Results 171 to 180 of about 57,431 (202)
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Down-regulation of ribosomal protein L22 in non-small cell lung cancer
Medical Oncology, 2013Ribosomal protein L22 (RPL22), an RNA-binding protein, is a constituent of the 60S large ribosomal subunit. As reported, RPL22 is not required in protein synthesis, and mutations of RPL22 were the main cause of macrolide resistance in bacteria. In vertebrates, RPL22 mutation might increase the proliferation of cells and then increase cancer risk ...
Haibo Sun, Xiaowei Yu
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L22 Ribosomal Protein and Effect of Its Mutation on Ribosome Resistance to Erythromycin
Journal of Molecular Biology, 2002The ribosomal protein L22 is a core protein of the large ribosomal subunit interacting with all domains of the 23S rRNA. The triplet Met82-Lys83-Arg84 deletion in L22 from Escherichia coli renders cells resistant to erythromycin which is known as an inhibitor of the nascent peptide chain elongation. The crystal structure of the Thermus thermophilus L22
Victor Streltsov +2 more
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2023
The Minor Planet Electronic Circulars contain information on unusual minor planets, routine data on comets and natural satellites, and occasional editorial announcements. They are published on behalf of Division F of the International Astronomical Union by the Minor Planet Center, Smithsonian Astrophysical Observatory, Cambridge, MA 02138, U.S.A.
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The Minor Planet Electronic Circulars contain information on unusual minor planets, routine data on comets and natural satellites, and occasional editorial announcements. They are published on behalf of Division F of the International Astronomical Union by the Minor Planet Center, Smithsonian Astrophysical Observatory, Cambridge, MA 02138, U.S.A.
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Prediction of resistance to erythromycin in the genus Rickettsia by mutations in L22 ribosomal protein [PDF]
Journal of Antimicrobial Chemotherapy, 2005 Typhus group (TG) rickettsiae are naturally susceptible to erythromycin whereas spotted fever group (SFG) rickettsioses are not. The aim of this study was to compare in silico genetic determinants known to be associated with resistance to macrolide compounds.Available sequences of the 23S RNA gene, and L4 and L22 ribosomal proteins of rickettsial ...
Jean-Marc Rolain
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Xenopus laevis ribosomal protein L22: full-length cDNA sequence and expression analysis
Gene, 1995A cDNA clone was isolated from a Xenopus laevis embryo library and sequenced. Primer extension experiments indicated the full-length nature of the insert and the encoded product was identified on a two dimensional gel as ribosomal protein (r-protein) L22. The 510-bp L22 cDNA sequence presents short untranslated regions and a 5'-end polypyrimidine tract
Rapanotti, MC +3 more
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Interaction of casein kinase II with ribosomal protein L22 of Drosophila melanogaster
Biochemical and Biophysical Research Communications, 2002The ubiquitous eukaryotic protein kinase CKII (casein kinase II) has been found to interact with a number of cellular proteins, either through the catalytic subunit or the regulatory subunit. Using the yeast two-hybrid screening method, we found that the catalytic subunit of Drosophila melanogaster CKII (DmCKII) interacts with Drosophila ribosomal ...
Wenfan, Zhao +2 more
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A Novel Heparin-Binding Protein, HBp15, Is Identified as Mammalian Ribosomal Protein L22
Biochemical and Biophysical Research Communications, 1994A 15kDa-protein (HBp15) was purified from mouse submandibular gland and bovine brain by virtue of its heparin-binding property. The amino acid sequences of mouse and bovine HBp15 showed a high degree of homology to a sea urchin protein encoded by gene called "development specific protein 217." Using reverse transcription-polymerase chain reaction ...
Y, Fujita +8 more
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A temperature-sensitive mutant ofEscherichia coli with an alteration in ribosomal protein L22
Genetica, 1994A temperature-sensitive, protein synthesis-defective mutant of Escherichia coli exhibiting an altered ribosomal protein L22 has been investigated. The temperature-sensitive mutation was mapped to the rplV gene for protein L22. The genes from the wild type and mutant strains were amplified by the polymerase chain reaction and the products were sequenced.
Burnette-Vick, Bonnie +2 more
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Acta Crystallographica Section D: Biological Crystallography, 2001
A mutant form of Thermus thermophilus ribosomal protein L22 responsible for erythromycin resistance has been overexpressed in Escherichia coli, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion technique. While several different crystallization conditions were found, only one set of conditions yielded crystals suitable ...
Victor Streltsov +2 more
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A mutant form of Thermus thermophilus ribosomal protein L22 responsible for erythromycin resistance has been overexpressed in Escherichia coli, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion technique. While several different crystallization conditions were found, only one set of conditions yielded crystals suitable ...
Victor Streltsov +2 more
exaly +3 more sources
The comparison of L11 and L22-norm minimization methods
2020L2-norm, also known as the least squares method was widely used in the adjustment calculus. The weaknesses of the least squares method were the effect of gross measurements error on the solution and the disturbance and absorbance of gross error on the solution. L1-norm, also known as the least absolute values method, was affected by almost none or very
Bektaş S., Şişman Y.
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