J. Mieyal

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Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress.

M. Gallogly, J. Mieyal, 2007, Current opinion in pharmacology.

Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300

P. Wingfield, H. Mitsuya, J. Mieyal, 2021, mBio.

Deglutathionylation of 2-Cys Peroxiredoxin Is Specifically Catalyzed by Sulfiredoxin*

P. B. Chock, S. Rhee, J. W. Park, 2009, The Journal of Biological Chemistry.

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia.

Y. Ho, J. Mieyal, Y. Xiong, 2007, Free radical biology & medicine.

pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis.

U. Srinivasan, J. Mieyal, U. Srinivasan, 1997, Biochemistry.

Acute Cadmium Exposure Inactivates Thioltransferase (Glutaredoxin), Inhibits Intracellular Reduction of Protein-glutathionyl-mixed Disulfides, and Initiates Apoptosis*

J. Mieyal, C. Chrestensen, D. W. Starke, 2000, The Journal of Biological Chemistry.

Thioltransferase (Glutaredoxin) Reactivates the DNA-binding Activity of Oxidation-inactivated Nuclear Factor I*

R. Gronostajski, J. Mieyal, D. W. Starke, 1998, The Journal of Biological Chemistry.

Hydroxylation and dealkylation reactions catalyzed by hemoglobin.

J. Mieyal, D. W. Starke, 1994, Methods in enzymology.

Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.

S. Gravina, J. Mieyal, 1993, Biochemistry.

Thioltransferase in human red blood cells: purification and properties.

S. Gravina, J. Mieyal, J. Chung, 1991, Biochemistry.

Hemoglobin catalysis of a monooxygenase-like aliphatic hydroxylation reaction.

J. Mieyal, D. W. Starke, 1989, Biochemical pharmacology.

NMR RELAXATION TIME STUDIES OF SUBSTRATE INTERACTIONS WITH P450 AND OTHER HEMOPROTEINS

I. Kapetanovic, R. Novak, J. Mieyal, 1977 .

Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases

J. Mieyal, Olga Gorelenkova Miller, 2015, Archives of Toxicology.

17 Disaccharide Phosphorylases

J. Mieyal, R. Abeles, 1972 .

Serum levels of lipid metabolites in age‐related macular degeneration

K. Palczewski, T. Maeda, A. Maeda, 2015, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Dysregulation of Glutathione Homeostasis in Neurodegenerative Diseases

A. Wilson-Delfosse, J. Mieyal, W. M. Johnson, 2012, Nutrients.

Sensitivity of protein sulfhydryl repair enzymes to oxidative stress.

Y. Chen, J. Mieyal, E. Lesnefsky, 1997, Free radical biology & medicine.

The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells

K. Biemann, S. Gravina, J. Mieyal, 1994, Protein science : a publication of the Protein Society.

Functional glutaredoxin (thioltransferase) activity in rat brain and liver mitochondria.

J. Mieyal, G. Zeevalk, J. Ehrhart, 2002, Parkinsonism & related disorders.

The roles of redox enzymes in Parkinson's disease: Focus on glutaredoxin.

Shu G. Chen, A. Wilson-Delfosse, J. Mieyal, 2015, Therapeutic targets for neurological diseases.

Regulation by reversible S-glutathionylation: molecular targets implicated in inflammatory diseases.

J. Mieyal, M. Shelton, 2008, Molecules and cells.

HSV Infection Induces Production of ROS, which Potentiate Signaling from Pattern Recognition Receptors: Role for S-glutathionylation of TRAF3 and 6

Zhijian J. Chen, H. Ichijo, S. Paludan, 2011, PLoS pathogens.

Covalent cross-linking of glutathione and carnosine to proteins by 4-oxo-2-nonenal.

V. Anderson, L. Sayre, M. Gallogly, 2009, Chemical research in toxicology.

Glutathione-Thiyl Radical Scavenging and Transferase Properties of Human Glutaredoxin (Thioltransferase)

J. Mieyal, D. W. Starke, P. Chock, 2003, The Journal of Biological Chemistry.

Radiation Response of Cells during Altered Protein Thiol Redox

C. Koch, J. Mieyal, T. Stamato, 2003, Radiation research.

Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.

