Evidence map›Paper›PMID 28346930›Full record

ReviewNestle Nutrition Institute workshop series2017

Enzymes in Human Milk.

David C Dallas, J Bruce German

Abstract readReview
In one paragraph

Review in Nestle Nutrition Institute workshop series, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

10 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Monitoring Human Milk β-Casein Phosphorylation andInternational journal of molecular sciences · 2021
    Article
  4. Breast Milk: A Meal Worth Having.Frontiers in nutrition · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Milk Proteins Are Predigested Within the Human Mammary Gland.Journal of mammary gland biology and neoplasia · 2017
    Article
  9. Article
  10. 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

2 authors at 2 institutions in 1 country.

David C Dallas
J Bruce German
Oregon State University · USUniversity of California, Davis · US

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
Deciphering the function of naturally occurring peptides in human milkR00HD079561 · NICHD · OREGON STATE UNIVERSITY · PI DALLAS, DAVID CHARLES · 2016 to 2018
$741k
NCCIH NIH HHS R01 AT007079NCCIH NIH HHS R01 AT008759NICHD NIH HHS R00 HD079561
6 · The paper itself

Abstract

Milk proteins are a complex and diverse source of biological activities. Beyond their function, intact milk proteins also act as carriers of encrypted functional sequences that, when released as peptides, exert biological functions, including antimicrobial and immunomodulatory activity, which could contribute to the infant's competitive success. Research has now revealed that the release of these functional peptides begins within the mammary gland itself. A complex array of proteases produced in mother's milk has been shown to be active in the milk, releasing these peptides. Moreover, our recent research demonstrates that these milk proteases continue to digest milk proteins within the infant's stomach, possibly even to a larger extent than the infant's own proteases. As the neonate has relatively low digestive capacity, the activity of milk proteases in the infant may provide important assistance to digesting milk proteins. The coordinated release of these encrypted sequences is accomplished by selective proteolytic action provided by an array of native milk proteases and infant-produced enzymes. The task for scientists is now to discover the selective advantages of this protein-protease-based peptide release system.

Indexed as

DigestionFemaleHumansInfantInfant, NewbornInfant Nutritional Physiological PhenomenaMilk, HumanMilk ProteinsPeptide HydrolasesProteolysisMilk ProteinsPeptide Hydrolases

Identifiers

PMID28346930
PMCPMC5486212
OpenAlexW2600283041

What OpenQuestion holds

Textmetadata
LicenceTDM
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.