Petros Giastas
About
Petros Giastas is a scholar working on Oncology, Molecular Biology and Materials Chemistry.
According to data from OpenAlex, Petros Giastas has authored 40 papers receiving a total of 823 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Oncology, 15 papers in Molecular Biology and 13 papers in Materials Chemistry. Recurrent topics in Petros Giastas's work include Peptidase Inhibition and Analysis (12 papers), Nicotinic Acetylcholine Receptors Study (7 papers) and Enzyme Structure and Function (7 papers). Petros Giastas is often cited by papers focused on Peptidase Inhibition and Analysis (12 papers), Nicotinic Acetylcholine Receptors Study (7 papers) and Enzyme Structure and Function (7 papers). Petros Giastas collaborates with scholars based in Greece, France and United States. Petros Giastas's co-authors include Socrates J. Tzartos, Irene M. Mavridis, Efstratios Stratikos, Athanasios Papakyriakou, Marios Zouridakis, Emmanuel Saridakis, Anastasia Mpakali, Dimitris Georgiadis, Pìotr Bregestovski and Eleftherios Zarkadas and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.
In The Last Decade
Petros Giastas
39 papers receiving 816 citations
Peers
Petros Giastas
Daniel Clayton Australia
Ralph Krätzner Germany
Anthony P. Duff Australia
Shaoyong Li China
Flavia Anna Mercurio Italy
Angelo Gallo Italy
Peter Hart United States
Andrew K. Lewis United States
Michele Fiore France
Arpita Agrawal United States
Citations per year, relative to Petros Giastas Petros Giastas (= 1×)
peers
Daniel Clayton
Countries citing papers authored by Petros Giastas
Since
Specialization
Citations
This map shows the geographic impact of Petros Giastas's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Petros Giastas with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Petros Giastas more than expected).
Fields of papers citing papers by Petros Giastas
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Petros Giastas. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Petros Giastas. The network helps show where Petros Giastas may publish in the future.
Co-authorship network of co-authors of Petros Giastas
This figure shows the co-authorship network connecting the top 25 collaborators of Petros Giastas. A scholar is included among the top collaborators of Petros Giastas based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Petros Giastas. Petros Giastas is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Mpakali, Anastasia, Liying Lu, Νikolaos S. Τhomaidis, et al.. (2024). Mechanisms of Allosteric Inhibition of Insulin-Regulated Aminopeptidase. Journal of Molecular Biology. 436(6). 168449–168449.
2.
Bratsos, I., et al.. (2020). High-resolution crystal structures of a “half sandwich”-type Ru(II) coordination compound bound to hen egg-white lysozyme and proteinase K. JBIC Journal of Biological Inorganic Chemistry. 25(4). 635–645.
3.
Mpakali, Anastasia, Emmanuel Saridakis, Petros Giastas, et al.. (2020). Structural Basis of Inhibition of Insulin-Regulated Aminopeptidase by a Macrocyclic Peptidic Inhibitor. ACS Medicinal Chemistry Letters. 11(7). 1429–1434.
4.
Giastas, Petros, Sofia Arnaouteli, Socrates J. Tzartos, et al.. (2019). The putative polysaccharide deacetylase Ba0331: cloning, expression, crystallization and structure determination. Acta Crystallographica Section F Structural Biology Communications. 75(4). 312–320.
5.
Zouridakis, Marios, Athanasios Papakyriakou, Igor A. Ivanov, et al.. (2019). Crystal Structure of the Monomeric Extracellular Domain of α9 Nicotinic Receptor Subunit in Complex With α-Conotoxin RgIA: Molecular Dynamics Insights Into RgIA Binding to α9α10 Nicotinic Receptors. Frontiers in Pharmacology. 10. 474–474.
6.
Giastas, Petros, Marios Zouridakis, & Socrates J. Tzartos. (2017). Understanding structure–function relationships of the human neuronal acetylcholine receptor: insights from the first crystal structures of neuronal subunits. British Journal of Pharmacology. 175(11). 1880–1891.
7.
