Development of ‘Redox Arrays’ for identifying novel glutathionylated proteins in the secretome

[1]  P. Ghezzi,et al.  Redox Proteomics of the Inflammatory Secretome Identifies a Common Set of Redoxins and Other Glutathionylated Proteins Released in Inflammation, Influenza Virus Infection and Oxidative Stress , 2015, PloS one.

[2]  Pietro Ghezzi,et al.  Linkage of inflammation and oxidative stress via release of glutathionylated peroxiredoxin-2, which acts as a danger signal , 2014, Proceedings of the National Academy of Sciences.

[3]  C. Lillig,et al.  Redox regulation by glutathione needs enzymes , 2014, Front. Pharmacol..

[4]  M. Mayr,et al.  Redox State of Pentraxin 3 as a Novel Biomarker for Resolution of Inflammation and Survival in Sepsis* , 2014, Molecular & Cellular Proteomics.

[5]  L. Flohé The fairytale of the GSSG/GSH redox potential. , 2013, Biochimica et biophysica acta.

[6]  P. Ghezzi Protein glutathionylation in health and disease. , 2013, Biochimica et biophysica acta.

[7]  Y. Chernajovsky,et al.  Increased disulphide dimer formation of latent associated peptide fusions of TGF-β by addition of L-cystine. , 2012, Journal of biotechnology.

[8]  A. Huttenlocher,et al.  Lyn is a redox sensor that mediates leukocyte wound attraction in vivo , 2011, Nature.

[9]  Arthur J. L. Cooper,et al.  Reversible and irreversible protein glutathionylation: biological and clinical aspects , 2011, Expert opinion on drug metabolism & toxicology.

[10]  D. Chan,et al.  Unbiased proteomic screen for binding proteins to modified lysines on histone H3 , 2009, Proteomics.

[11]  M. Pazin,et al.  S-glutathionylation impairs signal transducer and activator of transcription 3 activation and signaling. , 2009, Endocrinology.

[12]  C. Vulpe,et al.  Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins , 2008, Proteomics.

[13]  M. Gallogly,et al.  Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. , 2007, Current opinion in pharmacology.

[14]  P. Ghezzi,et al.  Glutathionylation pathways in drug response. , 2007, Current opinion in pharmacology.

[15]  M. Mann,et al.  In-gel digestion for mass spectrometric characterization of proteins and proteomes , 2006, Nature Protocols.

[16]  Katherine E. Talcott,et al.  Molecular basis for the redox control of nuclear transport of the structural chromatin protein Hmgb1. , 2006, Experimental cell research.

[17]  L. Lomas,et al.  Protein Equalizer™ Technology : The quest for a “democratic proteome” , 2006, Proteomics.

[18]  Liliana Gheorghiu,et al.  Reduction of the concentration difference of proteins in biological liquids using a library of combinatorial ligands , 2005, Electrophoresis.

[19]  G. Goch,et al.  Affinity of S100A1 protein for calcium increases dramatically upon glutathionylation , 2005, The FEBS journal.

[20]  J. Sears,et al.  Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone. , 2004, Experimental eye research.

[21]  A. Mantovani,et al.  High circulating levels of the IL‐1 type II decoy receptor in critically ill patients with sepsis: association of high decoy receptor levels with glucocorticoid administration , 2002, Journal of leukocyte biology.

[22]  M. Ward,et al.  Detection, Quantitation, Purification, and Identification of Cardiac Proteins S-Thiolated during Ischemia and Reperfusion* , 2002, The Journal of Biological Chemistry.

[23]  P. Ghezzi,et al.  Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[24]  P. Ghezzi,et al.  Protein glutathionylation: coupling and uncoupling of glutathione to protein thiol groups in lymphocytes under oxidative stress and HIV infection. , 2002, Molecular immunology.

[25]  P. Klatt,et al.  Glutathionylation of the p50 subunit of NF-kappaB: a mechanism for redox-induced inhibition of DNA binding. , 2001, Biochemistry.

[26]  Freya Q. Schafer,et al.  Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. , 2001, Free radical biology & medicine.

[27]  R. Levine,et al.  Identification of Oxidant-Sensitive Proteins: TNF-α Induces Protein Glutathiolation , 2000 .

[28]  J. Mieyal,et al.  Thioltransferase (Glutaredoxin) Is Detected Within HIV-1 and Can Regulate the Activity of Glutathionylated HIV-1 Protease in Vitro * , 1997, The Journal of Biological Chemistry.

[29]  C. Sen,et al.  Antioxidant and redox regulation of gene transcription , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[30]  K. Rokutan,et al.  S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: evidence against a role for glutathione disulfide. , 1994, Archives of biochemistry and biophysics.

[31]  I. Kawashima,et al.  Molecular cloning of cDNA encoding adipogenesis inhibitory factor and identity with interleukin‐11 , 1991, FEBS letters.

[32]  G. Windham,et al.  On the cysteine and cystine content of proteins , 1977, Journal of Molecular Evolution.

[33]  Ronald Jones Déja vu. , 2006, Veterinary anaesthesia and analgesia.

[34]  W. Dröge Free radicals in the physiological control of cell function. , 2002, Physiological reviews.

[35]  R. Levine,et al.  Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation. , 2000, Biochemistry.

[36]  S. Akira,et al.  Biological and clinical aspects of , 1990 .