Biomaterial Database

[Ribosomes and antibiotics. II. Mechanism of action of therapeutically used antibiotics on ribosomes]. 1974

J Delaunay, and G Schapira

UI	MeSH Term	Description	Entries
D008034	Lincomycin	An antibiotic produced by Streptomyces lincolnensis var. lincolnensis. It has been used in the treatment of staphylococcal, streptococcal, and Bacteroides fragilis infections.	Lincolnensin,Lincomycin, (2S-cis)-Isomer,Epilincomycin,Lincocin,Lincomycin A,Lincomycin Hydrochloride,Lincomycin Monohydrochloride,Lincomycin Monohydrochloride, (2S-cis)-Isomer,Lincomycin Monohydrochloride, (L-threo)-Isomer,Lincomycin Monohydrochloride, Hemihydrate,Lincomycin, (L-threo)-Isomer,Hemihydrate Lincomycin Monohydrochloride
D008938	Mitosis	A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.	M Phase, Mitotic,Mitotic M Phase,M Phases, Mitotic,Mitoses,Mitotic M Phases,Phase, Mitotic M,Phases, Mitotic M
D009827	Oleandomycin	Antibiotic macrolide produced by Streptomyces antibioticus.	Oleandomycin Phosphate,Phosphate, Oleandomycin
D010441	Peptide Chain Elongation, Translational	A process of GENETIC TRANSLATION, when an amino acid is transferred from its cognate TRANSFER RNA to the lengthening chain of PEPTIDES.	Chain Elongation, Peptide, Translational,Protein Biosynthesis Elongation,Protein Chain Elongation, Translational,Protein Translation Elongation,Translation Elongation, Genetic,Translation Elongation, Protein,Translational Elongation, Protein,Translational Peptide Chain Elongation,Biosynthesis Elongation, Protein,Elongation, Genetic Translation,Elongation, Protein Biosynthesis,Elongation, Protein Translation,Elongation, Protein Translational,Genetic Translation Elongation,Protein Translational Elongation
D010442	Peptide Chain Initiation, Translational	A process of GENETIC TRANSLATION whereby the formation of a peptide chain is started. It includes assembly of the RIBOSOME components, the MESSENGER RNA coding for the polypeptide to be made, INITIATOR TRNA, and PEPTIDE INITIATION FACTORS; and placement of the first amino acid in the peptide chain. The details and components of this process are unique for prokaryotic protein biosynthesis and eukaryotic protein biosynthesis.	Chain Initiation, Peptide, Translational,Protein Biosynthesis Initiation,Protein Chain Initiation, Translational,Protein Translation Initiation,Translation Initiation, Genetic,Translation Initiation, Protein,Translational Initiation, Protein,Translational Peptide Chain Initiation,Biosynthesis Initiation, Protein,Genetic Translation Initiation,Initiation, Genetic Translation,Initiation, Protein Biosynthesis,Initiation, Protein Translation,Initiation, Protein Translational,Protein Translational Initiation
D010443	Peptide Chain Termination, Translational	A process of GENETIC TRANSLATION whereby the terminal amino acid is added to a lengthening polypeptide. This termination process is signaled from the MESSENGER RNA, by one of three termination codons (CODON, TERMINATOR) that immediately follows the last amino acid-specifying CODON.	Chain Termination, Peptide, Translational,Protein Biosynthesis Termination,Protein Chain Termination, Translational,Protein Translation Termination,Translation Termination, Genetic,Translation Termination, Protein,Translational Peptide Chain Termination,Translational Termination, Protein,Biosynthesis Termination, Protein,Genetic Translation Termination,Protein Translational Termination,Termination, Genetic Translation,Termination, Protein Biosynthesis,Termination, Protein Translation,Termination, Protein Translational
D002701	Chloramphenicol	An antibiotic first isolated from cultures of Streptomyces venequelae in 1947 but now produced synthetically. It has a relatively simple structure and was the first broad-spectrum antibiotic to be discovered. It acts by interfering with bacterial protein synthesis and is mainly bacteriostatic. (From Martindale, The Extra Pharmacopoeia, 29th ed, p106)	Cloranfenicol,Kloramfenikol,Levomycetin,Amphenicol,Amphenicols,Chlornitromycin,Chlorocid,Chloromycetin,Detreomycin,Ophthochlor,Syntomycin
D003609	Dactinomycin	A compound composed of a two CYCLIC PEPTIDES attached to a phenoxazine that is derived from STREPTOMYCES parvullus. It binds to DNA and inhibits RNA synthesis (transcription), with chain elongation more sensitive than initiation, termination, or release. As a result of impaired mRNA production, protein synthesis also declines after dactinomycin therapy. (From AMA Drug Evaluations Annual, 1993, p2015)	Actinomycin,Actinomycin D,Meractinomycin,Cosmegen,Cosmegen Lyovac,Lyovac-Cosmegen,Lyovac Cosmegen,Lyovac, Cosmegen,LyovacCosmegen
D004352	Drug Resistance, Microbial	The ability of microorganisms, especially bacteria, to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS).	Antibiotic Resistance,Antibiotic Resistance, Microbial,Antimicrobial Resistance, Drug,Antimicrobial Drug Resistance,Antimicrobial Drug Resistances,Antimicrobial Resistances, Drug,Drug Antimicrobial Resistance,Drug Antimicrobial Resistances,Drug Resistances, Microbial,Resistance, Antibiotic,Resistance, Drug Antimicrobial,Resistances, Drug Antimicrobial
D004917	Erythromycin	A bacteriostatic antibiotic macrolide produced by Streptomyces erythreus. Erythromycin A is considered its major active component. In sensitive organisms, it inhibits protein synthesis by binding to 50S ribosomal subunits. This binding process inhibits peptidyl transferase activity and interferes with translocation of amino acids during translation and assembly of proteins.	Erycette,Erymax,Erythromycin A,Erythromycin C,Erythromycin Lactate,Erythromycin Phosphate,Ilotycin,T-Stat,Lactate, Erythromycin,Phosphate, Erythromycin,T Stat,TStat