Results 301 to 310 of about 188,278 (356)
Cryo-EM structure of the naked mole-rat ribosome reveals a stabilized split 28S rRNA
Gül M +4 more
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Tracing low-level structures in cryo-electron tomography. [PDF]
Alvarez Brecht P +5 more
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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
openaire +2 more sources
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
openaire +3 more sources
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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