Sentence examples for majority of substrates from inspiring English sources

Both cytoplasmic and nuclear proteins have been shown to be SUMO (small ubiquitin-related modifier) substrates, but the majority of substrates fall into the latter class, with one major function of SUMO being in transcriptional control (reviewed in [ 1– 3]).

In contrast with the majority of substrates used to study cell adhesion, the natural extracellular matrix (ECM) is dynamic and remodeled over time.

Interestingly, the majority of substrates did not appear to be capable of undergoing phosphorylation by MAP3K8 at all, thus the MAP3K8 enzyme is not capable of catalyzing the phosphorylation of any given peptide and phosphorylation by this enzyme appears to exhibit qualitative characteristics: even prolonged incubation times do not yield detectable phosphorylation of unfavourable peptides.

The majority of substrates (>40%) consist of an aromatic system, an ether moiety, and amine groups.

The majority of substrates of BACE1 are, like APP, Type I membrane proteins, while a few, like neuregulin 1 (NRG1), have more complex membrane topologies.

An examination of whether the binding mode provides a foundation for the ability of Srs2ΔC to unwind various DNA substrates revealed similar unwinding efficiencies for the majority of substrates, including the fork, 3′ flap, 5′ flap, and Y-form.

Arrays contained 1152 different oligopeptides, covering the majority of substrate peptides available through PhosphoBase (version 2.0).

Whereas the majority of substrate phosphorylations neither required FAK for v-Src-induced phosphorylation nor were enhanced in the presence of FAK, we identified a small number of substrates whose phosphorylation was affected by FAK and/or adherence state.

Therefore, a major unresolved question for the majority of SUMO substrates is exactly how SUMOylation is initiated and regulated.

However, the majority of these substrates serve as pharmacological targets in vitro, but few have been shown to be endogenous, physiological substrates (defined as peptides whose endogenous circulating level of intact versus N-terminally cleaved forms is altered after reduction or elimination of DPP4 activity in vivo) [ 44].

Although it was expected that the majority of the substrates would be involved in nucleosome assembly and histone binding categories, a significant number of the identified substrates were cytoplasmic proteins and metabolic enzymes [23].