Evidence map›Paper›PMID 23053637›Full record

ArticleGlycoconjugate journal2013

Characterization of N- and O-linked glycosylation changes in milk of the tammar wallaby (Macropus eugenii) over lactation.

Katherine Wongtrakul-Kish, Daniel Kolarich, Dana Pascovici, Janice L Joss, Elizabeth Deane, Nicolle H Packer

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Article in Glycoconjugate journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Trial
  2. Review
  3. State-of-the-Art Glycomics Technologies in Glycobiotechnology.Advances in biochemical engineering/biotechnology · 2021
    Article
  4. 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

6 authors at 2 institutions in 2 countries.

Katherine Wongtrakul-KishBiomolecular Frontiers Research Centre, Department of Chemistry and Biomolecular Sciences, Macquarie University, Building E8C, Room 307, North Ryde, NSW 2109, Australia.
Daniel Kolarich
Dana Pascovici
Janice L Joss
Elizabeth Deane
Nicolle H Packer
Macquarie University · AUAustralian Genome Research Facility · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As one of several biologically active compounds in milk, glycoproteins have been indicated to be involved in the protection of newborns from bacterial infection. As much of the physical and immune development of the tammar wallaby (Macropus eugenii) young occurs during the early phases of lactation and not in utero, the tammar is a model species for the characterization of potential developmental support agents provided by maternal milk.In the present study, the N- and O-linked glycans from tammar wallaby milk glycoproteins from six individuals at different lactation time points were subjected to glycomics analyses using porous graphitized carbon liquid chromatography electrospray ionization mass spectrometry. Structural characterization identified a diverse range of glycan structures on wallaby milk glycoproteins including sialylated, sulphated, core fucosylated and O-fucosylated structures. 30 % of N-linked structures contained a core (α1-6) fucose. Several of these structures may play roles in development, and exhibit statistically significant temporal changes over the lactation period. The N-glycome was found to contain structures with NeuGc residues, while in contrast the O-glycome did not. O-fucosylated structures were identified in the early stages of lactation indicating a potential role in the early stages of development of the pouch young. Overall the results suggest that wallaby milk contains structures known to have developmental and immunological significance in human milk and reproduction in other animals, highlighting the importance of glycoproteins in milk.

Indexed as

GlycomicsAnimalsAnimals, NewbornCarbohydrate SequenceChromatography, LiquidFemaleGlycosylationHumansInfant, NewbornLactationMacropodidaeMilkMilk ProteinsMolecular Sequence DataPolysaccharidesSpectrometry, Mass, Electrospray IonizationMilk ProteinsPolysaccharides

Identifiers

PMID23053637
OpenAlexW2035428261

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Registered trials

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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.