Evidence map›Paper›PMID 35975046›Full record

ArticleRSC advances2022

Zinc binding strength of proteins dominants zinc uptake in Caco-2 cells.

Tian Li, Ruonan Jiao, Jiaqi Ma, Jiachen Zang, Guanghua Zhao, Tuo Zhang

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Synergistic effects ofFrontiers in nutrition · 2026
    Article
  4. Article
  5. Influence of divalent metal cations on α-lactalbumin fibril formation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  6. 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 1 institution in 1 country.

Tian LiCollege of Food Science and Nutritional Engineering, Key Laboratory of Precision Nutrition and Food Quality, Ministry of Education, China Agricultural University Beijing 100083 China tuozhang@cau.edu.cn.
Ruonan JiaoCollege of Food Science and Nutritional Engineering, Key Laboratory of Precision Nutrition and Food Quality, Ministry of Education, China Agricultural University Beijing 100083 China tuozhang@cau.edu.cn.
Jiaqi MaCollege of Food Science and Nutritional Engineering, Key Laboratory of Precision Nutrition and Food Quality, Ministry of Education, China Agricultural University Beijing 100083 China tuozhang@cau.edu.cn.
Jiachen ZangCollege of Food Science and Nutritional Engineering, Key Laboratory of Precision Nutrition and Food Quality, Ministry of Education, China Agricultural University Beijing 100083 China tuozhang@cau.edu.cn.ORCID https://orcid.org/0000-0003-0566-9726
Guanghua ZhaoCollege of Food Science and Nutritional Engineering, Key Laboratory of Precision Nutrition and Food Quality, Ministry of Education, China Agricultural University Beijing 100083 China tuozhang@cau.edu.cn.ORCID https://orcid.org/0000-0001-8587-9680
Tuo ZhangCollege of Food Science and Nutritional Engineering, Key Laboratory of Precision Nutrition and Food Quality, Ministry of Education, China Agricultural University Beijing 100083 China tuozhang@cau.edu.cn.ORCID https://orcid.org/0000-0002-0900-9285
China Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Zinc plays a vital role in structural, catalysis, and signal regulation in the human body. Zinc deficiency leads to the dysfunction of many organs and immunity systems. Diet proteins have distinct effects on zinc uptake. However, the mechanisms are uncovered. Here we select three principal components from whey protein: alpha-lactalbumin, beta-lactoglobulin, and bovine serum albumin, which bind with zinc at different affinities, to evaluate the relationship between their potential zinc uptake and protein binding. The experimental data shows that beta-lactoglobulin could promote zinc uptake, alpha-lactalbumin has minor effects, whereas bovine serum albumin reduced zinc uptake in Caco-2 cell lines. Zinc binding effects on protein structure were thoroughly inspected through fluorescent spectroscopy and X-ray crystallography. Isothermal titration calorimetry revealed that three proteins have different binding affinities toward zinc ions. We speculate that protein binding eliminates toxic effects from free zinc, and the binding strength dominates zinc uptake.

Identifiers

PMID35975046
PMCPMC9341287
OpenAlexW4289323728

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.