Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The effects of C-terminal truncation of receptor activity modifying proteins on the induction of amylin receptor phenotype from human CTb receptors.

Regulatory peptides - 10 Jan 2008

Udawela Madhara, Christopoulos George, Morfis Maria, Tilakaratne Nanda, Christopoulos Arthur, Sexton Patrick M

Abstract excerpt

Receptor activity modifying proteins (RAMPs) interact with calcitonin receptors to produce novel amylin receptor phenotypes. We have recently demonstrated that the short intracellular C-terminus of RAMPs plays a key role in the function of amylin receptors derived from the CTa calcitonin receptor through the use of chimeric RAMPs and RAMPs that are truncated at the C-terminus [15, Udawela M, Christopoulos G,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP

Share to Glycosaminoglycans

Share to Islet Amyloid Polypeptide

Share to Receptors, Calcitonin

Share to Receptors, Peptide

Share to Salmon

Source

Identifiers

PMID: 17884192
DOI: 10.1016/j.regpep.2007.08.003

Genes

RAMP1
RAMP2
RAMP3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The effects of C-terminal truncation of receptor activity modifying proteins on the induction of amylin receptor phenotype from human CTb receptors.PMID 17884192Read ↗

A critical role for the short intracellular C terminus in receptor activity-modifying protein function.Semantic proximity Read ↗

Multiple ramp domains are required for generation of amylin receptor phenotype from the calcitonin receptor gene product.Semantic proximity Read ↗

Amylin receptor phenotypes derived from human calcitonin receptor/RAMP coexpression exhibit pharmacological differences dependent on receptor isoform and host cell environment.Semantic proximity Read ↗

Receptor activity modifying proteins.Semantic proximity Read ↗

Functions of the cytoplasmic tails of the human receptor activity-modifying protein components of calcitonin gene-related peptide and adrenomedullin receptors.Semantic proximity Read ↗

A structural basis for amylin receptor phenotype.Semantic proximity Read ↗

The extracellular domain of receptor activity-modifying protein 1 is sufficient for calcitonin receptor-like receptor function.Semantic proximity Read ↗

The seven amino acids of human RAMP2 (86) and RAMP3 (59) are critical for agonist binding to human adrenomedullin receptors.Semantic proximity Read ↗

Identification of an essential amino acid motif within the C terminus of the pituitary adenylate cyclase-activating polypeptide type I receptor that is critical for signal transduction but not for receptor internalization.Semantic proximity Read ↗

Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.Semantic proximity Read ↗

Amylin receptor subunit interactions are modulated by agonists and determine signalingSemantic proximity Read ↗

Methods to measure calcitonin receptor activity, up-regulated in cell stress, apoptosis and autophagySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.