P
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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The subcellular distribution and regulation of platelet phosphoprotein phosphatase
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Limited proteolysis by subtilisin reveals structural differences between phosphorylase a and b.
TL;DR: The limited proteolysis of rabbit skeletal muscle phosphorylase a and b was studied with subtilisin BPN' immoblized to Sepharose 4B and addition of AMP to phosphory lase b favours a conformation similar to--but not identical with--phosphoryl enzyme a as recognised by subtILisin action.
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The role of protein kinase C isoenzymes in the pathogenesis of human autoimmune diseases.
Sándor Sipka,Tamás Bíró,Gabriella Czifra,Zoltán Griger,Pál Gergely,Boglarka Brugos,Tünde Tarr +6 more
TL;DR: In this paper , the role of protein kinase C (PKC) enzymes in the immune system is discussed and the defects of seven PKC isoenzymes in the peripheral blood mononuclear cells (PBMC) demonstrate that these molecular impairments are not prerequisits of the pathogenesis of systemic lupus erythematosus (SLE), mixed connective tissue disease and Sjögren's syndrome.
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Phosphorylation-induced conformational changes in the phosphorylase ab hybrid as revealed by resolution of pyridoxal 5'-phosphate with imidazole citrate and cysteine.
TL;DR: It is concluded that partial phosphorylation of phosphorylaseb elicits conformational change(s) in both subunits which influence the monomer-monomer interactions and resolution of pyridoxal 5′-phosphates.
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Dephosphorylation of 32P-tetradecapeptide derived from phosphorylase a shows ligand sensitivity with phosphorylase b'.
Pál Gergely,György Bot +1 more
TL;DR: Phosphorylase b ′, a modified form of phosphorylases a in which the phosphorylated site has been removed by tryptic attack, can increase the liberation of 32 P from the tetradecapeptide.