Dr. Nikolaos E. Labrou

Professor
Department of Biotechnology, Agricultural University of Athens, Greece

Highest Degree
Ph.D. in Biotechnology from Agricultural University of Athens, Greece

My URL
https://livedna.org/30.10737

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Biography

Dr. Nikolaos Labrou received his BSc degree in Chemistry from the University of Patras Greece (1987-1991) and his PhD in Enzyme Biotechnology from the Agricultural University of Athens Greece in (1992-1996). He has conducted Postdoctoral Research in Leeds UK (1996-1998) and at Agricultural University of Athens (1998-2001). His research covers many areas of Biotechnology including Downstream Processing, Enzyme and Protein Engineering, Cell and Tissue Culture Technologies, Proteomics and Catalomics Analysis as well as the purification and characterization of Plant Enzymes, Proteins and other Biomolecules. The group offers an exciting and Stimulating Environment for research, education and training in Molecular Biology and Enzyme Biotechnology. Within the last 15 years Dr. Labrou has authored more than 98 peer-reviewed articles in leading international journals, 26 book chapters, more than 100 conference abstracts and established a strong global academic and industrial network. Dr. Labrou started his career as Assistant Professor at the Agricultural University of Athens (2002-2007) and he is currently Professor in Enzyme Technology. He is on the editorial board of nine scientific journals and he also serves as a reviewer for more than 50 scientific journals. Dr. Labrou serves as reviewer for multiple national and international grant agencies (EE, NATO, etc), he is an advisor for one international Biotech company. He has won many awards over the years including the first prize in Business Ideas Competition Green Dreams 2008, Athens. He has served as a member in four scientific conferences organization committee. Prestigious funding agencies that have supported his research include the EU (FP4, FP6, and FP7), NATO, Bill & Melinda GATES Foundation, A.S. Onassis, Public Benefit Foundation, etc. Dr. Labrou teaches at the postgraduate and undergraduate levels. Molecular Enzymology and Analytical Biotechnology are his primary teaching interests. He has supervised and works closely with several graduate students (>20) on their master’s and doctoral dissertations. His area of expertise Includes Enzymology, Enzyme Technology, Biochemistry, Enzyme Kinetics, Enzyme Engineering, Protein Purification, Downstream Processing, Bioactive Molecules, Gene Cloning, Chromatography, Affinity Chromatography, Protein Expression, and Bioactivity Assays.

Area of Interest:

Molecular Sciences
Enzymology
Bio-Chemistry
Enzyme Kinetics
Chromatography

Selected Publications

  1. Platis, M., D. Vlachakis, A.I. Foudah, M.M. Muharram, M.H. Alqarni, A.C. Papageorgiou and N.E. Labrou, 2021. The interaction of Schistosoma japonicum glutathione transferase with cibacron blue 3GA and its fragments. Medic. Chem., 17: 332-343.
    CrossRef  |  Direct Link  |  

  2. Saeed, H., A. Hemida, N. El-Nikhely, M. Abdel-Fattah and M. Shalaby et al., 2020. Highly efficient pyrococcus furiosus recombinant l-asparaginase with no glutaminase activity: expression, purification, functional characterization, and cytotoxicity on THP-1, A549 and Caco-2 cell lines. Int. J. Bio. Macromol., 156: 812-828.
    CrossRef  |  Direct Link  |  

