Georgios A. Spyroulias
University of Patras
146 Papers
1.1K Citations
Georgios A. Spyroulias is an academic researcher from University of Patras. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 22, co-authored 123 publications. Previous affiliations of Georgios A. Spyroulias include University of Cape Town & University of Florence.
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Papers
Replacement of heme by soluble guanylate cyclase (sGC) activators abolishes heme-nitric oxide/oxygen (H-NOX) domain structural plasticity
Aikaterini I. Argyriou,Garyfallia I. Makrynitsa,Georgios A. Dalkas,Dimitra A. Georgopoulou,Konstantinos Salagiannis,Vassiliki Vazoura,Andreas Papapetropoulos,Stavros Topouzis,Georgios A. Spyroulias +8 more
- 18 Nov 2021
TL;DR: In this paper, two sGC activators (BAY 58-2667 and BAY 60-2770) were shown to significantly decrease the conformational plasticity of the recombinant H-NOX protein domain of Nostoc sp. cyanobacterium.
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Electrochemical studies of protonated and deprotonated forms of heteroleptic and homoleptic europium(iii) and dysprosium(iii) porphyrin double-deckers
TL;DR: The cyclic voltammetric oxidation, of heteroleptic and homoleptic lanthanide porphyrin double-deckers demonstrates the presence of equilibrium protonated/deprotonated species present in CH2Cl2, DMF, and THF.
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Folding in solution of the C-catalytic protein fragment of angiotensin-converting enzyme.
Sotirios-Spyridon M. Vamvakas,Leondios Leondiadis,George Pairas,Evy Manessi-Zoupa,Georgios A. Spyroulias,Paul Cordopatis +5 more
TL;DR: The cloning, overexpression in Escherichia coli, purification and structural study of the Ala959 to Ser1066 region (ACE_C) that corresponds to the C‐catalytic domain of human somatic angiotensin‐I‐converting enzyme are presented.
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(1)H,(13)C and (15)N chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: "The SUD-M and SUD-C domains"
Angelo Gallo,Aikaterini C. Tsika,Nikolaos K. Fourkiotis,Francesca Cantini,Lucia Banci,Sridhar Sreeramulu,Harald Schwalbe,Georgios A. Spyroulias +7 more
TL;DR: In the absence of the 3D structures of SARS-CoV-2, the almost complete NMR backbone and side-chain resonance assignment (1H,13C,15N) was reported in this paper, and the NMR chemical shift-based prediction of their secondary structure elements.
NMR study of macro domains (MDs) from betacoronavirus: backbone resonance assignments of SARS-CoV and MERS-CoV MDs in the free and the ADPr-bound state.
Aikaterini C. Tsika,Nikolaos K. Fourkiotis,Periklis Charalampous,Angelo Gallo,Georgios A. Spyroulias +4 more
TL;DR: In this paper, the NMR backbone structure of SARS-CoV and MERS-coV macrodomains was analyzed in the free and ADP-ribosylation bound forms, and the chemical shift-based prediction of their secondary structure elements.