Frontiers in Science

Frontiers in Science is a peer-reviewed, open access journal that publishes original research articles as well as review articles in all areas of science and technology.

Nikolaos Labrou

Editorial Board Member of Frontiers in Science

Associate Professor, Department of Agr. Biotechnology, Agricultural University of Athens, Greece

Research Areas

Biotechnology, Biochemistry and Molecular Biology

Education

1996-1998Postdoctoral trainingUniversity of Leeds, Department of Biochemistry and Molecular Biology, UK
1996Ph.D Agricultural University of Athens, Greece
1991B.ScUniversity of Patras, Depart. of Chemistry, Greece

Experience

2007-presentAssociate Professor, Agricultural University of Athens, Department of Biotechnology, Greece
2003-2007 Assistant Professor, Agricultural University of Athens, Department of Biotechnology, Greece
2000-2002 Senior Research Scientist, Agricultural University of Athens, Greece
1998-2000 Research Scientist, 401 Military Hospital, Athens, Greece
1996-1998Postdoctoral Research Fellow, University of Leeds, Department of Biochemistry and Molecular Biology, UK

Academic Achievement

1996 BIOTECHNOLOGY Scholarship (EU, Fourth Framework Programme for RTD)
2003 NATO Research award, 2003
2008 First prize in Business Ideas Competition 'Green Dreams' 2008, Athens, Greece

Membership

1992-Member of the Association of the Greek Chemists
1992-Member of the Hellenic Biochemical and Molecular Biology Society
1999-Member of the European Federation of Biotechnology (Member of the Board 'Biodiversity')
2000-Member of the European Association of Pharma Biotechnology (Member of the Special Interest Group on Regulation Affairs)
2000-Member of the Biochemical Society (UK)
2004-Member of the Hellenic Proteomics society
2004-Member of the Member of the Ministry of Development scientific committee
2006-Member of the Institutional Post Graduate Committee (AUA)
2009-Member of the Institutional Evaluation Committee (AUA)

