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Pál Gergely

Researcher at University of Debrecen

Publications -  200
Citations -  6031

Pál Gergely is an academic researcher from University of Debrecen. The author has contributed to research in topics: Glycogen phosphorylase & Phosphorylase kinase. The author has an hindex of 42, co-authored 199 publications receiving 5643 citations. Previous affiliations of Pál Gergely include Hungarian Academy of Sciences & Novartis.

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Kinetic and crystallographic studies of glucopyranosylidene spirothiohydantoin binding to glycogen phosphorylase b

TL;DR: The structure of GPb-TH complex reveals that the inhibitor can be accommodated in the catalytic site of T-state GPb with very little change of the tertiary structure, and provides a basis of understanding potency and specificity of the inhibitor.
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Partial protection by poly(ADP-ribose) polymerase inhibitors from nitroxyl-induced cytotoxicity in thymocytes

TL;DR: The results demonstrate that NO(-)/HNO-induced PARP activation shifts the default apoptotic cell death toward necrosis in thymocytes, however, as total PARP inhibition resulted only in 30% cytoprotection, PARP-independent mechanisms dominate NO (-)/H NO-induced cytotoxicity inThymocytes.
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Effect of glucopyranosylidene-spiro-thiohydantoin on glycogen metabolism in liver tissues of streptozotocin-induced and obese diabetic rats.

TL;DR: Co-ordinated regulation of glycogen phosphorylase and synthase is demonstrated by 50 µM TH in liver extracts of Wistar rats, resulting in the activation of synthase by a shortening of the latency compared to control animals, which was effective in lowering blood glucose levels and restoring hepatic glycogen content in streptozotocin-induced diabetic rats.
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Protein phosphatase 2A is involved in the regulation of protein kinase A signaling pathway during in vitro chondrogenesis.

TL;DR: It is demonstrated that PP2A plays a role in the regulation of the PKA signaling pathway and that the phosphorylation level of CREB is influenced by the activity of both enzymes during in vitro chondrogenesis.
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Okadaic acid induces phosphorylation and translocation of myosin phosphatase target subunit 1 influencing myosin phosphorylation, stress fiber assembly and cell migration in HepG2 cells.

TL;DR: Results indicate that OA induces differential phosphorylation and translocation of MYPT1, dependent on PP2A and, to varying extents, on ROK, associated with an increased level of myosin II phosphorylated and attenuation of hepatic cell migration.