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Nickel binding sites in histone proteins: spectroscopic and structural characterization

Peana, Massimiliano Francesco and Medici, Serenella and Nurchi, Valeria Marina and Crisponi, Guido and Zoroddu, Maria Antonietta (2013) Nickel binding sites in histone proteins: spectroscopic and structural characterization. Coordination chemistry reviews, Vol. 257 (19-20), p. 2737-2751. eISSN 1873-3840. Article.

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DOI: 10.1016/j.ccr.2013.02.022


Nickel compounds are included among human carcinogens, though the molecular events related to them are not yet completely known.
It has been proposed that the basic element, in the mechanism of carcinogenesis exerted by nickel, is connected to its binding within the cell nucleus. DNA can weakly bind Ni(II), thus the nuclear proteins, in particular histones proteins which are abundantly present, could be important targets for Ni(II) ions.
The present review describes the interactions of nickel with histone H4, core tetramer (H3-H4)2 and several peptide fragments which have been selected as possible candidates for specific binding sites in the histone octamer.
The collected results allowed us to propose several mechanisms for nickel-induced damage triggering from metal coordination, including structural changes of histone proteins, as well as nucleobase oxidation and sequence-specific histone hydrolysis.

Item Type:Article
ID Code:9013
Uncontrolled Keywords:Ni(II) ions, histone proteins, peptide fragments, carcinogenesis
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Divisions:001 Università di Sassari > 01-a Nuovi Dipartimenti dal 2012 > Chimica e Farmacia
Publisher:Elsevier Science
Additional Information:Paper presented at the 11. European Biological Inorganic Chemistry Conference12-16 September 2012, Granada, Spain.
Deposited On:10 May 2013 09:18

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