Evidence map›Paper›PMID 33182731›Full record

ArticleBioengineering (Basel, Switzerland)2020

Comparison of Three Glycoproteomic Methods for the Analysis of the Secretome of CHO Cells Treated with 1,3,4-

Joseph L Mertz, Shisheng Sun, Bojiao Yin, Yingwei Hu, Rahul Bhattacharya, Michael J Bettenbaugh, Kevin J Yarema, Hui Zhang

Open access · goldAbstract read
In one paragraph

Article in Bioengineering (Basel, Switzerland), 2020. 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
0.3field-weighted citation impact, top 45% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. 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 at 1 institution in 1 country.

Joseph L MertzWilmer Eye Institute, Johns Hopkins University, Baltimore, MD 21287, USA.
Shisheng SunDepartment of Pathology, Johns Hopkins University, Baltimore, MD 21287, USA.
Bojiao YinDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.
Yingwei HuDepartment of Pathology, Johns Hopkins University, Baltimore, MD 21287, USA.ORCID 0000-0002-4629-0985
Rahul BhattacharyaDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.
Michael J BettenbaughDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.
Kevin J YaremaDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.
Hui ZhangDepartment of Pathology, Johns Hopkins University, Baltimore, MD 21287, USA.ORCID 0000-0001-8726-7098
Johns Hopkins University · US

Funding

Probing the Connections between Monosaccharide Analogs, Sialic Acid Metabolism, aR01CA112314 · NCI · JOHNS HOPKINS UNIVERSITY · PI YAREMA, KEVIN J · 2005 to 2022
$4.5M
OPTIMIZING THE PRE-CLINICAL DEVELOPMENT OF IMMUNOTHERAPEUTIC ANTIBODIES THROUGH GLYCOENGINEERINGR21CA249381 · NCI · JOHNS HOPKINS UNIVERSITY · PI SPANGLER, JAMIE BERTA, YAREMA, KEVIN J · 2020 to 2021
$410k
Division of Chemical, Bioengineering, Environmental, and Transport Systems CBET 1512265NCI NIH HHS R01 CA112314NCI NIH HHS R21 CA249381NIH HHS R01CA112314NIH HHS R21CA249381
6 · The paper itself

Abstract

Comprehensive analysis of the glycoproteome is critical due to the importance of glycosylation to many aspects of protein function. The tremendous complexity of this post-translational modification, however, makes it difficult to adequately characterize the glycoproteome using any single method. To overcome this pitfall, in this report we compared three glycoproteomic analysis methods; first the recently developed N-linked glycans and glycosite-containing peptides (NGAG) chemoenzymatic method, second, solid-phase extraction of N-linked glycoproteins (SPEG), and third, hydrophilic interaction liquid chromatography (HILIC) by characterizing N-linked glycosites in the secretome of Chinese hamster ovary (CHO) cells. Interestingly, the glycosites identified by SPEG and HILIC overlapped considerably whereas NGAG identified many glycosites not observed in the other two methods. Further, utilizing enhanced intact glycopeptide identification afforded by the NGAG workflow, we found that the sugar analog 1,3,4-

Indexed as

1,3,4-O-Bu3ManNAcCHOglycoproteomicssialylation

Identifiers

PMID33182731
PMCPMC7712478
OpenAlexW3104830341

What OpenQuestion 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 OpenQuestion graph.