Sentence examples for primary effector peptide from inspiring English sources

4– 8 Angiotensin II, the primary effector peptide of the renin-angiotensin system, not only increases blood pressure but also promotes vascular inflammation, leading to endothelial dysfunction and atherosclerosis, stimulates vascular smooth muscle hypertrophy, and vascular remodeling, and stimulates myocardial fibrosis and hypertrophy, leading to cardiac remodeling.

Cytotoxic T lymphocytes (CTLs) are known to be the primary effector cells to eradicate EBV-infected B cells that present LMP1 and LMP2 antigenic peptides in the context of appropriate HLA class I molecules [6], [7].

Finally, log2 ratios of the heavy (crosslinked in the presence of effector peptide) to light (absence of effector peptide) peak areas were determined.

However, with no effector peptide, present the fluorescence polarization signal decreases over time.

The reduction in Km for the peptide substrate alone suggests that effector peptide binding to the PHD1 domain allosterically promotes binding of peptide substrates in KDM5A.

b Michaelis Menten plot of KDM5A-catalyzed demethylation of Ac-H3K4me3 21mer peptide in the presence and absence of a saturating concentration (38 µM) of unmodified H3 10meffectortor peptide.

The complex with substrate and/or effector peptides refers to KDM5A with 50 µM FeSO4, 100 µM N-OG, and 500 µM Ac-H3K4me3 21mer substrate (25× [KDM5A]) with or without 100 µM H3 10meffectortor peptide.

For assays measuring the stimulation by the effector peptide on the Michaelis Menten kinetics, the effector peptide (differently modified H3 10mers Ala1-Ser10) was included in the reaction mix at 20× Kd concentrations.

Other than crosslinks between H3 effector peptide and KDM5A, few crosslinks were enriched in either condition more than twofold.

Isotopically coded reagents were used to probe changes in crosslinking between unoccupied KDM5A and KDM5A with effector peptide bound.

The enhancement in demethylation catalysis is largely independent of the type of modification present on the effector peptide.