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In order to better understand the favourable effect of this chemical modification, we performed a conformational analysis of these compounds mainly based on the position of the phenyl ring relative to the piperazine and tetrahydropyridine moiety.
To determine whether the inhibitory function of VHL on cell migration is also impaired by SUMO modification, we performed scratch wound assay to assess the effect of SUMO modification on the inhibition of VHL on 786-O cell motility.
To test if these two nucleotide positions within the ADAR2 exon 0 sequence may be subject to an RNA-based modification, we performed RT-PCR on human brain total RNA amplifying the exon 0 sequence encompassing both putative editing sites.
To explore potential effect measure modification, we performed analyses stratified by age (dichotomised according to median age of controls, i.e., <60 vs ⩾60 years) and gender.
In order to verify the quality of DNA modification, we performed a PCR on modified DNA with primers specific for two fragments flanking CDH1.
To rule out a decrease in fidelity of this enzyme induced by the proprietary modification, we performed polymerase fidelity assays (Flaman et al, 1994).
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As a first step towards identifying such post-translational modifications, we performed bioinformatic analysis of the Oct4 protein sequence and identified several potential phosphorylation sites.
To examine the phenotypes of placentas after various genetic modifications, we performed histological analyses.
To understand the function of H2A modifications, we performed a systematic analysis of the histone H2A methylation status.
To characterize the role of WDR5 in mediating additional histone modifications, we performed ChIP in cells transfected with WDR5 siRNA.
To identify the genes responsible for the plant tRNA modifications, we performed global analysis of the Arabidopsis genome for candidate genes.
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