Characterization of a novel affinity binding ligand for tyrosine nitrated peptides from a phage-displayed peptide library.

As an important post-translational modification in response to oxidative and nitrosative stress, protein tyrosine nitration is deeply involved in many physiological and pathological processes. Identifying tyrosine nitration in proteins is challenging due to its low abundance.Consequently, pre-separation and enrichment of tyrosine-nitrated peptides (TNPs) are necessary before submitting them to mass spectrometry analysis.

Insight into the proteomic profiling of exosomes secreted by human OM-MSCs reveals a new potential therapy.

Mesenchymal stromal cells (MSCs) have been used for the treatment of neuronal injury and neurodegenerative diseases. Their underlying mechanism may involve increased secretion of paracrine factors, which promotes tissue repair. Presently, exosomes have been regarded as important components of paracrine secretion and paracrine factors.

Changes in the mitochondrial proteome in human hepatocytes in response to alpha-amanitin hepatotoxicity.

Amanitin-induced apoptosis is proposed to have a significant effect on the pathogenesis of liver damage. However, few reports have focused on proteome changes induced by α-amanitin (α-AMA). Here, we evaluated changes in mitochondrial proteins of hepatocytes in response to 2 μM α-AMA, a concentration at which α-AMA-induced cell damage could be rescued at cellular level by common clinical drugs.