  3. Premetis, G.E. and N.E. Labrou, 2020. Reduce, reuse and recycle in protein chromatography: development of an affinity adsorbent from waste paper and its application for the purification of proteases from fish by-products. Biomolecules, Vol. 10. 10.3390/biom10060822.
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  4. Muharram, M.M., A.T. Abulhamd, M.F. Aldawsari, M.H. Alqarni and N.E. Labrou, 2020. Development of staphylococcus enzybiotics: The PH28 gene of Staphylococcus epidermidis phage PH15 is a two-domain endolysin. Antibiot., Vol. 9. 10.3390/antibiotics9040148.
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  5. Georgakis, N., N. Poudel, A.C. Papageorgiou and N.E. Labrou, 2020. Comparative structural and functional analysis of phi class glutathione transferases involved in multiple-herbicide resistance of grass weeds and crops. Plant Physiol. Biochem., 149: 266-276.
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  6. Tani, E., E. Chronopoulou, N. Labrou, E. Sarri and Μ. Goufa et al., 2019. Growth, physiological, biochemical, and transcriptional responses to drought stress in seedlings of Medicago sativa L., Medicago arborea L. and their hybrid (Alborea). Agronomy, Vol. 9. 10.3390/agronomy9010038.
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  7. Stavridou, E., N.A. Τzioutziou, P. Madesis, N.E. Labrou and I. Nianiou-Obeidat, 2019. Effect of different factors on regeneration and transformation efficiency of tomato (Lycopersicum esculentum) hybrids. Czech J. Genet. Plant Breed., 55: 120-127.
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  8. Stavridou, E., M. Michailidis, S. Gedeon, A. Ioakeim and S. Kostas et al., 2019. Tolerance of transplastomic tobacco plants overexpressing a theta class glutathione transferase to abiotic and oxidative stresses. Front. Plant Sci., Vol. 9. 10.3389/fpls.2018.01861.
    CrossRef  |  Direct Link  |  

  9. Csiszár, J., A. Hecker, N.E. Labrou, P. Schröder and D.E. Riechers, 2019. Editorial: plant glutathione transferases: diverse, multi-tasking enzymes with yet-to-be discovered functions. Front. Plant Sci., Vol. 10. 10.3389/fpls.2019.01304.
    CrossRef  |  Direct Link  |  

  10. Chronopoulou, E.G., D. Vlachakis, A.C. Papageorgiou, F.S. Ataya and N.E. Labrou, 2019. Structure-based design and application of an engineered glutathione transferase for the development of an optical biosensor for pesticides determination. Biochim. Biophys. Acta (BBA) Gen. Subjects, 1863: 565-576.
    CrossRef  |  Direct Link  |  

  11. Carballo, C., E.G. Chronopoulou, S. Letsiou, E. Spanidi, K. Gardikis, N.E. Labrou and M. Manchado, 2019. Genomic and phylogenetic analysis of choriolysins, and biological activity of hatching liquid in the flatfish senegalese sole. PLoS ONE, Vol. 14. 10.1371/journal.pone.0225666.
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  12. Alqarni, M.H., M.M. Muharram, S.M. Alshahrani and N.E. Labrou, 2019. Copper-induced oxidative cleavage of glutathione transferase F1-1 from Zea mays. Int. J. Bio. Macromol., 128: 493-498.
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  13. Theoharaki, C., E. Chronopoulou, D. Vlachakis, F.S. Ataya and P. Giannopoulos et al., 2018. Delineation of the functional and structural properties of the glutathione transferase family from the plant pathogen Erwinia carotovora. Funct.al Integr. Genomics, Vol. 19. 10.1007/s10142-018-0618-8.
    CrossRef  |  Direct Link  |  

  14. Mavrommatis, A., E.G. Chronopoulou, K. Sotirakoglou, N.E. Labrou, G. Zervas and E. Tsiplakou, 2018. The impact of the dietary supplementation level with Schizochytrium sp, on the oxidative capacity of both goats’ organism and milk. Livest. Sci., 218: 37-43.
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  15. Chronopoulou, E.G., F. Ataya and N.E. Labrou, 2018. A microplate-based platform with immobilized human glutathione transferase A1-1 for high-throughput screening of plant-origin inhibitors. Curr. Pharm. Biotechnol., 19: 925-931.
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  16. Chronopoulou, E.G., A.C. Papageorgiou, F. Ataya, I. Nianiou-Obeidat, P. Madesis and N.E. Labrou, 2018. Expanding the plant GSTome through directed evolution: DNA shuffling for the generation of new synthetic enzymes with engineered catalytic and binding properties. Front. Plant Sci., Vol. 9. 10.3389/fpls.2018.01737.
    CrossRef  |  Direct Link  |  

  17. Skopelitou, K., A.W. Muleta, A.C. Papageorgiou, E. Chronopoulou and N.E. Labrou, 2015. Catalytic features and crystal structure of a tau class glutathione transferase from Glycine max specifically upregulated in response to soybean mosaic virus infections. Biochem. Biophys. Acta: Proteins and Proteomics, 1854: 166-177.
    CrossRef  |  Direct Link  |  

