Lykourgos Chiniadis

Lykourgos Chiniadis
Agricultural University of Athens · Department of Biotechnology

Doctor of Philosophy

About

9
Publications
508
Reads
How we measure 'reads'
A 'read' is counted each time someone views a publication summary (such as the title, abstract, and list of authors), clicks on a figure, or views or downloads the full-text. Learn more
41
Citations
Citations since 2017
4 Research Items
39 Citations
2017201820192020202120222023051015
2017201820192020202120222023051015
2017201820192020202120222023051015
2017201820192020202120222023051015
Additional affiliations
September 2018 - present
National Center for Scientific Research Demokritos
Position
  • PhD Student
Description
  • Macromolecular crystallography of protein-bioinorganic compounds complexes.
September 2007 - August 2008
University of Florence
Position
  • Postgraduate training
Description
  • High field NMR structural determination of proteins-Protein expression and purification.
September 2005 - September 2012
Agricultural University of Athens
Position
  • PhD Student
Description
  • Cyclodextrin's/natural products compounds characterisation and their crystal structure determination by means of X-ray crystallography-Protein crystallization and Protein Crystallography.
Education
September 2010 - August 2020
Agricultural University of Athens
Field of study
  • Protein crystallography and protein dynamics
January 2007 - July 2007
Université de Reims Champagne-Ardenne
Field of study
  • R&D of natural products
September 2005 - January 2007
Agricultural University of Athens
Field of study
  • R&D of natural products

Publications

Publications (9)
Article
Full-text available
Insulin-Regulated aminopeptidase (IRAP) is a zinc-dependent aminopeptidase with several important biological functions and is an emerging pharmaceutical target for cognitive enhancement and immune system regulation. Aiming to discover lead-like IRAP inhibitors with enhanced selectivity versus homologous enzymes, we targeted an allosteric site at th...
Article
Full-text available
The high-resolution X-ray crystal structures of the adducts formed between the “half sandwich”-type Ru(II) coordination compound [RuII(1,4,7-trithiacyclononane)(ethane-1,2-diamine)Cl]+ and two proteins, namely hen egg-white lysozyme and proteinase K, are presented. The structures unveil that upon reaction with both enzymes the Ru(II) compound is co...
Article
Full-text available
Glutathione transferases (GSTs) are enzymes that contribute to cellular detoxification by catalysing the nucleophilic attack of glutathione (GSH) on the electrophilic centre of a number of xenobiotic compounds, including several chemotherapeutic drugs. In the present work we investigated the interaction of the chemotherapeutic drug chlorambucil (CB...
Data
Fo-Fc electron density map contoured at 2.7σ showing electron density corresponding to bound GSH–CBL, superimposed on refined crystal structure. (TIF)
Data
Root mean square deviations (RMSD) of GSH (black curve) and CBL moiety (red curve) atomic positions as a function of MD simulation time. Top graph is for monomer A and bottom graph is for monomer B. (TIF)
Data
Root mean square fluctuation (RMSF) of GST A1-1 Cα atoms calculated for the GSH (black) and the GSH–CBL (red) complexes from 10-ns molecular dynamics. The graph shows the mean RMSF value from the two monomers. (TIF)
Conference Paper
Full-text available
The glutathione transferases (GSTs) are detoxification enzymes that protect the cell from a wide range of potentially harmful electrophilic compounds [1]. Although this action of GSTs protects the organism from harmful environmental toxins, it results also in neutralization of certain therapeutic drugs such as chlorambucil, an anti-cancer drug used...

Network

Cited By