Kouvatsos, Nikolaos, et al.. (2016). Crystal structure of a human neuronal nAChR extracellular domain in pentameric assembly: Ligand-bound α2 homopentamer. Proceedings of the National Academy of Sciences. 113(34). 9635–9640.
8.
Arnaouteli, Sofia, Petros Giastas, Christine Aldridge, et al.. (2015). Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis. Journal of Biological Chemistry. 290(21). 13465–13478.
9.
Mpakali, Anastasia, et al.. (2015). Structural Basis for Antigenic Peptide Recognition and Processing by Endoplasmic Reticulum (ER) Aminopeptidase 2. Journal of Biological Chemistry. 290(43). 26021–26032.
10.
Azam, Layla, Athanasios Papakyriakou, Marios Zouridakis, et al.. (2015). Molecular Interaction of α-Conotoxin RgIA with the Rat α9α10 Nicotinic Acetylcholine Receptor. Molecular Pharmacology. 87(5). 855–864.
11.
Zouridakis, Marios, et al.. (2014). Crystal structures of free and antagonist-bound states of human α9 nicotinic receptor extracellular domain. Nature Structural & Molecular Biology. 21(11). 976–980.
12.
Lazaridis, Konstantinos, Paraskevi Zisimopoulou, Petros Giastas, et al.. (2013). Expression of human AChR extracellular domain mutants with improved characteristics. International Journal of Biological Macromolecules. 63. 210–217.
13.
Evnouchidou, Irini, James R. Birtley, Sergey S. Seregin, et al.. (2012). A Common Single Nucleotide Polymorphism in Endoplasmic Reticulum Aminopeptidase 2 Induces a Specificity Switch That Leads to Altered Antigen Processing. The Journal of Immunology. 189(5). 2383–2392.
14.
Saridakis, Emmanuel, et al.. (2009). Insight into the protein and solvent contributions to the reduction potentials of [4Fe–4S]2+/+ clusters: crystal structures of the Allochromatium vinosum ferredoxin variants C57A and V13G and the homologous Escherichia coli ferredoxin. JBIC Journal of Biological Inorganic Chemistry. 14(5). 783–799.
15.
Saridakis, Emmanuel, et al.. (2007). Comparison of ferredoxins fromPs. aeruginosa,E. coliand anAl. vinosummutant. Acta Crystallographica Section A Foundations of Crystallography. 63(a1). s176–s176.
16.
Giastas, Petros, Nikos Pinotsis, Matthias Wilmanns, et al.. (2006). The structure of the 2[4Fe–4S] ferredoxin from Pseudomonas aeruginosa at 1.32-Å resolution: comparison with other high-resolution structures of ferredoxins and contributing structural features to reduction potential values. JBIC Journal of Biological Inorganic Chemistry. 11(4). 445–458.
17.
Bethanis, Kostas, et al.. (2005). Inclusion compounds of plant growth regulators in cyclodextrins. V. 4-Chlorophenoxyacetic acid encapsulated in β-cyclodextrin and heptakis(2,3,6-tri-O-methyl)-β-cyclodextrin. Acta Crystallographica Section B Structural Science. 61(2). 207–217.
18.
Yoshizawa, Kazuhiro, Shinji Toyota, Fumio Toda, et al.. (2005). Control of Differential Inclusion Complexation in the Solid State by Seed Crystals. Angewandte Chemie International Edition. 44(32). 5097–5100.
19.
Giastas, Petros, et al.. (2004). X-ray crystallography and solution NMR spectroscopy characterization of heptakis(2,3-di-O-acetyl-6-bromo-6-deoxy)cyclomaltoheptaose. Carbohydrate Research. 339(6). 1189–1194.
20.
Giastas, Petros, Konstantina Yannakopoulou, & Irene M. Mavridis. (2003). Molecular structures of the inclusion complexes β-cyclodextrin–1,2-bis(4-aminophenyl)ethane and β-cyclodextrin–4,4′-diaminobiphenyl; packing of dimeric β-cyclodextrin inclusion complexes. Acta Crystallographica Section B Structural Science. 59(2). 287–299.
Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.
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