Evidence map›Paper›PMID 37929139›Full record

ArticleACS omega2023

In Vitro Glycosylation of the Membrane Protein γ-Sarcoglycan in Nanodiscs.

Michael S Harris, Rachel F Dolan, James R Bryce, Jonas G Ewusi, Gabriel A Cook

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. The Impact of Glycosylation on the Conformational Ensembles ofbioRxiv : the preprint server for biology · 2026
    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

5 authors at 1 institution in 1 country.

Michael S HarrisDepartment of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078, United States.
Rachel F DolanDepartment of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078, United States.
James R BryceDepartment of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078, United States.
Jonas G EwusiDepartment of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078, United States.
Gabriel A CookDepartment of Chemistry, Oklahoma State University, Stillwater, Oklahoma 74078, United States.ORCID https://orcid.org/0000-0002-3413-8361
Oklahoma State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane glycoproteins are proteins that reside in the membranes of cells and are post-translationally modified to have sugars attached to their amino acid side chains. Studies of this subset of proteins in their native states are becoming more important since they have been linked to numerous human diseases. However, these proteins are difficult to study due to their hydrophobic nature and their propensity to aggregate. Using membrane mimetics allows us to solubilize these proteins, which, in turn, allows us to perform glycosylation

Identifiers

PMID37929139
PMCPMC10620887
OpenAlexW4387807800

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.