  18. Pavlidi, N., V. Tseliou, M. Riga, R. Nauen, T. Van Leeuwen, N.E. Labrou and J. Vontas, 2015. Functional characterization of glutathione S-transferases associated with insecticide resistance in Tetranychus urticae. Pestic. Biochem. Physiol., 121: 53-60.
    CrossRef  |  Direct Link  |  

  19. Labrou, N.E., A.C. Papageorgiou, O. Pavli and E. Flemetakis, 2015. Plant GSTome: Structure and functional role in xenome network and plant stress response (2015). Curr. Opin. Biotechnol., 32: 186-194.
    CrossRef  |  Direct Link  |  

  20. Chronopoulou, E., K. Kontouri, M. Chantzikonstantinou, F. Pouliou and F. Perperopoulou et al., 2015. Plant glutathione transferases: Structure, antioxidant catalytic function and in planta protective role in biotic and abiotic stress. Curr. Chem. Biol., 8: 58-75.
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  21. Perperopoulou, F.D., P.G. Tsoungas, T.N. Thireou, V.E. Rinotas and E.K. Douni et al., 2014. 2,2'-Dihydroxybenzophenones and their carbonyl N-analogues as inhibitor scaffolds for MDR-involved human glutathione transferase isoenzyme A1-1. Bioorg. Med. Chem., 22: 3957-3970.
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  22. Maltezos, A., D. Platis, D. Vlachakis, S. Kossida, M. Marinou and N.E. Labrou, 2014. Design, synthesis and application of benzyl-sulfonate biomimetic affinity adsorbents for monoclonal antibody purification from transgenic corn. J. Mol. Recognit., 27: 19-31.
    CrossRef  |  Direct Link  |  

  23. Karamitros, C. and N.E. Labrou, 2014. Extracellular expression and affinity purification of L-asparaginase from E. chrysanthemi in E. coli. Sustainable Chem. Processes, Vol.2. 10.1186/s40508-014-0016-z.
    CrossRef  |  Direct Link  |  

  24. Chronopoulou, E., P. Madesis, A.Tsaftaris and N. E. Labrou, 2014. Cloning and characterization of a biotic stress inducible glutathione transferase from Phaseolus vulgaris. Applied Biochem. Biotechnol., 172: 595-609.
    CrossRef  |  Direct Link  |  

  25. Zoi, O., T.N. Thireou, V. Rinotas, P.G. Tsoungas and E.E. Eliopoulos et al., 2013. Designer xanthone: An inhibitor scaffold for human glutathione transferase isoenzyme A1-1. J. Biomol. Screen., 18: 1092-1102.
    CrossRef  |  Direct Link  |  

  26. Skopelitou, K., N. Georgakis, R. Efrose, E. Flemetakis and N.E. Labrou, 2013. Sol-gel immobilization of haloalkane dehalogenase from Bradyrhizobium japonicum for the remediation 1,2-dibromoethane. J. Mol. Catal. B: Enzym., 97: 5-11.
    CrossRef  |  Direct Link  |  

  27. Madesis, P., I. Nianiou-Obeidat, Α. Tsaftaris and N.Ε. Labrou, 2013. Impact of Transgene GSTs on Plant Stress Tolerance. In: Glutathione, Structure, Function And Biotechnological Implications, Labrou, N.E. and E. Flemetakis (Eds.)., Nova Publishers, USA, pp: 263-274.

  28. Kotzia, G. and N.E. Labrou, 2013. Structural and functional role of Gly281 in L-asparaginase from Erwinia carotovora. Prot Pept Lett., 20: 1302-1307.
    Direct Link  |  

  29. Chronopoulou, E., M. Chatzikonstantinou, P. Madesis, I. Nianiou-Obeidat and N.E. Labrou, 2013. Structure, Function and Catalytic Properties of Human Glutathione Transferase P1-1. In: Glutathione, Structure, Function and Biotechnological Implications, Labrou, N.E. and E. Flemetakis (Eds.)., Nova Publishers, USA, pp 187-198.

