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Susan W. Liebman

Researcher at University of Nevada, Reno

Publications -  113
Citations -  8081

Susan W. Liebman is an academic researcher from University of Nevada, Reno. The author has contributed to research in topics: Gene & Saccharomyces cerevisiae. The author has an hindex of 43, co-authored 111 publications receiving 7618 citations. Previous affiliations of Susan W. Liebman include Washington University in St. Louis & University of Illinois at Urbana–Champaign.

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Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].

TL;DR: It is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the yeast non-Mendelian factor [psi+], and that a certain level of chaper one expression can cure cells of prions without affecting viability.
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Prions Affect the Appearance of Other Prions: The Story of [PIN+]

TL;DR: It is shown that the presence of prions formed by Rnq1 or Ure2 is sufficient to make cells [PIN(+], suggesting the existence of a general mechanism by which the appearance ofPrions is enhanced by heterologous prion aggregates.
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Genesis and Variability of [ PSI ] Prion Factors in Saccharomyces cerevisiae

TL;DR: In this paper, it was shown that it is the overproduction of Sup35 protein, and not the excess of SUP35 DNA or mRNA, that causes the appearance of non-Mendelian factors.
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Genetic and Environmental Factors Affecting the de novo Appearance of the [PSI + ] Prion in Saccharomyces cerevisiae

TL;DR: It is hypothesized that in addition to the [PSI+] prion-determining domain in the Sup35p N-terminus, there is another self-propagating conformational determinant in the C-proximal part of Sup 35p and that this second prion is responsible for the Pin+ phenotype.
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Prions in Yeast

TL;DR: This review summarizes what has been learned from yeast prions and continues to lead the way in understanding cellular control of prion propagation, prion structure, mechanisms of de novo prion formation, specificity ofPrion transmission, and the biological roles of prions.