Self-Perpetuating Structural States in Biology, Disease, and Genetics (2002)
Chapter: Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
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Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
Next Chapter: The insulation of genes from external enhancers and silencing chromatin
Suggested Citation:
"Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity." National Academy of Sciences. 2002. Self-Perpetuating Structural States in Biology, Disease, and Genetics. Washington, DC: The National Academies Press.
doi: 10.17226/10620.
Suggested Citation:
"Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity." National Academy of Sciences. 2002. Self-Perpetuating Structural States in Biology, Disease, and Genetics. Washington, DC: The National Academies Press.
doi: 10.17226/10620.
Suggested Citation:
"Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity." National Academy of Sciences. 2002. Self-Perpetuating Structural States in Biology, Disease, and Genetics. Washington, DC: The National Academies Press.
doi: 10.17226/10620.
Suggested Citation:
"Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity." National Academy of Sciences. 2002. Self-Perpetuating Structural States in Biology, Disease, and Genetics. Washington, DC: The National Academies Press.
doi: 10.17226/10620.
Suggested Citation:
"Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity." National Academy of Sciences. 2002. Self-Perpetuating Structural States in Biology, Disease, and Genetics. Washington, DC: The National Academies Press.
doi: 10.17226/10620.
Suggested Citation:
"Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity." National Academy of Sciences. 2002. Self-Perpetuating Structural States in Biology, Disease, and Genetics. Washington, DC: The National Academies Press.
doi: 10.17226/10620.
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