  30. Chronopoulou, E. and N.E. Labrou, 2013. Synthesis and Application of Dye-Ligand Affinity Adsorbents. In: Methods in Molecular Biology, Protein Downstream Processing, Nikolaos, L.,(Eds.)., Springer, USA, pp: 263-276.

  31. Skopelitou, K., P. Dhavala, A.C. Papageorgiou and N.E. Labrou, 2012. A glutathione transferase from agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily. Plos One, Vol.7. 10.1371/journal.pone.0034263.
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  32. Skopelitou, K., A.W. Muleta, O. Pavli, G.N. Skaracis, E. Flemetakis, A.C. Papageorgiou and N.E. Labrou, 2012. Overlapping protective roles for glutathione transferase gene family members in chemical and oxidative stress response in Agrobacterium tumefaciens. Funct. Integ. Genomics, 12: 157-172.
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  33. Platis, D., G.A. Kotzia, I.Α. Axarli, E. Chronopoulou, C. Karamitros and N.E. Labrou, 2012. Biocatalysis, Enzyme Engineering and Enzyme Biotechnology. In: Food Biochemistry and Food Processing, Simpson, B.K., L.M.L. Nollet, F. Toldra, S. Benjakul, G. Paliyath and Y.H. Hui (Eds.). 2nd Edn., Blackwell Publishing Company, USA., pp: 125-165.

  34. Chronopoulou, E., P. Madesis, B. Asimakopoulou, D. PlatisChronopoulou, E., P. Madesis, B. Asimakopoulou, D. Platis, A. Tsaftaris and N.E. Labrou, A. Tsaftaris and N.E. Labrou, 2012. Catalytic and structural diversity of the fluazifop-inducible glutathione transferases from Phaseolus vulgaris. Planta, 235: 1253-1269.
    CrossRef  |  PubMed  |  Direct Link  |  

  35. Chronopoulou, E., A.C. Papageorgiou, A. Markoglou and N.E. Labrou, 2012. Inhibition of human glutathione transferases by pesticides: Development of a simple analytical assay for the quantification of pesticides in water. J. Mol. Cat. B: Enzymatic, 81: 43-51.
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  36. Tsikou, D., C. Stedel, E.D. Kouri, M.K. Udvardi and T.L. Wang et al., 2011. Characterization of two novel nodule-enhanced α-type carbonic anhydrases from Lotus japonicus. Biochim. Biophys. Acta, Proteins Proteomics, 1814: 496-504.
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  37. Kotzia, G.A. and N.E. Labrou, 2011. Engineering substrate specificity of E. carotovora L-asparaginase for the development of biosensor. J. Mol. Cat. B: Enzymatic, 72: 95-101.

  38. Chronopoulou, E., I. Axarli, I. Nianiou-Obeidat, P. Madesis, A. Tsaftaris, and N. Labrou, 2011. Structure and antioxidant catalytic function of plant glutathione transferases. Curr. Chem. Biol., 5: 64-74.
    Direct Link  |  

  39. Skopelitou, K. and E. Labrou-Nikolaos, 2010. A new colorimetric assay for glutathione transferase-catalyzed halogen ion release for high-throughput screening. Anal. Biochem., 405: 201-206.
    PubMed  |  Direct Link  |  

  40. Platis, D.and N. Labrou, 2010. Downstream Processing Strategies for the Purification of Recombinant Proteins from Transgenic Maize. Chromatographic Evaluation of the Affinity Ligand 4-Amino-phenyl-oxanilic. In: Agriculture Research and Technology, Bundgaard, K. and L. Isaksen, Nova Publishers USA, pp: 397-416.

  41. Melissis, S.C., A.C. Papageorgiou, N.E. Labrou and Y.D. Clonis, 2010. of Moloney Murine Leukemia virus reverse transcriptase lacking RNAse activity (Μ-MLVH− RT) on a 9-aminoethyladenine-[1,6-diamine-hexane]-triazine, selected from a combinatorial library of dNTP-mimetic ligands. J. Chromatogr. Sci., 48: 496-502.

  42. Mavridis, G. and N.E. Labrou, 2010. The Interaction of the Prion Protein with Triazine-Based Biomimetic Affinity Ligands. In: Biopharmaceutics and Drug Hypersensitivity, Mossillo, P. and J. Pinzini (Eds.)., Nova Publishers, USA, pp: 177-190.

