Results 271 to 280 of about 155,571 (316)
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Assaying protein ubiquitination in Saccharomyces cerevisiae
2002Publisher Summary The covalent modification of target proteins by the polypeptide ubiquitin (Ub) is involved in a wide array of cellular processes, ranging from cell cycle progression and receptor-mediated endocytosis to endoplasmic reticulum-associated degradation and cell-type specification.
Jeffrey D, Laney, Mark, Hochstrasser
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UV-inducible proteins in Saccharomyces cerevisiae
Current Genetics, 1985Two UV-inducible proteins have been detected in the yeast, Saccharomyces cerevisiae. The proteins have molecular weights of 78,000 Daltons and 23,000 Daltons. This induction is specific for UV-irradiation as exposure to X-rays, mitomycin C and heat shock does not result in the synthesis of the proteins.
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Detection of Protein Arginine Methylation in Saccharomyces cerevisiae
2014Protein 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.
Christopher A, Jackson, Michael C, Yu
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The Saccharomyces cerevisiae homologue of ribosomal protein S26
Gene, 1994The 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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Overview of Protein Expression in Saccharomyces cerevisiae
Current Protocols in Protein Science, 1995AbstractThis overview presents vectors and host strains that are available to direct gene expression in S. cerevisiae, including information on promoters, vector maintenance and copy number, transcription terminators, and selectable markers. Challenges to the expression of foreign proteins are also covered, including attainment of desired production ...
R L, Strausberg, S L, Strausberg
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Binding of Saccharomyces cerevisiae extracellular proteins to glucane
Archives of Biochemistry and Biophysics, 1992Interactions 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.
V, Mrsa, T, Ugarković, S, Barbarić
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High mobility group proteins of Saccharomyces cerevisiae
Biochemistry, 1980The yeast Saccharomyces cerevisiae contains four proteins having amino acid compositions typical of the high mobility group (HMG) proteins. Three of these are eluted from chromatin by 0.35 M NaCl; one is not, but it is eluted by 0.25 N HCl. It follows that HMGs cannot, in general, be defined by extractability criteria.
S, Weber, I, Isenberg
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Classical NLS Proteins from Saccharomyces cerevisiae
Journal of Molecular Biology, 2008Proteins 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 ...
Silvia, Hahn +3 more
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Scarless Genomic Protein Labeling in Saccharomyces cerevisiae
2020Labeling 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.
Qian, Wang, Yu V, Fu, Wei, Xiao
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Evaluation of Unconventional Protein Secretion in Saccharomyces cerevisiae
2014Recent development of large-scale analyses such as the secretome analysis has enabled the discovery of a vast number of intracellular proteins that are secreted outside the cell. Often, these proteins do not contain any known signal sequence required for conventional protein secretion.
Natsuko, Miura, Mitsuyoshi, Ueda
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