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Norbert W. Seidler
Researcher at Kansas City University of Medicine and Biosciences
Publications - 53
Citations - 1701
Norbert W. Seidler is an academic researcher from Kansas City University of Medicine and Biosciences. The author has contributed to research in topics: Glycation & Carnosine. The author has an hindex of 19, co-authored 53 publications receiving 1630 citations. Previous affiliations of Norbert W. Seidler include State University of New York System & University of Health Sciences Antigua.
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Journal ArticleDOI
Cyclopiazonic acid is a specific inhibitor of the Ca2+-ATPase of sarcoplasmic reticulum.
TL;DR: It is found that at low ATP concentrations (0.5-2 microM) the inhibition of ATPase activity was essentially complete at a CPA concentration of 6-8 nmol/mg protein, indicating stoichiometric reaction of CPA with the Ca2+-ATPase, which suggests that CPA interferes with the ATP-induced conformational changes related to Ca2- transport.
Journal ArticleDOI
Anti-crosslinking properties of carnosine: Significance of histidine
TL;DR: In this article, the authors showed that the imidazolium group of histidine or carnosine may stabilize adducts formed at the primary amino group, which is a potential treatment for Alzheimer's disease.
Book ChapterDOI
Basic Biology of GAPDH
TL;DR: The GAPDH protein exhibits an intrinsic asymmetry of the subunits, which may speak to its functional diversity and the role of inter-subunit interactions in catalysis still offers some mysteries, particularly with regards to other emerging enzymatic properties.
Journal ArticleDOI
Carnosine disaggregates glycated alpha-crystallin: an in vitro study.
TL;DR: The data support the hypothesis that carnosine disaggregates glycated alpha-crystallin, and Carnival increased peptide chain mobility, which may contribute to the controlled unfolding of glycated protein.
Journal ArticleDOI
Exercise causes oxidative damage to rat skeletal muscle microsomes while increasing cellular sulfhydryls
TL;DR: It is concluded that exercise profoundly effects membrane structures and the body compensates for this lipid peroxidation and protein damage by increasing total cellular sulfhydryls in blood plasma and skeletal muscle which would aid in repair of the damaged membranes.