Evidence map›Paper›PMID 28425960›Full record

ReviewInternational journal of molecular sciences2017

Studying Lactoferrin N-Glycosylation.

Sercan Karav, J Bruce German, Camille Rouquié, Annabelle Le Parc, Daniela Barile

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
–field-weighted citation impact
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

76 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Metal uptake systems underpinInfection and immunity · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Lactoferrin: Properties and Potential Uses in the Food Industry.International journal of molecular sciences · 2025
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review

16 more citing papers are in PubMed but not listed here.

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.

Sercan KaravDepartment of Molecular Biology and Genetics, Canakkale Onsekiz Mart University, 17100 Canakkale, Turkey. sercankarav@gmail.com.
J Bruce GermanDepartment of Food Science and Technology, University of California, One Shields Avenue, Davis, CA 95616, USA. jbgerman@ucdavis.edu.
Camille RouquiéDepartment of Food Science and Technology, University of California, One Shields Avenue, Davis, CA 95616, USA. camille.rouquie@hotmail.fr.
Annabelle Le ParcDepartment of Food Science and Technology, University of California, One Shields Avenue, Davis, CA 95616, USA. alebouedec@prolacta.com.
Daniela BarileDepartment of Food Science and Technology, University of California, One Shields Avenue, Davis, CA 95616, USA. dbarile@ucdavis.edu.

Funding

Activation of probiotic bifidobacteria by milk glyansR01AT008759 · NCCIH · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERMAN, BRUCE, LEBRILLA, CARLITO B · 2014 to 2018
$4.2M
Mechanism of Activation of Probiotic Bifidobacteria by Prebiotic Milk GlycansR01AT007079 · NCCIH · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERMAN, BRUCE, LEBRILLA, CARLITO B · 2012 to 2016
$2.2M
NCCIH NIH HHS R01 AT007079NCCIH NIH HHS R01 AT008759
6 · The paper itself

Abstract

Lactoferrin is a multifunctional glycoprotein found in the milk of most mammals. In addition to its well-known role of binding iron, lactoferrin carries many important biological functions, including the promotion of cell proliferation and differentiation, and as an anti-bacterial, anti-viral, and anti-parasitic protein. These functions differ among lactoferrin homologs in mammals. Although considerable attention has been given to the many functions of lactoferrin, its primary nutritional contribution is presumed to be related to its iron-binding characteristics, whereas the role of glycosylation has been neglected. Given the critical role of glycan binding in many biological processes, the glycan moieties in lactoferrin are likely to contribute significantly to the biological roles of lactoferrin. Despite the high amino acid sequence homology in different lactoferrins (up to 99%), each exhibits a unique glycosylation pattern that may be responsible for heterogeneity of the biological properties of lactoferrins. An important task for the production of biotherapeutics and medical foods containing bioactive glycoproteins is the assessment of the contributions of individual glycans to the observed bioactivities. This review examines how the study of lactoferrin glycosylation patterns can increase our understanding of lactoferrin functionality.

Indexed as

AnimalsGlycoproteinsGlycosylationHumansLactoferrinMass SpectrometryMilk ProteinsPolysaccharidesProtein IsoformsProtein Processing, Post-TranslationalProtein StabilityGlycoproteinsLactoferrinMilk ProteinsPolysaccharidesProtein Isoformsbioinfomatic librariesdeglycosylating enzymeslactoferrinmass spectrophotometryN-glycansstructure-activity studies

Identifiers

PMID28425960
PMCPMC5412451

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.