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Biomedical subjects

M Nirenberg

Publications and source records attributed to M Nirenberg.

At least 109 records · Page 6Linked to original sources
PubMed1970

Regulation of acetylcholinesterase in neuroblastoma cells.

The specific activity of mouse neuroblastoma acetylcholinesterase (EC 3.1.1.7) increased 25-fold when the rate of cell division was restricted. The results show that acetylcholinesterase activity is regulated in neuroblastoma cells and that the regulatory mechanism is inversely related to the rate of cell division. Under the same conditions the specific activity of catechol-O-methyl transferase (EC 2.1.1.6) did not change significantly.

Acetylcholinesterase↗
PubMed1969

Neuronal tumor cells with excitable membranes grown in vitro.

Mouse neuroblastoma cells grown in vitro are capable of generating action potentials in response to electrical stimulation. A wide spectrum of responses was observed with different cells ranging from passive responses to action potentials. A hypothesis is proposed concerning the acquisition of electrical excitability as neuroblasts mature into neurons.

Action Potentials↗
PubMed1968

Genetic memory.

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Adenine Nucleotides↗
PubMed1968

Sequential translation of trinucleotide codons for the initiation and termination of protein synthesis.

Terminal events in protein synthesis were studied with trinucleotide codons. Initiator and terminator trinucleotides sequentially stimulate N-formyl-methionyl-tRNA binding to ribosomes and the release of free N-formyl-methionine from the ribosomal intermediate. The release factor discovered by Capecchi is also required. The trinucleotides UGA, UAA, and UAG were found to be terminator codons. This pattern of codon degeneracy has not been observed with other trinucleotides and transfer RNA.

Bacterial Proteins↗
PubMed1967

Fine structure of RNA codewords recognized by bacterial, amphibian, and mammalian transfer RNA.

Nucleotide sequences of 50 RNA codons recognized by amphibian and mammalian liver transfer RNA preparations were determined and compared with those recognized by Escherichia coli transfer RNA. Almost identical translations were obtained with transfer RNA from guinea pig liver, Xenopus laevis liver (South African clawed toad), and E. coli. However, guinea pig and Xenopus transfer RNA differ markedly from E. coli transfer RNA in relative response to certain trinucleotides. Transfer RNA from mammalian liver, amphibian liver, and amphibian muscle respond similarly to trinucleotide codons. Thus the genetic code is essentially universal, but transfer RNA from one organism may differ from that of another in relative response to some codons.

Amino Acid Sequence↗