Sentence examples for binding and protein stability from inspiring English sources

Mutations in the nucleic acid-binding domain of CspA were previously evaluated for their impact on both nucleic acid binding and protein stability (Hilier et al., 1998).

Modification of these residues have also been shown to influence DNA binding and protein stability in their respective proteins [ 33, 34].

PTEN is transcriptionally regulated by transcription factors such as p53, Egr-1, NFκB and SMADs, while protein levels and activity are modulated by phosphorylation, oxidation, subcellular localisation, phospholipid binding and protein stability [ 29].

Similarly, the serine-acidic high mobility group I (HMG1) domains that occur in the C-terminus of HMG proteins, are known to affect both DNA binding and protein stability [ 32].

In those systems, Runx proteins function as heterodimers by forming complexes with CBFβ, a non-DNA-binding cofactor that enhances the DNA binding affinity and protein stability of Runx proteins (Adya et al., 2000).

However, specific carbohydrates can play key roles in cell-cell recognition, receptor-ligand binding, protein interactions, and protein stability in vivo [ 62].

This is shown further by the diverse effects of acetylation on protein function, including DNA binding, protein-protein interaction and protein stability.

This process neutralizes the positive charge on an amino acid and regulates DNA binding, protein-protein interaction, and protein stability [ 1, 2].

SOX factors appear to modulate β-CATENIN/TCF activity through a variety of mechanisms, including protein protein interactions, DNA binding, recruitment of cofactors, and protein stability.

Protein phosphorylation influences the activity of transcription factors through diverse mechanisms, such as modulation of their nucleo-cytoplasmic distributions, DNA-binding properties, and protein stabilities and modification of their interactions with other regulatory proteins [ 33, 38, 39].

The activity of FoxO3 is controlled by a variety of post-translational modifications that have been proposed to form a 'code' affecting FoxO3 subcellular localization, DNA binding ability, protein-protein interactions and protein stability.