title: [New aspects of research upon the yeast Saccharomyces cerevisiae [PSI+] prion].
abstract: One of the key feature of prions is the ability to be stable in two alternative conformations. Besides the intensively studied mammalian prions, there are also prion proteins present in the yeast Saccharomyces cerevisiae. Research in this field has lead to opposite hypotheses that explain the sense of presence of [PSI+] prion in yeast cells. Some authors postulate e of role of the prions in the evolution of S. cerevisiae, whereas other investigators point out the negative influence of these particles upon the yeast physiology. In recent years, yeast prions are used for anti-prion drug screening, because of common features with mammalian prions. This work presents the most intensively studied fields of the research carried out on [PSI+] prion in yeast.
authors.affiliation: Załdad Biologii Molekularnej, Instytut Biochemrnii, Wydział Biologii, Uniwersytet Warszawski, Warszawa. takao@biol.uw.edu.pl
authors.forename: Takao
authors.initials: T
authors.lastname: Ishikawa
mesh_terms: D000818:Animals; D004353:Drug Evaluation, Preclinical; D019143:Evolution, Molecular; D008954:Models, Biological; D010454:Peptide Termination Factors; D010641:Phenotype; D017096:Prion Diseases / Q000378:metabolism / Q000503:physiopathology; D011328:Prions / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D010454:Peptide Termination Factors; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins