Results 301 to 310 of about 343,033 (331)
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Current Opinion in Cell Biology, 2002
The past year has seen dramatic changes in our understanding of ribosome synthesis, fuelled largely by advances in proteomic analysis. It is now possible to outline the pathway of ribosome assembly, which is highly dynamic and involves a remarkable separation of the factors involved in the synthesis of the 40S and 60S ribosomal subunits.
FATICA, Alessandro, TOLLERVEY D.
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The past year has seen dramatic changes in our understanding of ribosome synthesis, fuelled largely by advances in proteomic analysis. It is now possible to outline the pathway of ribosome assembly, which is highly dynamic and involves a remarkable separation of the factors involved in the synthesis of the 40S and 60S ribosomal subunits.
FATICA, Alessandro, TOLLERVEY D.
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2012
Ribosome display is a powerful polymerase chain reaction-based in vitro display technology that is well suited to the selection and evolution of proteins. This technology exploits cell-free translation to achieve coupling of phenotype and genotype by the production of stabilized ribosome complexes, whereby translated protein and their cognate mRNA ...
George, Thom, Maria, Groves
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Ribosome display is a powerful polymerase chain reaction-based in vitro display technology that is well suited to the selection and evolution of proteins. This technology exploits cell-free translation to achieve coupling of phenotype and genotype by the production of stabilized ribosome complexes, whereby translated protein and their cognate mRNA ...
George, Thom, Maria, Groves
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Annual Review of Genetics, 2018
Protein synthesis consumes a large fraction of available resources in the cell. When bacteria encounter unfavorable conditions and cease to grow, specialized mechanisms are in place to ensure the overall reduction of costly protein synthesis while maintaining a basal level of translation.
Prossliner, Thomas +3 more
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Protein synthesis consumes a large fraction of available resources in the cell. When bacteria encounter unfavorable conditions and cease to grow, specialized mechanisms are in place to ensure the overall reduction of costly protein synthesis while maintaining a basal level of translation.
Prossliner, Thomas +3 more
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Ribosomes, ribosomal subunits and ribosomal proteins of Lactococcus lactis IL1403
Biochimie, 1992Abstract 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
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Ribosomal RNA and ribosomal proteins in corynebacteria
Journal of Biotechnology, 2003Ribosomal 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
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Ribosomal protein paralogues in ribosome specialization
Philosophical Transactions of the Royal Society B: Biological SciencesRibosomes 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
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Terbium binding to ribosomes and ribosomal RNA
Biochemistry, 1975Terbium 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
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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.
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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.
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Crystallization of Ribosomes, Ribosomal Subunits, and Individual Ribosomal Proteins
1991There 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
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Orthogonal Ribosome Biofirewall
ACS Synthetic Biology, 2017Biocontainment 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
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