  43. Lappa, K., G.A. Kotzia and N.E. Labrou, 2010. Studies on the Thermal Stability Of The Therapeutic Enzyme L-Asparaginase From Erwinia Carotovora. In: Biochemistry and Histocytochemistry Research Developments, Fuchs, S. and Max Auer, Nova Publishers, USA, pp: 323-334.

  44. Labrou. N.E., 2010. Random mutagenesis methods for in vitro directed enzyme evolution. Curr. Protein, 11: 91-100.
    PubMed  |  Direct Link  |  

  45. Labrou, N.E., A.C. Papageorgiou and V.I. Avramis 2010. Structure-function and clinical applications of L-asparaginases. Curr. Med. Chem., 17: 2183-2185.
    PubMed  |  Direct Link  |  

  46. Dowd, A.J., E. Morou, A. Steven, H. Ismael, N.E. Labrou, M. Paine and J. Vontas, 2010. Development of a colorimetric pH assay for the quantification of pyrethroids based on glutathione transferase. Int. J. Environm. Anal. Chem., 90: 1-10.

  47. Benekos, K., C. Kissoudis, I. Nianiou-Obeidat, N.E. Labrou and P. Madesis et al., 2010. Over-expression of a specific soybean GmGSTU4 isoenzyme improves diphenyl ether and chloroacetanilide herbicide tolerance of transgenic tobacco plants. J. Biotechnol., 150: 195-201.
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  48. Axarli, I., C. Georgiadou, P. Dhavala, A.C. Papageorgiou and N.E. Labrou, 2010. Investigation of the role of conserved residues Ser13, Asn48 and Pro49 in the catalytic mechanism of the tau class glutathione transferase from Glycine max. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1804: 662-667.
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  49. Axarli, I., A. Prigipaki and N.E. Labrou, 2010. Cytochrome P450 CYP102A2 catalyzes efficient oxidation of sodium dodecyl sulphate: a molecular tool for remediation. Enzyme Res., Vol.2010. 10.4061/2010/125429.
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  50. Axarli, I. and N.E. Labrou, 2010. Directed evolution of cytochrome P450 CYP102A2 from Bacillus subtilis. Dyn. Biochem. Process Biotechnol. Mole..Biol., 4: 19-24.

  51. Skopelitou, K., D. Platis, I. Axarli and N.E. Labrou, 2009. Glutathione Transferases In Drug Discovery And Development: Towards Safer And Efficacious Drugs. In: Frontiers in Drug, Design and Discovery. Rahman, A., M.Iqbal Choudhary (Eds.)., Bentham Science Publishers UAE, pp: 23-42.

  52. Sfetsas, C.C., K. Skopelitou, L. Milios, A. Venieraki and R. Todou et al., 2009. Characterization of 1,2-dibromoethane-degrading haloalkane dehalogenase from Bradyrhizobium japonicum USDA110. Enzyme Microb. Technol., 45: 397-404.
    CrossRef  |  Direct Link  |  

  53. Platis, D., A. Maltezos, J.K.C. Ma and N.E. Labrou, 2009. Combinatorial de novo design and application of a biomimetic affinity ligand for the purification of human anti-HIV mAb 4E10 from transgenic tobacco. J. Mol. Recognit., 22: 415-424.
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  54. Platis, D. and N.E. Labrou, 2009. Application of a PEG/salt aqueous two-phase partition system for the recovery of monoclonal antibodies from unclarified transgenic tobacco extract. Biotechnol. J., 4: 1320-1327.
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  55. Kouri, E.D., N.E. Labrou, S.D. Garbis, K.I. Kalliampakou and C. Stedelet al., 2009. Molecular and biochemical characterization of the Parvulin-Type PPIases in Lotus japonicus. Plant Physiol., 150: 1160-1173.
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  56. Kotzia, G.A. and N.E. Labrou, 2009. Engineering thermal stability of L-asparaginase by in vitro directed evolution. FEBS J., 276: 1750-1761.
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  57. Chronopoulou, E.G. and N.E. Labrou, 2009. Glutathione transferases: Emerging multidisciplinary tools in red and green biotechnology. Recent Pat. Biotechnol., 3: 211-223.
    PubMed  |  