Publications: Journals

[1]  N.E. Labrou & Y.D. Clonis (1994). The affinity technology in downstream processing. J. Biotechnol., 36, 95-119. (Impact Factor: 2,600)
[2]  N.E. Labrou & 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.(Impact Factor: 2,969)
[3]  N.E. Labrou & Y.D. Clonis (1995). Oxaloacetate decarboxylase: on the mode of interaction with substrate-mimetic affinity ligands. Arch. Biochem. Biophys. 321, 61-70.(Impact Factor: 2,969)
[4]  N.E. Labrou & Y.D. Clonis (1995). Biomimetic affinity ligands for oxalate-recognizing enzymes. Studies with oxalate oxidase and oxalate decarboxylase. J. Biotechnol., 40, 59-70. (Impact Factor: 2,6)
[5]  N.E. Labrou, A. Karagouni & 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. (Impact Factor: 2,999)
[6]  N.E. Labrou & Y.D. Clonis (1995). Biomimetic-dye affinity chromatography for the purification of bovine heart L-lactate dehydrogenase. J. Chromatogr A., 718, 35-44. (Impact Factor: 4.101)
[7]  N.E. Labrou, E. Eliopoulos & 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. (Impact Factor: 5,2)
[8]  N.E. Labrou, E. Eliopoulos & Y.D. Clonis (1996). Molecular modeling for the design of dye-ligands and their interaction with mitochondrial malate dehydrogenase. Biochem. J., 315, 695-703. (Impact Factor: 5,2)
[9]  N.E. Labrou & Y.D. Clonis (1996). Biomimetic-dye affinity chromatography for the purification of mitochondrial L-malate dehydrogenase from bovine heart. J. Biotechnol., 45, 185-194. (Impact Factor: 2,6)
[10]  N.E. Labrou & Y.D. Clonis (1997). Biomimetic-dye affinity chromatography for simultaneous separation and purification of lactate dehydrogenase and malate dehydrogenase from bovine heart. Bioprocess Engineering, 16, 157-161.(Impact Factor: 1,092)
[11]  N.E. Labrou & Y.D. Clonis (1997). L-malate dehydrogenase from Pseudomonas stutzeri: purification and characterization. Arch. Biochem. Biophys., 337, 103-114. (Impact Factor: 2,969)
[12]  N.E. Labrou, E. Eliopoulos & Y.D. Clonis (1999). Molecular Modelling for the Design of a Biomimetic Chimeric Ligand. Application to the Purification of Bovine Heart L-Lactate dehydrogenase. Biotechnol. Bioeng. 63, 322-332. (Impact Factor: 2,999)
[13]  N.E. Labrou, L.V. Mello, D.J. Rigden, J.N. Keen & J.B.C. Findlay (1999). Structure-activity studies on cysteine-substituted neurokinin A analogs. Peptides, 20, (7), 795-801. (Impact Factor: 2,442)
[14]  N.E. Labrou & Y.D. Clonis (1999). Oxaloacetate decarboxylase from Pseudomonas stutzeri: purification and characterization. Arch. Biochem. Biophys., 365, 17-24. (Impact Factor: 2,969)
[15]  N.E. Labrou (1999). Afinity labeling of oxaloacetate decarboxylase by novel dichlorotriazine linked α-ketoacids. J. Prot. Chem., 18, 729-733. (Impact Factor: 1,01)
[16]  N.E. Labrou (2000). Improved Purification of Candida boidinii Formate Dehydrogenase. Bioseparation, 9, 99-104. (Impact Factor: 1.077)
[17]  N.E. Labrou (2000). Dye Affinity Labelling of yeast Alcohol Dehydrogenase. J. Enzyme Inhibition, 15, 487-496. (Impact Factor: 1,636)
[18]  N.E. Labrou, D. J. Rigden & Y. D. Clonis (2000) Characterization of NAD+ binding site of Candida boidinii Formate Dehydrogenase by affinity labelling and site-directed mutagenesis. Eur. J. Biochem. 267, 6657-6664. (Impact Factor: 3,579)
[19]  Y.D. Clonis, N.E. Labrou, V. Kotsira, K. Mazitsos, S. Melissis, & G. Gogolas. (2000). Biomimetic Dyes as Affinity Chromatography Tools in Enzyme Purification. J. Chromatogr. A, 891, 33-44. (Impact Factor: 4.101)
[20]  N.E. Labrou & D. J. Rigden (2001) Active site characterization of Candida boidinii Formate Dehydrogenase. Biochem. J. 354, 455-463. (Impact Factor: 5,2)
[21]  N.E. Labrou (2001) Dye-ligand affinity adsorbents for enzyme purification Mol. Biotechnology, 20, 77-84. (Impact Factor: 2,041)
[22]  N.E. Labrou, L.V. Mello & 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. (Impact Factor: 5,2)
