The thiol redox proteome refers to all proteins whose cysteine thiols are subjected to various
redox-dependent posttranslational modifications (PTMs) including S-glutathionylation …

Fast changes in environmental oxygen availability translate into shifts in mitochondrial free
radical production. An increase in intraerythrocytic reduced glutathione (GSH) during …

Hemoglobin is one of the proteins that are more susceptible to S-glutathionylation and the
levels of its modified form, glutathionyl hemoglobin (HbSSG), increase in several human …

Native mass spectrometry involves transferring large biomolecular complexes into the gas
phase, enabling the characterization of their composition and stoichiometry. However, the …

Glutathionyl hemoglobin is a minor form of hemoglobin with intriguing properties. The
measurement of the redox potential of its reactive β-93-Cysteine is useful to improve …

Aromatic aldehydes that bind to sickle hemoglobin (HbS) to increase the protein oxygen
affinity and/or directly inhibit HbS polymer formation to prevent the pathological hypoxia …

Investigation of the interaction of hemoglobin (Hb) with therapeutic agents may be useful
from three perspectives. First, there are a few therapeutic agents targeting precisely Hb …

By preserving the noncovalent interactions of life long enough for analysis, the interrogation
of folded proteins, their modifications, and their complexes (native proteomics) aids our …

Fast changes in environmental oxygen availability translate into the shifts in mitochondrial
free radical production. Increase in intraerythrocytic reduced glutathione (GSH) during …

BST biotin switch technique CPT Cysteine-reactive phosphate tag DTT dithiothreitol eNOS
endothelial nitric oxide synthase IAA iodoacetamide IAM iodoacetamide ICAT isotope-coded …