M. Gallogly, J. Mieyal, D. W. Starke, 2008, Biochemistry.

Glutaredoxin regulates apoptosis in cardiomyocytes via NFkappaB targets Bcl-2 and Bcl-xL: implications for cardiac aging.

C. Hoppel, M. Gallogly, J. Mieyal, 2010, Antioxidants & redox signaling.

What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?

C. Hoppel, J. Mieyal, E. Lesnefsky, 2007, Antioxidants & redox signaling.

Glutaredoxin Regulates Nuclear Factor κ-B and Intercellular Adhesion Molecule in Müller Cells

T. Kern, J. Mieyal, M. Shelton, 2007, Journal of Biological Chemistry.

Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status.

L. Szweda, J. Mieyal, A. Nulton-Persson, 2003, Biochemistry.

A novel thiol oxidation‐based mechanism for adriamycin‐induced cell injury in human macrophages

Yanmei Wang, J. Mieyal, J. Begley, 2005, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Thioltransferase in human red blood cells: kinetics and equilibrium.

S. Gravina, J. Mieyal, B. A. Hocevar, 1991, Biochemistry.

Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFκB*

J. Mieyal, A. Nieminen, H. Pai, 2007, Journal of Biological Chemistry.

Metabolic structure-activity relationship for a homologous series of phenacetin analogs.

I. Kapetanovic, J. Strong, J. Mieyal, 1979, The Journal of pharmacology and experimental therapeutics.

Motor and non-motor features of Parkinson's disease in LRRK2 G2019S carriers versus matched controls

Shu G. Chen, A. Wilson-Delfosse, C. Tatsuoka, 2018, Journal of the Neurological Sciences.

Glutaredoxin Regulates Autocrine and Paracrine Proinflammatory Responses in Retinal Glial (Müller) Cells*

T. Kern, J. Mieyal, A. Distler, 2009, Journal of Biological Chemistry.

Characterization of Enzyme-like activity of human hemoglobin. Properties of the hemoglobin-P-450 reductase-coupled aniline hydroxylase system.

J. Mieyal, J. Blumer, R. S. Ackerman, 1976, The Journal of biological chemistry.

Reply to the Commentary “To Gorelenkova Miller and Mieyal (2015): Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases” by M. Kato

J. Mieyal, Olga Gorelenkova Miller, 2016, Archives of Toxicology.

Role of Vicinal Protein Thiols in Radiation and Cytotoxic Responses

C. Koch, J. Mieyal, J. Biaglow, 2006, Radiation research.

A method for measuring disulfide reduction by cultured mammalian cells: relative contributions of glutathione-dependent and glutathione-independent mechanisms.

J. Mieyal, J. Biaglow, C. Chrestensen, 2000, Analytical biochemistry.

Convergence of Parkinson’s disease and diabetes: focus on glia

T. Kern, J. Mieyal, O. Miller, 2017 .

Benzoyl and hydroxybenzoyl esters of coenzyme A. Purification and nuclear magnetic resonance characterization; conformation in solution.

J. Mieyal, L. T. Webster, U. Siddiqui, 1974, The Journal of biological chemistry.

Benzoyl and hydroxybenzoyl esters of coenzyme A. Ultraviolet characterization and reaction mechanisms.

J. Mieyal, L. T. Webster, U. Siddiqui, 1974, The Journal of biological chemistry.

Selective inactivation of glutaredoxin by sporidesmin and other epidithiopiperazinediones.

T. W. Jordan, J. Mieyal, U. Srinivasan, 2006, Biochemistry.

Rat Brain Thioltransferase : Regional Distribution, Immunological Characterization, and Localization by Fluorescent In Situ Hybridization

M. Boyd, V. Ravindranath, J. Mieyal, 1999, Journal of neurochemistry.

Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases

J. Mieyal, Olga Gorelenkova Miller, 2015, Archives of Toxicology.

Conformation in solution of coenzyme A thioesters: II. Butyryl-CoA and arylacetyl-CoA compounds☆

J. Mieyal, K. Blisard, U. Siddiqui, 1976 .

Coenzyme interactions. V. The second carbanion in reactions catalyzed by thiamine.

J. Mieyal, I. Rosner, G. Bantle, 1971, The Journal of biological chemistry.

Coenzyme interactions. IV. Molecular complexes of thiamine with indole derivatives--quantitative aspects.