[23]  N.E. Labrou, L.V. Mello & 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. (Impact Factor: 3,579)
[24]  N.E. Labrou, N. Bhogal., C.R. Hurrell & 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. (Impact Factor: 5,808)
[25]  N.E. Labrou (2003) Design and selection of affinity ligands for affinity chromatography. J. Chromatogr. Β, 790, 67-78. (Impact Factor: 2,935)
[26]  G.A. Kotzia & N.E. Labrou (2004). S-(2,3-dichlorotriazinyl)glutathione. A new affinity label for probing the structure and function of glutathione transferases. Eur J Biochem., 271(17):3503-3511. (Impact Factor: 3,579)
[27]  Ν. Katsos, N.E. Labrou & Clonis YD (2004). Interaction of L-glutamate oxidase with triazine dyes: selection of ligands for affinity chromatography. J Chromatogr B Analyt Technol Biomed Life Sci. 807, 277-285. (Impact Factor: 2,935)
[28]  Ι.Α. Axarli, Rigden D.J. & N.E. Labrou (2004). Characterization of the ligandin site of maize glutathione S-transferase I. Biochem J. 382, 885-893. (Impact Factor: 5,2)
[29]  N.E. Labrou, Rigden D.J. & Clonis Y.D. (2004). Engineering the pH-dependence of kinetic parameters of maize glutathione S-transferase I by site-directed mutagenesis. Biomol Eng. 21(2), 61-66. (Impact Factor: 4,246)
[30]  N.E. Labrou & Rigden D.J. (2004). The structure-function relationship in the clostripain family of peptidases. Eur J Biochem. 271(5), 983-992. (Impact Factor: 3,579)
[31]  N.E. Labrou, G. Kotzia & Y. D. Clonis (2004). Engineering the xenobiotic substrate specificity of maize glutathione S-transferase I. Prot. Eng. Des. Sel. 17(10):741-8. (Impact Factor: 3,00)
[32]  I. Axarli, A. Prigipaki & 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. (Impact Factor: 4,246)
[33]  G.A. Kotzia, and N.E. Labrou (2005). Cloning, expression and characterisation of Erwinia carotovora L-asparaginase, J. Biotechnol., 119(4):309-23. (Impact Factor: 2,600)
[34]  N.E. Labrou (2005) Directed enzyme evolution: Bridging the gap between natural enzymes and commercial applications. Biomol. Eng. (Editorial), 22, vii-ix. (Impact Factor: 4,246)
[35]  N.E. Labrou, M. Karavangeli, A. Tsaftaris & Y. D. Clonis (2005). Kinetic analysis of maize glutathione S-transferase I catalysing the detoxification from chloroacetanilide herbicides, Planta, 222(1):91-7. (Impact Factor: 2,963)
[36]  M. Karavangeli, N.E. Labrou, Y.D. Clonis, A. Tsaftaris (2005). Development of transgenic tobacco plants overexpressing maize glutathione S-transferase I for chloroacetanilide herbicides phytoremediation. Biomol Eng. 22(4):121-8. (Impact Factor: 4,246)
[37]  E.V. Filippova, , Polyakov, K.M., Tikhonova, T.V., Stekhanova, T.N., Boiko, K.M., Sadihov, I.G., Tishkov, V.I., Popov, V.O., N.E. Labrou (2006) Crystal structure of the complex of NAD-dependent formate dehydrogenase from metylotrophic bacterium Pseudomonas sp.101 with formate. Crystallography Reports v51 pp.627-631. (Impact Factor: 0,356)
[38]  S. Melissis, 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(1-2):63-75. (Impact Factor: 4.101)
[39]  D. Platis and N.E. Labrou (2006) Development of an Aqueous Two-Phase Partitioning System for Fractionating Therapeutic Proteins from Tobacco Extract. J. Chromatogr. A 1128(1-2):114-24. (Impact Factor: 4.101)
[40]  D. Platis, 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(1-2):138-51. (Impact Factor: 4.101)
[41]  B.J. Smith, T. Huyton, R.P. Joosten, J.L. McKimm-Breschkin, J-G. Zhang, C.S. Luo, M-Z. Lou, N. E. Labrou, and T.P.J. Garrett (2006). X-ray crystal structure of a calcium deficient form of influenza virus neuraminidase: implications for substrate binding. Acta Crystal D: Biological Crystallography 62(Pt 9):947-52. (Impact Factor: 2,62)
[42]  D. Platis, 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(2):215-23. (Impact Factor: 5,2)
