Evidence map›Paper›PMID 22574219›Full record

ArticlePloS one2012

Locating the binding sites of Pb(II) ion with human and bovine serum albumins.

Ahmed Belatik, Surat Hotchandani, Robert Carpentier, Heidar-Ali Tajmir-Riahi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Exploring biochemical considerations for diffusive alpha radiation therapy (DaRT) models.Physica medica : PM : an international journal devoted to the applications of physics to medicine and biology : official journal of the Italian Association of Biomedical Physics (AIFB) · 2025
    Review
  3. Article
  4. Simultaneous binding characterization of different chromium speciation to serum albumin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Article
  5. Article
  6. Article
  7. Pb(II) coordination to the nonclassical zinc finger tristetraprolin: retained function with an altered fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
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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

4 authors at 1 institution in 1 country.

Ahmed BelatikDépartement de Chimie-Biologie, Université du Québec à Trois-Rivières, Trois-Rivières, Québec, Canada.
Surat Hotchandani
Robert Carpentier
Heidar-Ali Tajmir-Riahi
Université du Québec à Trois-Rivières · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lead is a potent environmental toxin that has accumulated above its natural level as a result of human activity. Pb cation shows major affinity towards protein complexation and it has been used as modulator of protein-membrane interactions. We located the binding sites of Pb(II) with human serum (HSA) and bovine serum albumins (BSA) at physiological conditions, using constant protein concentration and various Pb contents. FTIR, UV-visible, CD, fluorescence and X-ray photoelectron spectroscopic (XPS) methods were used to analyse Pb binding sites, the binding constant and the effect of metal ion complexation on HSA and BSA stability and conformations. Structural analysis showed that Pb binds strongly to HSA and BSA via hydrophilic contacts with overall binding constants of K(Pb-HSA) = 8.2 (±0.8)×10(4) M(-1) and K(Pb-BSA) = 7.5 (±0.7)×10(4) M(-1). The number of bound Pb cation per protein is 0.7 per HSA and BSA complexes. XPS located the binding sites of Pb cation with protein N and O atoms. Pb complexation alters protein conformation by a major reduction of α-helix from 57% (free HSA) to 48% (metal-complex) and 63% (free BSA) to 52% (metal-complex) inducing a partial protein destabilization.

Indexed as

Spectrum AnalysisAnimalsBinding SitesCattleEnvironmental PollutantsHumansLeadModels, MolecularProtein BindingProtein ConformationProtein StabilitySerum Albumin, BovineEnvironmental PollutantsLeadSerum Albumin, Bovine

Identifiers

PMID22574219
PMCPMC3344939
OpenAlexW2058830685

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.