Πλοήγηση ανά Συγγραφέα "Choli-Papadopoulou, T."
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BIOFUNCTIONALIZATION OF PET/SiO2 SURFACES FOR SINGLE MOLECULE EXPERIMENTS AND MEDICAL APPLICATIONS
Katranidis, A.; Melachroinos, A.; Karagiannidis, P. G.; Lousinian, S.; Papadopoulos, G.; Logothetidis, S.; Choli-Papadopoulou, T. (2011)PET/SiO2 layers were chemically modified to maintain immobilization of functional single molecules. GFP molecules provide an ideal system due to their stability and intrinsic fluorescence. GFP in vivo biotinylated within ... -
The C-terminal Region of HPNAP Activates Neutrophils and Promotes Their Adhesion to Endothelial Cells
Kottakis, F.; Befani, C.; Asiminas, A.; Kontou, M.; Koliakos, G.; Choli-Papadopoulou, T. (2009)Entire Helicobacter Pylori Neutrophil Activated Protein (HPNAP) and its truncated forms NH(2)-terminal region HPNAP(1-57) and C-terminal region HPNAP(58-144) after cloning into pET29c vector, purification and removal of ... -
Changes in the level of poly(Phe) synthesis in Escherichia coli ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus can be explained by structural changes in the peptidyltransferase center: a molecular dynamics simulation analysis
Papadopoulos, G.; Grudinin, S.; Kalpaxis, D. L.; Choli-Papadopoulou, T. (2006)Data from polyphenylalanine [poly(Phe)] synthesis determination in the presence and in the absence of erythromycin have been used in conjunction with Molecular Dynamics Simulation analysis, in order to localize the functional ... -
The contribution of the zinc-finger motif to the function of Thermus thermophilus ribosomal protein S14
Xaplanteri, M. A.; Papadopoulos, G.; Leontiadou, F.; Choli-Papadopoulou, T.; Kalpaxis, D. L. (2007)In the crystal structure of the 30S ribosomal subunit from Thermus thermophilus, cysteine 24 of ribosomal protein S14 (TthS14) occupies the first position in a CXXC-X12-CXXC motif that coordinates a zinc ion. The structural ... -
Helicobacter pylori neutrophil activating protein as target for new drugs against H. pylori inflammation
Choli-Papadopoulou, T.; Kottakis, F.; Papadopoulos, G.; Pendas, S. (2011)Helicobacter pylori (H. pylon) infection is among the most common human infections and the major risk factor for peptic ulcer disease and gastric cancer. Within this work we present the implication of C-terminal region of ... -
Helicobacter pylori neutrophil-activating protein activates neutrophils by its C-terminal region even without dodecamer formation, which is a prerequisite for DNA protection - novel approaches against Helicobacter pylori inflammation
Kottakis, F.; Papadopoulos, G.; Pappa, E. V.; Cordopatis, P.; Pentas, S.; Choli-Papadopoulou, T. (2008)Helicobacter pylori neutrophil-activating protein (HP-NAP) protects DNA from free radicals as a dodecamer through its ferroxidase activity without, however, directly binding to it. The retardation that was observed at pH ... -
HP-NAP protein activates neutrophils by its C-terminal region even without dodecamer formation which is prerequisite for DNA protection: novel approaches against H-pylori inflammation
Kottakis, F.; Papadopoulos, G.; Pappa, E. V.; Cordopatis, P.; Pentas, S.; Choli-Papadopoulou, T. (2007) -
Natural agents against neutrophil involvement in H.Pylori induced chronic gastritis
Pendas, S.; Kottakis, F.; Asiminas, A.; Kontou, M.; Befani, C.; Koliakos, G.; Choli-Papadopoulou, T. (2010)Helicobacter pylori infection is one of the widely spread human infections and the major risk for peptic ulcer disease, and gastric cancer and cause for chronic gastric inflammation. The major virulence factors in the ... -
On the Intracellular Trafficking of Mouse S5 Ribosomal Protein from Cytoplasm to Nucleoli
Matragkou, C.; Papachristou, H.; Karetsou, Z.; Papadopoulos, G.; Papamarcaki, T.; Vizirianakis, I. S.; Tsiftsoglou, A. S.; Choli-Papadopoulou, T. (2009)The non-ribosomal functions of mammalian ribosomal proteins have recently attracted worldwide attention. The mouse ribosomal protein S5 (rpS5) derived from ribosomal material is an assembled non-phosphorylated protein. The ... -
On the structural and functional importance of the highly conserved Glu56 of Thermus thermophilus L4 ribosomal protein
Leontiadou, F.; Xaplanteri, M. A.; Papadopoulos, G.; Gerassimou, C.; Kalpaxis, D. L.; Choli-Papadopoulou, T. (2003)The structural and functional importance of the highly conserved amino acid residue glutamic acid 56 (Glu56) of the ribosomal protein L4 from Thermus thermophilus (TthL4) has been investigated by replacing this residue by ... -
Ribosomes containing mutants of L4 ribosomal protein from Thermus thermophilus display multiple defects in ribosomal functions and sensitivity against erythromycin
Tsagkalia, A.; Leontiadou, F.; Xaplanteri, M. A.; Papadopoulos, G.; Kalpaxis, D. L.; Choli-Papadopoulou, T. (2005)Protein L4 from Thermus thermophilus (TthL4) was heterologously overproduced in Escherichia coli cells. To study the implication of the extended loop of TthL4 in the exit-tunnel and peptidlyltransferase functions, the ...