Results 161 to 170 of about 254,282 (203)

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 ...
D, Sleep, G P, Belfield, D J, Ballance, J, Steven, S, Jones, L R, Evans, P D, Moir, A R, Goodey   +7 more
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Assaying protein ubiquitination in Saccharomyces cerevisiae

2002
Publisher 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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High mobility group proteins of Saccharomyces cerevisiae

Biochemistry, 1980
The 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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UV-inducible proteins in Saccharomyces cerevisiae

Current Genetics, 1985
Two 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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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.
Qian, Wang, Yu V, Fu, Wei, Xiao
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Saccharomyces cerevisiae Ssb proteins

1997
Abstract The SSB1, SSB2 genes (initially known as YG101, YG103) were isolated by virtue of their high degree of similarity to Drosophila HSP70 genes (Ingolia et al., 1982; Craig, Jacobsen, 1985).
T Ziegelhoffer, E A Craig
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Purification of Membrane Proteins Overexpressed in Saccharomyces cerevisiae

2022
Membrane protein (MP) functional and structural characterization requires large quantities of high-purity protein for downstream studies. Barriers to MP characterization include ample overexpression, solubilization, and purification of target proteins while maintaining native activity and structure.
Landon, Haslem, Marina, Brown, Xin A, Zhang, Jennifer M, Hays, Franklin A, Hays   +4 more
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Chromosomal proteins in Saccharomyces cerevisiae

Current Genetics, 1980
Proteins were isolated from purified yeast chromatin and subjected to two-dimensional electrophoresis. The cellular and the chromosomal content of the major nonhistone proteins was measured. Two polypeptides of molecular weights 55,000 and 53,000, identified as α and β tubulin, and a polypeptide of molecular weight 63,000, associated with the nuclear ...
K, Gulløv, J, Friis
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Protein-Tyrosine Kinase Activity in Saccharomyces cerevisiae

Science, 1986
Saccharomyces cerevisiae was examined for tyrosine kinase activity in vitro because this organism offers molecular and genetic approaches for analyzing the role of tyrosine phosphorylation in cellular growth control that are unavailable in higher eukaryotes.
G, Schieven, J, Thorner, G S, Martin
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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
E T, Bucovaz, S J, Tarnowski, W C, Morrison, R M, Macleod, J C, Morrison, C M, Sobhy, J L, Rhoades, J E, Fryer, J M, Wakim, W D, Whybrew   +9 more
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