Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Maria A. Xaplanteri"'
Autor:
Dimitrios L. Kalpaxis, Georgios Papadopoulos, Fotini Leontiadou, Maria A. Xaplanteri, Theodora Choli-Papadopoulou
Publikováno v:
Journal of Molecular Biology. 369:489-497
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 and functional importance
Publikováno v:
Nucleic Acids Research
Polyamine binding to 23S rRNA was investigated, using a photoaffinity labeling approach. This was based on the covalent binding of a photoreactive analog of spermine, N1-azidobenzamidino (ABA)-spermine, to Escherichia coli ribosomes or naked 23S rRNA
Autor:
Daniel N. Wilson, Alexandros D. Petropoulos, Maria A. Xaplanteri, Dimitrios L. Kalpaxis, George P. Dinos
Publikováno v:
Journal of Biological Chemistry. 279:26518-26525
The effects of spermine on peptidyltransferase inhibition by an aminohexosylcytosine nucleoside, blasticidin S, and by a macrolide, spiramycin, were investigated in a model system derived from Escherichia coli, in which a peptide bond is formed betwe
Autor:
Dimitrios L. Kalpaxis, George P. Dinos, Maria A. Xaplanteri, Michel Leotsinidis, Angella V Catsiki, Christos Theos
Publikováno v:
Environmental Research. 94:211-220
Specimens of Mytilus galloprovincialis were placed in bow nets and immersed at 3-10 m depth in a clean coastal region (reference area), Itea, and two marine stations along Gulf of Patras, N. Peloponnesus, Greece. One site is near the estuaries of the
Publikováno v:
Nucleic Acids Research. 31:5074-5083
Chloramphenicol is thought to interfere competitively with the binding of the aminoacyl-tRNA 3'-terminus to ribosomal A-site. However, noncompetitive or mixed-noncompetitive inhibition, often observed to be dependent on chloramphenicol concentration
Autor:
Ekaterini C. Kouvela, George V. Gerbanas, George P. Dinos, Maria A. Xaplanteri, Dimitrios L. Kalpaxis, Alexandros D. Petropoulos
Publikováno v:
Nucleic Acids Research
S rRNA is an integral component of the large ribosomal subunit in virtually all living organisms. Polyamine binding to 5S rRNA was investigated by cross-linking of N 1 -azidobenzamidino (ABA)- spermine to naked 5S rRNA or 50S ribosomal subunits and w
Autor:
Dimitrios L. Kalpaxis, Aikaterini Tsagkalia, Maria A. Xaplanteri, Georgios Papadopoulos, Fotini Leontiadou, Theodora Choli-Papadopoulou
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 peptidyltransferase functions, the highly conserved E56 was replaced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::437d901a2d2eb38edfcd9cd13c7250bc
https://europepmc.org/articles/PMC1370849/
https://europepmc.org/articles/PMC1370849/
Autor:
Alexandros D, Petropoulos, Maria A, Xaplanteri, George P, Dinos, Daniel N, Wilson, Dimitrios L, Kalpaxis
Publikováno v:
The Journal of biological chemistry. 279(25)
The effects of spermine on peptidyltransferase inhibition by an aminohexosylcytosine nucleoside, blasticidin S, and by a macrolide, spiramycin, were investigated in a model system derived from Escherichia coli, in which a peptide bond is formed betwe
Autor:
Fotini Leontiadou, Maria A. Xaplanteri, Theodora Choli-Papadopoulou, Georgios Papadopoulos, Dimitrios L. Kalpaxis, Christina Gerassimou
Publikováno v:
Journal of molecular biology. 332(1)
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 alanine or glutamine, and by
Publikováno v:
Biochemistry. 40(25)
The effect of two photoreactive analogues of spermine, N(1)-azidobenzamidino- (ABA-) spermine and N(1)-azidonitrobenzoyl- (ANB-) spermine, on ribosomal functions was studied in a cell-free system derived from Escherichia coli. In the dark, both analo