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D L Kalpaxis

Showing results (1-10 of 32) with videos related to

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Molecular Pharmacology|October 1, 1989
Type of inhibition of peptide bond formation by chloramphenicol depends on the temperature and the concentration of ammonium ionsD L Kalpaxis, C Coutsogeorgopoulos
Nucleic Acids Research|September 23, 2000
Photoaffinity polyamines: interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomesI Amarantos, D L Kalpaxis
Biochimica Et Biophysica Acta|September 21, 1994
Bimodal action of spermine on ribosomal peptidyltransferase at low concentration of magnesium ionsD Drainas, D L Kalpaxis
Molecular and Cellular Biochemistry|September 22, 1992
Effect of spermine on peptide-bond formation, catalyzed by ribosomal peptidyltransferaseD L Kalpaxis, D Drainas
Archives of Biochemistry and Biophysics|February 1, 1993
Inhibitory effect of spermine on ribosomal peptidyltransferaseD L Kalpaxis, D Drainas
Molecular Pharmacology|October 26, 1999
Slow sequential conformational changes in Escherichia coli ribosomes induced by lincomycin: kinetic evidenceS Kallia-Raftopoulos, D L Kalpaxis
Die Pharmazie|December 17, 1997
Heat and ionic limitations do not change the inhibition pattern of ribosomal peptidyltransferase by aminohexosyl-cytosine nucleoside antibioticsG P Dinos, D L Kalpaxis
Clinical Chemistry|May 1, 1989
Partial characterization of an abnormal lactate dehydrogenase isoenzyme, LDH-1ex, in serum from a patient with hepatocellular carcinomaD L Kalpaxis, E E Giannoulaki
Biochemistry|September 20, 2000
Kinetic studies on the interaction between a ribosomal complex active in peptide bond formation and the macrolide antibiotics tylosin and erythromycinG P Dinos, D L Kalpaxis
European Journal of Biochemistry|April 1, 1987
Inhibition of ribosomal peptidyltransferase by chloramphenicol. Kinetic studiesD Drainas, D L Kalpaxis, C Coutsogeorgopoulos
Pageof 4

Showing results (1-10 of 32) with videos related to

Sort By:
Pageof 4
Molecular Pharmacology|October 1, 1989
Type of inhibition of peptide bond formation by chloramphenicol depends on the temperature and the concentration of ammonium ionsD L Kalpaxis, C Coutsogeorgopoulos
Nucleic Acids Research|September 23, 2000
Photoaffinity polyamines: interactions with AcPhe-tRNA free in solution or bound at the P-site of Escherichia coli ribosomesI Amarantos, D L Kalpaxis
Biochimica Et Biophysica Acta|September 21, 1994
Bimodal action of spermine on ribosomal peptidyltransferase at low concentration of magnesium ionsD Drainas, D L Kalpaxis
Molecular and Cellular Biochemistry|September 22, 1992
Effect of spermine on peptide-bond formation, catalyzed by ribosomal peptidyltransferaseD L Kalpaxis, D Drainas
Archives of Biochemistry and Biophysics|February 1, 1993
Inhibitory effect of spermine on ribosomal peptidyltransferaseD L Kalpaxis, D Drainas
Molecular Pharmacology|October 26, 1999
Slow sequential conformational changes in Escherichia coli ribosomes induced by lincomycin: kinetic evidenceS Kallia-Raftopoulos, D L Kalpaxis
Die Pharmazie|December 17, 1997
Heat and ionic limitations do not change the inhibition pattern of ribosomal peptidyltransferase by aminohexosyl-cytosine nucleoside antibioticsG P Dinos, D L Kalpaxis
Clinical Chemistry|May 1, 1989
Partial characterization of an abnormal lactate dehydrogenase isoenzyme, LDH-1ex, in serum from a patient with hepatocellular carcinomaD L Kalpaxis, E E Giannoulaki
Biochemistry|September 20, 2000
Kinetic studies on the interaction between a ribosomal complex active in peptide bond formation and the macrolide antibiotics tylosin and erythromycinG P Dinos, D L Kalpaxis
European Journal of Biochemistry|April 1, 1987
Inhibition of ribosomal peptidyltransferase by chloramphenicol. Kinetic studiesD Drainas, D L Kalpaxis, C Coutsogeorgopoulos
Pageof 4