[43]  T. Dalakouras, 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(1):48-56. (Impact Factor: 4.101)
[44]  G. A. Kotzia, and N.E. Labrou (2007). L-Asparaginase from Erwinia chrysanthemi 3937: Cloning, Expression and Characterization. J. Biotechnol. 127(4):657-69. (Impact Factor: 2,600)
[45]  S. Melissis, N.E. Labrou, Y.D. Clonis (2007). One-step purification of Taq DNA polymerase using nucleotide-mimetic affinity chromatography. Biotechnol J. 2(1):121-32.
[46]  G.A. Kotzia, K. Lappa, and N.E. Labrou (2007). Tailoring structure-function properties of L-asparaginase: engineering resistance to trypsin cleavage. Biochem J. 404(2):337-343. (Impact Factor: 5,2)
[47]  G. Moschopoulou, I. Papanastasiou, O. Makri, N. Labrou, G. Economou, K. Soukouli, S.E. Kintzios (2007) Cellular redox-status is associated with regulation of frond division in Spirodela polyrrhiza. Plant Cell Rep. 26(12):2063-9. (Impact Factor: 1,974)
[48]  K. Ramessar, T. Rademacher, M. Sack M, Stadlmann J, Platis D, Stiegler G, Labrou N, Altmann F, Ma J, Stöger E, Capell T, Christou P. (2008) Cost-effective production of a vaginal protein microbicide to prevent HIV transmission. Proc Natl Acad Sci USA. 105(10):3727-32. (Impact Factor: 9,598)
[49]  Platis D, Labrou NE.(2008) Affinity chromatography for the purification of therapeutic proteins from transgenic maize using immobilized histamine. J. Sep. Sci. 31(4):636-45. (Impact Factor: 2.632)
[50]  E. Morou, H.M. Ismail, A.J. Dowd, J. Hemingway, N.E. Labrou, M. Paine, J. Vontas (2008) A dehydrochlorinase-based pH change assay for determination of DDT in sprayed surfaces. Analytical Biochemistry, 378(1):60-4. (Impact Factor: 3,002)
[51]  D. Platis and N.E. Labrou (2008) Chemical and Genetic Engineering Strategies to Improve the Potency of Pharmaceutical Proteins and Enzymes. Current Medicinal Chemistry, 19, 1940-1955. (Impact Factor: 4,944)
[52]  Kapoli P, Axarli IA, Platis D, Fragoulaki M, Paine M, Hemingway J, Vontas J, Labrou NE (2008) Engineering sensitive glutathione transferase for the detection of xenobiotics, Biosensors Bioelectronics, 24(3):498-503. (Impact Factor: 5,061)
[53]  Andreadeli, A. Platis, D. Tishkov, V. Popov, V., Labrou, N.E. (2008) Structure-guided alteration of coenzyme specificity of formate dehydrogenase by saturation mutagenesis to enable efficient utilization of NADP+. FEBS J, 275(15):3859-69. (Impact Factor: 3,396)
[54]  D. Platis, 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(1-2):80-9. (Impact Factor: 4.101)
[55]  D. Platis and N. E. Labrou (2008) Evaluation of a Synthetic Biomimetic Ligand for the Purification of Therapeutic Proteins, 1, (2), Proteomics Research Journal, 1-14
[56]  I. Axarli, P. Dhavala, A.C. Papageorgiou, N.E. Labrou. (2009) Crystallographic and functional characterization of the fluorodifen-inducible glutathione transferase from Glycine max reveals an active site topography suited for diphenylether herbicides and a novel L-site. J. Mol. Biol. 385(3):984-1002. (Impact Factor: 4,472)
[57]  I. Axarli, 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(5):2009-16. (Impact Factor: 2,301)
[58]  G.A. Kotzia, N.E. Labrou (2009) Engineering thermal stability of L-asparaginase by in vitro directed evolution. FEBS J, 276(6):1750-61. (Impact Factor: 3,396)
[59]  Andreadeli A, Flemetakis E, Axarli I, Dimou M, Udvardi MK, Katinakis P, Labrou NE (2009) Cloning and characterization of Lotus japonicus formate dehydrogenase: A possible correlation with hypoxia. Biochim Biophys Acta (Proteins and Proteomics), 1794(6):976-84. (Impact Factor: 3,078)
[60]  D. Platis, 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. Recognition, 22(6):415-24. (Impact Factor: 3,767)
[61]  D. Platis and N.E. Labrou (2009). Evaluation of a synthetic biomimetic ligand for the purification of therapeutic proteins. Int. J. Med. Biol. Front. Volume 15 Issue 11/12.