J. Mieyal, J. Biaglow, H. Z. Sable, 1969, The Journal of biological chemistry.

Coenzyme interactions. 3. Characteristics of the molecular complexes of thiamine with indole derivatives.

J. Mieyal, J. Biaglow, H. Z. Sable, 1969, The Journal of biological chemistry.

Accleration of autooxidation of human oxyhemoglobin by aniline and its relation to hemoglobin-catalyzed aniline hydroxylation.

J. Mieyal, J. Blumer, 1976, The Journal of biological chemistry.

Substrate specificity of the monooxygenase activity of hemoglobin.

J. Mieyal, D. W. Starke, K. Blisard, 1984, Molecular pharmacology.

Stable and controllable RNA interference: Investigating the physiological function of glutathionylated actin

E. Tekle, Jun Wang, E. Stadtman, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.

Molly M Gallogly, Suparna Qanungo, M. Gallogly, 2008, Antioxidants & redox signaling.

Critical Roles of Glutaredoxin in Brain Cells-Implications for Parkinson's Disease.

J. Mieyal, Olga Gorelenkova Miller, 2018, Antioxidants & redox signaling.

Protein-thiol oxidation and cell death: regulatory role of glutaredoxins.

J. Mieyal, E. Allen, 2012, Antioxidants & redox signaling.

Mechanisms of altered redox regulation in neurodegenerative diseases--focus on S--glutathionylation.

J. Mieyal, Xing-Huang Gao, Elizabeth A Sabens Liedhegner, 2012, Antioxidants & redox signaling.

Levodopa activates apoptosis signaling kinase 1 (ASK1) and promotes apoptosis in a neuronal model: implications for the treatment of Parkinson's disease.

J. Mieyal, Elizabeth S Liedhegner, Kelly M. Steller, 2011, Chemical research in toxicology.

Levodopa deactivates enzymes that regulate thiol-disulfide homeostasis and promotes neuronal cell death: implications for therapy of Parkinson's disease.

J. Mieyal, A. Distler, Elizabeth A. Sabens, 2010, Biochemistry.

Kinase inhibitors arrest neurodegeneration in cell and C. elegans models of LRRK2 toxicity.

Xiongwei Zhu, D. Alessi, Shu G. Chen, 2013, Human molecular genetics.

Regulation of DJ-1 by Glutaredoxin 1 in Vivo: Implications for Parkinson's Disease.

Wenzhang Wang, Xiongwei Zhu, V. Ravindranath, 2016, Biochemistry.

Glutathione depletion or radiation treatment alters respiration and induces apoptosis in R3230Ac mammary carcinoma.

M. Dewhirst, J. Mieyal, J. Biaglow, 2003, Advances in experimental medicine and biology.

Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation.

J. Mieyal, P. Chock, M. Shelton, 2005, Antioxidants & redox signaling.

Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation.

M. Gallogly, J. Mieyal, D. W. Starke, 2009, Antioxidants & redox signaling.

Upregulation of Glutaredoxin-1 Activates Microglia and Promotes Neurodegeneration: Implications for Parkinson's Disease.

Xiongwei Zhu, J. Mieyal, S. Siedlak, 2016, Antioxidants & redox signaling.

The reaction of β-propiolactone with derivatives of adenine and with DNA

J. Mieyal, D. Goldthwait, Ruyu Chen, 1981 .

Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells*

Henry M. Fales, John J. Mieyal, Emily S. Boja, 2001, The Journal of Biological Chemistry.

Cloning, expression and characterization of human thioltransferase (glutaredoxin) in E. coli

C. Eckman, J. Mieyal, C. Chrestensen, 1995, FEBS letters.

Glutaredoxin deficiency exacerbates neurodegeneration in C. elegans models of Parkinson's disease.

Wenzhang Wang, Xiongwei Zhu, G. Caldwell, 2015, Human molecular genetics.

Characterization of the aniline hydroxylase activity of erythrocytes.

J. Mieyal, K. Blisard, 1979, The Journal of biological chemistry.

Evidence for a second carbanion in the mecahnism of the thiamine catalysis

J. Mieyal, L. Krampitz, R. Votaw, 1967 .

The PTPRT pseudo-phosphatase domain is a denitrase

Yiqing Zhao, S. Markowitz, M. Miyagi, 2017, bioRxiv.

