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
NMR study of non-structural proteins--part II: (1)H, (13)C, (15)N backbone and side-chain resonance assignment of macro domain from Venezuelan equine encephalitis virus (VEEV).
Garyfallia I. Makrynitsa,Dioni Ntonti,Konstantinos D. Marousis,Aikaterini C. Tsika,Julie Lichière,Julie Lichière,Nicolas Papageorgiou,Nicolas Papageorgiou,Bruno Coutard,Bruno Coutard,Detlef Bentrop,Georgios A. Spyroulias +11 more
TL;DR: This study reports the high yield recombinant expression and preliminary solution NMR study of the macro domain of VEEV, a member of the Alphavirus genus that causes fatal encephalitis to equines and humans.
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NMR study of non-structural proteins–part III: 1 H, 13 C, 15 N backbone and side-chain resonance assignment of macro domain from Chikungunya virus (CHIKV)
Michail Lykouras,Aikaterini C. Tsika,Julie Lichière,Nicolas Papageorgiou,Bruno Coutard,Detlef Bentrop,Georgios A. Spyroulias +6 more
TL;DR: The high yield expression of the macro domain from Chikungunya Alphavirus and its preliminary structural analysis via solution NMR spectroscopy are described and the α/β/α sandwich topology with 4 α-helices and 6 β-strands was predicted by TALOS+.
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NMR conformational properties of an Anthrax Lethal Factor domain studied by multiple amino acid-selective labeling.
Dionysios J. Vourtsis,Christos T. Chasapis,George Pairas,Detlef Bentrop,Georgios A. Spyroulias +4 more
TL;DR: This work presents the successful overexpression of a polypeptide of 233 residues, corresponding to the structured part of the N-terminal domain of Anthrax Lethal Factor, using Escherichia coli expression system.
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Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through 1H-NMR and chemical shift perturbation mapping
Athanassios S. Galanis,Georgios A. Spyroulias,Roberta Pierattelli,Andreas G. Tzakos,Anastassios N. Troganis,Ioannis P. Gerothanassis,George Pairas,Evy Manessi-Zoupa,Paul Cordopatis +8 more
TL;DR: The design and synthesis through solid phase 9‐flourenylmethoxycarbonyl (Fmoc) chemistry of the two angiotensin‐I converting enzyme active sites possessing the general sequence HEMGHX23EAIGDX3 suggest possible coordination modes of zinc in the native enzyme.
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Evidence for Novel Action at the Cell-Binding Site of Human Angiogenin Revealed by Heteronuclear NMR Spectroscopy, in silico and in vivo Studies
Demetra S.M. Chatzileontiadou,Demetra S.M. Chatzileontiadou,Aikaterini C. Tsika,Zoi Diamantopoulou,Jean Delbé,Josette Badet,José Courty,Vassiliki T. Skamnaki,Vanessa Parmenopoulou,Dimitri Komiotis,Joseph Hayes,Georgios A. Spyroulias,Demetres D. Leonidas +12 more
TL;DR: This is the first time that a nucleoside inhibitor is reported to completely inhibit the angiogenic activity of human angiogenin in vivo by exerting dual inhibitory activity on hAng, blocking both the entrance of hAng into the cell and its ribonucleolytic activity.