[62]  D. Platis 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(9):1320-7.
[63]  Kouri ED, Labrou NE, Garbis SD, Kalliampakou KI, Stedel C, Dimou M, Udvardi MK, Katinakis P, Flemetakis E. (2009) Molecular and Biochemical characterization of the Parvulin-type PPIases in Lotus japonicus. Plant Physiol., 150(3):1160-73. (Impact Factor: 6.367)
[64]  C.C. Sfetsas, K. Skopelitou, L. Milios, A. Venieraki, R. Todou, E. Flemetakis, P. Katinakis, N. E. Labrou. (2009) Characterization of 1,2-dibromoethane-degrading haloalkane dehalogenase from Bradyrhizobium japonicum USDA110. Enzyme and Microbial Technology, 45, 397–404. (Impact Factor: 2.4)
[65]  Axarli, I. Dhavala, P., Papageorgiou, A.C., & Labrou, N. (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(2):247-56. (Impact Factor: 5,2)
[66]  E. Chronopoulou and N.E. Labrou (2009). Glutathione Transferases: Emerging Multidisciplinary Tools in Red and Green Biotechnology. Recent Patents in Biotechnology 3(3):211-23.
[67]  Axarli, I., Georgiadou, C., Dhavala, P., Papageorgiou, A.C. & Labrou, N. (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. Biochim Biophys Acta (Proteins and Proteomics). 1804, 662-667. (Impact Factor: 3,078)
[68]  Dowd A.J., Morou E., Steven A., Ismael H., Labrou, N.E, Paine M. Vontas J. (2010) Development of a colorimetric pH assay for the quantification of pyrethroids based on glutathione transferase. Int. J. Environm. Anal. Chem. 90 (12), 1-10. (Impact Factor: 1.703)
[69]  S.C. Melissis, A.C. Papageorgiou, N.E. Labrou, Y.D. Clonis. (2010) Purification 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, 6, 496-502
[70]  N.E. Labrou (2010). Random mutagenesis methods for in vitro directed enzyme evolution. Current Protein Peptide Science, 11, 91-100. (Impact Factor: 3,011)
[71]  I. Axarli, N.E. Labrou (2010). Directed Evolution of Cytochrome P450 CYP102A2 from Bacillus subtilis. Dynamic Biochemistry, Process Biotechnology and Molecular Biology, 4, (1), 19-24.
[72]  N.E. Labrou, A.C. Papageorgiou, V.I. Avramis (2010). Structure-function and clinical applications of L-asparaginases. Current Medicinal Chemistry, 17(20):2183-95.
[73]  I. Axarli, A. Prigipaki and N.E. Labrou (2010). Cytochrome P450 CYP102A2 catalyzes efficient oxidation of sodium dodecyl sulphate: a molecular tool for remediation. Enzyme Research, Volume 2010, Article ID 125429, 7 pages.
[74]  Skopelitou, K and N.E. Labrou (2010). A new colorimetric assay for glutathione transferase-catalyzed halogen ion release for high-throughput screening, Analytical Biochemistry, 405(2):201-6.
[75]  K. Benekos, C. Kissoudis, I. Nianiou-Obeidat, N.E. Labrou, P. Madesis, M. Kalamaki, A. Makris, A. Tsaftaris (2010). Over-expression of a specific soybean GmGSTU4 isoenzyme improves diphenyl ether and chloroacetanilide herbicide tolerance of transgenic tobacco plants, J. Biotechnol. 150(1):195-201.
[76]  E. Chronopoulou, I. Axarli, I. Nianiou-Obeidat, P. Madesis, A. Tsaftaris, and N. Labrou (2011). Structure and antioxidant catalytic function of plant glutathione transferases. Current Chemical Biology, 5, 64-74.
[77]  D. Tsikou, C. Stedel, E. D. Kouri; M.K. Udvardi, T.L. Wang, P. Katinakis, N.E. Labrou, E. Flemetakis (2011). Characterization of two novel nodule-enhanced α-type carbonic anhydrases from Lotus japonicus. Biochim Biophys Acta (Proteins and Proteomics), 1814(4):496-504.
[78]  G.A. Kotzia, N.E. Labrou (2011). Engineering substrate specificity of E. carotovora L-asparaginase for the development of biosensor. J. Mol. Cat. B: Enzymatic (in press).
[79]  K. Skopelitou, A.W. Muleta, O. Pavli, G.N. Skaracis, E. Flemetakis, A.C. Papageorgiou and N.E. Labrou. Overlapping protective roles for glutathione transferase gene family members in chemical and oxidative stress response in Agrobacterium tumefaciens. Functional & Integrative Genomics (in press).