Posttranslational modification of cysteine in redox signaling and oxidative stress: Focus on s-glutathionylation.

J. Mieyal, John J Mieyal, P Boon Chock, 2012, Antioxidants & redox signaling.

Molecular mechanism of glutathione-mediated protection from oxidized low-density lipoprotein-induced cell injury in human macrophages: role of glutathione reductase and glutaredoxin.

Reto Asmis, Yanmei Wang, J. Mieyal, 2006, Free radical biology & medicine.

N-acetyl-L-cysteine sensitizes pancreatic cancers to gemcitabine by targeting the NFκB pathway.

D. Townsend, J. Lemasters, J. Mieyal, 2014, Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie.

Computational and mutational analysis of human glutaredoxin (thioltransferase): probing the molecular basis of the low pKa of cysteine 22 and its role in catalysis.

C. Post, J. Mieyal, A. Berdis, 2006, Biochemistry.

Inhibition of acetaminophen-induced hepatotoxicity by phenacetin and its alkoxy analogs.

I. Kapetanovic, J. Mieyal, 1979, The Journal of pharmacology and experimental therapeutics.

Role of NADPH and the NADPH-dependent methemoglobin reductase in the hydroxylase activity of human erythrocytes.

J. Mieyal, K. Blisard, 1981, Archives of biochemistry and biophysics.

META. 2. A Dictionary Model of Mammalian Xenobiotic Metabolism

Gilles Klopman, John J. Mieyal, Joseph Talafous, 1994, J. Chem. Inf. Comput. Sci..

Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.

S. Nanduri, Y. Yang, J. Qin, 1998, Biochemistry.

Monooxygenase activity of human hemoglobin: role of quaternary structure in the preponderant activity of the beta subunits within the tetramer.

J. Mieyal, B. Ferraiolo, G. Onady, 1984, Biochemistry.

Differential monooxygenase-like activity of fetal and adult erythrocytes.

J. Mieyal, K. Blisard, 1980, Biochemical and biophysical research communications.

Monooxygenase activity of human hemoglobin: NMR demonstration of different modes of substrate binding corresponding to different activities of hemoglobin derivatives.

J. Mieyal, B. Ferraiolo, G. Onady, 1984, Biochemistry.

Mechanism of action of sucrose phosphorylase. 3. The reaction with water and other alcohols.

M. Simon, J. Mieyal, R. Abeles, 1972, The Journal of biological chemistry.

Dynamics of glutathione and ophthalmate traced with 2H-enriched body water in rats and humans.

Henri Brunengraber, Guo-Fang Zhang, J. Kelleher, 2009, American journal of physiology. Endocrinology and metabolism.

Supplemental Online Pharmacology Modules Increase Recognition and Production Memory in a Hybrid Problem-Based Learning (PBL) Curriculum

Peggy Y. Kim, Ruth A. Keri, David W. Allbritton, 2015 .

Supplemental Online Pharmacology Modules Increase Recognition and Production Memory in a Hybrid Problem-Based Learning (PBL) Curriculum

D. Allbritton, A. Wilson-Delfosse, J. Mieyal, 2015, The journal of the International Association of Medical Science Educators : JIAMSE.

Aging-dependent changes in rat heart mitochondrial glutaredoxins—Implications for redox regulation☆

C. Hoppel, J. Mieyal, E. Lesnefsky, 2013, Redox biology.

antioxidants

W. Qian, Matthew J. Gaffrey, J. Mieyal, 2020, Catalysis from A to Z.

Thioltransferase (Glutaredoxin) Is Detected Within HIV-1 and Can Regulate the Activity of Glutathionylated HIV-1 Protease in Vitro *

J. Mieyal, D. Davis, R. Yarchoan, 1997, The Journal of Biological Chemistry.

Mechanisms of altered redox regulation in neurodegenerative diseases--focus on S--glutathionylation.

J. Mieyal, Xing-Huang Gao, Elizabeth A Sabens Liedhegner, 2012, Antioxidants & redox signaling.

Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man.

J. Strong, J. Mieyal, S. Lucas, 1976, The Journal of biological chemistry.