Evidence map›Paper›PMID 33227824›Full record

ArticleFEBS open bio2021

Asn-linked N-acetylglucosamine of the amylin receptor 2 extracellular domain enhances peptide ligand affinity.

Sangmin Lee

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS open bio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 45% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Investigation of the effects ofComputational & theoretical chemistry · 2023
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Sangmin LeeDepartment of Basic Pharmaceutical Sciences, Fred Wilson School of Pharmacy, High Point University, High Point, NC, USA.ORCID 0000-0002-7262-159X
High Point University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The calcitonin receptor (CTR) has a large extracellular domain (ECD) with multiple N-glycosylation sites. An asparagine (Asn)-linked N-acetylglucosamine (GlcNAc) of CTR ECD N130 was previously reported to enhance peptide hormone binding affinity for CTR ECD. CTR forms a complex with an accessory protein RAMP, and the RAMP:CTR complex gains affinity for peptide hormone amylin as the amylin receptor (AMY). Although N-glycosylation of AMY ECD was reported to enhance peptide hormone affinity, it remains underexplored which N-glycosites of AMY ECD are responsible for peptide affinity enhancement and it is unclear whether an Asn-linked GlcNAc of the N-glycosites plays a critical role. Here, I investigated the role of the Asn-linked GlcNAc of CTR N130 in the affinity of an antagonistic amylin analog (AC413) for AMY

Indexed as

AcetylglucosamineAsparagineGlycosylationHEK293 CellsHumansIslet Amyloid PolypeptideProtein DomainsReceptor Activity-Modifying Protein 2Receptors, CalcitoninAcetylglucosamineAsparagineIslet Amyloid PolypeptideRAMP2 protein, humanReceptor Activity-Modifying Protein 2Receptors, Calcitoninamylin receptorsAsn-linked N-acetylglucosaminefluorescence polarizationpeptide hormones

Identifiers

PMID33227824
PMCPMC7780097
OpenAlexW3110402671

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.