Publications: Books/Book Chapters

[1]  N.E. Labrou & Y.D. Clonis (1999). The tachykinin family of peptides and their receptors. In Matsoukas J. & Mavromoustakos (Eds), 'Bioctive Peptides in Drug Discovery and Design: Medical Aspects'. IOS Press, Amsterdam, The Netherlands. 225-233.
[2]  N.E. Labrou (2000). Dye-ligand affinity chromatography for protein separation and purification. In: Bailon, P., Ehrlich, G., Fung, W.-J., Berthold, W., (Eds), Methods in Molecular Biology: 'Affinity Chromatography: Methods and Protocols'. Humana Press, Inc., Totowa, NJ, USA, vol. 147, 129-139.
[3]  N.E. Labrou & Y.D. Clonis (2002). Immobilised synthetic dyes in affinity chromatography. Biochromatography-Theory and Practice (M.A. Vijayalakshmi, ed.), Taylor and Francis Publishers, London, Chap. 8, 235-251.
[4]  N.E. Labrou (2002). Affinity Chromatography. In Gupta, M. N. (Ed.), Methods for Affinity-Based Separations Of Enzymes and Proteins. Birkhϊuser Verlag AG, Switzerland, 16-28.
[5]  N.E. Labrou (2004). Dye-ligand Affinity Chromatography in Proteomic Research. Proteins and Proteomics: A Laboratory Manual, Cold Spring Harbour Laboratory Press, 275-299.
[6]  N.E. Labrou, K. Mazitsos & Y. Clonis (2005). Dye-ligand and Biomimetic Affinity Chromatography. In D.S. Hage (Ed.), Handbook of Affinity Chromatography. Marcel Dekker, Inc, New York, pp231-255.
[7]  G.A. Kotzia, I.A. Axarli, and N.E. Labrou (2005). Evolutionary Methods in Enzyme Technology: High-Throughput Screening and Selection of New Enzyme Variants, In Pandalai, S.G. (Ed): Resent Research Developments in Biotechnology & Bioengineering Vol 7, Research Signpost, pp. 85-104.
[8]  Platis, D., Kotzia, G. A., Axarli, I. Α. & Labrou, N.E (2006). Enzyme Engineering and Technology, In Hui Y.H. et al., (Ed) Food Biochemistry and Food Processing, (1st Edition) Blackwell Publishing Company USA, pp. 175-223.
[9]  K. Skopelitou, 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 ", Bentham Science Publishers, Vol 4, pp. 23-42.
[10]  D. Platis 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, Eds: Kristian Bundgaard and Luke Isaksen. Nova Publishers, USA, 397-416.
[11]  G. Mavridis and N.E. Labrou (2010) The interaction of the prion protein with triazine-based biomimetic affinity ligands, In: Biopharmaceutics and Drug Hypersensitivity, Eds: Paul Mossillo and John Pinzini. Nova Publishers, USA, 177-190.
[12]  K. Lappa, 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, Eds: Stefan Fuchs and Max Auer, Nova Publishers, USA, Chapter 13, 323-334.
[13]  Chronopoulou, E., N.E. Labrou (2011). Site-saturation Mutagenesis: a powerful tool for structure-based design of combinatorial mutation libraries. In: Current Protocols in Protein Science, Ed: Ben Dunn, John Wiley & Sons, Chapter 26:Unit26.6:26.6.1-26.6.10.
[14]  Platis, D., Kotzia, G. A., Axarli, I. Α., Chronopoulou, E., Karamitros, C., Labrou, N.E. (2011). Biocatalysis, Enzyme Engineering and Enzyme Biotechnology, In B. Simpson, et al., (Ed) Food Biochemistry and Food Processing (2nd Edition), Blackwell Publishing Company USA, (in press).
[15]  N.E. Labrou. Clostripain. In: Handbook of Proteolytic Enzymes, Neil Rawlings and Guy Salvesen (Editors), Elsevier, UK, (in press).