Evidence map›Paper›PMID 35764435›Full record

ArticleAnalytical chemistry2022

Optimized Glycopeptide Enrichment Method-It Is All About the Sauce.

David Morgenstern, Hila Wolf-Levy, Nili Tickotsky-Moskovitz, Itzik Cooper, Aron S Buchman, David A Bennett, Michal Schnaider Beeri, Yishai Levin

Open access · hybridAbstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  11. Article
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  13. Plasma/Serum Proteomics based on Mass Spectrometry.Protein and peptide letters · 2024
    Review
  14. Review
  15. Article
  16. 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 4 institutions in 2 countries.

David MorgensternThe de Botton Institute for Protein Profiling, Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
Hila Wolf-LevyThe de Botton Institute for Protein Profiling, Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
Nili Tickotsky-MoskovitzIcahn School of Medicine at Mount Sinai, Department of Psychiatry, New York, New York 10029, United States.
Itzik CooperThe Jospeh Sagol Neuroscience Center, Sheba Medical Center, Tel Hashomer 52621, Israel.
Aron S BuchmanRush Alzheimer's Research Center, Rush University, Chicago, Illinois 60612, United States.
David A BennettRush Alzheimer's Research Center, Rush University, Chicago, Illinois 60612, United States.
Michal Schnaider BeeriIcahn School of Medicine at Mount Sinai, Department of Psychiatry, New York, New York 10029, United States.
Yishai LevinThe de Botton Institute for Protein Profiling, Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0002-7279-0246
Weizmann Institute of Science · ILRush University · USSheba Medical Center · ILIcahn School of Medicine at Mount Sinai · US

Funding

EPIDEMIOLOGY OF NEURAL RESERVE AND NEUROBIOLOGY IN AGINGR01AG017917 · NIA · RUSH UNIVERSITY MEDICAL CENTER · PI BENNETT, DAVID ALAN · 2001 to 2023
$43.3M
Systemic and dietary advanced glycation end products in type 2 diabetes-related cognitive decline and incident dementia: effects on Alzheimer's pathology and cerebrovascular diseaseR01AG061093 · NIA · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI SCHNAIDER BEERI, MICHAL · 2019 to 2024
$4.3M
NIA NIH HHS R01 AG017917NIA NIH HHS R01 AG061093
6 · The paper itself

Abstract

Protein glycosylation is a family of posttranslational modifications that play a crucial role in many biological pathways and diseases. The enrichment and analysis of such a diverse family of modifications are very challenging because of the number of possible glycan-peptide combinations. Among the methods used for the enrichment of glycopeptides, boronic acid never lived up to its promise. While most studies focused on improving the affinity of the boronic acids to the sugars, we discovered that the buffer choice is just as important for successful enrichment if not more so. We show that an amine-less buffer allows for the best glycoproteomic coverage, in human plasma and brain specimens, improving total quantified glycopeptides by over 10-fold, and reaching 1598 N-linked glycopeptides in the brain and 737 in nondepleted plasma. We speculate that amines compete with the glycans for boronic acid binding, and therefore the elimination of them improved the method significantly.

Indexed as

GlycopeptidesProteomicsBoronic AcidsGlycosylationHumansPolysaccharidesBoronic AcidsGlycopeptidesPolysaccharides

Identifiers

PMID35764435
PMCPMC9330304
OpenAlexW4283696149

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.