I. Protein Folding and Prions
II. Prions and Evolution
Part II: Prions and Evolution
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What do "mad cows", people with neurodegenerative diseases and yeast cells growing happily on a deadly antibiotic have in common? They are all experiencing the consequences of misfolded proteins. Each organism has thousands of different proteins, which define its nature. Like origami paper, they can take the right path and fold into a swan or take the wrong path and fold into a rapacious hawk. The consequences can be deadly, leading to devastating neurodegenerative diseases in humans. Remarkably, a very similar folding process has been discovered in yeast, where it does no harm and can be studied easily and inexpensively. More >>
Susan Lindquist is a member and former Director of the Whitehead Institute for Biomedical Research, which she guided as the Whitehead Genome Center was transformed into the neighboring Broad Institute.
She is also a Howard Hughes Medical Institute Investigator and Professor of Biology at Massachusetts Institute of Technology. She received her Ph.D. in biology from Harvard and was a postdoctoral fellow of the American Cancer Society. She was named the Albert D. Lasker Professor of Medical Sciences in 1999 at the University of Chicago. A pioneer in the study of protein folding, she established that protein homeostasis has profound and completely unexpected effects on normal biology and disease. More >>
- Arthur Horwich iBioSeminar: Chaperone-Assisted Protein Folding
- Susan Lindquist iBioEducation: Protein Folding and Disease
- Peter Walter iBioMagazine: Unfolding the Unfolded Protein Response
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True HL, Lindquist SL, 2000. A yeast prion provides an exploratory mechanism for genetic variation and phenotypic diversity. Nature 407: 477-83.
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Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu, J-J, Lindquist S, 1997. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of Saccharomyces cerevisiae. Cell 89: 811-19.
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