Sentence examples for modification sites in from inspiring English sources

Due to the existence of different post-translational modification sites in FUNDC1, further biochemical, structural and cellular experiments should be studied in order to elucidate how cells synergistically regulate these key residues for responding to stress.

Table 4 and Fig. 4E summarize the H4 modification sites in human, yeast and Arabidopsis.

In the present study we have used mass spectrometry in combination with high performance liquid chromatography (HPLC) separation and phospho-peptide enrichment to identify histone modification sites in the reference plant, Arabidopsis thaliana.

Analysis of known O-GlcNAc modification sites in various proteins revealed that proline at −/+1 and/or −/+3 position from O-GlcNAc site(s) is the most favored residue for O-GlcNAc modification in a protein (Table S1).

Therefore, we used two synthetic peptides (Pep I - Biotin-105RIFTSIGEDYDERVLPSIT123-NH2 and Pep II - Biotin-250QLSRSRNITYLPAGQSVLL268-NH2) biotinylated athehe N-terminus and amidated at the C-terminus spanning tyrosine phosphorylation and O-GlcNAc modification sites in PHB.

We used a combination of various mass spectrometric methods including LC/MS/MS, MALDI-TOF and MALDI-CID as well as HPLC purification to identify histone modification sites in Arabidopsis thaliana.

Alexa Fluor 555 or 488-conjugated goat anti-rabbit (1 500, Invitrogen) were used as secondary antibodies to determine the specific lysine modification site in vivo.

This promotes binding of Ubc9 to the target modification site in the substrate, allowing for transfer of the SUMO to the substrate.

A further complication is the propensity of ubiquitination complexes to generate chains of varying lengths at a given modification site in vivo, making detection of ubiquitination by traditional size separation techniques challenging.

Based on the published three-dimensional structure of yeast eEF1A [4], [4] and the high amino acid sequence homology between eEF1A from different organisms, the EPG modification site in T. brucei eEF1A, Glu362, is predicted to be on the surface of a β-sheet in domain III.

Using liquid chromatography tandem mass spectroscopy (LC MS/MS), in addition to quantitation, the d-SSwitch approach allows identification of each individual modification site in the cysteome.