FEBS Open Bio seeks an Editor-in-Chief

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Alapítói köszöntő a "Gerundium" Egyetemtörténeti Közlemények című folyóirat indításához

Alapítói köszöntő a "Gerundium" Egyetemtörténeti Közlemények című folyóirat indításáho

90 éves a Magyar Tudományos Akadémia Ökológiai Kutatóközpont Balatoni Limnológiai Intézete

The Lake Balaton Institute of Limnology of the Ecological Research Centre of the Hungarian Academy of Arts and Sciences is 90 years old. The Balaton Limnology Institute of the Hungarian Academy of Arts and Sciences celebrated the 90th anniversary of its opening on the 8th of September, 2017, in Tihany, where László Fésüs, chairman of the Biology Section of the Hungarian Academy of Sciences greeted the event with the address printed here. The institute, originally called "The Hungarian Biology Research Institute" was the very first independent research institution in Hungary, established and opened in 1927 by the famous politician Kúnó Klébelsberg who is also highly respected for developing university campuses and many new elementary schools. During nine decades the institute attracted leading life scientists from Hungary as well as abroad, its research areas covered the major trends in biology including broad topics in botany, zoology, molecular biology, neurobiology and has had a crucial role saving Lake Balaton from ecological catastrophes

Alapítói köszöntő a "Gerundium" Egyetemtörténeti Közlemények című folyóirat indításához

Alapítói köszöntő a "Gerundium" Egyetemtörténeti Közlemények című folyóirat indításáho

Protein-peptide based assay for the characterization of human blood coagulation factor XIII-A isopeptidase activity

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An involucrin-like protein in hepatocytes serves as a substrate for tissue transglutaminase during apoptosis

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Real-time kinetic method to monitor isopeptidase activity of transglutaminase 2 on protein substrate

Transglutaminase 2 (TG2) is a ubiquitously expressed multifunctional protein with Ca2+-dependent transamidase activity forming protease resistant Nε-(γ-glutamyl)lysine crosslinks between proteins. It can also function as an isopeptidase cleaving the previously formed crosslinks. The biological significance of this activity has not been revealed yet mainly because of the lack of protein based method for its characterization. Here we report development of a novel kinetic method for measuring isopeptidase activity of human TG2 by monitoring decrease in the fluorescence polarisation of a protein substrate previously formed by crosslinking fluorescently labelled glutamine donor FLpepT26 to S100A4 at a specific lysine residue. The developed method could be applied to test mutant enzymes and compounds which influence isopeptidase activity of TG2

Transglutaminase 2 Has Metabolic and Vascular Regulatory Functions Revealed by In Vivo Activation of Alpha1-Adrenergic Receptor

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