ReviewEnvironmental health perspectives2002
Molecular mechanisms in nickel carcinogenesis: modeling Ni(II) binding site in histone H4.
Review in Environmental health perspectives, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 56 citations in OpenAlex.
- Review
- Time- and concentration-dependent genomic responses of the rat airway to inhaled nickel sulfate.Environmental and molecular mutagenesis · 2017Article
- Toxicological effects of major environmental pollutants: an overview.Environmental monitoring and assessment · 2013Review
- Inhalable metal-rich air particles and histone H3K4 dimethylation and H3K9 acetylation in a cross-sectional study of steel workers.Environmental health perspectives · 2011Article
- Environmental epigenetics in metal exposure.Epigenetics · 2011Review
- Perturbations in nucleosome structure from heavy metal association.Nucleic acids research · 2010Article
- Effects of nickel on cyclin expression, cell cycle progression and cell proliferation in human pulmonary cells.Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology · 2009Article
- Epigenetics and environmental chemicals.Current opinion in pediatrics · 2009Review
- Genetic and epigenetic mechanisms in metal carcinogenesis and cocarcinogenesis: nickel, arsenic, and chromium.Chemical research in toxicology · 2008Review
- Silencing of mouse Aprt is a gradual process in differentiated cells.Molecular and cellular biology · 2003Article
- A purification system forJournal of radioanalytical and nuclear chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ni(II) compounds are well known as human carcinogens, though the molecular events which are responsible for this are not yet fully understood. It has been proposed that the binding of N(II) ions within the cell nucleus is a crucial element in the mechanism of carcinogenesis. The most abundant proteins in the cell nucleus are histones, and this makes them the prime candidates for this role. This article is a review of our recent studies of histone H4 models of Ni(II) binding. We analyzed the sequence of the N-terminal tail of the histone H4, Ac-SGRGKGGKGLGKGGAKRH(18)RKVL-Am, for Ni(II) binding. This site has been proposed mainly because of the potent inhibitory effect of Ni(II) on the acetylation of lysine residues near the histidine H(18), and also because of the accessibility of the H4 tail in the histone octamer. Combined potentiometric and spectroscopic studies showed that the histidine 18 acted as an anchoring binding site for metal ions in the peptide investigated. Comparison with the results for Cu(II) binding are also reported. The results allowed us to propose that the binding of Ni(II) is able to promote a secondary structure with organized side-chain orientation on the N-terminal tail of histone H4.
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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.