Evidence map›Paper›PMID 36766105›Full record

ArticleFoods (Basel, Switzerland)2023

Molecular Recognition Patterns between Vitamin B12 and Proteins Explored through STD-NMR and In Silico Studies.

Ruchira Ghosh, Donald S Thomas, Jayashree Arcot

Abstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2023. 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
–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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

3 authors.

Ruchira GhoshFood and Health, School of Chemical Engineering, UNSW Sydney, Sydney, NSW 2052, Australia.ORCID 0000-0003-1227-1505
Donald S ThomasNMR Facility, UNSW Sydney, Sydney, NSW 2052, Australia.ORCID 0000-0002-0582-2084
Jayashree ArcotFood and Health, School of Chemical Engineering, UNSW Sydney, Sydney, NSW 2052, Australia.ORCID 0000-0002-4254-7288

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ligand-receptor molecular recognition is the basis of biological processes. The Saturation Transfer Difference-NMR (STD-NMR) technique has been recently used to gain qualitative and quantitative information about physiological interactions at an atomic resolution. The molecular recognition patterns between the cyanocobalamin (CNBL)/aqua cobalamin (OHBL) and different plant and animal proteins were investigated via STD-NMR supplemented by molecular docking. This study demonstrates that myoglobin has the highest binding affinity and that gluten has the lowest affinity. Casein also shows a higher binding affinity for cyanocobalamin when compared with that of plant-based proteins. STD-NMR results showed the moderate binding capability of casein with both CNBL and OHBL. Computer simulation confirmed the recognition mode in theory and was compared with the experiments. This work is beneficial for understanding the binding affinity and biological action of cyanocobalamin and will attract researchers to use NMR technology to link the chemical and physiological properties of nutrients.

Indexed as

aqua cobalamincyanocobalamininteractionmolecular dockingproteinsSTD–NMR

Identifiers

PMID36766105
PMCPMC9914923

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.