Evidence map›Paper›PMID 34360914›Full record

ArticleInternational journal of molecular sciences2021

Monitoring Human Milk β-Casein Phosphorylation and

Kelly A Dingess, Inge Gazi, Henk W P van den Toorn, Marko Mank, Bernd Stahl, Karli R Reiding, Albert J R Heck

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. 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
3.6field-weighted citation impact, top 7% 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, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Autochthonous Human MilkFood technology and biotechnology
    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

7 authors at 2 institutions in 1 country.

Kelly A DingessBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, 3584 CH Utrecht, The Netherlands.ORCID 0000-0002-0732-2868
Inge GaziBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, 3584 CH Utrecht, The Netherlands.
Henk W P van den ToornBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, 3584 CH Utrecht, The Netherlands.ORCID 0000-0002-0270-5763
Marko MankDanone Nutricia Research, 3584 CT Utrecht, The Netherlands.ORCID 0000-0001-7695-3906
Bernd StahlDanone Nutricia Research, 3584 CT Utrecht, The Netherlands.ORCID 0000-0002-8898-7107
Karli R ReidingBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, 3584 CH Utrecht, The Netherlands.ORCID 0000-0003-3695-5274
Albert J R HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, 3584 CH Utrecht, The Netherlands.
Utrecht University · NLDanone (Netherlands) · NL

Funding

Nederlandse Organisatie voor Wetenschappelijk Onderzoek 184.034.019Nederlandse Organisatie voor Wetenschappelijk Onderzoek 731.017.202Nederlandse Organisatie voor Wetenschappelijk Onderzoek VI.Veni.192.058
6 · The paper itself

Abstract

Human milk is a vital biofluid containing a myriad of molecular components to ensure an infant's best start at a healthy life. One key component of human milk is β-casein, a protein which is not only a structural constituent of casein micelles but also a source of bioactive, often antimicrobial, peptides contributing to milk's endogenous peptidome. Importantly, post-translational modifications (PTMs) like phosphorylation and glycosylation typically affect the function of proteins and peptides; however, here our understanding of β-casein is critically limited. To uncover the scope of proteoforms and endogenous peptidoforms we utilized mass spectrometry (LC-MS/MS) to achieve in-depth longitudinal profiling of β-casein from human milk, studying two donors across 16 weeks of lactation. We not only observed changes in β-casein's known protein and endogenous peptide phosphorylation, but also in previously unexplored

Indexed as

Breast FeedingCaseinsChromatography, LiquidFemaleGlycopeptidesGlycosylationHealthy VolunteersHumansInfantLactationLongitudinal StudiesMilk, HumanPhosphorylationProtein Processing, Post-TranslationalProteomeTandem Mass SpectrometryCaseinsGlycopeptidesProteomeantimicrobial peptideshuman milkmass spectrometryO-glycosylationpeptidomics

Identifiers

PMID34360914
PMCPMC8347866
OpenAlexW3184387038

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.