D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Biology and Biochemistry D-index 46 Citations 8,903 92 World Ranking 15132 National Ranking 6312

Overview

What is he best known for?

The fields of study he is best known for:

  • Enzyme
  • Amino acid
  • Biochemistry

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.

His most cited work include:

  • Molecular Mechanisms and Clinical Implications of Reversible Protein S-Glutathionylation (427 citations)
  • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. (376 citations)
  • Glutaredoxin: Role in Reversible Protein S-Glutathionylation and Regulation of Redox Signal Transduction and Protein Translocation (324 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

  • Biochemistry (48.75%)
  • Glutaredoxin (47.50%)
  • Glutathione (35.00%)

What were the highlights of his more recent work (between 2011-2018)?

  • Cell biology (31.25%)
  • Glutaredoxin (47.50%)
  • Oxidative stress (15.00%)

In recent papers he was focusing on the following fields of study:

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.

Between 2011 and 2018, his most popular works were:

  • Dysregulation of glutathione homeostasis in neurodegenerative diseases. (193 citations)
  • Posttranslational Modification of Cysteine in Redox Signaling and Oxidative Stress: Focus on S-Glutathionylation (128 citations)
  • Protein-Thiol Oxidation and Cell Death: Regulatory Role of Glutaredoxins (117 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Amino acid
  • Biochemistry

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.

Best Publications

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)

686 Citations

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

Molly M Gallogly;John J Mieyal.
Current Opinion in Pharmacology (2007)

599 Citations

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)

510 Citations

Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells

Jun Wang;Emily S. Boja;Wuhong Tan;Ephrem Tekle.
Journal of Biological Chemistry (2001)

396 Citations

Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.

Stephen A. Gravina;John J. Mieyal.
Biochemistry (1993)

386 Citations

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)

380 Citations

Dysregulation of glutathione homeostasis in neurodegenerative diseases.

William M. Johnson;Amy L. Wilson-Delfosse;John. J. Mieyal.
Nutrients (2012)

338 Citations

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)

272 Citations

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)

249 Citations

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)

231 Citations

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