Evidence map›Paper›PMID 38470198›Full record

ArticleProteomics2024

Dysregulated proteome and N-glycoproteome in ALG1-deficient fibroblasts.

Rohit Budhraja, Neha Joshi, Silvia Radenkovic, Tamas Kozicz, Eva Morava, Akhilesh Pandey

Open access · hybridAbstract read
In one paragraph

Article in Proteomics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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

6 authors at 1 institution in 2 countries.

Rohit BudhrajaDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota, USA.ORCID 0000-0002-4209-2180
Neha JoshiDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota, USA.
Silvia RadenkovicDepartment of Clinical Genomics, Mayo Clinic, Rochester, Minnesota, USA.
Tamas KoziczDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota, USA.
Eva MoravaDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota, USA.
Akhilesh PandeyDepartment of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota, USA.ORCID 0000-0001-9943-6127
Mayo Clinic · US

Funding

Pilot and Feasibility CoreU54NS115198 · NINDS · MAYO CLINIC ROCHESTER · PI MORAVA-KOZICZ, EVA · 2019 to 2023
$8.2M
DBT-Wellcome Trust India Alliance IA/CRC/20/1/600002NINDS NIH HHS 1U54NS115198NINDS NIH HHS U54 NS115198Wellcome Trust DBT India Alliance IA/CRC/20/1/600002
6 · The paper itself

Abstract

Asparagine-linked glycosylation 1 protein is a β-1,4-mannosyltransferase, is encoded by the ALG1 gene, which catalyzes the first step of mannosylation in N-glycosylation. Pathogenic variants in ALG1 cause a rare autosomal recessive disorder termed as ALG1-CDG. We performed a quantitative proteomics and N-glycoproteomics study in fibroblasts derived from patients with one homozygous and two compound heterozygous pathogenic variants in ALG1. Several proteins that exhibited significant upregulation included insulin-like growth factor II and pleckstrin, whereas hyaluronan and proteoglycan link protein 1 was downregulated. These proteins are crucial for cell growth, survival and differentiation. Additionally, we observed a decrease in the expression of mitochondrial proteins and an increase in autophagy-related proteins, suggesting mitochondrial and cellular stress. N-glycoproteomics revealed the reduction in high-mannose and complex/hybrid glycopeptides derived from numerous proteins in patients explaining that defect in ALG1 has broad effects on glycosylation. Further, we detected an increase in several short oligosaccharides, including chitobiose (HexNAc

Indexed as

FibroblastsMannosyltransferasesProteomeProteomicsCongenital Disorders of GlycosylationGlycoproteinsGlycosylationHumansGlycoproteinsMannosyltransferasesProteomeALG1‐CDGbiomarkercongenital disorders of glycosylationglycoproteomicsLC‐MS/MSproteomics

Identifiers

PMID38470198
PMCPMC7616334
OpenAlexW4392703217

What Socratic 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 Socratic graph.