These findings suggest that nonspecific electrostatic interactions drive the formation of the enzyme−substrate complex (designated herein as E:S). An ensemble of different RNA−protein complexes best ...

The presence of 6–8% of cellular PRMT3 in the ribosome‐enriched preparations is consistent with the transient nature of an enzyme–substrate interaction that would be predicted for the ...

By systematically altering the enzyme-membrane affinity, we examined enzyme–substrate interactions under various conditions. Our findings reveal that while the membrane environment significantly ...

Proteomics with PP1-Neurabin fusion proteins identify the 4E-BP proteins as novel Neurabin/PP1 substrates, and interaction with the Neurabin PDZ domain shown to be the major determinant of ...

The use of the Escherichia coli enzyme β-glucuronidase (GUS) as a reporter in gene expression studies is limited due to loss of activity during tissue fixation by glutaraldehyde or formaldehyde ...