  58. Axarli, I., P. Dhavala, A.C. Papageorgiou, and N.E. Labrou, 2009. Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operated by the tau class glutathione transferases. Biochem. J., 422: 247-256.
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  59. Axarli, I., N.E. Labrou, C. Petrou, P. Kordopatis, N. Rassias and Y.D. Clonis, 2009. Sulphonamide-based bombesin prodrug analogues for glutathione transferase, useful in targeted cancer chemotherapy. Eur. J. Med. Chem., 44: 2009-2016.
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  60. Ramessar, K., T. Rademacher, M. Sack, J. Stadlmann and D. Platis et al., 2008. Cost-effective production of a vaginal protein microbicide to prevent HIV transmission. Proc. Nat. Acad. Sci. USA, 105: 3727-3732.
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  61. Platis, D., J. Drossard, R. Fischer, J.K.C. Ma and N.E. Labrou, 2008. New downstream processing strategy for the purification of monoclonal antibodies from transgenic tobacco plants. J. Chromatogr. A, 1211: 89-90.
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  62. Platis, D. and N.E. Labrou, 2008. Chemical and genetic engineering strategies to improve the potency of pharmaceutical proteins and enzymes. Curr. Med. Chem., 19: 1940-1955.
    PubMed  |  Direct Link  |  

  63. Platis, D. and N.E. Labrou, 2008. Affinity chromatography for the purification of therapeutic proteins from transgenic maize using immobilized histamine. J. Sep. Sci., 31: 636-645.
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  64. Morou, E., H.M. Ismail, A.J. Dowd, J. Hemingway, N.E. Labrou, M. Paine and J. Vontas, 2008. A dehydrochlorinase-based pH change assay for determination of DDT in sprayed surfaces. Anal. Biochem., 378: 60-64.
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  65. Kapoli, P., I.A. Axarli, D. Platis, M. Fragoulaki and M. Paine, Hemingway et al., 2008. Engineering sensitive glutathione transferase for the detection of xenobiotics. Biosens. Bioelectron., 24: 498-508.
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  66. Axarli, I., P. Dhavala, A.C. Papageorgiou and N.E. Labrou, 2008. Evaluation of a synthetic biomimetic ligand for the purification of therapeutic proteins. J. Mol. Biol., 385: 984-1002.
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  67. Andreadeli, A., D. Platis, V. Tishkov, V. Popov and N.E. Labrou, 2008. Structure-guided alteration of coenzyme specificity of formate dehydrogenase by saturation mutagenesis to enable efficient utilization of NADP. FEBS J., 15: 3859-3869.
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  68. Moschopoulou, G., I. Papanastasiou, O. Makri, N. Labrou, G. Economou, K. Soukouli and S.E. Kintzios, 2007. Cellular redox-status is associated with regulation of frond division in Spirodela polyrrhiza. Plant Cell Rep., 26: 2603-2609.
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  69. Melissis, S., N.E. Labrou and Y.D. Clonis, 2007. One-step purification of Taq DNA polymerase using nucleotide-mimetic affinity chromatography. Biotechnol. J., 2: 121-132.
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  70. Kotzia, G.A. and N.E. Labrou, 2007. L-Asparaginase from Erwinia chrysanthemi 3937: Cloning, expression and characterization. J. Biotechnol., 127: 657-669.
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  71. Smith, B.J., T. Huyton, R.P. Joosten, J.L. McKimm-Breschkin and J.G. Zhang et al., 2006. X-ray crystal structure of a calcium deficient form of influenza virus neuraminidase: implications for substrate binding Acta Crystal D: Biol. Crystallogr., 62: 947-952.

  72. Platis, D., G.A. Kotzia, I. Α. Axarli and N.E. Labrou, 2006. Enzyme Engineering and Technology, In: Food Biochemistry and Food Processing, Simpson, B.K., L.M.L Nollet, F. Toldrai, S. Benjakul, G. Paliyath and Y.H. Hui (Eds.)., Blackwell Publishing Company, USA, pp: 75-223..

