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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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3-Aminobenzamide protects primary human keratinocytes from UV-induced cell death by a poly(ADP-ribosyl)ation independent mechanism.

TL;DR: It is found that 3-aminobenzamide is photoprotective and acts by a PARP-independent mechanism at a premitochondrial step of phototoxicity and is a survival mechanism in UV-treated keratinocytes.
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Calcineurin regulates endothelial barrier function by interaction with and dephosphorylation of myosin phosphatase

TL;DR: CN may improve endothelial barrier function via inducing dephosphorylation of cofilin(pSer3) and by interaction withMYPT1 and activating MP through MYPT1(pThr696) deph phosphatelation, thereby affecting actin polymerization and decreasing myosin phosphorylation.
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Tethered derivatives of D-glucose and pentacyclic triterpenes for homo/heterobivalent inhibition of glycogen phosphorylase

TL;DR: Propargyl esters of the C-28 carboxylic acids of pentacyclic triterpenes were coupled with 2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl azide as well as N-(ω-azido-[C-2, C-6, and C-11]alkanoyl)-β- D-glUCopyrnosylamines under conditions of
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Synthesis of 1,2,3-triazoles from xylosyl and 5-thioxylosyl azides: evaluation of the xylose scaffold for the design of potential glycogen phosphorylase inhibitors

TL;DR: Deacetylation afforded 19 hydroxylated xylose and 5-thioxylose derivatives, found to be only sparingly water-soluble and much weaker inhibitors of glycogen phosphorylase than glucose-based analogues.
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Crystallographic Studies on α- and β-D-glucopyranosyl Formamide Analogues, Inhibitors of Glycogen Phosphorylase

TL;DR: In this article, three D-glucopyranosyl analogues, C-(1-azido-α-D-GLU-glU-poly(1-acetamido)-α,D-glUCU-DGLU(1)-formamide, and C-( 1-hydroxy-β-DglU-, β-DG-glugopyranoyl) formamide, were recognized as moderate competitive inhibitors of muscle GPb with Ki values of 1.80 (± 0.2) mM, 0.31