Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach

This publication has 54 references indexed in Scilit:

• Quantitative reactivity profiling predicts functional cysteines in proteomes
  Nature, 2010
• Identification of S-Nitrosylated Targets of Thioredoxin Using a Quantitative Proteomic Approach
  Biochemistry, 2010
• Protein S-nitrosylation in health and disease: a current perspective
  Trends in Molecular Medicine, 2009
• Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture
  Nature Biotechnology, 2009
• Nitrosothiol Reactivity Profiling Identifies S-Nitrosylated Proteins with Unexpected Stability
  Chemistry & Biology, 2008
• A strategy for direct identification of protein S-nitrosylation sites by quadrupole time-of-flight mass spectrometry
  Journal of the American Society for Mass Spectrometry, 2008
• Human spermatozoa contain multiple targets for protein S‐nitrosylation: An alternative mechanism of the modulation of sperm function by nitric oxide?
  Proteomics, 2007
• Balancing reactivity against selectivity: The evolution of protein S-nitrosylation as an effector of cell signaling by nitric oxide
  Cardiovascular Research, 2007
• Identification of S-nitrosylation motifs by site-specific mapping of the S -nitrosocysteine proteome in human vascular smooth muscle cells
  Proceedings of the National Academy of Sciences, 2006
• The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
  Nature, 1980