  73. Platis, D., C.A. Sotriffer, Y.D. Clonis and N.E. Labrou, 2006. Lock-and-key motif as a concept for designing affinity adsorbents for protein purification. J. Chromatogr A., 1128: 138-151.
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  74. Platis, D., B.J. Smith, T. Huyton and N.E. Labrou, 2006. Structure-guided design of a novel class of benzyl-sulfonate inhibitors for influenza virus neuraminidase. Biochem. J., 399: 215-223.
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  75. Plati, D. and N.E. Labrou, 2006. Development of an aqueous two-phase partitioning system for fractionating therapeutic proteins from tobacco extract. J. Chromatogr. A, 1128: 114-124.
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  76. Melissis, S., N.E. Labrou and Y.D. Clonis, 2006. A novel library of nucleotide-mimetic triazine ligands for DNA-recognizing enzymes: application to the purification of Pfu DNA polymerase by affinity chromatography. J. Chromatogr. A, 1122: 63-75.

  77. Filippova, E.V., K.M. Polyakov, T.V. Tikhonova, T.N. Stekhanova and K.M. Boiko et al., 2006. Crystal structure of the complex of NAD-dependent formate dehydrogenase from metylotrophic bacterium Pseudomonas sp. 101 with formate. Crystallogr. Rep., 51: 627-631.

  78. Dalakouras, T., B.J. Smith, D. Platis, M.M.J. Cox and N.E. Labrou, 2006. Development of recombinant protein-based influenza vaccine: Expression and purification of Η1Ν1 influenza virus neuraminidase. J. Chromatogr. A, 1136: 48-56.
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  79. Labrou, N.E., K. Mazitsos and Y. Clonis, 2005. Dye-ligand and Biomimetic Affinity Chromatography. In: Handbook of Affinity Chromatography, Hage, D.S.,(Ed.)., Marcel Dekker, Inc, New York, pp: 231-255..

  80. Labro, N.E., M. Karavangeli, A. Tsaftaris and Y.D. Clonis, 2005. Kinetic analysis of maize glutathione S-transferase I catalysing the detoxification from chloroacetanilide herbicides. Planta, 222: 91-97.
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  81. Kotzia, G.A., I.A. Axarli, and N.E. Labrou, 2005. Evolutionary Methods in Enzyme Technology: High-Throughput Screening and Selection of New Enzyme Variants. In: Resent Research Developments in Biotechnology and Bioengineering, Pandalai, S.G., (Ed.)., Research Signpost, India, pp: 85-104.

  82. Kotzia, G.A. and N.E. Labrou, 2005. Cloning, expression and characterisation of Erwinia carotovora L-asparaginase. J. Biotechnol., 119: 309-323.
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  83. Karavangel, M., N.E. Labrou, Y.D. Clonis and A. Tsaftaris, 2005. Development of transgenic tobacco plants overexpressing maize glutathione S-transferase I for chloroacetanilide herbicides phytoremediation. Biomol Eng., 22: 121-128.
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  84. Axarli, I., A. Prigipaki and N.E. Labrou, 2005. Engineering cytochrome P450 CYP102A2 substrate specificity by directed evolution: Production of an efficient enzyme for bioconversion of fine chemicals. Biomol. Eng., 22: 81-88.
    PubMed  |  Direct Link  |  

  85. Labrou, N.E., G. Kotzia and Y.D. Clonis, 2004. Engineering the xenobiotic substrate specificity of maize glutathione S-transferase I. Prot. Eng. Des. Sel., 17: 741-748.
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  86. Labrou, N.E., D.J. Rigden and Y.D. Clonis, 2004. Engineering the pH-dependence of kinetic parameters of maize glutathione S-transferase I by site-directed mutagenesis. Biomol Eng., 21: 61-66.
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  87. Labrou, N.E., 2004. Dye-ligand Affinity Chromatography in Proteomic Research. In: Proteins and Proteomics: A Laboratory Manual, Simpson, R.J. (Ed.)., Cold Spring Harbour Laboratory Press, USA, pp: 275-299.

