The scientist’s investigation covers issues in Biochemistry, Reactive oxygen species, Peptide, Cysteine and Peroxynitrite. Biochemistry is a component of his Methionine sulfoxide, Calmodulin, Protein oxidation, Methionine and Endoplasmic reticulum studies. Christian Schöneich has included themes like Organic chemistry, Oxygen and Drug in his Reactive oxygen species study.
His biological study spans a wide range of topics, including Calcitonin, Degradation pathway and Membrane protein. The Cysteine study combines topics in areas such as Chemical modification and Trypsin. The study incorporates disciplines such as Nitric oxide and Dithiothreitol in addition to Peroxynitrite.
Christian Schöneich mainly focuses on Biochemistry, Photochemistry, Radical, Peptide and Stereochemistry. When carried out as part of a general Biochemistry research project, his work on Endoplasmic reticulum, Cysteine, Peroxynitrite and Tyrosine is frequently linked to work in In vivo, therefore connecting diverse disciplines of study. He usually deals with Photochemistry and limits it to topics linked to Sulfur and Aqueous solution.
His work is dedicated to discovering how Radical, Medicinal chemistry are connected with Thioether and other disciplines. His research in Peptide intersects with topics in Thiyl radicals, Reactive oxygen species and Chromatography. His Stereochemistry research incorporates themes from Residue, Organic chemistry, Methionine, Side chain and Histidine.
His primary areas of investigation include Biochemistry, Chromatography, Photochemistry, Amino acid and Stereochemistry. Many of his studies involve connections with topics such as Monoclonal antibody and Biochemistry. His Chromatography research is multidisciplinary, relying on both Size-exclusion chromatography, Protein aggregation and Monomer.
The concepts of his Photochemistry study are interwoven with issues in Condensation, Redox and Radical. His Stereochemistry research includes elements of Side chain, Organic chemistry, Isomerization and Methionine. Christian Schöneich combines subjects such as HEK 293 cells, Molecular biology and Endoplasmic reticulum with his study of SERCA.
Biochemistry, Chromatography, Photochemistry, Redox and Protein degradation are his primary areas of study. As part of his studies on Biochemistry, Christian Schöneich frequently links adjacent subjects like Monoclonal antibody. His Photochemistry study combines topics from a wide range of disciplines, such as Hydrolysis and Controlled degradation.
His Redox study also includes fields such as
Oxidative stress which connect with Thiol redox, Reaction rate constant, Reactivity and Intramolecular force,
Thiyl radicals, Hydrogen transfer, Proteolysis and Chemical kinetics most often made with reference to Glutathione. Christian Schöneich interconnects Cystine and Stereochemistry in the investigation of issues within Radical. His Stereochemistry study also includes
Covalent bond that intertwine with fields like Histidine,
Residue which connect with Peptide.
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.
S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide.
Takeshi Adachi;Robert M Weisbrod;David R Pimentel;Jia Ying.
Nature Medicine (2004)
SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model
Maged M. Harraz;Jennifer J. Marden;Weihong Zhou;Yulong Zhang.
Journal of Clinical Investigation (2008)
Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease
Biochimica et Biophysica Acta (2005)
Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle.
Rosa I. Viner;Deborah A. Ferrington;Todd D. Williams;Diana J. Bigelow.
Biochemical Journal (1999)
Chemical instability of protein pharmaceuticals: Mechanisms of oxidation and strategies for stabilization
Shihong Li;Christian Schöneich;Ronald T. Borchardt.
Biotechnology and Bioengineering (1995)
Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase.
Rosa I. Viner;Todd D. Williams;Christian Schoneich.
Oxidative degradation of pharmaceuticals: theory, mechanisms and inhibition.
Susan W. Hovorka;Christian Schöneich.
Journal of Pharmaceutical Sciences (2001)
Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging.
Jaroslaw Kanski;Antje Behring;Jill Pelling;Christian Schöneich.
American Journal of Physiology-heart and Circulatory Physiology (2005)
Protein instability and immunogenicity: Roadblocks to clinical application of injectable protein delivery systems for sustained release
Wim Jiskoot;Theodore W. Randolph;David B. Volkin;C. Russell Middaugh.
Journal of Pharmaceutical Sciences (2012)
Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry.
Jaroslaw Kanski;Sung J. Hong;Christian Schöneich.
Journal of Biological Chemistry (2005)
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