Evidence map›Paper›PMID 37397928›Full record

ReviewToxicology research2023

Interaction of mercury species with proteins: towards possible mechanism of mercurial toxicology.

Sharmin Akther Rupa, Md Abdul Majed Patwary, Mohammed Mahbubul Matin, William Emmanuel Ghann, Jamal Uddin, Mohsin Kazi

Abstract readReview
In one paragraph

Review in Toxicology research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Mercury toxicity resulting from enzyme alterations- minireview.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
    Review
  8. 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.

Sharmin Akther RupaDepartment of Chemistry, Comilla University, Cumilla 3506, Bangladesh.
Md Abdul Majed PatwaryDepartment of Chemistry, Comilla University, Cumilla 3506, Bangladesh.ORCID https://orcid.org/0000-0003-4680-957X
Mohammed Mahbubul MatinDepartment of Chemistry, University of Chittagong, Chittagong 4331, Bangladesh.
William Emmanuel GhannCenter for Nanotechnology, Department of Natural Sciences, Coppin State University, Baltimore, MD 21216, USA.
Jamal UddinCenter for Nanotechnology, Department of Natural Sciences, Coppin State University, Baltimore, MD 21216, USA.
Mohsin KaziDepartment of Pharmaceutics, College of Pharmacy, King Saud University, P.O. BOX-2457, Riyadh 11451, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nature of the binding of mercurials (organic and inorganic) and their subsequent transformations in biological systems is a matter of great debate as several different hypotheses have been proposed and none of them has been conclusively proven to explain the characteristics of Hg binding with the proteins. Thus, the chemical nature of Hg-protein binding through the possible transportation mechanism in living tissues is critically reviewed herein. Emphasis is given to the process of transportation, and binding of Hg species with selenol-containing biomolecules that are appealing for toxicological studies as well as the advancement of environmental and biological research.

Indexed as

mercurymethylmercuryproteinseleniumtoxicology

Identifiers

PMID37397928
PMCPMC10311172

What OpenQuestion holds

Textmetadata
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.