  88. Labrou, N.E. and D.J. Rigden, 2004. The structure-function relationship in the clostripain family of peptidases. Eur. J. Biochem., 271: 983-992.
    PubMed  |  Direct Link  |  

  89. Kotzia, G.A. and N.E. Labrou, 2004. A new affinity label for probing the structure and function of glutathione transferases. Eur. J. Biochem., 271: 3503-3511.
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  90. Katsos, Ν., N.E. Labrou and Y.D. Clonis, 2004. Interaction of L-glutamate oxidase with triazine dyes: selection of ligands for affinity chromatography. J. Chromatogr. B 807: 277-285.
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  91. Labrou, N.E., 2003. Design and selection of affinity ligands for affinity chromatography. J. Chromatogr. Β, 790: 67-78.
    CrossRef  |  Direct Link  |  

  92. Labrou, N.E., 2002. Dye-ligand affinity adsorbents for enzyme purification. Mol Biotechnol., 20: 77-84.
    CrossRef  |  Direct Link  |  

  93. Labrou, N.E., 2002. Affinity Chromatography, In: Methods for Affinity-Based Separations of Enzymes and Proteins, Gupta, M.N., (Ed.)., Birkhiuser Verlag AG, Switzerland, pp: 16-28.

  94. Labrou, N.E. and Y.D. Clonis, 2002. Immobilized Synthetic Dyes in Affinity Chromatography. Vijayalakshmi, M.A., (Ed.)., Taylor and Francis Publishers, London, pp: 235-251.

  95. Labrou, N.E., N. Bhogal, C.R. Hurrell and J.B.C. Findlay, 2001. Interaction of met297 in the seventh transmembrane segment of the tachykinin NK2 receptor with neurokinin A. J. Biol. Chem., 276: 37944-37949.
    CrossRef  |  

  96. Labrou, N.E., L.V. Mello and Y.D. Clonis, 2001. The conserved Asn49 of maize glutathione S-transferase I modulates substrate binding, catalysis and intersubunit communication. Eur. J. Biochem., 268: 3950-3957.
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  97. Labrou, N.E., L.V. Mello and Y.D. Clonis, 2001. Functional and structural roles of the glutathione binding residues in maize (Zea mays) glutathione S-transferase Ι. Biochem. J., 358: 101-110.
    CrossRef  |  Direct Link  |  

  98. Labrou, N.E. and D.J. Rigden, 2001. Active site characterization of Candida boidinii formate dehydrogenase. Biochem. J., 354: 455-463.
    CrossRef  |  Direct Link  |  

  99. Labrou, N., E. Eliopoulos and Y.D. Clonis, 1996. Molecular modeling for the design of dye-ligands and their interaction with mitochondrial malate dehydrogenase. Biochem. J., 315: 695-703.
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  100. Labrou, N., E. Eliopoulos and Y.D. Clonis, 1996. Dye-affinity labelling of bovine heart mitochondrial malate dehydrogenase and study of the NADH-binding site. Biochem. J., 315: 687-693.
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  101. Labrou, N. and Y.D. Clonis, 1996. Biomimetic-dye affinity chromatography for the purification of mitochondrial L-malate dehydrogenase from bovine heart. J. Biotechnol., 45: 185-194.
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  102. Labrou, N., A. Karagouni and Y.D. Clonis, 1995. Biomimetic-dye affinity adsorbents for enzyme purification: application to the one-step purification of Candida boidinii formate dehydrogenase. Biotech. Bioeng., 48: 278-288.
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  103. Labrou, N. and Y.D. Clonis, 1995. The interaction of Candida boidinii formate dehydrogenase with a new family of chimeric biomimetic dye-ligands. Arch. Biochem. Biophys., 316: 169-178.
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  104. Labrou, N. and Y.D. Clonis, 1995. Oxaloacetate decarboxylase: on the mode of interaction with substrate-mimetic affinity ligands. Arch. Biochem. Biophys., 321: 61-70.
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  105. Labrou, N. and Y.D. Clonis, 1995. Biomimetic-dye affinity chromatography for the purification of bovine heart L-lactate dehydrogenase. J. Chromatogr., 718: 35-44.
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  106. Labrou, N. and Y.D. Clonis, 1995. Biomimetic affinity ligands for oxalate-recognizing enzymes. Studies with oxalate oxidase and oxalate decarboxylase. J. Biotechnol., 40: 59-70.
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  107. Labrou, N. and Y.D. Clonis, 1994. The affinity technology in downstream processing. J. Biotechnol., 36: 95-119.
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