Results 211 to 220 of about 82,783 (260)
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Transformation of yeast by infectious prion particles
Methods, 2006We present methods to prepare infectious Sup35 protein aggregates and use them for genetic transformation of yeast. The protein aggregates are prepared from bacterially expressed recombinant protein, which is converted to amyloid fibers by extended incubation or by nucleated growth using yeast prion particles as seeds.
Chih-Yen KING
exaly +3 more sources
Generation of Sendai virus nucleocapsid-like particles in yeast
Virus Research, 2005The gene encoding Sendai virus nucleocapsid protein was cloned into the yeast Saccharomyces cerevisiae expression vector pFGG3 under control of GAL7 promoter. The high level of recombinant Sendai virus nucleocapsid protein expression (12-14 mg/l of yeast culture) was obtained.
Takemasa Sakaguchi +2 more
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Ribosomal precursor particles from yeast
Experimental Cell Research, 1975Abstract Ribosomal precursor particles were extracted from the yeast Saccharomyces carlsbergensis and analysed. After a brief labelling of yeast protoplasts with 3 H-uridine, three basic ribonucleoprotein components were detected, sedimenting at approx. 90S, 66S and 43S in sucrose gradients containing magnesium. The 90S particles contained the 37S
J, Trapman, J, Retèl, R J, Planta
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Annual Review of Microbiology, 1980
INTRODUCTION ......... .. ..... ..... ..... .. ... ....... 49 The Killer Character 50 The killing reaction ....... ..... 51 Other killer systems .. ......... ......... ..... ...... ...... 51 ScVas a model system 52 PHYSICAL PROPERTIES OF ScV PARTICLES 52 CAPSID POLYPEPTIDES ........ 55 ScV RNAs 56 Structure .. .
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INTRODUCTION ......... .. ..... ..... ..... .. ... ....... 49 The Killer Character 50 The killing reaction ....... ..... 51 Other killer systems .. ......... ......... ..... ...... ...... 51 ScVas a model system 52 PHYSICAL PROPERTIES OF ScV PARTICLES 52 CAPSID POLYPEPTIDES ........ 55 ScV RNAs 56 Structure .. .
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Analysis of Lipid Particles from Yeast
2009Quantitative analysis of components from different subcellular fractions is a key to the understanding of metabolic function as well as to the origin, the biogenesis, and the crosstalk of organelles. The yeast is an excellent model organism to address such questions from the biochemical, molecular biological, and cell biological viewpoints.
Melanie, Connerth +3 more
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Synthesis and assembly of human vault particles in yeast
Biotechnology and Bioengineering, 2018AbstractVault particles are the largest naturally occurring ribonucleoprotein complexes found in the cytoplasm. In all 78 copies of major vault protein (MVP) assemble on polyribosome templates, forming recombinant vault particles, which are of great interest as encapsulation carriers for therapeutics delivery and enzyme stabilization.
Meng Wang +4 more
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Yeast Retrotransposon Particles as Antigen Delivery Systems
Annals of the New York Academy of Sciences, 1995The development of technologies to produce recombinant proteins for use in the pharmaceutical industry has made substantial advances, in particular in the area of generating antigens containing multiple copies of important immunological regions. One such antigen-carrier system is based on the ability of a protein encoded by the yeast retrotransposon ...
A J, Kingsman +3 more
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The yeast Ty virus-like particles
Yeast, 2000Virus-like particle (VLP) assembly is a crucial step of the life cycle of retrotransposons. The S. cerevisiae Ty elements represent an interesting model for the analysis of these particles and thus have been studied extensively. Our current knowledge of the organisation and assembly of Ty1 and Ty3 VLPs is reviewed here.
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Virus-like particles in yeast: Isolation and infectivity
Zeitschrift für allgemeine Mikrobiologie, 1978Virus-like particles containing electron dense cores are seen in thin sections of intact and degenerated cells of a thermosensitive (ts) strain of Candida tropicalis. A particulate fraction not present in wild-type cells has been isolated from the ts cells disrupted by pressure. The particles are 80-120 nm in diameter.
G F, Nesterova +3 more
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