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Denise Faustmann
Titel
Previous and current research
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Assays to detect protein aggregation and prion formation in yeast cells. (A) Yeast cells show a change in the colony color depending on the absence ([prion-]) or presence ([PRION+]) of a prion. (B) Using fluorescence microscopy to detect aggregation of a prion protein that is fused to GFP. (C) Detecting prion aggregates in lysates of yeast cells expressing a GFP-tagged prion protein.
Future prospects and goals
Perform proteome-wide screens to identify a comprehensive set of aggregating proteins in different model organisms.
Identify and characterize sequence patterns and domains that drive or prevent the assembly of aggregates.
Identify physiological stimuli that induce aggregation and characterize the factors that regulate the formation of aggregates with a particular focus on the protein quality control machinery and the cytoskeleton.
- Investigate how aggregation affects the physiological state of a cell, and how it impacts developmental decisions and contributes to the adaptation to stress and environmental change.
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Selected publications
Alberti S, Halfmann R, Lindquist S (2010): Biochemical, cell biological and genetic assays to analyze amyloid and prion aggregation in yeast. Methods in Enzymology, in press.
Halfmann R, Alberti S, Lindquist S (2010): Prions, protein homeostasis and phenotypic diversity. Trends in Cell Biology, in press.
Alberti S, Halfmann R, King O, Kapila A, Lindquist S (2009): A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell, 137,146-158.
Alberti S, Gitler AD, Lindquist S (2007): A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast, 24, 913-919.