Evidence map›Paper›PMID 22136231›Full record

ArticleJournal of proteome research2012

Mapping N-linked glycosylation sites in the secretome and whole cells of Aspergillus niger using hydrazide chemistry and mass spectrometry.

Lu Wang, Uma K Aryal, Ziyu Dai, Alisa C Mason, Matthew E Monroe, Zhi-Xin Tian, Jian-Ying Zhou, Dian Su, Karl K Weitz, Tao Liu and 4 more

Abstract read
In one paragraph

Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

23 citing papers in PubMed, 68 citations in OpenAlex.

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  6. Biochemical properties of a native β-1,4-mannanase fromBiochemistry and biophysics reports · 2021
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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

14 authors at 2 institutions in 1 country.

Lu WangBiological Science Division, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.
Uma K Aryal
Ziyu Dai
Alisa C Mason
Matthew E Monroe
Zhi-Xin Tian
Jian-Ying Zhou
Dian Su
Karl K Weitz
Tao Liu
David G Camp
Richard D Smith
Scott E Baker
Wei-Jun Qian
Environmental Molecular Sciences Laboratory · USPacific Northwest National Laboratory · US

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2003 to 2011
$25.1M
NCRR NIH HHS P41 RR018522NCRR NIH HHS RR18522
6 · The paper itself

Abstract

Protein glycosylation (e.g., N-linked glycosylation) is known to play an essential role in both cellular functions and secretory pathways; however, our knowledge of in vivo N-glycosylated sites is very limited for the majority of fungal organisms including Aspergillus niger. Herein, we present the first extensive mapping of N-glycosylated sites in A. niger by applying an optimized solid phase glycopeptide enrichment protocol using hydrazide-modified magnetic beads. The enrichment protocol was initially optimized using both mouse blood plasma and A. niger secretome samples, and it was demonstrated that the protein-level enrichment protocol offered superior performance over the peptide-level protocol. The optimized protocol was then applied to profile N-glycosylated sites from both the secretome and whole cell lysates of A. niger. A total of 847 N-glycosylated sites from 330 N-glycoproteins (156 proteins from the secretome and 279 proteins from whole cells) were confidently identified by LC-MS/MS. The identified N-glycoproteins in the whole cell lysate were primarily localized in the plasma membrane, endoplasmic reticulum, Golgi apparatus, lysosome, and storage vacuoles, supporting the important role of N-glycosylation in the secretory pathways. In addition, these glycoproteins are involved in many biological processes including gene regulation, signal transduction, protein folding and assembly, protein modification, and carbohydrate metabolism. The extensive coverage of N-glycosylated sites and the observation of partial glycan occupancy on specific sites in a number of enzymes provide important initial information for functional studies of N-linked glycosylation and their biotechnological applications in A. niger.

Indexed as

Peptide MappingAmino Acid SequenceAnimalsAspergillus nigerBlood ProteinsFungal ProteinsGlycoproteinsGlycosylationHydrazinesMiceMolecular Sequence DataProtein Processing, Post-TranslationalSolid Phase ExtractionTandem Mass SpectrometryBlood ProteinsFungal ProteinsGlycoproteinsHydrazines

Identifiers

PMID22136231
PMCPMC6752052
OpenAlexW2077065650

What OpenQuestion holds

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LicenceTDM
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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.