Biomedical subjects

R E Monro

Publications and source records attributed to R E Monro.

18 recordsLinked to original sources

PubMed1971

Substrate- and antibiotic-binding sites at the peptidyl-transferase centre of Escherichia coli ribosomes. Studies on the chloramphenicol. lincomycin and erythromycin sites.

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Anti-Bacterial Agents↗

PubMed1971

Ribosomes, G-factor and siomycin.

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Anti-Bacterial Agents↗

PubMed1969

Protein synthesis: uncoupling of polymerization from template control.

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Alcohols↗

PubMed1969

Action of sparsomycin on ribosome-catalysed peptidyl transfer.

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Anti-Bacterial Agents↗

PubMed1969

On the catalytic center of peptidyl transfer: a part of the 50 S ribosome structure.

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Bacterial Proteins↗

PubMed1969

The peptidyl transferase activity of ribosomes.

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1-Propanol↗

PubMed1969

The function of 80 S ribosomal subunits and effects of some antibiotics.

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Anti-Bacterial Agents↗

PubMed1969

[Peptidyl transfer to human ribosomes and their subunits from spleen, tonsils and tumors].

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Humans↗

PubMed1968

Ribosome-catalysed peptidyl transfer: the polyphenylalanine system.

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Carbon Isotopes↗

PubMed1968

Ribosome-catalyzed peptidyl transfer: substrate specificity at the P-site.

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Bacterial Proteins↗

PubMed1968

Ribosome-catalyzed peptidyl transfer. Effects of cations and pH value.

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Calcium↗

PubMed1968

Antibiotics affecting the peptidyltransferase activity of ribosomes.

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Anti-Bacterial Agents↗

PubMed1967

Ribosome-catalysed peptidyl transfer: effects of some inhibitors of protein synthesis.

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Anti-Bacterial Agents↗

PubMed1967

Effects of some inhibitors of protein synthesis on the binding of aminoacyl tRNA to ribosomal subunits.

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Anti-Bacterial Agents↗

PubMed1967

Catalysis of peptide bond formation by 50 S ribosomal subunits from Escherichia coli.

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Ammonium Chloride↗

PubMed1967

Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide.

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Electrophoresis↗

PubMed1966

A competitive inhibitor of the GTP reaction in protein synthesis.

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Carbon Isotopes↗

PubMed1965

Studies on the structure of parasporal inclusions from Bacillus thuringiensis.

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Bacillus↗