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Ribosomes, ribosomal subunits and ribosomal proteins of Lactococcus lactis IL1403

Biochimie, 1992
Abstract The preparation of ribosomes and ribosomal subunits of Lactococcus lactis and the characterization of the proteins of the subunits by one- and two-dimensional polyacrylamide gel electrophoresis and ion exchange chromatography are described.
N, Limas Nzouzi, M F, Guerin, D H, Hayes
openaire   +2 more sources

Specialized ribosomes and the control of translation.

Biochemical Society Transactions, 2018
The control of translation is increasingly recognized as a major factor in determining protein levels in the cell. The ribosome - the cellular machine that mediates protein synthesis - is typically seen as a key, but invariant, player in this process ...
Huili Guo
semanticscholar   +1 more source

Ribosomal RNA and ribosomal proteins in corynebacteria

Journal of Biotechnology, 2003
Ribosomal RNAs (rRNAs) (16S, 23S, 5S) encoded by the rrn operons and ribosomal proteins play a very important role in the formation of ribosomes and in the control of translation. Five copies of the rrn operon were reported by hybridization studies in Brevibacterium (Corynebacterium) lactofermentum but the genome sequence of Corynebacterium glutamicum ...
Juan F, Martín   +3 more
openaire   +2 more sources

Ribosomal protein paralogues in ribosome specialization

Philosophical Transactions of the Royal Society B: Biological Sciences
Ribosomes are macromolecular complexes responsible for protein synthesis, comprising ribosomal proteins (RPs) and ribosomal RNA. While most RPs are present as single copies in higher eukaryotes, a handful of them have paralogues that emerged through duplication events.
Ivan Milenkovic, Eva Maria Novoa
openaire   +2 more sources

Terbium binding to ribosomes and ribosomal RNA

Biochemistry, 1975
Terbium binding to rat liver ribosomes and ribosomal RNA (rRNA) was examined by equilibrium dialysis and fluorescence spectroscopy. Upon binding to ribosomes and rRNA, the enhancement of terbium fluorescence emission at both 488 and 541 nm was dependent only upon the amount of bound terbium and independent of ionic strength.
T D, Barela, S, Burchett, D E, Kizer
openaire   +2 more sources

Structure of Ribosomes

Canadian Journal of Biochemistry, 1979
Ribosomes are multicomponent particles on which biosynthesis of proteins occurs in all organisms. The best known ribosome, namely that of Escherichia coli, consists of three RNAs and 53 different proteins. All proteins have been isolated and characterized by chemical, physical, and immunological methods. The primary sequences of 47 E.
openaire   +2 more sources

Crystallization of Ribosomes, Ribosomal Subunits, and Individual Ribosomal Proteins

1991
There is interest in the three-dimensional structure of the ribosome since it is a unique multicomponent biological system responsible for the biosynthesis of protein in the cell. The exceedingly complex structure of ribosomes (for example, the Escherichia coli ribosome, the molecular weight of which is 2.15•106 Da, consists of three types of RNA and ...
B. K. Vainshtein, S. D. Trakhanov
openaire   +1 more source

Orthogonal Ribosome Biofirewall

ACS Synthetic Biology, 2017
Biocontainment systems are crucial for preventing genetically modified organisms from escaping into natural ecosystems. Here, we describe the orthogonal ribosome biofirewall, which consists of an activation circuit and a degradation circuit. The activation circuit is a genetic AND gate based on activation of the encrypted pathway by the orthogonal ...
Bin Jia   +7 more
openaire   +3 more sources

Ribosome-inactivating proteins

Toxicon, 1997
Abstract Ribosome-inactivating proteins (RIPs, review by Barbieri et a/. 1993) are a class of proteins present in various tissues of several plants which inactivate mammalian ribosomes and, with less activity and to variable extent, plant, fungal, and bacterial ribosomes. They are enzymes, N-glycosidases, which release adenine from rRNA.
openaire   +3 more sources

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