Covalent amino acid modification significantly expands protein functional capability in
regulating biological processes. Tyrosine residues can undergo phosphorylation, sulfation …

Significance: The systematic investigation of oxidative modification of proteins by reactive
oxygen species started in 1980. Later, it was shown that reactive nitrogen species could also …

Numerous inflammatory diseases and autoimmune disorders by therapeutic peptides have
received substantial consideration; however, the exploration of anti-inflammatory peptides …

In general, hydrolyzed proteins, plant-derived alkaloids and toxins displays unpleasant bitter
taste. Thus, the perception of bitter taste plays a crucial role in protecting animals from …

The inhibition of dipeptidyl peptidase IV (DPP-IV, EC 3.4. 14.5) is well recognized as a new
avenue for the treatment of Type 2 diabetes (T2D). Until now, peptide-like DDP-IV inhibitors …

Mycobacterium tuberculosis is one of the most dangerous pathogens in humans. It acts as
an etiological agent of tuberculosis (TB), infecting almost one-third of the world's population …

Cancer is a leading killer disease globally, it occurs when the cellular changes cause the
abnormal growth and division of the cells. Conventional treatment such as therapies and wet …

Antioxidant proteins have been discovered closely associated with disease control due to its
capability to eradicate excess free radicals. The accurate identification of antioxidant …

Fast, accurate identification and characterization of amyloid proteins at a large-scale is
essential for understating their role in therapeutic intervention strategies. As a matter of fact …

Cysteine S-nitrosylation is a type of reversible post-translational modification of proteins,
which controls diverse biological processes. It is associated with redox-based cellular …