Evidence map›Paper›PMID 41843583›Full record

ArticleAnalytical chemistry2026

Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk between Glycosylation and Phosphorylation in EGF Signaling Pathways.

Hongyi Liu, Ding Chiao Lin, Yingwei Hu, Zhenyu Sun, Yuanyu Huang, Yuanwei Xu, Hui Zhang

Abstract read
In one paragraph

Article in Analytical chemistry, 2026. 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
–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

2 citing papers in PubMed.

  1. Article
  2. 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

7 authors.

Hongyi LiuDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0002-9444-3632
Ding Chiao LinDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.
Yingwei HuDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0002-4629-0985
Zhenyu SunDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0009-0002-5004-5904
Yuanyu HuangDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0009-0002-5930-8424
Yuanwei XuDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.
Hui ZhangDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, United States.ORCID 0000-0001-8726-7098

Funding

Proteogenomic Characterization of Tumor Tissues and Preclinical Models with High PrecisionU24CA271079 · NCI · JOHNS HOPKINS UNIVERSITY · PI DANIEL Wanyui CHAN, Hui Zhang · 2022 to 2026
$6.6M
Biomarker Reference LaboratoryU2CCA271895 · NCI · JOHNS HOPKINS UNIVERSITY · PI DANIEL Wanyui CHAN · 2023 to 2026
$4.6M
Development of a panel of multiplex biomarkers for the early detection of pancreatic ductal adenocarcinoma and high-risk lesionsU01CA274514 · NCI · JOHNS HOPKINS UNIVERSITY · PI Randall Brand, DANIEL Wanyui CHAN · 2023 to 2026
$3.2M
NCI NIH HHS U01 CA274514NCI NIH HHS U24 CA271079NCI NIH HHS U2C CA271895
6 · The paper itself

Abstract

Protein glycosylation and phosphorylation play critical roles in regulating diverse cellular processes, yet their interplay remains underexplored. This study employed dose-dependent glycosylation inhibition to investigate the function of glycosylation, especially in phosphorylation in epidermal growth factor (EGF) signaling. Using quantitative proteomics, we analyzed global protein expression, glycopeptides, and phosphopeptides in EGF-stimulated and unstimulated conditions. Results revealed that glycosylation inhibition disrupted phosphorylation patterns in EGF-regulated pathways. Notably, 215 EGF-regulated phosphopeptides exhibited dose-dependent changes, with pathways such as ERBB, MAPK, and mTOR signaling being significantly affected. Protein-protein interaction analysis highlighted glycosylation-dependent modulation of phosphorylation in cytoskeletal remodeling and growth factor signaling. Correlation analysis identified site-specific glycopeptides, such as Asn568 of EGFR, that influenced phosphorylation of downstream signaling proteins. Additionally, individual proteins like RCN1 and SLC4A7 demonstrated glycosylation- and phosphorylation-regulated patterns. These findings underscored the role of glycosylation in maintaining phosphorylation-dependent signaling fidelity, providing insights into the function of glycosylation on cell signaling pathways.

Indexed as

Epidermal Growth FactorSignal TransductionGlycosylationHumansPhosphorylationProteomicsEpidermal Growth Factor

Identifiers

PMID41843583
PMCPMC13044880

What Socratic 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 Socratic graph.