Evidence map›Paper›PMID 33008897›Full record

ArticleScience advances2020

Integrative glycoproteomics reveals protein N-glycosylation aberrations and glycoproteomic network alterations in Alzheimer's disease.

Qi Zhang, Cheng Ma, Lih-Shen Chin, Lian Li

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

76 citing papers in PubMed, 116 citations in OpenAlex.

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16 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Qi ZhangDepartment of Pharmacology and Chemical Biology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, GA 30322, USA.ORCID 0000-0002-4536-273X
Cheng MaCenter for Diagnostics and Therapeutics, Department of Chemistry, Georgia State University, Atlanta, GA 30303, USA.ORCID 0000-0002-0017-2182
Lih-Shen ChinDepartment of Pharmacology and Chemical Biology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, GA 30322, USA. lli5@emory.edu lchin@emory.edu.ORCID 0000-0002-0817-0368
Lian LiDepartment of Pharmacology and Chemical Biology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, GA 30322, USA. lli5@emory.edu lchin@emory.edu.ORCID 0000-0003-4700-1134
Emory University · USGeorgia State University · US

Funding

The Goizueta Alzheimer's Disease Research CenterP30AG066511 · NIA · EMORY UNIVERSITY · PI Amy D Rodriguez · 2020 to 2026
$29.0M
The Emory Alzheimer's Disease CenterP50AG025688 · NIA · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2005 to 2019
$25.7M
ENNCF - Viral Vector CoreP30NS055077 · NINDS · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2008 to 2018
$6.8M
ALZHEIMER'S DISEASE PATHWAYS AND BIOMARKER DISCOVERY BY INTEGRATIVE PROTEOMICS, GLYCOPROTEOMICS, AND GLYCOMICSRF1AG057965 · NIA · EMORY UNIVERSITY · PI LI, LIAN · 2018 to 2018
$3.2M
NIA NIH HHS P30 AG066511NIA NIH HHS P50 AG025688NIA NIH HHS RF1 AG057965NINDS NIH HHS P30 NS055077
6 · The paper itself

Abstract

Protein N-glycosylation plays critical roles in controlling brain function, but little is known about human brain N-glycoproteome and its alterations in Alzheimer's disease (AD). Here, we report the first, large-scale, site-specific N-glycoproteome profiling study of human AD and control brains using mass spectrometry-based quantitative N-glycoproteomics. The study provided a system-level view of human brain N-glycoproteins and in vivo N-glycosylation sites and identified disease signatures of altered N-glycopeptides, N-glycoproteins, and N-glycosylation site occupancy in AD. Glycoproteomics-driven network analysis showed 13 modules of co-regulated N-glycopeptides/glycoproteins, 6 of which are associated with AD phenotypes. Our analyses revealed multiple dysregulated N-glycosylation-affected processes and pathways in AD brain, including extracellular matrix dysfunction, neuroinflammation, synaptic dysfunction, cell adhesion alteration, lysosomal dysfunction, endocytic trafficking dysregulation, endoplasmic reticulum dysfunction, and cell signaling dysregulation. Our findings highlight the involvement of N-glycosylation aberrations in AD pathogenesis and provide new molecular and system-level insights for understanding and treating AD.

Indexed as

Alzheimer DiseaseGlycopeptidesGlycoproteinsGlycosylationHumansProteomeProteomicsGlycopeptidesGlycoproteinsProteome

Identifiers

PMID33008897
PMCPMC7852392
OpenAlexW3090668577

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.