptor Activity-modifying Proteins 2 and 3 Generate Adrenomedullin Receptor Subtypes with Distinct Molecular Properties. J Biol Chem. 2016 May 27; 291(22):11657-75.
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Calcitonin and Amylin Receptor Peptide Interaction Mechanisms: INSIGHTS INTO PEPTIDE-BINDING MODES AND ALLOSTERIC MODULATION OF THE CALCITONIN RECEPTOR BY RECEPTOR ACTIVITY-MODIFYING PROTEINS. J Biol Chem. 2016 Apr 15; 291(16):8686-700.
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Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor. Mol Cell. 2015 Jun 18; 58(6):1040-52.
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Bacterial expression and purification of a heterodimeric adrenomedullin receptor extracellular domain complex using DsbC-assisted disulfide shuffling. Protein Expr Purif. 2013 Mar; 88(1):107-13.