UD-GENOMED Medical Genomic Technologies Ltd.


Center for Clinical Genomics and Personalised Medicine


Richter Gedeon Pharmaceuticals, PLC

Roche Magyarország Kft


University of Debrecen, Medical and Health Sciences Center




Jana Krenkova, Ákos Szekrényes, Zsolt Keresztessy, Frantisek Foret and  András Guttman (2013) Oriented Immobilization of Peptide-N-glycosidase F on a Monolithic Support for Glycosylation Analysis. Journal of Chromatography A, in press.  (IF  4.6/2012) LINK

Király, R., Csősz, E., Kurtán, T., Antus, S., Szigeti, K., Vecsei, Z., Korponay-Szabó, I. R., Keresztessy, Z., and Fésüs, L. (2009) Functional significance of five non-canonical Ca2+-binding sites of transglutaminase 2 characterized by site directed mutagenesis. FEBS Journal, 276, 7083-7096. (IF 3.396 /2008) LINK

Keresztessy, Z., Bodnár, M., Ber, E., Hajdú, I., Zhang, M., Hartmann, J. F., Minko, T. and Borbély, J. (2009) Self-assembling chitosan/poly g-glutamic acid nanoparticles for targeted drug delivery. Colloid and Polymer Science 287, 759-765. (IF 1.736 / 2008) LINK

Keresztessy, Z., Csosz, E., Harsfalvi, J., Csomos, K., Gray, J., Lightowlers, R.N., Lakey, J.H., Balajthy, Z., and Fesus, L. (2006) Phage-Display Selection of Efficient Glutamine-Donor Substrate Sequences for Transglutaminase 2. Protein Science 15, 2466-2480. (IF 3.618 / 2005) LINK

Csosz, E., Keresztessy, Z., and Fesus, L. (2002) Transglutaminase substrates: from test tube experiments to living cells and tissues. Minerva Biotechnologica 14, 149-153. (IF 0.167 /2005)

Keresztessy, Z., Brown, K., Dunn, M.A., and Hughes, M.A. (2001) Identification of essential active-site residues in the cyanogenic b-glucosidase (linamarase) from cassava (Manihot esculenta Crantz) by site-directed mutagenesis. Biochemical Journal 353, 199-205. (IF 4.224 /2005) LINK

Ambrus, A., Bányai, I., Weiss, M.S., Hilgenfeld, R., Keresztessy, Z., Muszbek, L., and Fésüs, L. (2001) Calcium binding of transglutaminases: A 43Ca-NMR study combined with surface polarity analysis. J. Biomolecular Structure and Dynamics, 19, 59-74. (IF 1.430/2005) LINK

Nagy, Z., Keresztessy, Z., Szentirmai, A., Biró, S.(2001) Carbon source regulation of ß-galactosidase biosynthesis in Penicillium chrysogenum. Journal of Basic Microbiology 41, 351-362. (IF 1.000 /2005) LINK

Keresztessy, Z., and Hughes, M.A. (1998) Homology modelling of lipid-transfer proteins encoded by the barley low-temperature-inducible gene family blt4 and molecular dynamics aided analysis of fatty acid and lipid complexes. Plant Journal 14, 523-533. (IF 6.969 /2005) LINK

Hughes, J. Keresztessy, Z., Brown, K., Suhandono, S., and Hughes, M.A. (1998) Genomic organisation and srtucture of a-hydroxynitrile lyase in cassava (Manihot esculenta Crants). Archives of Biochemistry and Biophysics 356, 107-116. (IF 3.152/2005) LINK

Keresztessy, Z., Hughes, J., Kiss, L., and Hughes, M.A. (1996) Co-purification from E.coli of a plant b-glucosidase-GST fusion protein with the bacterial chaperonin GroEL. Biochemical Journal 314, 41-47. (IF 4.224 /2005) LINK

Keresztessy, Z., Kiss, L., and Hughes, M.A. (1994) Investigation of the active site of the cyanogenic b-glucosidase (linamarase) from Manihot esculenta Crantz (cassava). II. Identification of Glu-198 as an active site carboxylate with acid catalytic function. Archives of Biochemistry and Biophysics 315, 323-330. (IF 3.152/2005) LINK

Hughes, M.A., and Hughes, J., Liddle, S., and Keresztessy, Z.: Biochemistry and molecular biology of cyanogenesis. Proc. Second Int. Meeting of the Cassava Biotechnology Network, August 20-27, 1994, Jakarta, Indonesia; CIAT Working Doc. No. 150, 385-395.

Keresztessy, Z., Kiss, L., and Hughes, M.A. (1994) Investigation of the active site of the cyanogenic b-glucosidase (linamarase) from Manihot esculenta Crantz (cassava). I. Evidence for an essential carboxylate and a reactive histidine group in a single catalytic center. Archives of Biochemistry and Biophysics 314, 142-152. (IF 3.152/2005) LINK


Borbély, J., Bodnár, M., Hajdu, I., Hartmann, J.F., Keresztessy, Z., Nagy, L., Vamosi, G. Polymeric Nanoparticles by Ion-Ion Interactions. US Utility Patent Application No. US 60/833,672. PCT Patent Application No. WO/2009/035438. LINK