Provided for Non-commercial Research and Educational Use Only. Not for Reproduction, Distribution or Commercial Use. Use of Dimedone-based Chemical Probes for Sulfenic Acid Detection: Methods to Visualize and Identify Labeled Proteins Author's Personal Copy

[1]  W. Lowther,et al.  Provided for Non-commercial Research and Educational Use Only. Not for Reproduction, Distribution or Commercial Use , 2022 .

[2]  Kate S Carroll,et al.  Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. , 2009, ACS chemical biology.

[3]  P. Karplus,et al.  Cysteine pK(a) values for the bacterial peroxiredoxin AhpC. , 2008, Biochemistry.

[4]  P. Witting,et al.  Redox control of endothelial function and dysfunction: molecular mechanisms and therapeutic opportunities. , 2008, Antioxidants & redox signaling.

[5]  Kate S. Carroll,et al.  A chemical approach for detecting sulfenic acid-modified proteins in living cells. , 2008, Molecular bioSystems.

[6]  L. Poole,et al.  Discovering mechanisms of signaling-mediated cysteine oxidation. , 2008, Current opinion in chemical biology.

[7]  J. Fetrow,et al.  Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins. , 2007, Bioconjugate chemistry.

[8]  Claus Schneider,et al.  Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. , 2007, Chemistry & biology.

[9]  D. Liebler,et al.  Protein targets of reactive electrophiles in human liver microsomes. , 2007, Chemical research in toxicology.

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

[11]  Dean P. Jones.  Disruption of mitochondrial redox circuitry in oxidative stress. , 2006, Chemico-biological interactions.

[12]  Yen-Ling Chen,et al.  Reactive Oxygen Species Generation Is Involved in Epidermal Growth Factor Receptor Transactivation through the Transient Oxidization of Src Homology 2-Containing Tyrosine Phosphatase in Endothelin-1 Signaling Pathway in Rat Cardiac Fibroblasts , 2006, Molecular Pharmacology.

[13]  S. Mongkolsuk,et al.  Novel Organic Hydroperoxide-Sensing and Responding Mechanisms for OhrR, a Major Bacterial Sensor and Regulator of Organic Hydroperoxide Stress , 2006, Journal of bacteriology.

[14]  Yu Shyr,et al.  Cytosolic and nuclear protein targets of thiol-reactive electrophiles. , 2006, Chemical research in toxicology.

[15]  R. Brennan,et al.  Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. , 2005, Molecular cell.

[16]  J. Kwon,et al.  Receptor‐stimulated oxidation of SHP‐2 promotes T‐cell adhesion through SLP‐76–ADAP , 2005, The EMBO journal.

[17]  N. Tonks.  Redox Redux: Revisiting PTPs and the Control of Cell Signaling , 2005, Cell.

[18]  Kap-Seok Yang,et al.  Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[19]  R. Matthews,et al.  Oxidative Stress Inactivates Cobalamin-Independent Methionine Synthase (MetE) in Escherichia coli , 2004, PLoS biology.

[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]  P. Karplus,et al.  Protein sulfenic acids in redox signaling. , 2004, Annual review of pharmacology and toxicology.

[22]  Woojin Jeong,et al.  Reversible Inactivation of the Tumor Suppressor PTEN by H2O2 * , 2002, The Journal of Biological Chemistry.

[23]  J. Helmann,et al.  The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[24]  Toshiyuki Fukada,et al.  Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. , 2002, Molecular cell.

[25]  I. Schuppe-Koistinen,et al.  S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: role of thiol oxidation and catalysis by glutaredoxin. , 2002, Methods in enzymology.

[26]  Yoshiharu Inoue,et al.  Regulation of the Yeast Yap1p Nuclear Export Signal Is Mediated by Redox Signal-Induced Reversible Disulfide Bond Formation , 2001, Molecular and Cellular Biology.

[27]  Joanne I. Yeh,et al.  Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. , 1999, Biochemistry.

[28]  J. Hahn,et al.  RsrA, an anti‐sigma factor regulated by redox change , 1999, The EMBO journal.

[29]  V. Muronetz,et al.  Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities , 1999, FEBS letters.

[30]  U. Jakob,et al.  Chaperone Activity with a Redox Switch , 1999, Cell.

[31]  G. Storz,et al.  Activation of the OxyR transcription factor by reversible disulfide bond formation. , 1998, Science.

[32]  L. Poole,et al.  Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. , 1996, Biochemistry.

[33]  P. Tegtmeyer,et al.  Role of cysteine residues in regulation of p53 function , 1995, Molecular and cellular biology.

[34]  P. Witting,et al.  Redox control of endothelial function and dysfunction: molecular mechanisms and therapeutic opportunities. , 2008, Antioxidants & redox signaling.

[35]  Claus Schneider,et al.  Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. , 2007, Chemistry & biology.

[36]  D. Liebler,et al.  Protein targets of reactive electrophiles in human liver microsomes. , 2007, Chemical research in toxicology.

[37]  Dean P. Jones.  Disruption of mitochondrial redox circuitry in oxidative stress. , 2006, Chemico-biological interactions.

[38]  S. Mongkolsuk,et al.  Novel Organic Hydroperoxide-Sensing and Responding Mechanisms for OhrR, a Major Bacterial Sensor and Regulator of Organic Hydroperoxide Stress , 2006, Journal of bacteriology.

[39]  Yu Shyr,et al.  Cytosolic and nuclear protein targets of thiol-reactive electrophiles. , 2006, Chemical research in toxicology.

[40]  J. Kwon,et al.  Receptor‐stimulated oxidation of SHP‐2 promotes T‐cell adhesion through SLP‐76–ADAP , 2005, The EMBO journal.

[41]  R. Matthews,et al.  Oxidative Stress Inactivates Cobalamin-Independent Methionine Synthase (MetE) in Escherichia coli , 2004, PLoS biology.

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

[43]  P. Karplus,et al.  Protein sulfenic acids in redox signaling. , 2004, Annual review of pharmacology and toxicology.

[44]  Woojin Jeong,et al.  Reversible Inactivation of the Tumor Suppressor PTEN by H2O2 * , 2002, The Journal of Biological Chemistry.

[45]  J. Helmann,et al.  The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[46]  Toshiyuki Fukada,et al.  Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. , 2002, Molecular cell.

[47]  Yoshiharu Inoue,et al.  Regulation of the Yeast Yap1p Nuclear Export Signal Is Mediated by Redox Signal-Induced Reversible Disulfide Bond Formation , 2001, Molecular and Cellular Biology.

[48]  Joanne I. Yeh,et al.  Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. , 1999, Biochemistry.

[49]  J. Hahn,et al.  RsrA, an anti‐sigma factor regulated by redox change , 1999, The EMBO journal.

[50]  V. Muronetz,et al.  Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities , 1999, FEBS letters.

[51]  U. Jakob,et al.  Chaperone Activity with a Redox Switch , 1999, Cell.

[52]  G. Storz,et al.  Activation of the OxyR transcription factor by reversible disulfide bond formation. , 1998, Science.

[53]  L. Poole,et al.  Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. , 1996, Biochemistry.

[54]  P. Tegtmeyer,et al.  Role of cysteine residues in regulation of p53 function , 1995, Molecular and cellular biology.

[55]  P. Tulkens,et al.  Author's Personal Copy Author's Personal Copy , 2022 .