Evidence map›Paper›PMID 28921966›Full record

ArticleAnalytical chemistry2017

Tool for Rapid Analysis of Glycopeptide by Permethylation via One-Pot Site Mapping and Glycan Analysis.

Asif Shajahan, Nitin T Supekar, Christian Heiss, Mayumi Ishihara, Parastoo Azadi

Abstract read
In one paragraph

Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-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

17 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. The Hitchhiker's guide to glycoproteomics.Biochemical Society transactions · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Generation ofACS infectious diseases · 2019
    Article
  14. Article
  15. Review
  16. Article
  17. 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

5 authors at 1 institution in 1 country.

Asif ShajahanComplex Carbohydrate Research Center, The University of Georgia , 315 Riverbend Road, Athens, Georgia 30602, United States.ORCID 0000-0002-4804-1130
Nitin T SupekarComplex Carbohydrate Research Center, The University of Georgia , 315 Riverbend Road, Athens, Georgia 30602, United States.
Christian HeissComplex Carbohydrate Research Center, The University of Georgia , 315 Riverbend Road, Athens, Georgia 30602, United States.
Mayumi IshiharaComplex Carbohydrate Research Center, The University of Georgia , 315 Riverbend Road, Athens, Georgia 30602, United States.
Parastoo AzadiComplex Carbohydrate Research Center, The University of Georgia , 315 Riverbend Road, Athens, Georgia 30602, United States.
University of Georgia · US

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Orbitrap Fusion Tribrid Mass SpectrometerS10OD018530 · OD · UNIVERSITY OF GEORGIA · PI AZADI, PARASTOO · 2014 to 2014
$750k
Glycan linkage and sequence plus determination of site of glycosylation by permethylation of glycopeptides and MSn analysis in a one pot experimentR21GM122633 · NIGMS · UNIVERSITY OF GEORGIA · PI AZADI, PARASTOO · 2016 to 2017
$582k
NIGMS NIH HHS P41 GM103490NIGMS NIH HHS R21 GM122633NIH HHS S10 OD018530
6 · The paper itself

Abstract

To overcome the challenges in the analysis of protein glycosylation, we have developed a comprehensive and universal tool through permethylation of glycopeptides and their tandem mass spectrometric analysis. This method has the potential to simplify glycoprotein analysis by integrating glycan sequencing and glycopeptide analysis in a single experiment. Moreover, glycans with unique glycosidic linkages, particularly from prokaryotes, which are resistant to enzymatic or chemical release, could also be detected and analyzed by this methodology. Here we present a strategy for the permethylation of intact glycopeptides, obtained via controlled protease digest, and their characterization by using advanced mass spectrometry. We used bovine RNase B, human transferrin, and bovine fetuin as models to demonstrate the feasibility of the method. Remarkably, the glycan patterns, glycosylation site, and their occupancy by N-glycans are all detected and identified in a single experimental procedure. Acquisition on a high resolution tandem-MS

Indexed as

Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAmino AcidsAnimalsCarbohydrate SequenceCattleChromatography, High Pressure LiquidFetuinsGlycopeptidesGlycosylationHumansMethylationPolysaccharidesRibonucleasesTransferrinAmino AcidsFetuinsGlycopeptidesPolysaccharidesribonuclease BRibonucleasesTransferrin

Identifiers

PMID28921966
PMCPMC5973789
OpenAlexW2754475126

What OpenQuestion holds

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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.