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Identification of CBS2 as a mitochondrial protein in Saccharomyces cerevisiae

Molecular and General Genetics MGG, 1990
The nuclear genome encoded yeast protein CBS2 is required for translational activation of mitochondrial cytochrome b RNA. Genetic studies have shown that the target sequence of the CBS2 protein is the 5' untranslated leader sequence of cytochrome b RNA. Here we report on the intracellular localization of CBS2.
Uwe Michaelis, Gerhard Rödel
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Coenzyme a-synthesizing protein complex of Saccharomyces cerevisiae

Molecular and Cellular Biochemistry, 1980
The coenzyme A-synthesizing protein complex (CoA-SPC) is a multienzyme complex of Saccharomyces cerevisiae (Bakers' yeast), which has a molecular weight in excess of 200,000 as determined by Sephadex G-200 column chromatography. This multienzyme complex, which is insoluble in the crude yeast cell lysate, has been purified 229-fold. A cellular component
Robert M. Macleod   +9 more
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Saccharomyces Cerevisiae Strains that Overexpress Heterologous Proteins

Nature Biotechnology, 1991
We describe a system that facilitates the selection of host mutants that overproduce a range of secreted and internally produced heterologous proteins in Saccharomyces cerevisiae. These mutants were initially selected for their ability to oversecrete recombinant human albumin (rHA), as detected by a direct visual assay that relies upon antibody ...
P.D. Moir   +7 more
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The Saccharomyces cerevisiae homologue of ribosomal protein S26

Gene, 1994
The nucleotide sequence of RPS26, the gene encoding a homologue of ribosomal protein small subunit S26 in Saccharomyces cerevisiae, was determined. The deduced amino-acid sequence showed significant identity with its counterparts from Neurospora crassa, human, rat and Arabidopsis thaliana. Disruption of RPS26 resulted in the formation of micro-colonies,
Wu, M., Tan, H.-M.
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Detection of Protein Arginine Methylation in Saccharomyces cerevisiae

2014
Protein arginine methylation has emerged to be an important regulator of cellular protein functions. Techniques that uncover the presence of methylarginines on a protein provide an important step towards understanding the functional role of arginine methylation.
Michael C. Yu, Christopher A. Jackson
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Binding of Saccharomyces cerevisiae extracellular proteins to glucane

Archives of Biochemistry and Biophysics, 1992
Interactions of Saccharomyces cerevisiae cell wall proteins with purified yeast glucane were studied. Using the beta-glucanase (BGL2 gene product) as the model cell wall protein, strong binding to glucane was demonstrated at pH lower than 7, while at pH higher than 8 the reaction did not occur.
Slobodan Barbarić   +2 more
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Classical NLS Proteins from Saccharomyces cerevisiae

Journal of Molecular Biology, 2008
Proteins can enter the nucleus through various receptor-mediated import pathways. One class of import cargos carries a classical nuclear localization signal (cNLS) containing a short cluster of basic residues. This pathway involves importin alpha (Impalpha), which possesses the cNLS binding site, and importin beta (Impbeta), which translocates the ...
Stefanie Caesar   +3 more
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Adaptation of Saccharomyces cerevisiae expressing a heterologous protein

Journal of Biotechnology, 2008
Production of the heterologous protein, bovine aprotinin, in Saccharomyces cerevisiae was shown to affect the metabolism of the host cell to various extent depending on the strain genotype. Strains with different genotypes, industrial and laboroatory, respectively, were investigated.
Lisbeth Olsson   +5 more
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Scarless Genomic Protein Labeling in Saccharomyces cerevisiae

2020
Labeling a protein of interest is widely used to examine its quantity, modification, localization, and dynamics in the budding yeast Saccharomyces cerevisiae. Fluorescent proteins and epitope tags are often used as protein fusion tags to study target proteins.
Yu V. Fu, Qian Wang, Wei Xiao, Wei Xiao
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Protein methylation in the yeast Saccharomyces cerevisiae

1982
Beside cytochrome c. little is known on the occurence and nature of methylated proteins in yeast. Cannon et al. (1977) and Kruiswijk et al. (1978) have used the classical method of double labelling with methionine to detect methylated proteins in yeast ribosomes.
Eric Costers   +2 more
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