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National Academy of Sciences. 2002. Self-Perpetuating Structural States in Biology, Disease, and Genetics. Washington, DC: The National Academies Press. https://doi.org/10.17226/10620.

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Publication Info

140 pages |  8.5 x 11 |  DOI: https://doi.org/10.17226/10620
Chapters skim
Front Matter i-vi
Self-perpetuating structural states in biology, disease, and genetics 1-1
Transmission of prions 2-7
Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein 8-15
Interactions among prions and prion “strains” in yeast 16-23
Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington 24-30
Chaperoning brain degeneration 31-35
Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity 36-42
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases 43-50
Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity 51-56
The insulation of genes from external enhancers and silencing chromatin 57-61
Histone H3 lysine 4 methylation is mediated by Set1 and promotes maintenance of active chromatin states in fission yeast 62-69
Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+] 70-77
Heritable chromatin structure: Mapping “memory” in histones H3 and H4 78-85
Does heterochromatin protein 1 always follow code? 86-93
Self-perpetuating epigenetic pili switches in bacteria 94-100
Histone H3 variants specify modes of chromatin assembly 101-108
Induction and maintenance of nonsymmetrical DNA methylation in Neurospora 109-114
Locus-specific control of asymmetric and CpNpG methylation by the DRM and CMT3 methyltransferase genes 115-122
RNA-directed DNA methylation in Arabidopsis 123-134

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