Parcourir par auteur "Kalpaxis, D. L."
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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 ... -
Clindamycin binding to ribosomes revisited: foot printing and computational detection of two binding sites within the peptidyl transferase center
Kostopoulou, O. N.; Papadopoulos, G.; Kouvela, E. C.; Kalpaxis, D. L. (2013)Clindamycin is a semi-synthetic lincosamide, active against most Gram-positive bacteria and some protozoa. It binds to the 50S ribosomal subunit and inhibits early peptide chain elongation. By kinetic analysis it has been ... -
Conjugation with polyamines enhances the antibacterial and anticancer activity of chloramphenicol
Kostopoulou, O. N.; Kouvela, E. C.; Magoulas, G. E.; Garnelis, T.; Panagoulias, I.; Rodi, M.; Papadopoulos, G.; Mouzaki, A.; Dinos, G. P.; Papaioannou, D.; Kalpaxis, D. L. (2014)Chloramphenicol (CAM) is a broad-spectrum antibiotic, limited to occasional only use in developed countries because of its potential toxicity. To explore the influence of polyamines on the uptake and activity of CAM into ... -
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 ... -
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 ... -
On the structural and functional importance of the highly conserved Glu56 of Thermus thermophilus L4 ribosomal protein (vol 332, pg 73, 2003)
Leontiadou, F.; Xaplanteri, M. A.; Papadopoulos, G.; Gerassimou, C.; Kalpaxis, D. L.; Choli-Papadopou, T. (2004) -
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 ... -
Synthesis and Evaluation of Chloramphenicol Homodimers: Molecular Target, Antimicrobial Activity, and Toxicity against Human Cells
Kostopoulou, O. N.; Magoulas, G. E.; Papadopoulos, G. E.; Mouzaki, A.; Dinos, G. P.; Papaioannou, D.; Kalpaxis, D. L. (2015)As fight against antibiotic resistance must be strengthened, improving old drugs that have fallen in reduced clinical use because of toxic side effects and/or frequently reported resistance, like chloramphenicol (CAM), is ...