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

Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.

Biochimica et biophysica acta - 28 May 2001

Kamitani S, Sakata T

Abstract excerpt

Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3. RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and...

Read the complete abstract on PubMed

Topics

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

Share to Calcitonin Gene-Related Peptide
Share to Cyclic AMP
Share to Glycosylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Peptides

Share to Receptors, Calcitonin

Share to Receptors, Peptide

Share to Tunicamycin

Source

Identifiers

PMID: 11389975
DOI: 10.1016/s0167-4889(01)00100-8

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

Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.PMID 11389975Read ↗

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

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

N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.Semantic proximity Read ↗

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

Receptor activity modifying proteins.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 ↗

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

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

N-glycosylation of the human neuropeptide QRFP receptor (QRFPR) is essential for ligand binding and receptor activation.Semantic proximity Read ↗

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

N-linked glycosylation of protease-activated receptor-1 second extracellular loop: a critical determinant for ligand-induced receptor activation and internalization.Semantic proximity Read ↗

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