The HLA-G dimer modulates the function of LILRB1-expressing antigen-presenting cells by principally binding to LILRB1.
Among the cytokines produced by different tissues, VEGF (Vascular Endothelial Growth Factor) mediates its biological effects by binding to a series of transmembrane tyrosine kinase receptors, principally VEGFR-1 and VEGFR-2 [9].
Their regulation is principally by oxygen-dependent degradation, which is initiated by hydroxylation of specific proline residues followed by binding of von Hippel-Lindau (VHL) protein.
The integrin αvβ6, which is expressed principally in epithelial cells, is one of the αv-integrins which has the ability to activate latent TGF-β by binding to the tripeptide RGD sequence on TGF-β latency-associated peptide (LAP).
NO regulates physiological processes by modulating the activity of proteins principally by nitrosylation, a process referring to the binding of NO to a transition metal centre or cysteine residues [ 1].
Antibodies attack antigens by binding to them.
The beta-lactam agents act principally by causing irreversible inhibition of bacterial cell wall synthesis, achieved by covalent binding to penicillin-binding proteins [11,12].
We supposed that SOCS3-KIR mutant interacted with PYK2 principally by the central SH2 domain, generating the inhibition effects, however the binding was a functional interaction, unstable and readily reversible, and the effects would be transient without the help of KIR domain, thus could not be detected by immunoprecipitation in vitro.
From absorption, steady-state emission, the effect of ferrocyanide ion-induced steady-state fluorescence quenching, circular dichroism, the mode of binding of these dyes into the tRNA helix has been substantiated to be principally by intercalative in nature.
