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In 2006 Stiller et al. [19] by repeated amplifications of mitochondrial DNA sequences from a large number of ancient wolf remains, showed that C→T/G→A transitions are the predominant type of nucleotide misincorporations which are caused mainly by modifications of C residues.

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Signaling by these reactive molecules is achieved mainly by targeted modifications of specific residues in proteins (25).

Previous studies have demonstrated that abnormal phenotypes in cloned animals are caused mainly by epigenetic modifications rather than genetic mutations, as their offspring of the abnormal cloned animals tend to show normal epigenetic status and phenotypes [ 45, 46].

Lipohypertrophy has been managed mainly by lifestyle modification, ie, a hypocaloric diet and increased exercise.

To address the needs of the confectionery industry for saturated fatty acids, high stearic acid content oils have been developed mainly by genetic modification of the FatA stearoyl-ACP thioesterase and the SAD stearoyl-ACP desaturase [ 10, 11].

Estimation of true and false selections are based on the proposition that after arbitrarily chosen split the resulting subgroups have only changes in gene expression produced mainly by the controlled modifications in one of the subgroups.

Thus, the regulation of sFRP1 by genistein may be mainly by chromatin histone modifications rather than DNA methylation.

The DDR pathway is composed of a complex protein network, regulated mainly by post-translational modifications such as phosphorylation, ubiquitylation, SUMOylation, acetylation and PARylation [ 1].

Inhibition of TA was caused mainly by post-translational modifications: dephosphorylation of AKT and, to a smaller extent, by early downregulation of hTERT (the catalytic subunit of the enzyme) transcription.

Epigenetic information is contained within DNA and protein components of chromatin; the former is represented mainly by 5-methylcytosine modification of DNA [1], whereas the latter has more complex constituents consisting of histone and non-histone proteins as well as their post-translational modifications [2].

Although we did detect some phosphorylation of Ser using a phospho-specific antibody and this was abolished in a S491A mutant, P-labelling was not affected by the S491A mutation, suggesting that the low level of α2 phosphorylation by Akt was mainly accounted for by modification at other site(s).

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