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The immobilization of bioactive peptides as key molecules in numerous biological and physiological functions holds promise for designing advanced biomaterials.
Due to the wide range of biological activities of benzofurans, their structure activity relationships have generated interest among medicinal chemists, and this has culminated in the discovery of several lead molecules in numerous disease conditions.
Since the first reports on chemokine function, much information has been generated on the implications of these molecules in numerous physiological and pathological processes, as well as on the signaling events activated through their binding to receptors.
Peptidylglycine monooxygenase (PHM) catalyzes the final step in the biosynthesis of amidated peptides that serve as important signaling molecules in numerous endocrine pathways.
Peptidylglycine monooxygenase catalyzes the final step in the biosynthesis of amidated peptides that serve as important signaling molecules in numerous endocrine pathways.
Glycans are important molecules in numerous essential biological processes, including cell adhesion, molecular trafficking and clearance, receptor activation, signal transduction, and endocytosis [ 53].
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Such an amino acid response would likely also inhibit mTOR, as mTORC1 is a nutrient-sensing signaling molecule in numerous cell environments (Avruch et al., 2009).
Oxysterols are bioactive molecules involved in numerous biological processes including cholesterol efflux [ 11], lipoprotein and calcium metabolisms [ 12], cell differentiation [ 13], and apoptosis [ 14] and are potential candidates for changing the fate of mesenchymal stem cell (MSC) differentiation [ 15].
These factors are recruited by RNA, the single-stranded molecule implicated in numerous cellular processes, from coding and decoding genes to protein synthesis.
Glycoproteins are biologically significant large molecules that participate in numerous cellular activities.
The small circular double-stranded mitochondrial DNA (mtDNA) molecule is present in numerous copies in each mitochondrion and encodes 13 of the dozens of proteins that constitute the OXPHOS complexes.
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