John J. Mieyal mostly deals with Glutaredoxin, Biochemistry, Glutathione, Protein glutathionylation and Glutaredoxin 2. His Glutaredoxin study is associated with Enzyme. His work on Oxidative stress as part of general Biochemistry research is often related to Acetylcysteine, thus linking different fields of science.
He focuses mostly in the field of Glutathione, narrowing it down to topics relating to Cysteine and, in certain cases, Iron–sulfur cluster and Protein deglutathionylation. The Protein glutathionylation study combines topics in areas such as S-Glutathionylation and Intracellular. His S-Glutathionylation research incorporates themes from Redox and Cell biology.
John J. Mieyal spends much of his time researching Biochemistry, Glutaredoxin, Glutathione, Cell biology and Protein glutathionylation. In most of his Biochemistry studies, his work intersects topics such as Redox. He has researched Glutaredoxin in several fields, including Cysteine and Intracellular.
His research in the fields of Glutathione disulfide overlaps with other disciplines such as Glutathione reductase. The various areas that John J. Mieyal examines in his Cell biology study include S-Glutathionylation, Oxidative stress and Apoptosis, Programmed cell death. His studies deal with areas such as Protein deglutathionylation and Mitochondrion as well as Protein glutathionylation.
The scientist’s investigation covers issues in Cell biology, Glutaredoxin, Oxidative stress, Glutathione and Parkinson's disease. John J. Mieyal interconnects Oxidative phosphorylation and Neuroprotection in the investigation of issues within Cell biology. His Glutaredoxin research includes elements of Cysteine and Cell type.
His Oxidative stress study combines topics in areas such as Disease and Bioinformatics. The concepts of his Glutathione study are interwoven with issues in Gemcitabine, Cancer research, Internal medicine and Pancreatic cancer. Reactive nitrogen species is a subfield of Biochemistry that John J. Mieyal studies.
His main research concerns Reactive oxygen species, Oxidative phosphorylation, Glutathione, Cell biology and Reactive nitrogen species. His Reactive oxygen species research is multidisciplinary, relying on both S-Glutathionylation, Cysteine, Oxidative stress and Glutaredoxin. His S-Glutathionylation study combines topics from a wide range of disciplines, such as Cysteine metabolism, Peroxiredoxin and Mitochondrion.
Oxidative stress is closely attributed to Bioinformatics in his research. His Protein glutathionylation study in the realm of Glutaredoxin interacts with subjects such as ASK1. His biological study spans a wide range of topics, including Alzheimer's disease, Amyotrophic lateral sclerosis, Disease and Biomarker.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Molecular Mechanisms and Clinical Implications of Reversible Protein S-Glutathionylation
John J. Mieyal;John J. Mieyal;Molly M. Gallogly;Suparna Qanungo;Elizabeth A. Sabens;Elizabeth A. Sabens.
Antioxidants & Redox Signaling (2008)
Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress.
Molly M Gallogly;John J Mieyal.
Current Opinion in Pharmacology (2007)
Glutaredoxin: Role in Reversible Protein S-Glutathionylation and Regulation of Redox Signal Transduction and Protein Translocation
Melissa D. Shelton;P. Boon Chock;John J. Mieyal.
Antioxidants & Redox Signaling (2005)
Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells
Jun Wang;Emily S. Boja;Wuhong Tan;Ephrem Tekle.
Journal of Biological Chemistry (2001)
Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.
Stephen A. Gravina;John J. Mieyal.
Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis
Carol A. Chrestensen;David W. Starke;John J. Mieyal.
Journal of Biological Chemistry (2000)
Dysregulation of glutathione homeostasis in neurodegenerative diseases.
William M. Johnson;Amy L. Wilson-Delfosse;John. J. Mieyal.
Mechanistic and Kinetic Details of Catalysis of Thiol-Disulfide Exchange by Glutaredoxins and Potential Mechanisms of Regulation
Molly M. Gallogly;David W. Starke;John J. Mieyal;John J. Mieyal.
Antioxidants & Redox Signaling (2009)
Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction.
David W. Starke;P. Boon Chock;John J. Mieyal.
Journal of Biological Chemistry (2003)
Thioltransferase (Glutaredoxin) Is Detected Within HIV-1 and Can Regulate the Activity of Glutathionylated HIV-1 Protease in Vitro
David A. Davis;Fonda M. Newcomb;David W. Starke;David E. Ott.
Journal of Biological Chemistry (1997)
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