Evidence map›Paper›PMID 41000156›Full record

ArticleBio-protocol2025

Verification of N-Linked Glycosylation of Proteins Isolated from Plant or Mammalian Cell Lines Using PNGase Enzyme.

Wuqiang Hong, Cong Lei, Yahong Qiu, Yilan Zhou, Yili Hu, Xing Chen, Xilong Li, Jiayang Li

Abstract read
In one paragraph

Article in Bio-protocol, 2025. 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
–field-weighted citation impact
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.

  1. Review
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

8 authors.

Wuqiang HongYazhouwan National Laboratory, Sanya, China.
Cong LeiCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Yahong QiuYazhouwan National Laboratory, Sanya, China.
Yilan ZhouYazhouwan National Laboratory, Sanya, China.
Yili HuYazhouwan National Laboratory, Sanya, China.
Xing ChenCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Xilong LiYazhouwan National Laboratory, Sanya, China.
Jiayang LiYazhouwan National Laboratory, Sanya, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-glycosylation is a ubiquitous post-translational modification (PTM) that regulates protein folding, stability, and biological function. Accurate identification and validation of N-glycosylation are therefore critical for understanding how glycosylation modulates protein activity. Here, we present a robust workflow for analyzing protein N-glycosylation in both animal and plant systems using peptide-

Indexed as

DeglycosylationEnzymatic assayMW shiftPNGase APNGase FWB

Identifiers

PMID41000156
PMCPMC12457834

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.